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Conserved domains on  [gi|15597620|ref|NP_251114|]
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peptide synthase [Pseudomonas aeruginosa PAO1]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 11481510)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK05691 PRK05691
peptide synthase; Validated
1-4342 0e+00

peptide synthase; Validated


:

Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 8278.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAFELPTTLVQALRRRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAA 80
Cdd:PRK05691    1 MMDAFELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAqLSAANAPQLLCVDQLDPAVAEAWD 160
Cdd:PRK05691   81 FFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEE-LAAANAPELLCVDTLDPALAEAWQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   161 EPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGI--GADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 238
Cdd:PRK05691  160 EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdlNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   239 LMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRF 318
Cdd:PRK05691  240 LMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   319 DASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNVGE 398
Cdd:PRK05691  320 DPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   399 IWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARK 478
Cdd:PRK05691  400 IWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   479 GRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLE 558
Cdd:PRK05691  480 GRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   559 DGSLDSYALFPGLQAVQEAQPPAGDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQ 638
Cdd:PRK05691  560 DGSLDSYALFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQ 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   639 LFEAPTLQAFSATVARQLAAGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASF 718
Cdd:PRK05691  640 LFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASF 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   719 QRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQ 798
Cdd:PRK05691  720 QRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDE 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   799 EHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPV 878
Cdd:PRK05691  800 EHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPV 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   879 LELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQG 958
Cdd:PRK05691  880 LELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQG 959
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   959 LVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQ--LFQVLFNHQQRDLSALRRLPGLL 1036
Cdd:PRK05691  960 LVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREqgLFQVMFNHQQRDLSALRRLPGLL 1039
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1037 ADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLA 1116
Cdd:PRK05691 1040 AEELPWHSREAKFDLQLHSEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA 1119
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1117 EWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLL 1196
Cdd:PRK05691 1120 QWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLL 1199
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1197 AIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVI 1276
Cdd:PRK05691 1200 AILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVI 1279
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1277 YTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVEL 1356
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAEL 1359
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1357 VRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED 1436
Cdd:PRK05691 1360 VQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAED 1439
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1437 GERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADG 1516
Cdd:PRK05691 1440 GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADG 1519
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1517 VLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEqnqRLRAALQAELPE 1596
Cdd:PRK05691 1520 ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPE 1596
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1597 YMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIV 1676
Cdd:PRK05691 1597 YMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIV 1676
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1677 SRTRQACDVELPLRALFEASELEAFCEQVRAAQAAGRTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGL 1756
Cdd:PRK05691 1677 SRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGM 1756
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1757 ARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDL 1836
Cdd:PRK05691 1757 ARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDL 1836
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1837 ESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQ 1916
Cdd:PRK05691 1837 ERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQ 1916
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1917 RQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDL 1996
Cdd:PRK05691 1917 RQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDL 1996
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1997 RIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQV 2076
Cdd:PRK05691 1997 RIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQV 2076
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2077 MCNVQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQ 2156
Cdd:PRK05691 2077 MCNVQRWEFQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ 2156
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2157 RRIAELPLFAAEERKQLL--LAGTAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVG 2234
Cdd:PRK05691 2157 QRLAELPLLAAAEQQQLLdsLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVG 2236
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2235 PEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVARWCLEEDGP 2314
Cdd:PRK05691 2237 PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLEDDAA 2316
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2315 ALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPL 2394
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPL 2396
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2395 LCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPAS 2474
Cdd:PRK05691 2397 LCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQL 2476
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2475 FFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAER 2554
Cdd:PRK05691 2477 FFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAER 2556
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2555 FVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYV 2634
Cdd:PRK05691 2557 FVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYL 2636
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2635 ASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAG 2714
Cdd:PRK05691 2637 VSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQ 2716
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2715 VWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQAEQGPVQGDSALTP 2794
Cdd:PRK05691 2717 IWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTP 2796
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2795 IQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFD 2874
Cdd:PRK05691 2797 IQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELLWQVTVADFA 2876
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2875 ECAELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRD 2954
Cdd:PRK05691 2877 ECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRD 2956
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2955 WAGRLQAYAGSESLREELGWWQARLGGQPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTA 3034
Cdd:PRK05691 2957 WAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTA 3036
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3035 LARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAQ----SPGESIKAIKEQLRAVPHKGLGYGV 3110
Cdd:PRK05691 3037 LARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPgddaARGESIKAIKEQLRAVPHKGLGYGV 3116
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3111 LRYLADPAVRQAMAALPTAPITFNYLGQFDQSFA-DALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRE 3189
Cdd:PRK05691 3117 LRYLADAAVREAMAALPQAPITFNYLGQFDQSFAsDALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAE 3196
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3190 RYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPG 3269
Cdd:PRK05691 3197 RYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPG 3276
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3270 TGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEFLDWSELPEDGHEERLQALH 3349
Cdd:PRK05691 3277 TGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALH 3356
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3350 KREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESRPANLPTPPRYRDYIAWLQ 3429
Cdd:PRK05691 3357 KQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQ 3436
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3430 RQDLEQSRRWWSESLRGFERPTLVPSDRPFLREHAGESGGMIVGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALT 3509
Cdd:PRK05691 3437 RQDLAQARQWWQDNLRGFERPTPIPSDRPFLREHAGDSGGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALV 3516
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3510 LRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAGQRCTVREWLNRLFERNLELREHEHLPLVAIQES 3589
Cdd:PRK05691 3517 LRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQEC 3596
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3590 SELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTVVCYPGDDLGLHLSYDQRYFEAPTVERLLGEF 3669
Cdd:PRK05691 3597 SELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEF 3676
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3670 KRLLLALADGFHGELEALPLLGEDERDFLLDGCNRSARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRAN 3749
Cdd:PRK05691 3677 KRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAAN 3756
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3750 RLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALFD 3829
Cdd:PRK05691 3757 RLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLD 3836
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3830 ELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQT 3909
Cdd:PRK05691 3837 ELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQT 3916
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3910 ASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQALDGLRWMLPTGEAMP 3989
Cdd:PRK05691 3917 ASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMP 3996
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3990 PELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVA 4069
Cdd:PRK05691 3997 PELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLL----DEALELVPLGAVGELCVA 4072
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4070 GTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE 4149
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE 4152
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4150 AAVAVQEGANGKYLVGYLVPGETPrssadspaglmVEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKA 4229
Cdd:PRK05691 4153 AAVAVQEGVNGKHLVGYLVPHQTV-----------LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKA 4221
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4230 LPALDIGQMQNQAYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTV 4309
Cdd:PRK05691 4222 LPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTV 4301
                        4330      4340      4350
                  ....*....|....*....|....*....|...
gi 15597620  4310 EELASYIESLAPSEISEQKAERLNDLMSKLEML 4342
Cdd:PRK05691 4302 EELAEYIEGLAGSAIDEQKVDRLSDLMAELEGL 4334
 
Name Accession Description Interval E-value
PRK05691 PRK05691
peptide synthase; Validated
1-4342 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 8278.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAFELPTTLVQALRRRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAA 80
Cdd:PRK05691    1 MMDAFELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAqLSAANAPQLLCVDQLDPAVAEAWD 160
Cdd:PRK05691   81 FFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEE-LAAANAPELLCVDTLDPALAEAWQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   161 EPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGI--GADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 238
Cdd:PRK05691  160 EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdlNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   239 LMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRF 318
Cdd:PRK05691  240 LMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   319 DASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNVGE 398
Cdd:PRK05691  320 DPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   399 IWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARK 478
Cdd:PRK05691  400 IWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   479 GRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLE 558
Cdd:PRK05691  480 GRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   559 DGSLDSYALFPGLQAVQEAQPPAGDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQ 638
Cdd:PRK05691  560 DGSLDSYALFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQ 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   639 LFEAPTLQAFSATVARQLAAGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASF 718
Cdd:PRK05691  640 LFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASF 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   719 QRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQ 798
Cdd:PRK05691  720 QRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDE 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   799 EHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPV 878
Cdd:PRK05691  800 EHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPV 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   879 LELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQG 958
Cdd:PRK05691  880 LELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQG 959
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   959 LVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQ--LFQVLFNHQQRDLSALRRLPGLL 1036
Cdd:PRK05691  960 LVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREqgLFQVMFNHQQRDLSALRRLPGLL 1039
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1037 ADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLA 1116
Cdd:PRK05691 1040 AEELPWHSREAKFDLQLHSEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA 1119
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1117 EWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLL 1196
Cdd:PRK05691 1120 QWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLL 1199
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1197 AIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVI 1276
Cdd:PRK05691 1200 AILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVI 1279
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1277 YTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVEL 1356
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAEL 1359
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1357 VRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED 1436
Cdd:PRK05691 1360 VQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAED 1439
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1437 GERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADG 1516
Cdd:PRK05691 1440 GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADG 1519
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1517 VLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEqnqRLRAALQAELPE 1596
Cdd:PRK05691 1520 ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPE 1596
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1597 YMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIV 1676
Cdd:PRK05691 1597 YMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIV 1676
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1677 SRTRQACDVELPLRALFEASELEAFCEQVRAAQAAGRTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGL 1756
Cdd:PRK05691 1677 SRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGM 1756
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1757 ARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDL 1836
Cdd:PRK05691 1757 ARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDL 1836
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1837 ESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQ 1916
Cdd:PRK05691 1837 ERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQ 1916
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1917 RQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDL 1996
Cdd:PRK05691 1917 RQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDL 1996
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1997 RIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQV 2076
Cdd:PRK05691 1997 RIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQV 2076
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2077 MCNVQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQ 2156
Cdd:PRK05691 2077 MCNVQRWEFQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ 2156
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2157 RRIAELPLFAAEERKQLL--LAGTAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVG 2234
Cdd:PRK05691 2157 QRLAELPLLAAAEQQQLLdsLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVG 2236
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2235 PEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVARWCLEEDGP 2314
Cdd:PRK05691 2237 PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLEDDAA 2316
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2315 ALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPL 2394
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPL 2396
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2395 LCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPAS 2474
Cdd:PRK05691 2397 LCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQL 2476
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2475 FFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAER 2554
Cdd:PRK05691 2477 FFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAER 2556
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2555 FVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYV 2634
Cdd:PRK05691 2557 FVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYL 2636
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2635 ASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAG 2714
Cdd:PRK05691 2637 VSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQ 2716
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2715 VWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQAEQGPVQGDSALTP 2794
Cdd:PRK05691 2717 IWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTP 2796
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2795 IQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFD 2874
Cdd:PRK05691 2797 IQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELLWQVTVADFA 2876
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2875 ECAELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRD 2954
Cdd:PRK05691 2877 ECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRD 2956
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2955 WAGRLQAYAGSESLREELGWWQARLGGQPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTA 3034
Cdd:PRK05691 2957 WAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTA 3036
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3035 LARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAQ----SPGESIKAIKEQLRAVPHKGLGYGV 3110
Cdd:PRK05691 3037 LARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPgddaARGESIKAIKEQLRAVPHKGLGYGV 3116
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3111 LRYLADPAVRQAMAALPTAPITFNYLGQFDQSFA-DALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRE 3189
Cdd:PRK05691 3117 LRYLADAAVREAMAALPQAPITFNYLGQFDQSFAsDALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAE 3196
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3190 RYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPG 3269
Cdd:PRK05691 3197 RYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPG 3276
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3270 TGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEFLDWSELPEDGHEERLQALH 3349
Cdd:PRK05691 3277 TGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALH 3356
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3350 KREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESRPANLPTPPRYRDYIAWLQ 3429
Cdd:PRK05691 3357 KQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQ 3436
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3430 RQDLEQSRRWWSESLRGFERPTLVPSDRPFLREHAGESGGMIVGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALT 3509
Cdd:PRK05691 3437 RQDLAQARQWWQDNLRGFERPTPIPSDRPFLREHAGDSGGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALV 3516
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3510 LRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAGQRCTVREWLNRLFERNLELREHEHLPLVAIQES 3589
Cdd:PRK05691 3517 LRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQEC 3596
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3590 SELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTVVCYPGDDLGLHLSYDQRYFEAPTVERLLGEF 3669
Cdd:PRK05691 3597 SELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEF 3676
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3670 KRLLLALADGFHGELEALPLLGEDERDFLLDGCNRSARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRAN 3749
Cdd:PRK05691 3677 KRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAAN 3756
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3750 RLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALFD 3829
Cdd:PRK05691 3757 RLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLD 3836
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3830 ELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQT 3909
Cdd:PRK05691 3837 ELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQT 3916
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3910 ASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQALDGLRWMLPTGEAMP 3989
Cdd:PRK05691 3917 ASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMP 3996
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3990 PELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVA 4069
Cdd:PRK05691 3997 PELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLL----DEALELVPLGAVGELCVA 4072
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4070 GTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE 4149
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE 4152
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4150 AAVAVQEGANGKYLVGYLVPGETPrssadspaglmVEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKA 4229
Cdd:PRK05691 4153 AAVAVQEGVNGKHLVGYLVPHQTV-----------LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKA 4221
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4230 LPALDIGQMQNQAYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTV 4309
Cdd:PRK05691 4222 LPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTV 4301
                        4330      4340      4350
                  ....*....|....*....|....*....|...
gi 15597620  4310 EELASYIESLAPSEISEQKAERLNDLMSKLEML 4342
Cdd:PRK05691 4302 EELAEYIEGLAGSAIDEQKVDRLSDLMAELEGL 4334
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
658-1988 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1062.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  658 AGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDG 737
Cdd:COG1020    1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  738 AALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLN 817
Cdd:COG1020   81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  818 LLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAAR 897
Cdd:COG1020  161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  898 YSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQ 977
Cdd:COG1020  241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  978 PFAALLGEAREATLGAQANQDLPFDQVLAACGQ-----GGQLFQVLFNHQQRDLSALRrLPGLLADELPWHSREAKFDLQ 1052
Cdd:COG1020  321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPerdlsRNPLFQVMFVLQNAPADELE-LPGLTLEPLELDSGTAKFDLT 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1053 LQSEEDArGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALV-DAEQAAHLAEW-GSAPCEPARAWL 1130
Cdd:COG1020  400 LTVVETG-DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLtAAERQQLLAEWnATAAPYPADATL 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1131 PELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDP 1210
Cdd:COG1020  479 HELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDP 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1211 DYPSERLAYMLADSGVELLLTQAHLFERLPgAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGN 1290
Cdd:COG1020  559 AYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMV 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1291 THAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPP 1370
Cdd:COG1020  638 EHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPS 717
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 LLQLFIDEpGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED--GERSPIGRPLGN 1448
Cdd:COG1020  718 LLRALLDA-APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDadGGSVPIGRPIAN 796
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1449 VVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQV 1528
Cdd:COG1020  797 TRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQV 876
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1529 KLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYtgAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQ 1608
Cdd:COG1020  877 KIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAY--VVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLP 954
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1609 MPLGPSGKLDTRALPEPVWQQREH-VEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVEL 1687
Cdd:COG1020  955 LPLTGNGKLDRLALPAPAAAAAAAaAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLL 1034
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1688 PLRALFEASELEAfceqVRAAQAAGRTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVAR 1767
Cdd:COG1020 1035 LLLLLFLAAAAAA----AAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1768 FEAALQALVQRHETLRTTFPSVDGVPVQRVHGDggLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMV 1847
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVA--LAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLL 1188
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1848 KMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLG 1927
Cdd:COG1020 1189 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLA 1268
                       1290      1300      1310      1320      1330      1340
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 1928 NEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLY 1988
Cdd:COG1020 1269 LALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
17-559 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 711.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   17 RRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP 96
Cdd:cd05931    1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   97 PEsaRRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTS 176
Cdd:cd05931   81 PT--PGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  177 GSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAI 256
Cdd:cd05931  159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  257 SQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSFFACYGLAEATLFV 336
Cdd:cd05931  239 SRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  337 TGGQRGQGIPALAVDGEALARNRIAEGEGS----VLMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWR 412
Cdd:cd05931  319 SGGPPGTGPVVLRVDRDALAGRAVAVAADDpaarELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWG 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  413 NPEASAKAFVER---DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARKGRVAAFAVTVD 489
Cdd:cd05931  399 RPEATAETFGALaatDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPDD 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  490 GEEGIGIAAEIGRGVQKsVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLED 559
Cdd:cd05931  479 GEERLVVVAEVERGADP-ADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1156-1555 5.53e-161

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 504.88  E-value: 5.53e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1156 YAELHARANRLAHYLRD-KGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH 1234
Cdd:TIGR01733    2 YRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1235 LFERLPGAeGVTPICLDSLKLDNWPSQAPGLHL----HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDG 1310
Cdd:TIGR01733   82 LASRLAGL-VLPVILLDPLELAALDDAPAPPPPdapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1311 DDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVE-LVRQFGVTTLHFVPPLLQLfIDEPGVAACGSLRR 1389
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLAL-LAAALPPALASLRL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1390 LFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED---GERSPIGRPLGNVVCRVLDAEFNLLPAGVA 1466
Cdd:TIGR01733  240 VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDaprESPVPIGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1467 GELCIGGLGLARGYLGRPALSAERFVADPFSA-AGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFAGgDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 15597620   1546 AQPGVAQAVV 1555
Cdd:TIGR01733  400 RHPGVREAVV 409
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
9-562 2.33e-125

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 411.04  E-value: 2.33e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFL---AEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCL 85
Cdd:NF038339   18 ATLVDHVERNARERADTLAYRFIdysRERDGEARDLTWAQFGARLRAVAARLQQVTKPGDRVAILAPQGLDYVVSFFAAI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAVPAYPPESArrHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVR 165
Cdd:NF038339   98 YAGNIAVPLFDPDEP--GHTDRLHAVLGDCKPSAILTATSSAEGVRKFFRSLPAKERPRVIAVDAVPDSVGSTWVRPDAD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFsGVPCVLMSPRYF 245
Cdd:NF038339  176 LDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDENSRGVTWLPLFHDMGLLTVILPALG-GKYITIMSPAAF 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   246 LERPVRW---LEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASS 322
Cdd:NF038339  255 VRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARGLPKEGEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   323 FFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRI----AEGEGSVL-MCCGRSQPEHAVLIVDAASGEVLGDDNVG 397
Cdd:NF038339  335 IKPSYGMAEATLFVSSTPREDEAKVIYVDREELNAGRIvevdPDAPNAVAqVSCGYVARSQWAVIVDPETGTELPDGQVG 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   398 EIWAAGPSIAHGYWRNPEASAKAF----VER-----------DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYP 462
Cdd:NF038339  415 EIWLHGNNIGTGYWGRPEETEETFhnklKSRleegshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYP 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   463 QDIERTVESEVPSARKGRVAAFAVTV--------------------DGEEGIGIAAEIGRGVQKSVPaQELIDSIRQAVA 522
Cdd:NF038339  495 QDLEYSAQEASKALRPGFVAAFSVPAnqlpaevfenshsglkydadDSSEQLVIVAERAPGAGKADP-QPIADAVRAAIA 573
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 15597620   523 EAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGSL 562
Cdd:NF038339  574 VRHGVTVRDVLLVPAGSIPRTSSGKIARRACKAAYIDGTL 613
AMP-binding pfam00501
AMP-binding enzyme;
1134-1531 8.20e-113

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 366.64  E-value: 8.20e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1134 LERQLAQSAERVALEWDGG-SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1213 PSERLAYMLADSGVELLLTQAHL-FERLPGAEG-----VTPICLDSL-----------KLDNWPSQAPGLHLHGDNLAYV 1275
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkLEELLEALGklevvKLVLVLDRDpvlkeeplpeeAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1276 IYTSGSTGQPKGVGNTHAALAERLQWMQATYT----LDGDDVLMQKAPVSFDVSV-WECFWPLVTGCRLVLAAPGEHRDP 1350
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1351 ARLVELVRQFGVTTLHFVPPLLQLFID--EPGVAACGSLRRLFSGGEALPAELRNRVLQRLPaVALHNRYGPTETAINVT 1428
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1429 HWQCRAEDGERSP-IGRPLGNVVCRVLDAEF-NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADpfsaageRLYRT 1506
Cdd:pfam00501  320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 15597620   1507 GDRARWNADGVLEYLGRLDQQVKLR 1531
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
24-554 6.71e-107

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 357.42  E-value: 6.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    24 ERLALRFLA-EDDGEGVVLSY--RDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESA 100
Cdd:NF040633   43 DRVCIRFWDySESREGTAVEYtrAEVNTRIKAVAARLQQVGKPGDRVAILANNSPEYIFGFLGALYAGMVPVPLYDPNEP 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   101 rrHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEH------------ 168
Cdd:NF040633  123 --GHADHLRAVLADSGPTVVLTNKTSAPAVRAHFADLPAAERPRILSVDSLPDSLAESWVNPMATIEGqpllapagtdps 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   169 --IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFsGVPCVLMSPRYFL 246
Cdd:NF040633  201 ddTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAFVTIL-GLEFELMSPRDFI 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   247 ERPVRWLEAISQYGGTV---SGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSF 323
Cdd:NF040633  280 QQPKRWVDQLSRREDDVnvyTVVPNFALELAARYANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTAL 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   324 FACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSV-----LMCCGRSQPEHAVLIVDAASGEVLGDDNVGE 398
Cdd:NF040633  360 RPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAVEVAEDSenavpFASNGQVVRPQVLAIVDPETGQELPDGTVGE 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   399 IWAAGPSIAHGYWRNPEASAKAF-------VERDGRT-------WLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQD 464
Cdd:NF040633  440 IWVHGDNMAAGYLDREEETAETFrntlgerLAENSRAegapednWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQD 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   465 IERTVESEVPSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAqELIDSIRQAVAEAYQEAPKVVALLNPGALPKTS 544
Cdd:NF040633  520 IEATVQEASDHIRPDSVAAFAVPGDDVEKLVILAERDDEADESGDA-EAIEAIRAAVTSAHGVVPADIRIVAPGEIARSS 598
                         570
                  ....*....|
gi 15597620   545 SGKLQRSACR 554
Cdd:NF040633  599 SGKIARRVNA 608
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
9-553 3.06e-105

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 351.10  E-value: 3.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFLA-EDDGEGVV--LSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCL 85
Cdd:NF038337    4 SSVVSLLRERAGLQPDDVAFRYTDyEQDWAGVTetLTWAQLYRRTLNVAHEVRRHGTTGDRAVILAPQGLPYIVAFLGAM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAVPAYPPESARrhHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAwdePQVR 165
Cdd:NF038337   84 QAGLIAVPLSVPQPGS--HDERVSAVLADTSPSVVLTTSAAAAAVAEYLHRPDTGAVPAVIEIDSLDLDGPNS---PSIR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 ---PEHIAFLQYTSGSTALPKGVQVSHGNLVAN-EVLIRRGF----GIGA-DDVIVSWLPLYHDMGLIGGLLQPIFSGVP 236
Cdd:NF038337  159 isdAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNfQQLMAAYFpdtnGVAPrDTTIVSWLPFYHDMGLVLGVIAPILGGYR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   237 CVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAAS 316
Cdd:NF038337  239 SELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPY 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   317 RFDASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALAR---NRIAEGEGSVLMCCGRSQPEhAVLIVDAASGEVLGD 393
Cdd:NF038337  319 NFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEPEKLSEgsaQRCEARTGSPLLSYGTPTSP-TVRIVDPDTCIECPA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   394 DNVGEIWAAGPSIAHGYWRNPEASAKAF----VERDGRT----WLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDI 465
Cdd:NF038337  398 GTVGEIWVHGDNVAEGYWQKPEETRRTFggvlANPSPGTpegpWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   466 ERTVEsevpSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKV----VALLNPGALP 541
Cdd:NF038337  478 ESTVQ----EITGGRVAAISVPVDETEKLVTIIELKKRGDSDEEAMRKLDAVKNNVTAAISRSHGLnvadLVLVPPGSIP 553
                         570
                  ....*....|..
gi 15597620   542 KTSSGKLQRSAC 553
Cdd:NF038337  554 TTTSGKIRRAAC 565
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4247-4316 6.16e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 47.24  E-value: 6.16e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620    4247 RNELEETLARIWAEVLKVERVGVFD---NFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYI 4316
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
 
Name Accession Description Interval E-value
PRK05691 PRK05691
peptide synthase; Validated
1-4342 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 8278.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAFELPTTLVQALRRRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAA 80
Cdd:PRK05691    1 MMDAFELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAqLSAANAPQLLCVDQLDPAVAEAWD 160
Cdd:PRK05691   81 FFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEE-LAAANAPELLCVDTLDPALAEAWQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   161 EPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGI--GADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 238
Cdd:PRK05691  160 EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdlNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   239 LMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRF 318
Cdd:PRK05691  240 LMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   319 DASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNVGE 398
Cdd:PRK05691  320 DPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   399 IWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARK 478
Cdd:PRK05691  400 IWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   479 GRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLE 558
Cdd:PRK05691  480 GRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   559 DGSLDSYALFPGLQAVQEAQPPAGDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQ 638
Cdd:PRK05691  560 DGSLDSYALFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQ 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   639 LFEAPTLQAFSATVARQLAAGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASF 718
Cdd:PRK05691  640 LFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASF 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   719 QRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQ 798
Cdd:PRK05691  720 QRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDE 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   799 EHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPV 878
Cdd:PRK05691  800 EHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPV 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   879 LELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQG 958
Cdd:PRK05691  880 LELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQG 959
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   959 LVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQ--LFQVLFNHQQRDLSALRRLPGLL 1036
Cdd:PRK05691  960 LVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREqgLFQVMFNHQQRDLSALRRLPGLL 1039
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1037 ADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLA 1116
Cdd:PRK05691 1040 AEELPWHSREAKFDLQLHSEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA 1119
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1117 EWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLL 1196
Cdd:PRK05691 1120 QWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLL 1199
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1197 AIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVI 1276
Cdd:PRK05691 1200 AILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVI 1279
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1277 YTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVEL 1356
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAEL 1359
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1357 VRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED 1436
Cdd:PRK05691 1360 VQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAED 1439
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1437 GERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADG 1516
Cdd:PRK05691 1440 GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADG 1519
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1517 VLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEqnqRLRAALQAELPE 1596
Cdd:PRK05691 1520 ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAE---RLKAALAAELPE 1596
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1597 YMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIV 1676
Cdd:PRK05691 1597 YMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIV 1676
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1677 SRTRQACDVELPLRALFEASELEAFCEQVRAAQAAGRTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGL 1756
Cdd:PRK05691 1677 SRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGM 1756
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1757 ARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDL 1836
Cdd:PRK05691 1757 ARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDL 1836
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1837 ESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQ 1916
Cdd:PRK05691 1837 ERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQ 1916
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1917 RQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDL 1996
Cdd:PRK05691 1917 RQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDL 1996
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1997 RIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQV 2076
Cdd:PRK05691 1997 RIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQV 2076
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2077 MCNVQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQ 2156
Cdd:PRK05691 2077 MCNVQRWEFQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQ 2156
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2157 RRIAELPLFAAEERKQLL--LAGTAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVG 2234
Cdd:PRK05691 2157 QRLAELPLLAAAEQQQLLdsLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVG 2236
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2235 PEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVARWCLEEDGP 2314
Cdd:PRK05691 2237 PQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLEDDAA 2316
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2315 ALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPL 2394
Cdd:PRK05691 2317 ALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPL 2396
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2395 LCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPAS 2474
Cdd:PRK05691 2397 LCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQL 2476
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2475 FFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAER 2554
Cdd:PRK05691 2477 FFNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAER 2556
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2555 FVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYV 2634
Cdd:PRK05691 2557 FVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYL 2636
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2635 ASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAG 2714
Cdd:PRK05691 2637 VSAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQ 2716
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2715 VWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQAEQGPVQGDSALTP 2794
Cdd:PRK05691 2717 IWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTP 2796
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2795 IQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFD 2874
Cdd:PRK05691 2797 IQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELLWQVTVADFA 2876
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2875 ECAELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRD 2954
Cdd:PRK05691 2877 ECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRD 2956
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2955 WAGRLQAYAGSESLREELGWWQARLGGQPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTA 3034
Cdd:PRK05691 2957 WAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTA 3036
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3035 LARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAQ----SPGESIKAIKEQLRAVPHKGLGYGV 3110
Cdd:PRK05691 3037 LARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAPgddaARGESIKAIKEQLRAVPHKGLGYGV 3116
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3111 LRYLADPAVRQAMAALPTAPITFNYLGQFDQSFA-DALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRE 3189
Cdd:PRK05691 3117 LRYLADAAVREAMAALPQAPITFNYLGQFDQSFAsDALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAE 3196
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3190 RYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPG 3269
Cdd:PRK05691 3197 RYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPG 3276
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3270 TGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEFLDWSELPEDGHEERLQALH 3349
Cdd:PRK05691 3277 TGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALH 3356
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3350 KREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESRPANLPTPPRYRDYIAWLQ 3429
Cdd:PRK05691 3357 KQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQ 3436
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3430 RQDLEQSRRWWSESLRGFERPTLVPSDRPFLREHAGESGGMIVGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALT 3509
Cdd:PRK05691 3437 RQDLAQARQWWQDNLRGFERPTPIPSDRPFLREHAGDSGGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALV 3516
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3510 LRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAGQRCTVREWLNRLFERNLELREHEHLPLVAIQES 3589
Cdd:PRK05691 3517 LRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLPAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQEC 3596
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3590 SELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTVVCYPGDDLGLHLSYDQRYFEAPTVERLLGEF 3669
Cdd:PRK05691 3597 SELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEF 3676
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3670 KRLLLALADGFHGELEALPLLGEDERDFLLDGCNRSARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRAN 3749
Cdd:PRK05691 3677 KRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAAN 3756
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3750 RLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALFD 3829
Cdd:PRK05691 3757 RLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLD 3836
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3830 ELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQT 3909
Cdd:PRK05691 3837 ELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQT 3916
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3910 ASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQALDGLRWMLPTGEAMP 3989
Cdd:PRK05691 3917 ASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMP 3996
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3990 PELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVA 4069
Cdd:PRK05691 3997 PELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLL----DEALELVPLGAVGELCVA 4072
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4070 GTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE 4149
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE 4152
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4150 AAVAVQEGANGKYLVGYLVPGETPrssadspaglmVEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKA 4229
Cdd:PRK05691 4153 AAVAVQEGVNGKHLVGYLVPHQTV-----------LAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKA 4221
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4230 LPALDIGQMQNQAYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTV 4309
Cdd:PRK05691 4222 LPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTV 4301
                        4330      4340      4350
                  ....*....|....*....|....*....|...
gi 15597620  4310 EELASYIESLAPSEISEQKAERLNDLMSKLEML 4342
Cdd:PRK05691 4302 EELAEYIEGLAGSAIDEQKVDRLSDLMAELEGL 4334
PRK12467 PRK12467
peptide synthase; Provisional
675-4316 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3975.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   675 LPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFV 754
Cdd:PRK12467   50 IPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   755 DLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQ 834
Cdd:PRK12467  130 DLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGR 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   835 PADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAA 914
Cdd:PRK12467  210 EPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALA 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   915 LDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQ 994
Cdd:PRK12467  290 QREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQ 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   995 ANQDLPFDQVLAA------CGQGgQLFQVLFNHQQ----RDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGrLT 1064
Cdd:PRK12467  370 AHQDLPFEQLVEAlqpersLSHS-PLFQVMFNHQNtatgGRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQG-LW 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1065 LNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDA-EQAAHLAEWGSAPCEPARAWLPELLERQLAQSAE 1143
Cdd:PRK12467  448 AAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAeERARELVRWNAPATEYAPDCVHQLIEAQARQHPE 527
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1144 RVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLAD 1223
Cdd:PRK12467  528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD 607
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1224 SGVELLLTQAHLFERLPGAEGVTPICLDslKLDNWPSQAPGLH----LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERL 1299
Cdd:PRK12467  608 SGVRLLLTQSHLLAQLPVPAGLRSLCLD--EPADLLCGYSGHNpevaLDPDNLAYVIYTSGSTGQPKGVAISHGALANYV 685
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1300 QWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEP 1379
Cdd:PRK12467  686 CVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQAS 765
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1380 GVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAE--DGERSPIGRPLGNVVCRVLDAE 1457
Cdd:PRK12467  766 RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEerDFGNVPIGQPLANLGLYILDHY 845
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1458 FNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEP 1537
Cdd:PRK12467  846 LNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIEL 925
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1538 EEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEQ--NQRLRAALQAELPEYMVPTQLMRLAQMPLGPSG 1615
Cdd:PRK12467  926 GEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNG 1005
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1616 KLDTRALPEPV--WQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALF 1693
Cdd:PRK12467 1006 KLDRKALPKPDasAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLF 1085
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1694 EASELEAFCEQVrAAQAAGRTdshGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQ 1773
Cdd:PRK12467 1086 EHQTLAGFAQAV-AAQQQGAQ---PALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFD 1161
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1774 ALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQDFSALDRDSRQqhLQTLADSEAHRPFDLESGPLLRVCMVKMAERE 1853
Cdd:PRK12467 1162 ALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQ--LKVYVEAEARQPFDLEQGPLLRVGLLRLAADE 1239
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1854 HYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLL 1933
Cdd:PRK12467 1240 HVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVL 1319
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1934 ELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGL 2013
Cdd:PRK12467 1320 ELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGL 1399
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2014 IGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQTRQLAG 2093
Cdd:PRK12467 1400 IGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPG 1479
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2094 MTVEYIANDARATKFDLNLEVTDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQL 2173
Cdd:PRK12467 1480 LSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQI 1559
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2174 LLAGTAGEAG--LQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVV 2251
Cdd:PRK12467 1560 LEGWNATHTGypLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVV 1639
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2252 GLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALgELPAGVARWCLEEDGPALDAEDPAPLAALSGPQ 2331
Cdd:PRK12467 1640 GLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL-PLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQ 1718
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2332 HQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQW-GA 2410
Cdd:PRK12467 1719 NLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHrDP 1798
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2411 EEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLA 2490
Cdd:PRK12467 1799 EQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTH 1878
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2491 CLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRT 2570
Cdd:PRK12467 1879 WTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGSRLYRT 1958
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2571 GDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAE--QDEDAQAA 2648
Cdd:PRK12467 1959 GDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGlvDDDEAQVA 2038
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2649 LREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAGVWREVLNVERVGLG 2728
Cdd:PRK12467 2039 LRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLH 2118
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2729 DNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQSLAAVARHSQAS-QAEQGPVQGDSALTPIQHWFFDLPLARR 2807
Cdd:PRK12467 2119 DNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTvSIDQGPVTGDLPLLPIQQMFFADDIPER 2198
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2808 EHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLRE--QELLWHVPVQSFDECAELFAKAQR 2885
Cdd:PRK12467 2199 HHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQerRPLLWQVVVADKEELEALCEQAQR 2278
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2886 SLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGS 2965
Cdd:PRK12467 2279 SLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAAS 2358
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2966 ESLREELGWWQARLGGQPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQ 3045
Cdd:PRK12467 2359 AALADELGYWQAQLQGASTELPCDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQ 2438
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3046 PSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAQSPGESIKAIKEQLRAVPHKGLGYGVLRYLADPAVRQAMAA 3125
Cdd:PRK12467 2439 ASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQA 2518
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3126 LPTAPITFNYLGQFDQSF---ADALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRERYDARTVNELAQA 3202
Cdd:PRK12467 2519 LPVPRITFNYLGQFDGSFdaeKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADA 2598
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3203 YLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRID 3282
Cdd:PRK12467 2599 YAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVE 2678
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3283 SpLDPERFAAAWQAVVARHEALRASFVWNAG-ETMLQVIHKPGRTRIEFLDWSELPedGHEERLQALHKREREAGFDLLE 3361
Cdd:PRK12467 2679 G-LDVERFRTAWQAVIDRHEILRSGFLWDGElEEPLQVVYKQARLPFSRLDWRDRA--DLEQALDALAAADRQQGFDLLS 2755
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3362 QPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSalGESRPanlPTPPRYRDYIAWLQRQDLEQSRRWWS 3441
Cdd:PRK12467 2756 APLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF--GQPPP---AREGRYRDYIAWLQAQDAEASEAFWK 2830
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3442 ESLRGFERPTLVPsdRPFLREHAGESGGMivGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLF 3521
Cdd:PRK12467 2831 EQLAALEEPTRLA--RALYPAPAEAVAGH--GAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCF 2906
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3522 GVTVAGRPVGMPEMQRTVGLFINSIPLrVQMPAAGQrcTVREWLNRLFERNLELREHEHLPLVAIQESSELPkGQPLFDS 3601
Cdd:PRK12467 2907 GATVAGRPAQLRGAEQQLGLFINTLPV-IASPRAEQ--TVSDWLQQVQAQNLALREFEHTPLADIQRWAGQG-GEALFDS 2982
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3602 LFVFENAPVEVSVLDRA-QSLNASSDSGRTHTNFPLTVVCYPGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGF 3680
Cdd:PRK12467 2983 ILVFENYPISEALKQGApSGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNP 3062
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3681 HGELEALPLLGEDERDFLLDGCNRSARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGV 3760
Cdd:PRK12467 3063 AARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGV 3142
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3761 GIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQalalfdeLGCVDRPRLL 3840
Cdd:PRK12467 3143 GPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQ-------LPAPAGDTAL 3215
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3841 VWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQ 3920
Cdd:PRK12467 3216 TLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER 3295
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3921 FLAAPLFGARVAIVPNAVaHDPQGLLAHVGEQGITVLESVPSLIQGMLA-EERQALDGLRWMLPTGEAMPPELARQWLKR 3999
Cdd:PRK12467 3296 FLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEdAGGADCASLDIYVFGGEAVPPAAFEQVKRK 3374
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4000 YPRIGLVNAYGPAECSDDVAFFRVDL-ASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYV 4078
Cdd:PRK12467 3375 LKPRGLTNGYGPTEAVVTVTLWKCGGdAVCEAPYAPIGRPVAGRSIYVL----DGQLNPVPVGVAGELYIGGVGLARGYH 3450
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4079 GDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGA 4158
Cdd:PRK12467 3451 QRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA 3530
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4159 NGKYLVGYLVPGEtprssadspaglmvEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIgqM 4238
Cdd:PRK12467 3531 GGKQLVAYVVPAD--------------PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA--K 3594
                        3610      3620      3630      3640      3650      3660      3670
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  4239 QNQAYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYI 4316
Cdd:PRK12467 3595 GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS 3672
PRK12316 PRK12316
peptide synthase; Provisional
637-4340 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 3281.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   637 RQLFEAPTLQAFSATVARQLAAGL------------PAEAPMAHL------------PRGVDL-PQSAAQQRLWLTWQID 691
Cdd:PRK12316 1494 REMFAEATVQRLADDYARELQALIehccdernrgvtPSDFPLAGLsqaqldalplpaGEIADIyPLSPMQQGMLFHSLYE 1573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   692 PQSAAYniPGGLRLRGE-LDEAALRASFQRLVERHEALRTRFLERDG--AALQRIDERGEFawQFVDLAALAEHERAAAA 768
Cdd:PRK12316 1574 QEAGDY--INQLRVDVQgLDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVEL--PFAELDWRGREDLGQAL 1649
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   769 AQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAeacgGQPadLAPLELHYAEF 848
Cdd:PRK12316 1650 DALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYA----GQP--VAAPGGRYRDY 1723
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   849 AAW-QRQWLDAGEgarqlAYWRERLGDTAPVLELAtDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLA 927
Cdd:PRK12316 1724 IAWlQRQDAAASE-----AFWKEQLAALEEPTRLA-QAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQA 1797
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   928 AFQALLHRHSGQGEIRIGVPSANRQrLETQGL---VGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQV 1004
Cdd:PRK12316 1798 AWLLLLQRYTGQETVAFGATVAGRP-AELPGIeqqIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI 1876
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1005 LAACGQGGQ-LFQVLFNHQQRDLS-ALRR-LPGLLADELPWHSREAKFDLQLQSEEDARgrLTLNFDYAADLFDEASIRR 1081
Cdd:PRK12316 1877 QRWAGQGGEaLFDSLLVFENYPVAeALKQgAPAGLVFGRVSNHEQTNYPLTLAVTLGET--LSLQYSYDRGHFDAAAIER 1954
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1082 FAAQYLELLRQVAEDPQRCLGDIALVDA-EQAAHLAEWGSAPCE-PARAWLPELLERQLAQSAERVALEWDGGSLGYAEL 1159
Cdd:PRK12316 1955 LDRHLLHLLEQMAEDAQAALGELALLDAgERQRILADWDRTPEAyPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAEL 2034
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1160 HARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERL 1239
Cdd:PRK12316 2035 DSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL 2114
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1240 PGAEGVTPICLD-SLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKA 1318
Cdd:PRK12316 2115 PLPAGVARLPLDrDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFM 2194
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1319 PVSFDVSVWECFWPLVTGCRlVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC-GSLRRLFSGGEAL 1397
Cdd:PRK12316 2195 SFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRpPAVRVYCFGGEAV 2273
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1398 PAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERS---PIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGL 1474
Cdd:PRK12316 2274 PAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAayvPIGRALGNRRAYILDADLNLLAPGMAGELYLGGE 2353
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1475 GLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAV 1554
Cdd:PRK12316 2354 GLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAV 2433
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1555 VVIREGVAGSQLVGYytgAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEP--VWQQREH 1632
Cdd:PRK12316 2434 VVAQDGASGKQLVAY---VVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPdvSQLRQAY 2510
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1633 VEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELEAFCeqvrAAQAAG 1712
Cdd:PRK12316 2511 VAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA----ASLESG 2586
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1713 RTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGV 1792
Cdd:PRK12316 2587 QTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQ 2666
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1793 PVQRVHGDGGLHMDWQDfSALDRDSRQQHLqtlADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDI 1872
Cdd:PRK12316 2667 TRQVILPNMSLRIVLED-CAGVADAAIRQR---VAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQV 2742
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1873 FARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLY 1952
Cdd:PRK12316 2743 MVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARL 2822
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1953 RFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMS 2032
Cdd:PRK12316 2823 DVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLA 2902
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2033 VGELLEQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQTrQLAGMTVEYIANDARATKFDLNL 2112
Cdd:PRK12316 2903 FRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAA-QLPGLHIESFAWDGAATQFDLAL 2981
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2113 EVTDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLA--GTAGEAGLQDTLHG 2190
Cdd:PRK12316 2982 DTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAwnATAAEYPLERGVHR 3061
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2191 LFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2271 PLERLQYMIEDSGVRLLLSHAALFEALgelPAGVARWCLEEDGPALDAEDPAplaALSGPQHQAYLIYTSGSTGKPKGVA 2350
Cdd:PRK12316 3142 PEERLAYMLEDSGAQLLLSQSHLRLPL---AQGVQVLDLDRGDENYAEANPA---IRTMPENLAYVIYTSGSTGKPKGVG 3215
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2351 VSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGAEE-ICELIRAEGVSILGFTP 2429
Cdd:PRK12316 3216 IRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPAlLVELINSEGVDVLHAYP 3295
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2430 SygsQLAQWLESQG--RQLPVRMCITGGEALTGEHLQRirqAFAPASFFNAYGPTETVVMPLAclaPERLEEGAASVPIG 2507
Cdd:PRK12316 3296 S---MLQAFLEEEDahRCTSLKRIVCGGEALPADLQQQ---VFAGLPLYNLYGPTEATITVTH---WQCVEEGKDAVPIG 3366
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2508 SVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAaEGGRLYRTGDLVRLCDNGQVEYVGR 2587
Cdd:PRK12316 3367 RPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFV-PGERLYRTGDLARYRADGVIEYIGR 3445
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2588 IDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDspsGKQLAGYVASavaeqdEDAQAALREALKTHLKQQLPDYMVP 2667
Cdd:PRK12316 3446 VDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD---GRQLVAYVVP------EDEAGDLREALKAHLKASLPEYMVP 3516
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2668 AHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSILSIQVVSR 2747
Cdd:PRK12316 3517 AHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSR 3596
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2748 ARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQAEQGPVQGDSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLL 2827
Cdd:PRK12316 3597 ARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAAL 3676
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2828 RKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLRE-QELLWHVPVQSFDECAELFAKAQRSLDLEQGPLLRAVLVDGPAGE 2906
Cdd:PRK12316 3677 EAALQALVEHHDALRLRFVEDAGGWTAEHLPVELgGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGS 3756
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2907 QRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGGQPVEW 2986
Cdd:PRK12316 3757 QRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSSEL 3836
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2987 PCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDL 3066
Cdd:PRK12316 3837 PCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDL 3916
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3067 TRSVGWFTSAYPLRLTPAQSPGESIKAIKEQLRAVPHKGLGYGVLRYLADPAVRQAMAALPTAPITFNYLGQFDQSFAD- 3145
Cdd:PRK12316 3917 SRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFDGSFDEe 3996
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3146 -ALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHCLEDGAGGLTP 3224
Cdd:PRK12316 3997 mALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERHGVTP 4076
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3225 SDFPLAQLSQAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSpLDPERFAAAWQAVVARHEAL 3304
Cdd:PRK12316 4077 SDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVL 4155
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3305 RASFVW-NAGETMLQVIHKPGRTRIEFLDWSELPEdgHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSN 3383
Cdd:PRK12316 4156 RSGFVWqGELGRPLQVVHKQVSLPFAELDWRGRAD--LQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTN 4233
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3384 HHILIDAWCRGLLMNDFFEIYSALGESRPANlptppRYRDYIAWLQRQDLEQSRRWWSESLRGFERPT-LVPS-DRPFLR 3461
Cdd:PRK12316 4234 HHILMDGWSNSQLLGEVLERYSGRPPAQPGG-----RYRDYIAWLQRQDAAASEAFWREQLAALDEPTrLAQAiARADLR 4308
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3462 EHAGesggmiVGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGL 3541
Cdd:PRK12316 4309 SANG------YGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGL 4382
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3542 FINSIPLrVQMPAAGQRctVREWLNRLFERNLELREHEHLPLVAIQESSELpKGQPLFDSLFVFENAPVEvSVLDRAQSL 3621
Cdd:PRK12316 4383 FINTLPV-IATPRAQQS--VVEWLQQVQRQNLALREHEHTPLYEIQRWAGQ-GGEALFDSLLVFENYPVS-EALQQGAPG 4457
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3622 NASSDSGRTH--TNFPLTVVCYPGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDFLL 3699
Cdd:PRK12316 4458 GLRFGEVTNHeqTNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIV 4537
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3700 DGCNRSARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGM 3779
Cdd:PRK12316 4538 ALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVG 4617
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3780 IVGSFKAGAGYLPLDPGHPTQRLTRIVELSRtLVLVCTQACREQALALFDELGCVDRPRLLVWDEIqqgegAEHDPQVYS 3859
Cdd:PRK12316 4618 LLAVLKAGGAYVPLDPEYPRERLAYMMEDSG-AALLLTQSHLLQRLPIPDGLASLALDRDEDWEGF-----PAHDPAVRL 4691
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3860 GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVaIVPNAVA 3939
Cdd:PRK12316 4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV-VIRDDSL 4770
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3940 HDPQGLLAHVGEQGITVLESVPSLIQGML--AEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDD 4017
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVT 4850
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4018 VAFFRV-DLASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAP 4096
Cdd:PRK12316 4851 VLLWKArDGDACGAAYMPIGTPLGNRSGYVL----DGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAP 4926
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4097 GERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRSS 4176
Cdd:PRK12316 4927 GGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALAD 5006
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4177 ADSpaglmvEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQnQAYQAPRNELEETLAR 4256
Cdd:PRK12316 5007 ADE------AQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQ-QAYVAPRSELEQQVAA 5079
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4257 IWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFEcttVEELASYIESLAPSEISEQ-KAERLNDL 4335
Cdd:PRK12316 5080 IWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQ---TPTLAAFVELAAAAGSGDDeKFDDLEEL 5156

                  ....*
gi 15597620  4336 MSKLE 4340
Cdd:PRK12316 5157 LSELE 5161
PRK12316 PRK12316
peptide synthase; Provisional
1726-4322 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 2666.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1726 EQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHM 1805
Cdd:PRK12316   47 AERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1806 DWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFL 1885
Cdd:PRK12316  127 EFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1886 DDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVR 1965
Cdd:PRK12316  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALR 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1966 RFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVI 2045
Cdd:PRK12316  287 GTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVL 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2046 DGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW--EFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGC 2123
Cdd:PRK12316  367 GAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLvaDIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHA 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2124 CLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLA--GTAGEAGLQDTLHGLFAARVAASPQ 2201
Cdd:PRK12316  447 ALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGwnATAAEYPLQRGVHRLFEEQVERTPE 526
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2202 APALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIED 2281
Cdd:PRK12316  527 APALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLED 606
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2282 SGVRLLLSHAALFEALgELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCA 2361
Cdd:PRK12316  607 SGVQLLLSQSHLGRKL-PLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2362 AVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQG-QWGAEEICELIRAEGVSILGFTPSYGSQLAQwLE 2440
Cdd:PRK12316  686 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DE 764
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2441 SQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVmPLACLApeRLEEGAASVPIGSVVGARVAYILDA 2520
Cdd:PRK12316  765 DVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAI-DVTHWT--CVEEGGDSVPIGRPIANLACYILDA 841
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2521 DLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIE 2600
Cdd:PRK12316  842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIE 920
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2601 LGEIEARLLEHPQVREALVLALDspsGKQLAGYVASavaeqdEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTA 2680
Cdd:PRK12316  921 LGEIEARLLEHPWVREAAVLAVD---GKQLVGYVVL------ESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTP 991
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2681 NGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDL 2760
Cdd:PRK12316  992 NGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDL 1071
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2761 FQHQTVQSLAAVARHSQASQAEQGPVQGDSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDA 2840
Cdd:PRK12316 1072 FQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDA 1151
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2841 LRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFDECAELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDG 2920
Cdd:PRK12316 1152 LRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDG 1231
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2921 VSWRVLLEDLQQVYRQfaegAEPALPAKTSAFRDWAGRLQAYAGSESlrEELGWWQARLGGQPVEWPCDRPQGDNREALA 3000
Cdd:PRK12316 1232 VSWRILLEDLQRAYAD----LDADLPARTSSYQAWARRLHEHAGARA--EELDYWQAQLEDAPHELPCENPDGALENRHE 1305
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3001 ESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLR 3080
Cdd:PRK12316 1306 RKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGWFTSLFPVR 1385
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3081 LTPAQSPGESIKAIKEQLRAVPHKGLGYGVLRYLADPAVRQAMAALPTAPITFNYLGQFDQSFAD-ALFQPLDQPTGPIH 3159
Cdd:PRK12316 1386 LTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNYLGQFDRQFDEaALFVPATESAGAAQ 1465
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3160 DEQAPLPNELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDA 3239
Cdd:PRK12316 1466 DPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLAGLSQAQLDA 1545
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3240 LAVPAGEIEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSpLDPERFAAAWQAVVARHEALRASFVWNAG-ETMLQ 3318
Cdd:PRK12316 1546 LPLPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGlEQPLQ 1624
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3319 VIHKPGRTRIEFLDWSelPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMN 3398
Cdd:PRK12316 1625 VIHKQVELPFAELDWR--GREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLG 1702
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3399 DFFEIYSalGESRPAnlpTPPRYRDYIAWLQRQDLEQSRRWWSESLRGFERPTLVpsdrpfLREHAGESGGMIVGDRYTR 3478
Cdd:PRK12316 1703 EVLQRYA--GQPVAA---PGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRL------AQAARTEDGQVGYGDHQQL 1771
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3479 LDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLrVQMPAAGQR 3558
Cdd:PRK12316 1772 LDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPV-IAAPRPDQS 1850
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3559 ctVREWLNRLFERNLELREHEHLPLVAIQESSELpKGQPLFDSLFVFENAPVEVSVLDRA-QSLNASSDSGRTHTNFPLT 3637
Cdd:PRK12316 1851 --VADWLQEVQALNLALREHEHTPLYDIQRWAGQ-GGEALFDSLLVFENYPVAEALKQGApAGLVFGRVSNHEQTNYPLT 1927
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3638 VVCYPGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDFLLDGCNRSARDYPLEQGYVR 3717
Cdd:PRK12316 1928 LAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQ 2007
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3798 PTQRLTRIVELSRTLVLVCTQACREQaLALFDELgcvdrPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLP 3877
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQRHLLER-LPLPAGV-----ARLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLP 2161
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3878 KGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVaHDPQGLLAHVGEQGITVL 3957
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLYDEMERHGVTIL 2240
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3958 ESVPSLIQgMLAEErQALDG----LRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTE-STY 4032
Cdd:PRK12316 2241 DFPPVYLQ-QLAEH-AERDGrppaVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgAAY 2318
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4033 LPIGSPTDNNRLYLLGAGaddaFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRAD 4112
Cdd:PRK12316 2319 VPIGRALGNRRAYILDAD----LNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRAD 2394
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4113 GVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPgetprssaDSPAGLMVEQgawfe 4192
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVP--------DDAAEDLLAE----- 2461
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4193 rIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQnQAYQAPRNELEETLARIWAEVLKVERVGVFDN 4272
Cdd:PRK12316 2462 -LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR-QAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDH 2539
                        2570      2580      2590      2600      2610
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620  4273 FFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESLAPS 4322
Cdd:PRK12316 2540 FFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTS 2589
PRK12467 PRK12467
peptide synthase; Provisional
2-1998 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1377.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     2 MDAFELPTTLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAA 80
Cdd:PRK12467  505 PATEYAPDCVHQLIEAQARQHPERPALVF------GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVgIAVERSIEMVVG 578
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGVIAVPAYPpesarRHHQERLLSIIADAEPRLVLTTADLRepllqmnAQLSAANAPQLLCVDQLDPAV---AE 157
Cdd:PRK12467  579 LLAVLKAGGAYVPLDP-----EYPQDRLAYMLDDSGVRLLLTQSHLL-------AQLPVPAGLRSLCLDEPADLLcgySG 646
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   158 AWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPC 237
Cdd:PRK12467  647 HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGALASGATL 725
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   238 VLMSPRYFLErPVRWLEAISQYGGTVSGGPDFAYR--LCSERVAE-SALQRLDLSGWRVAFSGSEPIRQDSLErfaekfa 314
Cdd:PRK12467  726 HLLPPDCARD-AEAFAALMADQGVTVLKIVPSHLQalLQASRVALpRPQRALVCGGEALQVDLLARVRALGPG------- 797
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   315 asrfdaSSFFACYGLAEATLFVTGGQ-RGQGIPALAVDgealarnriaegegsvlmcCGRSQPEHAVLIVDAASGEVLGd 393
Cdd:PRK12467  798 ------ARLINHYGPTETTVGVSTYElSDEERDFGNVP-------------------IGQPLANLGLYILDHYLNPVPV- 851
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   394 DNVGEIWAAGPSIAHGYWRNPEASAKAFVE----RDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERT 468
Cdd:PRK12467  852 GVVGELYIGGAGLARGYHRRPALTAERFVPdpfgADGGRLYRTGDLARYRaDGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   469 VEsEVPSARKgrvaAFAVTVDGEEG-IGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQE--APKVVALLNpgALPKTSS 545
Cdd:PRK12467  932 LL-AQPGVRE----AVVLAQPGDAGlQLVAYLVPAAVADGAEHQATRDELKAQLRQVLPDymVPAHLLLLD--SLPLTPN 1004
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   546 GKLQRSAcrLRLEDGSldsyalfpglqAVQEA-QPPAGddELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVA 624
Cdd:PRK12467 1005 GKLDRKA--LPKPDAS-----------AVQATfVAPQT--ELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVIS 1069
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   625 QVRDSLGVALDLRQLFEAPTLQAFsatvARQLAAGLPAEAP-MAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGL 703
Cdd:PRK12467 1070 RVRQRLGIQVPLRTLFEHQTLAGF----AQAVAAQQQGAQPaLPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQAL 1145
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   704 RLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFawQFVDLAALAEHERAAAAAQRREAEAQQPFDLE 783
Cdd:PRK12467 1146 RLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSL--TLEEPLLLAADKDEAQLKVYVEAEARQPFDLE 1223
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   784 KGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGAR 863
Cdd:PRK12467 1224 QGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERAR 1303
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   864 QLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIR 943
Cdd:PRK12467 1304 QLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIR 1383
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   944 IGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACG-----QGGQLFQVL 1018
Cdd:PRK12467 1384 VGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQperslSHSPLFQVM 1463
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1019 FNHQQRDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGrLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQ 1098
Cdd:PRK12467 1464 FNHQRDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSEG-LQASLTYATDLFEASTIERLAGHWLNLLQGLVADPE 1542
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1099 RCLGDIALVD-AEQAAHLAEWGSAPCE-PARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVG 1176
Cdd:PRK12467 1543 RRLGELDLLDeAERRQILEGWNATHTGyPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVG 1622
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1177 PDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLK-- 1254
Cdd:PRK12467 1623 PEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEDdw 1702
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1255 LDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLV 1334
Cdd:PRK12467 1703 LEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLI 1782
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1335 TGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPG-VAACGSLRRLFSGGEALPAELRNRVLQRLPAVA 1413
Cdd:PRK12467 1783 NGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEqVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG 1862
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1414 LHNRYGPTETAINVTHWQCRAEDGE---RSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAER 1490
Cdd:PRK12467 1863 LFNLYGPTETAVDVTHWTCRRKDLEgrdSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAER 1942
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1491 FVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYY 1570
Cdd:PRK12467 1943 FVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYV 2022
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1571 T-----GAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALP--EPVWQQREHVEPRTELQRRI 1643
Cdd:PRK12467 2023 VptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPapDASELQQAYVAPQSELEQRL 2102
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1644 AAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQAcDVELPLRALFEASELEAFCEQVRAAQAAGRTDsHGAIRRI 1723
Cdd:PRK12467 2103 AAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDGTVSID-QGPVTGD 2180
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1724 DREQPVplsysqQRMWFLwQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFpsvdgvpvqrVHGDGGL 1803
Cdd:PRK12467 2181 LPLLPI------QQMFFA-DDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGF----------VQEDGGW 2243
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1804 HMDWQDFSALDRDSRQQH-------LQTLADsEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARE 1876
Cdd:PRK12467 2244 SAMHRAPEQERRPLLWQVvvadkeeLEALCE-QAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLED 2322
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1877 LGALYEAFLDDResPLEpLPVQYLDYSVWQrEWLE----SGERQRQLDYWKAQLGNEHplLELPGDRPRPPVQSHQGDLY 1952
Cdd:PRK12467 2323 LQTAYRQLQGGQ--PVK-LPAKTSAFKAWA-ERLQtyaaSAALADELGYWQAQLQGAS--TELPCDHPQGGLQRRHAASV 2396
                        2010      2020      2030      2040
                  ....*....|....*....|....*....|....*....|....*...
gi 15597620  1953 RFDLSPELAERVRRF--NAARGLTMFMTMTAtLAALLYRYSGQQDLRI 1998
Cdd:PRK12467 2397 TTHLDSEWTRRLLQEapAAYRTQVNDLLLTA-LARVIARWTGQASTLI 2443
PRK12467 PRK12467
peptide synthase; Provisional
1727-3271 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1230.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1727 QPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMD 1806
Cdd:PRK12467   48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1807 WQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLD 1886
Cdd:PRK12467  128 LDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQ 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1887 DRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRR 1966
Cdd:PRK12467  208 GREPSLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKA 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1967 FNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVID 2046
Cdd:PRK12467  288 LAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALG 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2047 GQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCN----VQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLG 2122
Cdd:PRK12467  368 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNhqntATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLW 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2123 CCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLAGTAGEAG-LQDTLHGLFAARVAASPQ 2201
Cdd:PRK12467  448 AAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEyAPDCVHQLIEAQARQHPE 527
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2202 APALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIED 2281
Cdd:PRK12467  528 RPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDD 607
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2282 SGVRLLLSHAALFEALgELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCA 2361
Cdd:PRK12467  608 SGVRLLLTQSHLLAQL-PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVC 686
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2362 AVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQ-WGAEEICELIRAEGVSILGFTPSYGSQLAQwLE 2440
Cdd:PRK12467  687 VIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCaRDAEAFAALMADQGVTVLKIVPSHLQALLQ-AS 765
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2441 SQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMpLACLAPERLEEGAASVPIGSVVGARVAYILDA 2520
Cdd:PRK12467  766 RVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVG-VSTYELSDEERDFGNVPIGQPLANLGLYILDH 844
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2521 DLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIE 2600
Cdd:PRK12467  845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIE 924
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2601 LGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAeQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTA 2680
Cdd:PRK12467  925 LGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAV-ADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2681 NGKLDRRALPAPDPALNRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRD 2759
Cdd:PRK12467 1004 NGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQrLGIQVPLRT 1083
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2760 LFQHQTVQSLA-AVARHSQASQAEQGPVQGDSAL----TPIQHWF-FDL-PLARREHWNQALLLqpRQAIDLGLLRKSLQ 2832
Cdd:PRK12467 1084 LFEHQTLAGFAqAVAAQQQGAQPALPDVDRDQPLplsyAQERQWFlWQLePGSAAYHIPQALRL--KGPLDIEALERSFD 1161
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2833 RLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFDECAELFA----KAQRSLDLEQGPLLRAVLVDGPAGEQR 2908
Cdd:PRK12467 1162 ALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQLKVyveaEARQPFDLEQGPLLRVGLLRLAADEHV 1241
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2909 LLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAG-RLQAYAGSESLReELGWWQARLGG-QPV-E 2985
Cdd:PRK12467 1242 LVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVwQRQWMDAGERAR-QLAYWKAQLGGeQPVlE 1320
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2986 WPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTqVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALfddiD 3065
Cdd:PRK12467 1321 LPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVT-LFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA----E 1395
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3066 LTRSVGWFTSAYPLR--LTPAQSPGESIKAIKEQ-LRAVPHKGLGYgvlryladpavRQAMAALptapitfnylgQFDQS 3142
Cdd:PRK12467 1396 TEGLIGFFVNTQVLRaeVDGQASFQQLLQQVKQAaLEAQAHQDLPF-----------EQLVEAL-----------QPERS 1453
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3143 FADA-LFQPLDQPTGPIHDEQAPLPN---------------ELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAE 3206
Cdd:PRK12467 1454 LSHSpLFQVMFNHQRDDHQAQAQLPGlsveslswesqtaqfDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNL 1533
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3207 LQALI--------EHCLEDGAGGL--------TPSDFPLAQL--------SQAQLDALAVPAGEIEDVYPLTPMQEGLLL 3262
Cdd:PRK12467 1534 LQGLVadperrlgELDLLDEAERRqilegwnaTHTGYPLARLvhqliedqAAATPEAVALVFGEQELTYGELNRRANRLA 1613

                  ....*....
gi 15597620  3263 HTLLEPGTG 3271
Cdd:PRK12467 1614 HRLIALGVG 1622
PRK12316 PRK12316
peptide synthase; Provisional
675-1993 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1227.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   675 LPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFV 754
Cdd:PRK12316   50 DRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   755 DLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQ 834
Cdd:PRK12316  130 DCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   835 PADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAA 914
Cdd:PRK12316  210 EPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTA 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   915 LDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQ 994
Cdd:PRK12316  290 RRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQ 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   995 ANQDLPFDQVLAACG-----QGGQLFQVLFNHQQR--DLSALRRLPGLLADELPWHSREAKFDLQLQSEEDArGRLTLNF 1067
Cdd:PRK12316  370 AHQDLPFERLVEALKverslSHSPLFQVMYNHQPLvaDIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKG-GRLHAAL 448
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1068 DYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLAE-WGSAPCE-PARAWLPELLERQLAQSAERV 1145
Cdd:PRK12316  449 TYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEgWNATAAEyPLQRGVHRLFEEQVERTPEAP 528
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1146 ALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSG 1225
Cdd:PRK12316  529 ALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSG 608
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1226 VELLLTQAHLFERLPGAEGVTPICLD--SLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQ 1303
Cdd:PRK12316  609 VQLLLSQSHLGRKLPLAAGVQVLDLDrpAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQ 688
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1304 ATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA 1383
Cdd:PRK12316  689 QAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS 768
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1384 CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPA 1463
Cdd:PRK12316  769 CTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPV 848
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1464 GVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQAR 1543
Cdd:PRK12316  849 GVLGELYLAGRGLARGYHGRPGLTAERFVPSPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEAR 927
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1544 LLAQPGVAQAVVVIregVAGSQLVGYytgAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALP 1623
Cdd:PRK12316  928 LLEHPWVREAAVLA---VDGKQLVGY---VVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP 1001
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1624 EP--VWQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQAcDVELPLRALFEASELEAF 1701
Cdd:PRK12316 1002 APeaSVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSL 1080
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1702 CEQVRAAQAAgrtdshgAIRRIDREQPVPLSYSQQrmWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHET 1781
Cdd:PRK12316 1081 ALVAKAGQAT-------AADQGPASGEVALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDA 1151
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1782 LRTTFPSVDGVPVQRVHGDGGLHMDWQDfSALDrdsrQQHLQTLADsEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLH 1861
Cdd:PRK12316 1152 LRLRFREEDGGWQQAYAAPQAGEVLWQR-QAAS----EEELLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIH 1225
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1862 HIVTEGWAMDIFARELGALYEAFLDDresplepLPVQYLDYSVWQREWLE-SGERQRQLDYWKAQLGNEHPllELPGDRP 1940
Cdd:PRK12316 1226 HLVVDGVSWRILLEDLQRAYADLDAD-------LPARTSSYQAWARRLHEhAGARAEELDYWQAQLEDAPH--ELPCENP 1296
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  1941 RPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMF--MTMTAtLAALLYRYSGQ 1993
Cdd:PRK12316 1297 DGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVndLLLTA-LARVTCRWSGQ 1350
PRK12316 PRK12316
peptide synthase; Provisional
13-1998 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1202.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    13 QALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
Cdd:PRK12316 2007 QRIAEQAARAPEAIAVVF------GDQHLSYAELDSRAnRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    92 VP---AYPpesarrhhQERLLSIIADAEPRLVLTTADLREPLLqmnaqlSAANAPQLLCVDQLD-PAVAEAWDEPQVRPE 167
Cdd:PRK12316 2081 VPldpNYP--------AERLAYMLEDSGAALLLTQRHLLERLP------LPAGVARLPLDRDAEwADYPDTAPAVQLAGE 2146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   168 HIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDmGLIGGLLQPIFSGVPcVLMSPRYfLE 247
Cdd:PRK12316 2147 NLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGAR-VLIRDDE-LW 2223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   248 RPVRWLEAISQYGGTVSGGPDFAYRLCSErVAESALQRLDLsgwRVAFSGSEPIRQDSLERfaekfAASRFDASSFFACY 327
Cdd:PRK12316 2224 DPEQLYDEMERHGVTILDFPPVYLQQLAE-HAERDGRPPAV---RVYCFGGEAVPAASLRL-----AWEALRPVYLFNGY 2294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   328 GLAEATLFVTggqrgqgipalavdgeaLARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASgEVLGDDNVGEIWAAGPSIA 407
Cdd:PRK12316 2295 GPTEAVVTPL-----------------LWKCRPQDPCGAAYVPIGRALGNRRAYILDADL-NLLAPGMAGELYLGGEGLA 2356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   408 HGYWRNPEASAKAFV----ERDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKgrva 482
Cdd:PRK12316 2357 RGYLNRPGLTAERFVpdpfSASGERLYRTGDLARYRaDGVVEYLGRIDHQVKIRGFRIELGEIEARLQ-AHPAVRE---- 2431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   483 AFAVTVDGEEGIGIAAE-IGRGVQKSVPaQELIDSIRQAVAEAYQEApkvvALLNPGALPKTSSGKLQRSAcrLRLEDGS 561
Cdd:PRK12316 2432 AVVVAQDGASGKQLVAYvVPDDAAEDLL-AELRAWLAARLPAYMVPA----HWVVLERLPLNPNGKLDRKA--LPKPDVS 2504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   562 ldsyalfpglQAVQEAQPPAgdDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFE 641
Cdd:PRK12316 2505 ----------QLRQAYVAPQ--EGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFE 2572
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   642 APTLQAFSATVARQLAAGLPAEAPmahLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRL 721
Cdd:PRK12316 2573 RPTLAAFAASLESGQTSRAPVLQK---VTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDAL 2649
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   722 VERHEALRTRFLERDGAALQRIDERGEFAwqfvDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQ 801
Cdd:PRK12316 2650 VLRHETLRTRFVEVGEQTRQVILPNMSLR----IVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV 2725
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   802 LWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLEL 881
Cdd:PRK12316 2726 LVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLEL 2805
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   882 ATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVG 961
Cdd:PRK12316 2806 PLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIG 2885
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   962 FFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACG-----QGGQLFQVLFNHQQrDLSALRRLPGLL 1036
Cdd:PRK12316 2886 FFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQperslSHSPLFQVMYNHQS-GERAAAQLPGLH 2964
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1037 ADELPWHSREAKFDLQLQSEEDARGrLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLA 1116
Cdd:PRK12316 2965 IESFAWDGAATQFDLALDTWESAEG-LGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLL 3043
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1117 E-WGSAPCE-PARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVG 1194
Cdd:PRK12316 3044 EaWNATAAEyPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVG 3123
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1195 LLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLfeRLPGAEGVTPICLDSlKLDNWPSQAPGLHLHGDNLAY 1274
Cdd:PRK12316 3124 LLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHL--RLPLAQGVQVLDLDR-GDENYAEANPAIRTMPENLAY 3200
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1275 VIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLV 1354
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLV 3280
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1355 ELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPavaLHNRYGPTETAINVTHWQCRA 1434
Cdd:PRK12316 3281 ELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVE 3357
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1435 EDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNA 1514
Cdd:PRK12316 3358 EGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRTGDLARYRA 3436
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1515 DGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLVGYytgAVGAEAEAEQNQRLRAALQAEL 1594
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL---AVDGRQLVAY---VVPEDEAGDLREALKAHLKASL 3510
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1595 PEYMVPTQLMRLAQMPLGPSGKLDTRALPEP--VWQQREHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLA 1672
Cdd:PRK12316 3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPdaALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1673 TRIVSRTRQAcDVELPLRALFEASELEAFCEQVR--AAQAAGRTDSHGAIRRI-DREQPVPLSYSQQRMWFLWQlepdsp 1749
Cdd:PRK12316 3591 LQVVSRARQA-GIRFTPKDLFQHQTIQGLARVARvgGGVAVDQGPVSGETLLLpIQQQFFEEPVPERHHWNQSL------ 3663
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1750 aynvggLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGV-PVQRVHGDGGLHMDWQdfsaLDRDSRQQhLQTLADs 1828
Cdd:PRK12316 3664 ------LLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGwTAEHLPVELGGALLWR----AELDDAEE-LERLGE- 3731
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1829 EAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRE 1908
Cdd:PRK12316 3732 EAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQE 3811
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1909 WLESGERQRQLDYWKAQLGNEHPllELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTAT-LAALL 1987
Cdd:PRK12316 3812 HARGEALKAELAYWQEQLQGVSS--ELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTaLARVV 3889
                        2010
                  ....*....|.
gi 15597620  1988 YRYSGQQDLRI 1998
Cdd:PRK12316 3890 CRWTGEASALV 3900
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
658-1988 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1062.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  658 AGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDG 737
Cdd:COG1020    1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  738 AALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLN 817
Cdd:COG1020   81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  818 LLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAAR 897
Cdd:COG1020  161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  898 YSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQ 977
Cdd:COG1020  241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  978 PFAALLGEAREATLGAQANQDLPFDQVLAACGQ-----GGQLFQVLFNHQQRDLSALRrLPGLLADELPWHSREAKFDLQ 1052
Cdd:COG1020  321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPerdlsRNPLFQVMFVLQNAPADELE-LPGLTLEPLELDSGTAKFDLT 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1053 LQSEEDArGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALV-DAEQAAHLAEW-GSAPCEPARAWL 1130
Cdd:COG1020  400 LTVVETG-DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLtAAERQQLLAEWnATAAPYPADATL 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1131 PELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDP 1210
Cdd:COG1020  479 HELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDP 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1211 DYPSERLAYMLADSGVELLLTQAHLFERLPgAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGN 1290
Cdd:COG1020  559 AYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMV 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1291 THAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPP 1370
Cdd:COG1020  638 EHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPS 717
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 LLQLFIDEpGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED--GERSPIGRPLGN 1448
Cdd:COG1020  718 LLRALLDA-APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDadGGSVPIGRPIAN 796
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1449 VVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQV 1528
Cdd:COG1020  797 TRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQV 876
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1529 KLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYtgAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQ 1608
Cdd:COG1020  877 KIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAY--VVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLP 954
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1609 MPLGPSGKLDTRALPEPVWQQREH-VEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVEL 1687
Cdd:COG1020  955 LPLTGNGKLDRLALPAPAAAAAAAaAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLL 1034
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1688 PLRALFEASELEAfceqVRAAQAAGRTDSHGAIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVAR 1767
Cdd:COG1020 1035 LLLLLFLAAAAAA----AAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1768 FEAALQALVQRHETLRTTFPSVDGVPVQRVHGDggLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMV 1847
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVA--LAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLL 1188
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1848 KMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLG 1927
Cdd:COG1020 1189 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLA 1268
                       1290      1300      1310      1320      1330      1340
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 1928 NEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLY 1988
Cdd:COG1020 1269 LALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1719-3039 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1037.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1719 AIRRIDREQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVH 1798
Cdd:COG1020    8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1799 GDGGLHMDWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELG 1878
Cdd:COG1020   88 PVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1879 ALYEAFLDDRESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSP 1958
Cdd:COG1020  168 RLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1959 ELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLE 2038
Cdd:COG1020  248 ELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2039 QVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQtRQLAGMTVEYIANDARATKFDLNLEVTDLD 2118
Cdd:COG1020  328 RVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADE-LELPGLTLEPLELDSGTAKFDLTLTVVETG 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2119 QRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLA--GTAGEAGLQDTLHGLFAARV 2196
Cdd:COG1020  407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEwnATAAPYPADATLHELFEAQA 486
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2197 AASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQ 2276
Cdd:COG1020  487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2277 YMIEDSGVRLLLSHAALFEALGELpaGVARWCLeeDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEI 2356
Cdd:COG1020  567 YMLEDAGARLVLTQSALAARLPEL--GVPVLAL--DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL 642
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2357 AMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL-RAQGQWGAEEICELIRAEGVSILGFTPSYgsqL 2435
Cdd:COG1020  643 VNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLaPPEARRDPAALAELLARHRVTVLNLTPSL---L 719
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2436 AQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLAClAPERLEEGAASVPIGSVVGARV 2514
Cdd:COG1020  720 RALLDAAPEALPsLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYY-EVTPPDADGGSVPIGRPIANTR 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2515 AYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKI 2594
Cdd:COG1020  799 VYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKI 878
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2595 RGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVASavaeqdEDAQAALREALKTHLKQQLPDYMVPAHLLLL 2673
Cdd:COG1020  879 RGFRIELGEIEAALLQHPGVREAVVVAReDAPGDKRLVAYVVP------EAGAAAAAALLRLALALLLPPYMVPAAVVLL 952
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2674 ASLPLTANGKLDRRALPAPDPALnRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGI 2753
Cdd:COG1020  953 LPLPLTGNGKLDRLALPAPAAAA-AAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLL 1031
                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2754 HFSPRDLFQHQTVQSLAAVARHSQASQAEQGPVQG--DSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSL 2831
Cdd:COG1020 1032 LLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAaaPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLAL 1111
                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2832 QRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLW--------HVPVQSFDECAELFAKAQRSLDLEQGPLLRAVLVDGP 2903
Cdd:COG1020 1112 LLLLALLLALLAALRARRAVRQEGPRLRLLVALAAalalaallALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLL 1191
                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2904 AGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGGQP 2983
Cdd:COG1020 1192 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALAL 1271
                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2984 VEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTALARVL 3039
Cdd:COG1020 1272 LLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
PRK12467 PRK12467
peptide synthase; Provisional
637-1920 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 839.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   637 RQLFEAPTLQAFSATVARQLAAGL------------PAEAPMAH--------LPRGV----DL-PQSAAQQRLWLTWQID 691
Cdd:PRK12467 2584 QEMFDEATIQRLADAYAEELRALIehccsndqrgvtPSDFPLAGlsqeqldrLPVAVgdieDIyPLSPMQQGMLFHTLYE 2663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   692 PQSAAYNIPGGLRLRGeLDEAALRASFQRLVERHEALRTRFLERDGAA--LQRIDERGEFAwqFVDLAALAEHERAAAAA 769
Cdd:PRK12467 2664 GGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEepLQVVYKQARLP--FSRLDWRDRADLEQALD 2740
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   770 QRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYaeacGGQPadLAPLELHYAEFA 849
Cdd:PRK12467 2741 ALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY----FGQP--PPAREGRYRDYI 2814
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   850 AW-QRQWLDAGEgarqlAYWRERLGD-TAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLA 927
Cdd:PRK12467 2815 AWlQAQDAEASE-----AFWKEQLAAlEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRVTLNTLVQG 2889
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   928 AFQALLHRHSGQGEIRIGVPSANR----QRLETQglVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQ 1003
Cdd:PRK12467 2890 AWLLLLQRFTGQDTVCFGATVAGRpaqlRGAEQQ--LGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLAD 2967
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1004 VLAACGQGGQ-LFQ--VLFNHQQRDLSALRRLP-GLLADELpwHSREAK---FDLQLQSEEdargRLTLNFDYAADLFDE 1076
Cdd:PRK12467 2968 IQRWAGQGGEaLFDsiLVFENYPISEALKQGAPsGLRFGAV--SSREQTnypLTLAVGLGD----TLELEFSYDRQHFDA 3041
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1077 ASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLAE-W-GSAPCEPARAWLPELLERQLAQSAERVALEWDGGSL 1154
Cdd:PRK12467 3042 AAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHaWnATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQL 3121
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1155 GYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH 1234
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH 3201
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1235 LFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVL 1314
Cdd:PRK12467 3202 LLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRV 3281
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1315 MQKAPVSFDVSVWECFWPLVTGCRLVLAaPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGG 1394
Cdd:PRK12467 3282 LLFMSFSFDGAQERFLWTLICGGCLVVR-DNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGG 3360
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1395 EALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAE---DGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCI 1471
Cdd:PRK12467 3361 EAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDavcEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYI 3440
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1472 GGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVA 1551
Cdd:PRK12467 3441 GGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1552 QAVVVIREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQ-QR 1630
Cdd:PRK12467 3521 EAVVLARDGAGGKQLVAYVVPADPQGDWRET---LRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKgSR 3597
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1631 EHVEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELEAFCeqvraaqa 1710
Cdd:PRK12467 3598 EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-------- 3669
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1711 agrtdshgairridreqpvplsysqqrmwflwqlepdspAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFpsvD 1790
Cdd:PRK12467 3670 ---------------------------------------GYSPLGDVPVNLLLDLNRLETGFPALFCRHEGLGTVF---D 3707
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1791 GVPVQRVhgdgglhmdwqdfsaldrdsrqqhlqtladseahrpfdlesgpllrvcmvkMAEREHYLVVTLHHIVTEGWAm 1870
Cdd:PRK12467 3708 YEPLAVI---------------------------------------------------LEGDRHVLGLTCRHLLDDGWQ- 3735
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620  1871 difarelgalyeaflddrESPLEPLPVQYLDYSVWQREWLESGERQRQLD 1920
Cdd:PRK12467 3736 ------------------DTSLQAMAVQYADYILWQQAKGPYGLLGWSLG 3767
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3234-4331 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 804.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3234 QAQLDALAVPAGEIEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVwNAG 3313
Cdd:COG1020    1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLR-TRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3314 ETMLQVIHKPGRTRIEFLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCR 3393
Cdd:COG1020   80 GRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3394 GLLMNDFFEIYSALGESRPANLPTPP-----RYRDYIAWLQRQDLEQSRRWWSESLRGFERPTLVPSDRPflREHAGESG 3468
Cdd:COG1020  160 GLLLAELLRLYLAAYAGAPLPLPPLPiqyadYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRP--RPAVQSYR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3469 GmivGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVgmPEMQRTVGLFINSIPL 3548
Cdd:COG1020  238 G---ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3549 RVQMPAAGqrcTVREWLNRLFERNLELREHEHLPLVAIQESSELPKGQ---PLFDSLFVFENAPVEVSVLDRAQSLNASS 3625
Cdd:COG1020  313 RVDLSGDP---SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLsrnPLFQVMFVLQNAPADELELPGLTLEPLEL 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3626 DSGRTHtnFPLTVVCYP-GDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDFLLDGCNR 3704
Cdd:COG1020  390 DSGTAK--FDLTLTVVEtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNA 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3705 SARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSF 3784
Cdd:COG1020  468 TAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3785 KAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQalalFDELGCvdrpRLLVWDEIQQGEGAEHDPQVYSGPQNL 3864
Cdd:COG1020  548 KAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAAR----LPELGV----PVLALDALALAAEPATNPPVPVTPDDL 619
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3865 AYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQG 3944
Cdd:COG1020  620 AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAA 699
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3945 LLAHVGEQGITVLESVPSLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVD 4024
Cdd:COG1020  700 LAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVT 779
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4025 LASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTG 4104
Cdd:COG1020  780 PPDADGGSVPIGRPIANTRVYVL----DAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTG 855
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4105 DLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRSSADspaglm 4184
Cdd:COG1020  856 DLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAA------ 929
                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4185 veqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMqnQAYQAPRNELEETLARIWAEVLKV 4264
Cdd:COG1020  930 -------ALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA--AAAAAPPAEEEEEEAALALLLLLV 1000
                       1050      1060      1070      1080      1090      1100
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 4265 ERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESLAPSEISEQKAER 4331
Cdd:COG1020 1001 VVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAA 1067
PRK12467 PRK12467
peptide synthase; Provisional
3221-4326 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 747.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3221 GLTPSDFPLAQLsqaqldalavpAGEIEDVyPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVAR 3300
Cdd:PRK12467   32 GVSFANLPIPQV-----------RSAFERI-PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVAR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3301 HEALRASFVwNAGETMLQVIHKPGRTRIEFLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFM 3380
Cdd:PRK12467  100 HESLRTRFV-QDEEGFRQVIDASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3381 MSNHHILIDAWCRGLLMNDFFEIYSALGESRPANLPT-PPRYRDYIAWlQRQDLEQSRR-----WWSESLrGFERPTL-V 3453
Cdd:PRK12467  179 VTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPAlPIQYADYAIW-QRSWLEAGERerqlaYWQEQL-GGEHTVLeL 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3454 PSD--RPFLREHAGESggmivgdRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRpvG 3531
Cdd:PRK12467  257 PTDrpRPAVPSYRGAR-------LRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR--N 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3532 MPEMQRTVGLFINSIPLRVQMPAagqRCTVREWLNRLFERNLELREHEHLP----LVAIQESSELPKgQPLFDSLFVFEN 3607
Cdd:PRK12467  328 RVETERLIGFFVNTQVLKAEVDP---QASFLELLQQVKRTALGAQAHQDLPfeqlVEALQPERSLSH-SPLFQVMFNHQN 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3608 --APVEVSVLDRAQSLNASSDSGRTHT-NFPLTVVCYPGDD-LGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGE 3683
Cdd:PRK12467  404 taTGGRDREGAQLPGLTVEELSWARHTaQFDLALDTYESAQgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3684 LEALPLLGEDERDFLLDGCNRSARDYpLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGID 3763
Cdd:PRK12467  484 LGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPD 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3764 QPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSrTLVLVCTQacrEQALALFDElgCVDRPRLLVWD 3843
Cdd:PRK12467  563 VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDS-GVRLLLTQ---SHLLAQLPV--PAGLRSLCLDE 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3844 EIQQGEG-AEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFL 3922
Cdd:PRK12467  637 PADLLCGySGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELF 716
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3923 AAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQALD-GLRWMLPTGEAMPPELARQWLKRYP 4001
Cdd:PRK12467  717 GALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPrPQRALVCGGEALQVDLLARVRALGP 796
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4002 RIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDP 4081
Cdd:PRK12467  797 GARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYIL----DHYLNPVPVGVVGELYIGGAGLARGYHRRP 872
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4082 LRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGK 4161
Cdd:PRK12467  873 ALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGL 952
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4162 YLVGYLVPGETPRSSadspaglmvEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQnQ 4241
Cdd:PRK12467  953 QLVAYLVPAAVADGA---------EHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQ-A 1022
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4242 AYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESLAP 4321
Cdd:PRK12467 1023 TFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQ 1102

                  ....*
gi 15597620  4322 SEISE 4326
Cdd:PRK12467 1103 GAQPA 1107
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
675-1701 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 714.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   675 LPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFA-WQF 753
Cdd:PRK10252    8 LPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPlPEI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   754 VDLaaLAEHERAAAAAQRREAEAQQPFDLEKG-PLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACG 832
Cdd:PRK10252   88 IDL--RTQPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   833 GQPAD---LAPLELHYAEFAAWQrqwldAGEgARQL--AYWRERLGDTAPVLELAtDHPRTARQASP-AARYSLRVD-EA 905
Cdd:PRK10252  166 GEPTPaspFTPFADVVEEYQRYR-----ASE-AWQRdaAFWAEQRRQLPPPASLS-PAPLPGRSASAdILRLKLEFTdGA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   906 LARAIREAALDHEASVFMWLLAAFqalLHRHSGQGEIRIGVPSANR---QRLETQGLVgffINTLVLRGTPRARQPFAAL 982
Cdd:PRK10252  239 FRQLAAQASGVQRPDLALALVALW---LGRLCGRMDYAAGFIFMRRlgsAALTATGPV---LNVLPLRVHIAAQETLPEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   983 LGeareatlgaqanqdlpfdqvlaacGQGGQLFQVLfNHQQRDLSALRRLPGLLADELPWHS---------REAKF---- 1049
Cdd:PRK10252  313 AT------------------------RLAAQLKKMR-RHQRYDAEQIVRDSGRAAGDEPLFGpvlnikvfdYQLDFpgvq 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1050 ------------DLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHLAE 1117
Cdd:PRK10252  368 aqthtlatgpvnDLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQ 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1118 WGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLA 1197
Cdd:PRK10252  448 VNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHA 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1198 IVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDnwPSQAPGLHLHGDNLAYVIY 1277
Cdd:PRK10252  528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHTAYIIF 605
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1278 TSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELV 1357
Cdd:PRK10252  606 TSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFF 685
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1358 RQFGVTTLHFVPPLLQLFIDEPGV----AACGSLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTETAINVTHWQCR 1433
Cdd:PRK10252  686 AEYGVTTTHFVPSMLAAFVASLTPegarQSCASLRQVFCSGEALPADLCRE-WQQLTGAPLHNLYGPTEAAVDVSWYPAF 764
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1434 AED-----GERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGD 1508
Cdd:PRK10252  765 GEElaavrGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGD 843
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1509 RARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIRE-------GVAGSQLVGYYTGAVGAEAEAE 1581
Cdd:PRK10252  844 VARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVinqaaatGGDARQLVGYLVSQSGLPLDTS 923
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1582 QnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREH-VEPRTELQRRIAAIWSEVLGLPRVGLRD 1660
Cdd:PRK10252  924 A---LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPgRAPKTGTETIIAAAFSSLLGCDVVDADA 1000
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|.
gi 15597620  1661 DFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELEAF 1701
Cdd:PRK10252 1001 DFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKL 1041
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
17-559 0e+00

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 711.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   17 RRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP 96
Cdd:cd05931    1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   97 PEsaRRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTS 176
Cdd:cd05931   81 PT--PGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  177 GSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAI 256
Cdd:cd05931  159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRWLRLI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  257 SQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSFFACYGLAEATLFV 336
Cdd:cd05931  239 SRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEATLFV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  337 TGGQRGQGIPALAVDGEALARNRIAEGEGS----VLMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWR 412
Cdd:cd05931  319 SGGPPGTGPVVLRVDRDALAGRAVAVAADDpaarELVSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWG 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  413 NPEASAKAFVER---DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARKGRVAAFAVTVD 489
Cdd:cd05931  399 RPEATAETFGALaatDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPDD 478
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  490 GEEGIGIAAEIGRGVQKsVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLED 559
Cdd:cd05931  479 GEERLVVVAEVERGADP-ADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
PRK12316 PRK12316
peptide synthase; Provisional
3240-4314 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 710.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3240 LAVPAG-EIEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQ 3318
Cdd:PRK12316   38 FPIPAGvSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3319 ViHKPGRTRIEFLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMN 3398
Cdd:PRK12316  118 V-PLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3399 DFFEIYSALGESRPANLPT-PPRYRDYIAWlQRQDL---EQSRR--WWSESLrGFERPTL-VPSDRPflrEHAGESggmI 3471
Cdd:PRK12316  197 EFSRFYSAYATGAEPGLPAlPIQYADYALW-QRSWLeagEQERQleYWRAQL-GEEHPVLeLPTDHP---RPAVPS---Y 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3472 VGDRYT-RLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGmpEMQRTVGLFINSIPLRV 3550
Cdd:PRK12316  269 RGSRYEfSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGFFVNTQVLRS 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3551 QMPAagqRCTVREWLNRLFERNLELREHEHLPLVAIQESSELPKG---QPLFDSLFVFENAPVEVSVLDRAQ--SLNASS 3625
Cdd:PRK12316  347 VFDG---RTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSlshSPLFQVMYNHQPLVADIEALDTVAglEFGQLE 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3626 DSGRThTNFPLTVVCY-PGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDFLLDGCNR 3704
Cdd:PRK12316  424 WKSRT-TQFDLTLDTYeKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNA 502
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3705 SARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSF 3784
Cdd:PRK12316  503 TAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAIL 582
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3785 KAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQA-CREQALALFDELGCVDRPRLlvWDEIQqgegAEHDPQVYSGPQN 3863
Cdd:PRK12316  583 KAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHlGRKLPLAAGVQVLDLDRPAA--WLEGY----SEENPGTELNPEN 656
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3864 LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQ 3943
Cdd:PRK12316  657 LAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPA 736
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3944 GLLAHVGEQGITVLESVPSLIQGMLAEER-QALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFF- 4021
Cdd:PRK12316  737 KLVELINREGVDTLHFVPSMLQAFLQDEDvASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWt 816
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4022 RVDLASTEstyLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGApGERLY 4101
Cdd:PRK12316  817 CVEEGGDS---VPIGRPIANLACYIL----DANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMY 888
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4102 RTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEganGKYLVGYLVPGEtprssadspa 4181
Cdd:PRK12316  889 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GKQLVGYVVLES---------- 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4182 glmvEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQnQAYQAPRNELEETLARIWAEV 4261
Cdd:PRK12316  956 ----EGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQ-QGYVAPRNALERTLAAIWQDV 1030
                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  4262 LKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPlRAMFECTTVEELAS 4314
Cdd:PRK12316 1031 LGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSP-RDLFQHQTIRSLAL 1082
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
2200-2690 0e+00

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 685.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd17649    1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLSHaalfealgelpagvarwcleedgpaldaedpaplaalsGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd17649   81 EDSGAGLLLTH--------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAH 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWG-AEEICELIRAEGVSILGFTPSYGSQLAQW 2438
Cdd:cd17649  123 CQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWAsADELAEMVRELGVTVLDLPPAYLQQLAEE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 LES--QGRQLPVRMCITGGEALTGEHLQRIRQAfaPASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAY 2516
Cdd:cd17649  203 ADRtgDGRPPSLRLYIFGGEALSPELLRRWLKA--PVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAY 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2517 ILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRG 2596
Cdd:cd17649  281 ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2597 FRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAEqdedAQAALREALKTHLKQQLPDYMVPAHLLLLASL 2676
Cdd:cd17649  361 FRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAA----AQPELRAQLRTALRASLPDYMVPAHLVFLARL 436
                        490
                 ....*....|....
gi 15597620 2677 PLTANGKLDRRALP 2690
Cdd:cd17649  437 PLTPNGKLDRKALP 450
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1131-1622 0e+00

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 649.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1131 PELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDP 1210
Cdd:cd17646    1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1211 DYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTpiCLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGN 1290
Cdd:cd17646   81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVA--LLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1291 THAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPP 1370
Cdd:cd17646  159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 LLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAvALHNRYGPTETAINVTHWQCRAEDGERS-PIGRPLGNV 1449
Cdd:cd17646  239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGA-ELHNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNT 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1450 VCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVK 1529
Cdd:cd17646  318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVK 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1530 LRGFRIEPEEIQARLLAQPGVAQAVVVIRE-GVAGSQLVGYYTGAVGAEAEAEqnQRLRAALQAELPEYMVPTQLMRLAQ 1608
Cdd:cd17646  397 IRGFRVEPGEIEAALAAHPAVTHAVVVARAaPAGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEYMVPAAFVVLDA 474
                        490
                 ....*....|....
gi 15597620 1609 MPLGPSGKLDTRAL 1622
Cdd:cd17646  475 LPLTANGKLDRAAL 488
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1728-2155 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 645.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1728 PVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDW 1807
Cdd:cd19531    1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDD 1887
Cdd:cd19531   81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1888 RESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRF 1967
Cdd:cd19531  161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1968 NAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDG 2047
Cdd:cd19531  241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2048 QSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCLTY 2127
Cdd:cd19531  321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAP-AAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEY 399
                        410       420
                 ....*....|....*....|....*...
gi 15597620 2128 SRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19531  400 NTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
1142-1622 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 634.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1142 AERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML 1221
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1222 ADSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQW 1301
Cdd:cd05930   81 EDSGAKLVLTDP------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1302 MQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGV 1381
Cdd:cd05930  125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1382 AACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED--GERSPIGRPLGNVVCRVLDAEFN 1459
Cdd:cd05930  205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDeeDGRVPIGRPIPNTRVYVLDENLR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1460 LLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEE 1539
Cdd:cd05930  285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF-GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGE 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1540 IQARLLAQPGVAQAVVVIREGVAGSQ-LVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLD 1618
Cdd:cd05930  364 IEAALLAHPGVREAAVVAREDGDGEKrLVAYVVPDEGGELDEEE---LRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440

                 ....
gi 15597620 1619 TRAL 1622
Cdd:cd05930  441 RKAL 444
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
674-1097 6.86e-179

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 556.97  E-value: 6.86e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  674 DLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQF 753
Cdd:cd19531    1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  754 VDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGG 833
Cdd:cd19531   81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  834 QPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREA 913
Cdd:cd19531  161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  914 ALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGA 993
Cdd:cd19531  241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  994 QANQDLPFDQVLAACgqggQ---------LFQVLFNHQQRDLSALrRLPGLLADELPWHSREAKFDLQLQSEEDArGRLT 1064
Cdd:cd19531  321 YAHQDLPFEKLVEAL----QperdlsrspLFQVMFVLQNAPAAAL-ELPGLTVEPLEVDSGTAKFDLTLSLTETD-GGLR 394
                        410       420       430
                 ....*....|....*....|....*....|...
gi 15597620 1065 LNFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19531  395 GSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
3250-3678 1.44e-177

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 552.96  E-value: 1.44e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3250 VYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIE 3329
Cdd:cd19543    1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3330 FLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGE 3409
Cdd:cd19543   81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 SRPANLPTPPRYRDYIAWLQRQDLEQSRRWWSESLRGFERPTLVPSDRPflrehAGESGGMIVGDRYTRLDAADGARLRE 3489
Cdd:cd19543  161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELP-----ADADGSYEPGEVSFELSAELTARLQE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3490 LAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAagqRCTVREWLNRLF 3569
Cdd:cd19543  236 LARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDP---DQTVLELLKDLQ 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3570 ERNLELREHEHLPLVAIQESSELpkGQPLFDSLFVFENAPVEVSVL--DRAQSLNASSDSGRTHTNFPLTVVCYPGDDLG 3647
Cdd:cd19543  313 AQQLELREHEYVPLYEIQAWSEG--KQALFDHLLVFENYPVDESLEeeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELT 390
                        410       420       430
                 ....*....|....*....|....*....|.
gi 15597620 3648 LHLSYDQRYFEAPTVERLLGEFKRLLLALAD 3678
Cdd:cd19543  391 IKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
2200-2689 4.29e-171

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 535.57  E-value: 4.29e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLSHaalfealgelpagvarwcleedgpaldaedpaplaalsgPQHQAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd05930   81 EDSGAKLVLTD---------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWG-AEEICELIRAEGVSILGFTPSYGSQLAQW 2438
Cdd:cd05930  122 LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdPEALADLLAEEGITVLHLTPSLLRLLLQE 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 LESQgRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPERlEEGAASVPIGSVVGARVAYIL 2518
Cdd:cd05930  202 LELA-ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPD-DEEDGRVPIGRPIPNTRVYVL 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2519 DADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFR 2598
Cdd:cd05930  280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYR 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2599 IELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVASavaeqdEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLP 2677
Cdd:cd05930  359 IELGEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVP------DEGGELDEEELRAHLAERLPDYMVPSAFVVLDALP 432
                        490
                 ....*....|..
gi 15597620 2678 LTANGKLDRRAL 2689
Cdd:cd05930  433 LTPNGKVDRKAL 444
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2789-3214 5.41e-171

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 534.52  E-value: 5.41e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2789 DSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHV 2868
Cdd:cd19534    1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2869 -PVQSFD---ECAELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPA 2944
Cdd:cd19534   81 vDLSSLAqaaAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2945 LPAKTSaFRDWAGRLQAYAGSESLREELGWWQARLGGQPVEWPCDRPQgdnREALAESVSLRLDPQRTRQLLQQAPAAYR 3024
Cdd:cd19534  161 LPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANAAYR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3025 TQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTPAQS--PGESIKAIKEQLRAVP 3102
Cdd:cd19534  237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASedLGDTLKRVKEQLRRIP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3103 HKGLGYGVLRYLADPAvRQAMAALPTAPITFNYLGQFDQSF-ADALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGELV 3181
Cdd:cd19534  317 NKGIGYGILRYLTPEG-TKRLAFHPQPEISFNYLGQFDQGErDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGGQLV 395
                        410       420       430
                 ....*....|....*....|....*....|...
gi 15597620 3182 LRWTYSRERYDARTVNELAQAYLAELQALIEHC 3214
Cdd:cd19534  396 ITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1132-1622 2.91e-170

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 534.86  E-value: 2.91e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:cd12117    1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1212 YPSERLAYMLADSGVELLLTQAHLFERLPGaEGVTPICLDSlkLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNT 1291
Cdd:cd12117   81 LPAERLAFMLADAGAKVLLTDRSLAGRAGG-LEVAVVIDEA--LDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1292 HAALAeRLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPL 1371
Cdd:cd12117  158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1372 LQLFIDEpGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERS--PIGRPLGNV 1449
Cdd:cd12117  237 FNQLADE-DPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGsiPIGRPIANT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1450 VCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVK 1529
Cdd:cd12117  316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDGRLEFLGRIDDQVK 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1530 LRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGS-QLVGYYTGAVGAEAEAeqnqrLRAALQAELPEYMVPTQLMRLAQ 1608
Cdd:cd12117  395 IRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDkRLVAYVVAEGALDAAE-----LRAFLRERLPAYMVPAAFVVLDE 469
                        490
                 ....*....|....
gi 15597620 1609 MPLGPSGKLDTRAL 1622
Cdd:cd12117  470 LPLTANGKVDRRAL 483
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3727-4230 1.99e-167

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 524.78  E-value: 1.99e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRtlvlvctqacreqalalfdelgcvdrPRLLVwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd05930   81 EDSG--------------------------AKLVL-----------------TDPDDLAYVIYTSGSTGKPKGVMVEHRG 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:cd05930  118 LVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRL 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAE-ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLY 4045
Cdd:cd05930  198 LLQElELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVY 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4046 LLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGDLARRRADGVLEYVGRIDHQV 4125
Cdd:cd05930  278 VL----DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQV 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4126 KIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPGEtprssadspaglmvEQGAWFERIKQQLRADLPD 4204
Cdd:cd05930  353 KIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDE--------------GGELDEEELRAHLAERLPD 418
                        490       500
                 ....*....|....*....|....*.
gi 15597620 4205 YMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05930  419 YMVPSAFVVLDALPLTPNGKVDRKAL 444
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1726-2786 1.64e-166

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 553.88  E-value: 1.64e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1726 EQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHM 1805
Cdd:PRK10252    5 SQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1806 -DWQDFSalDRDSRQQHLQTLADSEAHRPFDLESG-PLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEA 1883
Cdd:PRK10252   85 pEIIDLR--TQPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1884 FLDDRESPLEPLPVQYLDYSVWQReWLESGERQRQLDYWKAQLGNEHPLLELPGDRPrpPVQSHQGDLYRFDLSPELAER 1963
Cdd:PRK10252  163 WLRGEPTPASPFTPFADVVEEYQR-YRASEAWQRDAAFWAEQRRQLPPPASLSPAPL--PGRSASADILRLKLEFTDGAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1964 VRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQT 2043
Cdd:PRK10252  240 RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2044 VIDGQSHQDLPFDHLVEALQppRSAAYNPLFQVMCNVQRWEFQ--------QTRQLAGMTVEyiandaratkfDLNLEV- 2114
Cdd:PRK10252  320 LKKMRRHQRYDAEQIVRDSG--RAAGDEPLFGPVLNIKVFDYQldfpgvqaQTHTLATGPVN-----------DLELALf 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2115 TDLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLAGTAGEAGLQDTLHGLFAA 2194
Cdd:PRK10252  387 PDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2195 RVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLER 2274
Cdd:PRK10252  467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2275 LQYMIEDSGVRLLLSHAALFEALGELPaGVARWCLEEdgpALDAEDPAPLaALSGPQHQAYLIYTSGSTGKPKGVAVSHG 2354
Cdd:PRK10252  547 LKMMLEDARPSLLITTADQLPRFADVP-DLTSLCYNA---PLAPQGAAPL-QLSQPHHTAYIIFTSGSTGRPKGVMVGQT 621
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2355 EIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRA-QGQWGAEEICELIRAEGVSILGFTPSYGS 2433
Cdd:PRK10252  622 AIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEpEAHRDPLAMQQFFAEYGVTTTHFVPSMLA 701
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2434 QLAQWLESQGRQLPV---RMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVV----MPlAClAPERLEEGAASVPI 2506
Cdd:PRK10252  702 AFVASLTPEGARQSCaslRQVFCSGEALPADLCREWQQLTG-APLHNLYGPTEAAVdvswYP-AF-GEELAAVRGSSVPI 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2507 GSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVG 2586
Cdd:PRK10252  779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAP-GERMYRTGDVARWLDDGAVEYLG 857
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2587 RIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL----DSPSG---KQLAGYVasaVAEQDEDAQAAlreALKTHLKQ 2659
Cdd:PRK10252  858 RSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAATGgdaRQLVGYL---VSQSGLPLDTS---ALQAQLRE 931
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2660 QLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALnRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSI 2739
Cdd:PRK10252  932 RLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKA-QVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSL 1010
                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*...
gi 15597620  2740 LSIQVVSR-ARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQAEQGPV 2786
Cdd:PRK10252 1011 LAMKLAAQlSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFG 1058
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
1143-1623 2.15e-164

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 516.54  E-value: 2.15e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd17649    2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQahlferlpgaegvtpicldslkldnwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1302
Cdd:cd17649   82 DSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1303 QATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDE---- 1378
Cdd:cd17649  127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEadrt 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1379 -PGVAacGSLRRLFSGGEALPAELRNRVLQrlPAVALHNRYGPTETAINVTHWQCRAED---GERSPIGRPLGNVVCRVL 1454
Cdd:cd17649  207 gDGRP--PSLRLYIFGGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEAGAaraGASMPIGRPLGGRSAYIL 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1455 DAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFR 1534
Cdd:cd17649  283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFR 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1535 IEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGyYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPS 1614
Cdd:cd17649  363 IELGEIEAALLEHPGVREAAVVALDGAGGKQLVA-YVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441

                 ....*....
gi 15597620 1615 GKLDTRALP 1623
Cdd:cd17649  442 GKLDRKALP 450
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1134-1623 1.22e-161

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 510.35  E-value: 1.22e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1134 LERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYP 1213
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1214 SERLAYMLADSGVELLLTQAHLFERLPGAEgVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHA 1293
Cdd:cd17651   81 AERLAFMLADAGPVLVLTHPALAGELAVEL-VAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1294 ALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQ 1373
Cdd:cd17651  160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1374 LFIDEPGVAACGS--LRRLFSGGEALPAELRNRVL-QRLPAVALHNRYGPTETAINVTHW--QCRAEDGERSPIGRPLGN 1448
Cdd:cd17651  240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDLREFcAGLPGLRLHNHYGPTETHVVTALSlpGDPAAWPAPPPIGRPIDN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1449 VVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSaAGERLYRTGDRARWNADGVLEYLGRLDQQV 1528
Cdd:cd17651  320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGRADDQV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1529 KLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGS-QLVGYYTGAVGAEAEAEqnqRLRAALQAELPEYMVPTQLMRLA 1607
Cdd:cd17651  399 KIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEkRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLD 475
                        490
                 ....*....|....*.
gi 15597620 1608 QMPLGPSGKLDTRALP 1623
Cdd:cd17651  476 ALPLTPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1156-1555 5.53e-161

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 504.88  E-value: 5.53e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1156 YAELHARANRLAHYLRD-KGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH 1234
Cdd:TIGR01733    2 YRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1235 LFERLPGAeGVTPICLDSLKLDNWPSQAPGLHL----HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDG 1310
Cdd:TIGR01733   82 LASRLAGL-VLPVILLDPLELAALDDAPAPPPPdapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1311 DDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVE-LVRQFGVTTLHFVPPLLQLfIDEPGVAACGSLRR 1389
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLAL-LAAALPPALASLRL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1390 LFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAED---GERSPIGRPLGNVVCRVLDAEFNLLPAGVA 1466
Cdd:TIGR01733  240 VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDaprESPVPIGRPLANTRLYVLDDDLRPVPVGVV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1467 GELCIGGLGLARGYLGRPALSAERFVADPFSA-AGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:TIGR01733  320 GELYIGGPGVARGYLNRPELTAERFVPDPFAGgDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
                          410
                   ....*....|
gi 15597620   1546 AQPGVAQAVV 1555
Cdd:TIGR01733  400 RHPGVREAVV 409
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1132-1625 4.87e-157

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 496.85  E-value: 4.87e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:cd17655    1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1212 YPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLD-----NWPSQApglhlhgDNLAYVIYTSGSTGQPK 1286
Cdd:cd17655   81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEesenlEPVSKS-------DDLAYVIYTSGSTGKPK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1287 GVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLH 1366
Cdd:cd17655  154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIID 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1367 FVPPLLQLfIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRL-PAVALHNRYGPTETAINVTHWQCRAED--GERSPIG 1443
Cdd:cd17655  234 LTPAHLKL-LDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1444 RPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGR 1523
Cdd:cd17655  313 KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEFLGR 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1524 LDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQ-LVGYYTgavgAEAEAEQNQrLRAALQAELPEYMVPTQ 1602
Cdd:cd17655  392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNyLCAYIV----SEKELPVAQ-LREFLARELPDYMIPSY 466
                        490       500
                 ....*....|....*....|...
gi 15597620 1603 LMRLAQMPLGPSGKLDTRALPEP 1625
Cdd:cd17655  467 FIKLDEIPLTPNGKVDRKALPEP 489
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
1143-1622 5.65e-155

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 490.27  E-value: 5.65e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd12116    2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPglhLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1302
Cdd:cd12116   82 DAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTP---VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1303 QATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVA 1382
Cdd:cd12116  159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1383 ACGSlrRLFSGGEALPAELRNRVLQRlpAVALHNRYGPTETAInvthWQCRAEDGERS---PIGRPLGNVVCRVLDAEFN 1459
Cdd:cd12116  239 RAGL--TALCGGEALPPDLAARLLSR--VGSLWNLYGPTETTI----WSTAARVTAAAgpiPIGRPLANTQVYVLDAALR 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1460 LLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEE 1539
Cdd:cd12116  311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1540 IQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEqnqRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDT 1619
Cdd:cd12116  391 IEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAA---ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDR 467

                 ...
gi 15597620 1620 RAL 1622
Cdd:cd12116  468 KAL 470
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
2191-2689 1.23e-154

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 489.79  E-value: 1.23e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2191 LFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:cd12117    2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2271 PLERLQYMIEDSGVRLLLSHAALFEALGELPagvarwCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVA 2350
Cdd:cd12117   82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLE------VAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2351 VSHGEI---AMHCAAVIEcfgmRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQ-WGAEEICELIRAEGVSILG 2426
Cdd:cd12117  156 VTHRGVvrlVKNTNYVTL----GPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTlLDPDALGALIAEEGVTVLW 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2427 FTPSYGSQLA----QWLESqgrqlpVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPErLEEGAA 2502
Cdd:cd12117  232 LTAALFNQLAdedpECFAG------LRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTE-LDEVAG 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2503 SVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQV 2582
Cdd:cd12117  305 SIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGP-GERLYRTGDLARWLPDGRL 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2583 EYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaVAEQDEDAqaalrEALKTHLKQQL 2661
Cdd:cd12117  384 EFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVReDAGGDKRLVAYV---VAEGALDA-----AELRAFLRERL 455
                        490       500
                 ....*....|....*....|....*...
gi 15597620 2662 PDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd12117  456 PAYMVPAAFVVLDELPLTANGKVDRRAL 483
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3252-4318 3.21e-153

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 514.59  E-value: 3.21e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3252 PLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMlQVIHKPGRT-RIEF 3330
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVW-QWVDPALTFpLPEI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3331 LDWSElpEDGHEERLQALHKREREAGFDLL-EQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGE 3409
Cdd:PRK10252   88 IDLRT--QPDPHAAAQALMQADLQQDLRVDsGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3410 SRPANLPTPPRYRD----YIAWLQRQDLEQSRRWWSESLRGFERP-TLVPSDRPflrehagesgGMIVGDRYTRLD-AAD 3483
Cdd:PRK10252  166 GEPTPASPFTPFADvveeYQRYRASEAWQRDAAFWAEQRRQLPPPaSLSPAPLP----------GRSASADILRLKlEFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3484 GARLREL-AQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRpVGMPEMQRTvGLFINSIPLRVQMPAAGqrcTVR 3562
Cdd:PRK10252  236 DGAFRQLaAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRR-LGSAALTAT-GPVLNVLPLRVHIAAQE---TLP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3563 EWLNRLFERNLELREHEHLPLVAIQESSELPKGQ-PLFDSLfvfenapVEVSVLDRAqsLNASSDSGRTHT--NFP---L 3636
Cdd:PRK10252  311 ELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDePLFGPV-------LNIKVFDYQ--LDFPGVQAQTHTlaTGPvndL 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3637 TVVCYPGDDLGLHLSYD---QRYFEApTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDfLLDGCNRSARDYPlEQ 3713
Cdd:PRK10252  382 ELALFPDEHGGLSIEILanpQRYDEA-TLIAHAERLKALIAQFAADPALLCGDVDILLPGEYA-QLAQVNATAVEIP-ET 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3714 GYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3793
Cdd:PRK10252  459 TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPL 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3794 DPGHPTQRLTRIVELSRTLVLVCTQAcreqALALFDELGCVDRPRLLVWDEIQQGEgaehdPQVYSGPQNLAYVIYTSGS 3873
Cdd:PRK10252  539 DTGYPDDRLKMMLEDARPSLLITTAD----QLPRFADVPDLTSLCYNAPLAPQGAA-----PLQLSQPHHTAYIIFTSGS 609
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3874 TGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQG 3953
Cdd:PRK10252  610 TGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYG 689
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3954 ITVLESVPSLIQGMLAE-----ERQALDGLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPAECSDDVAF---FRVDL 4025
Cdd:PRK10252  690 VTTTHFVPSMLAAFVASltpegARQSCASLRQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWypaFGEEL 768
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4026 ASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGD 4105
Cdd:PRK10252  769 AAVRGSSVPIGYPVWNTGLRIL----DARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGD 843
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4106 LARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-------AVQEGANGKYLVGYLVPGETprSSAD 4178
Cdd:PRK10252  844 VARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSG--LPLD 921
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4179 SPAglmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGqmQNQAYQAPRNELEETLARIW 4258
Cdd:PRK10252  922 TSA------------LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELK--AQVPGRAPKTGTETIIAAAF 987
                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4259 AEVLKVERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIES 4318
Cdd:PRK10252  988 SSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDA 1047
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
2189-2689 5.97e-152

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 482.16  E-value: 5.97e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2189 HGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2268
Cdd:cd17646    1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2269 EYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVArwcleEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKG 2348
Cdd:cd17646   81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVAL-----LGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2349 VAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL-RAQGQWGAEEICELIRAEGVSILGF 2427
Cdd:cd17646  156 VMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVaRPGGHRDPAYLAALIREHGVTTCHF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2428 TPSYGSQLAQWLESQGRQlPVRMCITGGEALTGEHLQRIRQAFaPASFFNAYGPTETVVMPLAClaPERLEEGAASVPIG 2507
Cdd:cd17646  236 VPSMLRVFLAEPAAGSCA-SLRRVFCSGEALPPELAARFLALP-GAELHNLYGPTEAAIDVTHW--PVRGPAETPSVPIG 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2508 S-VVGARVaYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVG 2586
Cdd:cd17646  312 RpVPNTRL-YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGP-GSRMYRTGDLARWRPDGALEFLG 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2587 RIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVASAVAEQDEDAqaalrEALKTHLKQQLPDYM 2665
Cdd:cd17646  390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGaARLVGYVVPAAGAAGPDT-----AALRAHLAERLPEYM 464
                        490       500
                 ....*....|....*....|....
gi 15597620 2666 VPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd17646  465 VPAAFVVLDALPLTANGKLDRAAL 488
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3740-4152 2.74e-151

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 477.14  E-value: 2.74e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3740 SYAELNRRANRLGHALRAA-GVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTq 3818
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3819 acrEQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL 3898
Cdd:TIGR01733   80 ---SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3899 ELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQG-ITVLESVPSLIQGMLAEERQALDG 3977
Cdd:TIGR01733  157 GLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPPALAS 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3978 LRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTY-LPIGSPTDNNRLYLLgagaDDAFE 4056
Cdd:TIGR01733  237 LRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVL----DDDLR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4057 LVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPF-GAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELG 4135
Cdd:TIGR01733  313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
                          410
                   ....*....|....*..
gi 15597620   4136 EIEARLHERADVREAAV 4152
Cdd:TIGR01733  393 EIEAALLRHPGVREAVV 409
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
2191-2693 4.04e-150

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 477.21  E-value: 4.04e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2191 LFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:cd17655    2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2271 PLERLQYMIEDSGVRLLLSHAALfeALGELPAGVarwCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVA 2350
Cdd:cd17655   82 PEERIQYILEDSGADILLTQSHL--QPPIAFIGL---IDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2351 VSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL-RAQGQWGAEEICELIRAEGVSILGFTP 2429
Cdd:cd17655  157 IEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIvRKETVLDGQALTQYIRQNRITIIDLTP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2430 SYGSQLAQwlESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPA-SFFNAYGPTETVVmplaCLAPERLEEGAA---SVP 2505
Cdd:cd17655  237 AHLKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTV----DASIYQYEPETDqqvSVP 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2506 IGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYV 2585
Cdd:cd17655  311 IGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVP-GERMYRTGDLARWLPDGNIEFL 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2586 GRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVASavaeqDEDAQAAlreALKTHLKQQLPDY 2664
Cdd:cd17655  390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGqNYLCAYIVS-----EKELPVA---QLREFLARELPDY 461
                        490       500
                 ....*....|....*....|....*....
gi 15597620 2665 MVPAHLLLLASLPLTANGKLDRRALPAPD 2693
Cdd:cd17655  462 MIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
1143-1623 9.46e-150

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 473.66  E-value: 9.46e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd17652    2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1302
Cdd:cd17652   82 DARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1303 QATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDepgvA 1382
Cdd:cd17652  126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPP----D 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1383 ACGSLRRLFSGGEALPAELrnrVLQRLPAVALHNRYGPTETAINVTHWQCRaEDGERSPIGRPLGNVVCRVLDAEFNLLP 1462
Cdd:cd17652  202 DLPDLRTLVVAGEACPAEL---VDRWAPGRRMINAYGPTETTVCATMAGPL-PGGGVPPIGRPVPGTRVYVLDARLRPVP 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1463 AGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQA 1542
Cdd:cd17652  278 PGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1543 RLLAQPGVAQAVVVIRE-GVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRA 1621
Cdd:cd17652  358 ALTEHPGVAEAVVVVRDdRPGDKRLVAYVVPAPGAAPTAAE---LRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434

                 ..
gi 15597620 1622 LP 1623
Cdd:cd17652  435 LP 436
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3717-4230 4.37e-149

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 474.00  E-value: 4.37e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:cd12117    1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3797 HPTQRLTRIVELSRTLVLVCTQACREQAlalfdelgcvDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGL 3876
Cdd:cd12117   81 LPAERLAFMLADAGAKVLLTDRSLAGRA----------GGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3877 PKGVMVEQAGMLnnQLSKVP-YLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGIT 3955
Cdd:cd12117  151 PKGVAVTHRGVV--RLVKNTnYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3956 VLESVPSLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPI 4035
Cdd:cd12117  229 VLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPI 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4036 GSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGDLARRRADGVL 4115
Cdd:cd12117  309 GRPIANTRVYVL----DEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPDGRL 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4116 EYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPGETPrssadSPAGLmveqgawferi 4194
Cdd:cd12117  384 EFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGdKRLVAYVVAEGAL-----DAAEL----------- 447
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 15597620 4195 KQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd12117  448 RAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1143-1622 1.91e-148

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 470.64  E-value: 1.91e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd17643    2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1302
Cdd:cd17643   82 DSGPSLLLTDP------------------------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1303 QATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDepgvA 1382
Cdd:cd17643  126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVE----A 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1383 ACG------SLRRLFSGGEALPAELRNRVLQR--LPAVALHNRYGPTETAINVTHWQCRAED---GERSPIGRPLGNVVC 1451
Cdd:cd17643  202 ADRdgrdplALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAADlpaAAASPIGRPLPGLRV 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1452 RVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLR 1531
Cdd:cd17643  282 YVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIR 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1532 GFRIEPEEIQARLLAQPGVAQAVVVIREGVAG-SQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMP 1610
Cdd:cd17643  362 GFRIELGEIEAALATHPSVRDAAVIVREDEPGdTRLVAYVVADDGAAADIAE---LRALLKELLPDYMVPARYVPLDALP 438
                        490
                 ....*....|..
gi 15597620 1611 LGPSGKLDTRAL 1622
Cdd:cd17643  439 LTVNGKLDRAAL 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
2213-2619 5.06e-147

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 464.82  E-value: 5.06e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2213 SYAELDARSNRLARVLRS-HGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHA 2291
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2292 ALFEALGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRA 2371
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2372 EDCELHFYSINFDAASERLLAPLLCGARVVL--RAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLpvR 2449
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALASL--R 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2450 MCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGA 2529
Cdd:TIGR01733  239 LVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2530 TGELYVGGAGLARGYHERPALSAERFVPDPFAAE-GGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARL 2608
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
                          410
                   ....*....|.
gi 15597620   2609 LEHPQVREALV 2619
Cdd:TIGR01733  399 LRHPGVREAVV 409
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3717-4234 1.28e-145

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 464.11  E-value: 1.28e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:cd17655    1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3797 HPTQRLTRIVELSRTLVLvCTQacrEQALALFDELGCVDrprLLVWDEIQQGEGAEHDPQvySGPQNLAYVIYTSGSTGL 3876
Cdd:cd17655   81 YPEERIQYILEDSGADIL-LTQ---SHLQPPIAFIGLID---LLDEDTIYHEESENLEPV--SKSDDLAYVIYTSGSTGK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3877 PKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITV 3956
Cdd:cd17655  152 PKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIQgMLAEERQALD-GLRWMLPTGEAMPPELARQWLKRYPR-IGLVNAYGPAECSDDVAFFRVDLASTESTYLP 4034
Cdd:cd17655  232 IDLTPAHLK-LLDAADDSEGlSLKHLIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYEPETDQQVSVP 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4035 IGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgAPGERLYRTGDLARRRADGV 4114
Cdd:cd17655  311 IGKPLGNTRIYIL----DQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGN 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4115 LEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVpgetprSSADSPAglmveqgawfER 4193
Cdd:cd17655  386 IEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGqNYLCAYIV------SEKELPV----------AQ 449
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15597620 4194 IKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALD 4234
Cdd:cd17655  450 LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
2200-2689 3.08e-144

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 458.31  E-value: 3.08e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd17643    1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLShaalfealgelpagvarwcleedgpalDAEDPaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd17643   81 ADSGPSLLLT---------------------------DPDDL------------AYVIYTSGSTGRPKGVVVSHANVLAL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQW-GAEEICELIRAEGVSILGFTPSYGSQLAQW 2438
Cdd:cd17643  122 FAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVArSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 LESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPAS--FFNAYGPTETVV-MPLACLAPERLEEGAASvPIGSVVGARV 2514
Cdd:cd17643  202 ADRDGRDPLaLRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTVhVTFRPLDAADLPAAAAS-PIGRPLPGLR 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2515 AYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKI 2594
Cdd:cd17643  281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2595 RGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVAsavaeqDEDAQAALREALKTHLKQQLPDYMVPAHLLLL 2673
Cdd:cd17643  361 RGFRIELGEIEAALATHPSVRDAAVIVReDEPGDTRLVAYVV------ADDGAAADIAELRALLKELLPDYMVPARYVPL 434
                        490
                 ....*....|....*.
gi 15597620 2674 ASLPLTANGKLDRRAL 2689
Cdd:cd17643  435 DALPLTVNGKLDRAAL 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
2200-2690 5.43e-144

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 457.10  E-value: 5.43e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd17652    1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLSHaalfealgelpagvarwcleedgpaldaedpaplaalsgPQHQAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd17652   81 ADARPALLLTT---------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGA-EEICELIRAEGVSILGFTPSYGSQLaqw 2438
Cdd:cd17652  122 AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgEPLADLLREHRITHVTLPPAALAAL--- 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 leSQGRQLPVRMCITGGEALTGEHLQRirqaFAPA-SFFNAYGPTETVVmplaCLAPERLEEGAASVPIGSVVGARVAYI 2517
Cdd:cd17652  199 --PPDDLPDLRTLVVAGEACPAELVDR----WAPGrRMINAYGPTETTV----CATMAGPLPGGGVPPIGRPVPGTRVYV 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2518 LDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGF 2597
Cdd:cd17652  269 LDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGF 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2598 RIELGEIEARLLEHPQVREALVLALDS-PSGKQLAGYVasaVAEQDEdaqAALREALKTHLKQQLPDYMVPAHLLLLASL 2676
Cdd:cd17652  349 RIELGEVEAALTEHPGVAEAVVVVRDDrPGDKRLVAYV---VPAPGA---APTAAELRAHLAERLPGYMVPAAFVVLDAL 422
                        490
                 ....*....|....
gi 15597620 2677 PLTANGKLDRRALP 2690
Cdd:cd17652  423 PLTPNGKLDRRALP 436
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1130-1622 1.45e-142

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 453.70  E-value: 1.45e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:cd12115    1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1210 PDYPSERLAYMLADSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVG 1289
Cdd:cd12115   81 PAYPPERLRFILEDAQARLVLTDP------------------------------------DDLAYVIYTSGSTGRPKGVA 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1290 NTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHrdparLVELVRQFGVTTLHFVP 1369
Cdd:cd12115  125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLA-----LPDLPAAAEVTLINTVP 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1370 PLLQLFIDEPGVAAcgSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPLGNV 1449
Cdd:cd12115  200 SAAAELLRHDALPA--SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANT 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1450 VCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSaAGERLYRTGDRARWNADGVLEYLGRLDQQVK 1529
Cdd:cd12115  278 QAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLEFLGRADNQVK 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1530 LRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGS-QLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQ 1608
Cdd:cd12115  357 VRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGAAGLVED---LRRHLGTRLPAYMVPSRFVRLDA 433
                        490
                 ....*....|....
gi 15597620 1609 MPLGPSGKLDTRAL 1622
Cdd:cd12115  434 LPLTPNGKIDRSAL 447
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
2192-2690 2.50e-142

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 454.88  E-value: 2.50e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2192 FAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2271
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2272 LERLQYMIEDSGVRLLLSHAALFEALgelpAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAV 2351
Cdd:cd17651   81 AERLAFMLADAGPVLVLTHPALAGEL----AVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2352 SHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL-RAQGQWGAEEICELIRAEGVSILGFTPS 2430
Cdd:cd17651  157 PHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLpPEEVRTDPPALAAWLDEQRISRVFLPTV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2431 YGSQLAQWLESQGRQLP-VRMCITGGEALTGEHlqRIRQAFAPASF---FNAYGPTETVVMPLACLAPERLEEGAAsVPI 2506
Cdd:cd17651  237 ALRALAEHGRPLGVRLAaLRYLLTGGEQLVLTE--DLREFCAGLPGlrlHNHYGPTETHVVTALSLPGDPAAWPAP-PPI 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2507 GSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVG 2586
Cdd:cd17651  314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLG 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2587 RIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVasaVAEQDEDAQAAlreALKTHLKQQLPDYM 2665
Cdd:cd17651  393 RADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYV---VGDPEAPVDAA---ELRAALATHLPEYM 466
                        490       500
                 ....*....|....*....|....*
gi 15597620 2666 VPAHLLLLASLPLTANGKLDRRALP 2690
Cdd:cd17651  467 VPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3716-4230 3.48e-142

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 454.04  E-value: 3.48e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3716 VRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:cd17646    1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3796 GHPTQRLTRIVELSRTLVLVCTqacREQALALFDElgcvdrPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTG 3875
Cdd:cd17646   81 GYPADRLAYMLADAGPAVVLTT---ADLAARLPAG------GDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3876 LPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGIT 3955
Cdd:cd17646  152 RPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3956 VLESVPSLIQGMLAE-ERQALDGLRWMLPTGEAMPPELARQWLKRyPRIGLVNAYGPAECSDDVAFFRVDlASTESTYLP 4034
Cdd:cd17646  232 TCHFVPSMLRVFLAEpAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVR-GPAETPSVP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4035 IGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGDLARRRADGV 4114
Cdd:cd17646  310 IGRPVPNTRLYVL----DDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGA 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4115 LEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQE-GANGKYLVGYLVPgetprssadSPAGLMVEQGAWFER 4193
Cdd:cd17646  385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAaPAGAARLVGYVVP---------AAGAAGPDTAALRAH 455
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15597620 4194 ikqqLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd17646  456 ----LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
2200-2689 3.93e-142

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 453.29  E-value: 3.93e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd12116    1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLSHAALFEALgelPAGVARWCLEEDGPALDAEDPAPLAAlsgPQHQAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd12116   81 EDAEPALVLTDDALPDRL---PAGLPVLLLALAAAAAAPAAPRTPVS---PDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL-RAQGQWGAEEICELIRAEGVSILGFTPSYGSQL--A 2436
Cdd:cd12116  155 LHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIaPRETQRDPEALARLIEAHSITVMQATPATWRMLldA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2437 QWlesQGRQlPVRMcITGGEALTGEHLQRIrqAFAPASFFNAYGPTETVVMPLAClapeRLEEGAASVPIGSVVGARVAY 2516
Cdd:cd12116  235 GW---QGRA-GLTA-LCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAA----RVTAAAGPIPIGRPLANTQVY 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2517 ILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRG 2596
Cdd:cd12116  304 VLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2597 FRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVasavaeQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASL 2676
Cdd:cd12116  384 HRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYV------VLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDAL 457
                        490
                 ....*....|...
gi 15597620 2677 PLTANGKLDRRAL 2689
Cdd:cd12116  458 PLTANGKLDRKAL 470
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3727-4230 4.85e-134

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 430.17  E-value: 4.85e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd12116    1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRTLVLVCTQACREQALalfdelGCVDRPRLLVWDeiqqGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd12116   81 EDAEPALVLTDDALPDRLP------AGLPVLLLALAA----AAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:cd12116  151 LVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRM 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAEERQALDGLRwMLPTGEAMPPELARQWLKRYPRigLVNAYGPAECSDDVAFFRVDLASTestYLPIGSPTDNNRLYL 4046
Cdd:cd12116  231 LLDAGWQGRAGLT-ALCGGEALPPDLAARLLSRVGS--LWNLYGPTETTIWSTAARVTAAAG---PIPIGRPLANTQVYV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4047 LgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVK 4126
Cdd:cd12116  305 L----DAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVK 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4127 IRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRSSADspaglmveqgawfeRIKQQLRADLPDYM 4206
Cdd:cd12116  381 IRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAA--------------ALRAHLRATLPAYM 446
                        490       500
                 ....*....|....*....|....
gi 15597620 4207 VPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd12116  447 VPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
2187-2690 6.94e-134

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 429.55  E-value: 6.94e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2187 TLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL 2266
Cdd:cd17644    1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2267 DPEYPLERLQYMIEDSGVRLLLSHaalfealgelpagvarwcleedgpaldaedpaplaalsgPQHQAYLIYTSGSTGKP 2346
Cdd:cd17644   81 DPNYPQERLTYILEDAQISVLLTQ---------------------------------------PENLAYVIYTSGSTGKP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2347 KGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLR-AQGQWGAEEICELIRAEGVSIL 2425
Cdd:cd17644  122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRpEEMRSSLEDFVQYIQQWQLTVL 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2426 GFTPSYGSQLAQWLESQGRQLP--VRMCITGGEALTGEHLQRIRQAFAP-ASFFNAYGPTETVVMPLACLAPERLEEGAA 2502
Cdd:cd17644  202 SLPPAYWHLLVLELLLSTIDLPssLRLVIVGGEAVQPELVRQWQKNVGNfIQLINVYGPTEATIAATVCRLTQLTERNIT 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2503 SVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFA-AEGGRLYRTGDLVRLCDNGQ 2581
Cdd:cd17644  282 SVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNsSESERLYKTGDLARYLPDGN 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2582 VEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVasaVAEQDEdaqAALREALKTHLKQQ 2660
Cdd:cd17644  362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGnKRLVAYI---VPHYEE---SPSTVELRQFLKAK 435
                        490       500       510
                 ....*....|....*....|....*....|
gi 15597620 2661 LPDYMVPAHLLLLASLPLTANGKLDRRALP 2690
Cdd:cd17644  436 LPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3727-4231 8.36e-134

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 428.33  E-value: 8.36e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd17649    1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRTLVLVCtqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd17649   81 EDSGAGLLLT------------------------------------------HHPRQLAYVIYTSGSTGTPKGVAVSHGP 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:cd17649  119 LAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQ 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAEERQALDG----LRWMLPTGEAMPPELARQWLKRYPRigLVNAYGPAECSDDVAFFRVDLASTES-TYLPIGSPTDN 4041
Cdd:cd17649  199 LAEEADRTGDGrppsLRLYIFGGEALSPELLRRWLKAPVR--LFNAYGPTEATVTPLVWKCEAGAARAgASMPIGRPLGG 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4042 NRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRI 4121
Cdd:cd17649  277 RSAYIL----DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRV 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4122 DHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRssadspaglmveQGAWFERIKQQLRAD 4201
Cdd:cd17649  353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAA------------QPELRAQLRTALRAS 420
                        490       500       510
                 ....*....|....*....|....*....|
gi 15597620 4202 LPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17649  421 LPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3719-4231 1.61e-132

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 426.37  E-value: 1.61e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3719 FEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHP 3798
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3799 TQRLTRIVELSRtLVLVCTQAcreqalALFDELGcVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPK 3878
Cdd:cd17651   81 AERLAFMLADAG-PVLVLTHP------ALAGELA-VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3879 GVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLE 3958
Cdd:cd17651  153 GVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVF 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3959 SVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPP-ELARQWLKRYPRIGLVNAYGPAECSDDVAF-FRVDLASTESTyL 4033
Cdd:cd17651  233 LPTVALRALAEHGRPLgvrLAALRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTETHVVTALsLPGDPAAWPAP-P 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4034 PIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGDLARRRADG 4113
Cdd:cd17651  312 PIGRPIDNTRVYVL----DAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDG 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4114 VLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQE-GANGKYLVGYLVPGETPRSSAdspaglmveqgawfE 4192
Cdd:cd17651  387 ELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVAYVVGDPEAPVDA--------------A 452
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 15597620 4193 RIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17651  453 ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1728-2155 5.32e-132

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 422.60  E-value: 5.32e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1728 PVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDW 1807
Cdd:cd19540    1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDfsaldRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDD 1887
Cdd:cd19540   81 TV-----VDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1888 RESPLEPLPVQYLDYSVWQREWLESGERQ-----RQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAE 1962
Cdd:cd19540  156 RAPDWAPLPVQYADYALWQRELLGDEDDPdslaaRQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1963 RVRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQ 2042
Cdd:cd19540  236 RLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2043 TVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQTRQLAGMTVEYIANDARATKFDLNLEVTDL----- 2117
Cdd:cd19540  316 TDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTA-AATLELPGLTVEPVPVDTGVAKFDLSFTLTERrdadg 394
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 15597620 2118 -DQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19540  395 aPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1132-1623 4.49e-131

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 421.46  E-value: 4.49e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:cd17644    4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1212 YPSERLAYMLADSGVELLLTQAHlferlpgaegvtpicldslkldnwpsqapglhlhgdNLAYVIYTSGSTGQPKGVGNT 1291
Cdd:cd17644   84 YPQERLTYILEDAQISVLLTQPE------------------------------------NLAYVIYTSGSTGKPKGVMIE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1292 HAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAaPGEHR-DPARLVELVRQFGVTTLHFVPP 1370
Cdd:cd17644  128 HQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLR-PEEMRsSLEDFVQYIQQWQLTVLSLPPA 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 LLQLFIDEPGVAAC---GSLRRLFSGGEA-LPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERS---PIG 1443
Cdd:cd17644  207 YWHLLVLELLLSTIdlpSSLRLVIVGGEAvQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNItsvPIG 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1444 RPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPF-SAAGERLYRTGDRARWNADGVLEYLG 1522
Cdd:cd17644  287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEYLG 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1523 RLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGS-QLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPT 1601
Cdd:cd17644  367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNkRLVAYIVPHYEESPSTVE---LRQFLKAKLPDYMIPS 443
                        490       500
                 ....*....|....*....|..
gi 15597620 1602 QLMRLAQMPLGPSGKLDTRALP 1623
Cdd:cd17644  444 AFVVLEELPLTPNGKIDRRALP 465
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3727-4230 8.15e-131

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 419.79  E-value: 8.15e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd17643    1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRtlvlvctqacreqalalfdelgcvdrPRLLVWDeiqqgegaehdpqvysgPQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd17643   81 ADSG--------------------------PSLLLTD-----------------PDDLAYVIYTSGSTGRPKGVVVSHAN 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:cd17643  118 VLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQ 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAEERQ---ALDGLRWMLPTGEAMPPELARQWLKRYPRIG--LVNAYGPAECSDDVAFFRVDLASTE-STYLPIGSPTD 4040
Cdd:cd17643  198 LVEAADRdgrDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpqLVNMYGITETTVHVTFRPLDAADLPaAAASPIGRPLP 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4041 NNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGR 4120
Cdd:cd17643  278 GLRVYVL----DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGR 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4121 IDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPGEtprSSADSPAGLmveqgawferiKQQLR 4199
Cdd:cd17643  354 ADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGdTRLVAYVVADD---GAAADIAEL-----------RALLK 419
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15597620 4200 ADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd17643  420 ELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3727-4231 6.78e-130

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 416.65  E-value: 6.78e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd17652    1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRtLVLVCTQacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvysgPQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd17652   81 ADAR-PALLLTT------------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRG 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:cd17652  118 LANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAEerqALDGLRWMLPTGEAMPPELARQWLkryPRIGLVNAYGPAECSddVAFFRVDLASTESTyLPIGSPTDNNRLYL 4046
Cdd:cd17652  198 LPPD---DLPDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETT--VCATMAGPLPGGGV-PPIGRPVPGTRVYV 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4047 LgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVK 4126
Cdd:cd17652  269 L----DARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVK 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4127 IRGFRIELGEIEARLHERADVREAAVAVQE-GANGKYLVGYLVPGETPRSSAdspaglmveqgawfERIKQQLRADLPDY 4205
Cdd:cd17652  345 IRGFRIELGEVEAALTEHPGVAEAVVVVRDdRPGDKRLVAYVVPAPGAAPTA--------------AELRAHLAERLPGY 410
                        490       500
                 ....*....|....*....|....*.
gi 15597620 4206 MVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17652  411 MVPAAFVVLDALPLTPNGKLDRRALP 436
PRK05850 PRK05850
acyl-CoA synthetase; Validated
10-553 2.69e-127

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 415.11  E-value: 2.69e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFLA-EDDGEGVV--LSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLY 86
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFIDyEQDPAGVAetLTWSQLYRRTLNVAEELRRHGSTGDRAVILAPQGLEYIVAFLGALQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    87 AGVIAVPAYPPesARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRP 166
Cdd:PRK05850   82 AGLIAVPLSVP--QGGAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   167 EHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGF----GIGA--DDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM 240
Cdd:PRK05850  160 PSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtGGVPppDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   241 SPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDA 320
Cdd:PRK05850  240 SPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDMAGLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   321 SSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALAR---NRIAEGEGSVLMCCGRSQPEhAVLIVDAASGEVLGDDNVG 397
Cdd:PRK05850  320 TAIRPSYGLAEATVYVATREPGQPPESVRFDYEKLSAghaKRCETGGGTPLVSYGSPRSP-TVRIVDPDTCIECPAGTVG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   398 EIWAAGPSIAHGYWRNPEASAKAFVER---------DGrTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERT 468
Cdd:PRK05850  399 EIWVHGDNVAAGYWQKPEETERTFGATlvdpspgtpEG-PWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEAT 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   469 VEsEVPSarkGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKV----VALLNPGALPKTS 544
Cdd:PRK05850  478 IQ-EITG---GRVAAISVPDDGTEKLVAIIELKKRGDSDEEAMDRLRTVKREVTSAISKSHGLsvadLVLVAPGSIPITT 553

                  ....*....
gi 15597620   545 SGKLQRSAC 553
Cdd:PRK05850  554 SGKIRRAAC 562
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
9-583 1.03e-125

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 412.59  E-value: 1.03e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFL---AEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCL 85
Cdd:PRK07769   21 TNLVRHVERWAKVRGDKLAYRFLdfsTERDGVARDLTWSQFGARNRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGAL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAVPAYPPESArrHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVR 165
Cdd:PRK07769  101 YAGRIAVPLFDPAEP--GHVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERPRVIAVDAVPDEVGATWVPPEAN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFsGVPCVLMSPRYF 245
Cdd:PRK07769  179 EDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALL-GHYITFMSPAAF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   246 LERPVRWLEAISQY----GGTVSGGPDFAYRLCSER-VAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDA 320
Cdd:PRK07769  258 VRRPGRWIRELARKpggtGGTFSAAPNFAFEHAAARgLPKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPP 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   321 SSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRI----AEGEGSVL-MCCGR-SQPEHAVlIVDAASGEVLGDD 394
Cdd:PRK07769  338 TAIKPSYGMAEATLFVSTTPMDEEPTVIYVDRDELNAGRFvevpADAPNAVAqVSAGKvGVSEWAV-IVDPETASELPDG 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   395 NVGEIWAAGPSIAHGYWRNPEASAKAFVER--------------DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNL 460
Cdd:PRK07769  417 QIGEIWLHGNNIGTGYWGKPEETAATFQNIlksrlseshaegapDDALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNH 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   461 YPQDIERTVESEVPSARKGRVAAFAVTV--------------------DGEEGIGIAAEIGRGVQKSVPaQELIDSIRQA 520
Cdd:PRK07769  497 YPQDLEYTAQEATKALRTGYVAAFSVPAnqlpqvvfddshaglkfdpeDTSEQLVIVAERAPGAHKLDP-QPIADDIRAA 575
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   521 VAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGSLDSyalfpglQAVQEAQPPAGD 583
Cdd:PRK07769  576 IAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRS-------GYGQPAFPDASD 631
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
9-562 2.33e-125

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 411.04  E-value: 2.33e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFL---AEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCL 85
Cdd:NF038339   18 ATLVDHVERNARERADTLAYRFIdysRERDGEARDLTWAQFGARLRAVAARLQQVTKPGDRVAILAPQGLDYVVSFFAAI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAVPAYPPESArrHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVR 165
Cdd:NF038339   98 YAGNIAVPLFDPDEP--GHTDRLHAVLGDCKPSAILTATSSAEGVRKFFRSLPAKERPRVIAVDAVPDSVGSTWVRPDAD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFsGVPCVLMSPRYF 245
Cdd:NF038339  176 LDDIAYLQYTSGSTRVPAGVEITHRAVATNVLQMVDAIELDENSRGVTWLPLFHDMGLLTVILPALG-GKYITIMSPAAF 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   246 LERPVRW---LEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASS 322
Cdd:NF038339  255 VRRPGRWireLAAVSDGAGTFAAAPNFAFEHAAARGLPKEGEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   323 FFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRI----AEGEGSVL-MCCGRSQPEHAVLIVDAASGEVLGDDNVG 397
Cdd:NF038339  335 IKPSYGMAEATLFVSSTPREDEAKVIYVDREELNAGRIvevdPDAPNAVAqVSCGYVARSQWAVIVDPETGTELPDGQVG 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   398 EIWAAGPSIAHGYWRNPEASAKAF----VER-----------DGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYP 462
Cdd:NF038339  415 EIWLHGNNIGTGYWGRPEETEETFhnklKSRleegshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYP 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   463 QDIERTVESEVPSARKGRVAAFAVTV--------------------DGEEGIGIAAEIGRGVQKSVPaQELIDSIRQAVA 522
Cdd:NF038339  495 QDLEYSAQEASKALRPGFVAAFSVPAnqlpaevfenshsglkydadDSSEQLVIVAERAPGAGKADP-QPIADAVRAAIA 573
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 15597620   523 EAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGSL 562
Cdd:NF038339  574 VRHGVTVRDVLLVPAGSIPRTSSGKIARRACKAAYIDGTL 613
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
1143-1622 1.71e-124

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 401.46  E-value: 1.71e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd17650    2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1302
Cdd:cd17650   82 DSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1303 QATYTLDGDDV-LMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPL---LQLFIDE 1378
Cdd:cd17650  126 RREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALirpVMAYVYR 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1379 PGVAAcGSLRRLFSGGEALPAE----LRNRVLQRLPAValhNRYGPTETAINVTHWQ---CRAEDGERSPIGRPLGNVVC 1451
Cdd:cd17650  206 NGLDL-SAMRLLIVGSDGCKAQdfktLAARFGQGMRII---NSYGVTEATIDSTYYEegrDPLGDSANVPIGRPLPNTAM 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1452 RVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLR 1531
Cdd:cd17650  282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1532 GFRIEPEEIQARLLAQPGVAQAVVVIREGVAG-SQLVGYytgaVGAEAEAEQNQrLRAALQAELPEYMVPTQLMRLAQMP 1610
Cdd:cd17650  361 GFRIELGEIESQLARHPAIDEAVVAVREDKGGeARLCAY----VVAAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALP 435
                        490
                 ....*....|..
gi 15597620 1611 LGPSGKLDTRAL 1622
Cdd:cd17650  436 LTPNGKVDRRAL 447
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
2188-2689 1.91e-124

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 401.31  E-value: 1.91e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2188 LHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2267
Cdd:cd12115    1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2268 PEYPLERLQYMIEDSGVRLLLShaalfealgelpagvarwcleedgpaldaedpaplaalsGPQHQAYLIYTSGSTGKPK 2347
Cdd:cd12115   81 PAYPPERLRFILEDAQARLVLT---------------------------------------DPDDLAYVIYTSGSTGRPK 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2348 GVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLraqgqwgAEEICELI---RAEGVSI 2424
Cdd:cd12115  122 GVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVL-------ADNVLALPdlpAAAEVTL 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2425 LGFTPSYGSQLaqwLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPErleEGAASV 2504
Cdd:cd12115  195 INTVPSAAAEL---LRHDALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPP---GASGEV 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2505 PIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEY 2584
Cdd:cd12115  269 SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGP-GARLYRTGDLVRWRPDGLLEF 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2585 VGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVASavaeqdEDAQAALREALKTHLKQQLPD 2663
Cdd:cd12115  348 LGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIgDAAGERRLVAYIVA------EPGAAGLVEDLRRHLGTRLPA 421
                        490       500
                 ....*....|....*....|....*.
gi 15597620 2664 YMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd12115  422 YMVPSRFVRLDALPLTPNGKIDRSAL 447
PRK09192 PRK09192
fatty acyl-AMP ligase;
40-567 2.47e-124

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 406.31  E-value: 2.47e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    40 VLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPES--ARRHHQERLLSIIADAE 116
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALgLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfgGRESYIAQLRGMLASAQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   117 PRLVLTTADLREPLlqmNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANE 196
Cdd:PRK09192  129 PAAIITPDELLPWV---NEATHGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   197 VLI-RRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCS 275
Cdd:PRK09192  206 RAIsHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCA 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   276 ERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEAL 355
Cdd:PRK09192  286 RRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEVDRDRL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   356 ARNRIAEGEG------SVLMCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVerDGrtW 429
Cdd:PRK09192  366 EYQGKAVAPGaetrrvRTFVNCGKALPGHEIEIRNEA-GMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAA--DG--W 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   430 LRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEvPSARKGRVAAFAVTVDGEEgiGIAAEIGRGVQKSVP 509
Cdd:PRK09192  441 LDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQE-PELRSGDAAAFSIAQENGE--KIVLLVQCRISDEER 517
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620   510 AQELIDSIRQAVAEAYQeAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGSLDSYAL 567
Cdd:PRK09192  518 RGQLIHALAALVRSEFG-VEAAVELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
1143-1622 4.89e-121

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 392.79  E-value: 4.89e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd12114    2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQAHLFERLPGAEgvTPICLDSLKLDNWPSQAPGLHLHGDnLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1302
Cdd:cd12114   82 DAGARLVLTDGPDAQLDVAVF--DVLILDLDALAAPAPPPPVDVAPDD-LAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1303 QATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVA 1382
Cdd:cd12114  159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1383 --ACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPI--GRPLGNVVCRVLDAEF 1458
Cdd:cd12114  239 qaLLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLDPRG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1459 NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPfsaAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPE 1538
Cdd:cd12114  319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELG 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1539 EIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAAlqAELPEYMVPTQLMRLAQMPLGPSGKLD 1618
Cdd:cd12114  396 EIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLA--QTLPAYMIPSRVIALEALPLTANGKVD 473

                 ....
gi 15597620 1619 TRAL 1622
Cdd:cd12114  474 RAAL 477
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3718-4231 1.73e-120

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 390.64  E-value: 1.73e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:cd17644    5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3798 PTQRLTRIVELSRTLVLVcTQacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvysgPQNLAYVIYTSGSTGLP 3877
Cdd:cd17644   85 PQERLTYILEDAQISVLL-TQ------------------------------------------PENLAYVIYTSGSTGKP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3878 KGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVL 3957
Cdd:cd17644  122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVL 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3958 ESVPSLIQGMLAEERQAL----DGLRWMLPTGEAMPPELARQWLK-RYPRIGLVNAYGPAECSDDVAFFRV-DLASTEST 4031
Cdd:cd17644  202 SLPPAYWHLLVLELLLSTidlpSSLRLVIVGGEAVQPELVRQWQKnVGNFIQLINVYGPTEATIAATVCRLtQLTERNIT 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4032 YLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPF-GAPGERLYRTGDLARRR 4110
Cdd:cd17644  282 SVPIGRPIANTQVYIL----DENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYL 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4111 ADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPgetprssaDSPAGLMVEQga 4189
Cdd:cd17644  358 PDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGnKRLVAYIVP--------HYEESPSTVE-- 427
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 15597620 4190 wferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17644  428 ----LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
6-564 6.97e-120

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 394.88  E-value: 6.97e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     6 ELP--TTLVQALRRRAVQEPERLALRFL---AEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAA 80
Cdd:PRK12476   29 ALPpgTTLISLIERNIANVGDTVAYRYLdhsHSAAGCAVELTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGIDYVAG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGVIAVPAYPPESArrHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWD 160
Cdd:PRK12476  109 FFAAIKAGTIAVPLFAPELP--GHAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRPRVIAIDAIPDSAGESFV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   161 EPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANevLIRRGFGIGADDV---IVSWLPLYHDMGLIGgLLQPIFSGVPC 237
Cdd:PRK12476  187 PVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTN--LVQMILSIDLLDRnthGVSWLPLYHDMGLSM-IGFPAVYGGHS 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   238 VLMSPRYFLERPVRWLEAIS---QYGGTVSGGPDFAYRLCSERVAESALQRLDLSGwRVAFSGSEPIRQDSLERFAEKFA 314
Cdd:PRK12476  264 TLMSPTAFVRRPQRWIKALSegsRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDLSN-VVLIIGSEPVSIDAVTTFNKAFA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   315 ASRFDASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNR---IAEG--EGSVLMCCG---RSQpeHAVlIVDAA 386
Cdd:PRK12476  343 PYGLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRavrVAADapNAVAHVSCGqvaRSQ--WAV-IVDPD 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   387 SGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVER---------------DGRTWLRTGDLGFLRDGELFVTGRLKD 451
Cdd:PRK12476  420 TGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKlqsrlaegshadgaaDDGTWLRTGDLGVYLDGELYITGRIAD 499
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   452 MLIVRGHNLYPQDIERTVESEVPSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPaQELIDSIRQAVAEAYQEAPKV 531
Cdd:PRK12476  500 LIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADP-APAIDAIRAAVSRRHGLAVAD 578
                         570       580       590
                  ....*....|....*....|....*....|...
gi 15597620   532 VALLNPGALPKTSSGKLQRSACRLRLEDGSLDS 564
Cdd:PRK12476  579 VRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1130-1622 3.49e-119

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 387.67  E-value: 3.49e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVALE-WDGgSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPL 1208
Cdd:cd05918    1 VHDLIEERARSQPDAPAVCaWDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1209 DPDYPSERLAYMLADSGVELLLTqahlferlpgaegvtpicldslkldnwpSQApglhlhgDNLAYVIYTSGSTGQPKGV 1288
Cdd:cd05918   80 DPSHPLQRLQEILQDTGAKVVLT----------------------------SSP-------SDAAYVIFTSGSTGKPKGV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1289 GNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTG-CrlvLAAPGEHRDPARLVELVRQFGVTTLHF 1367
Cdd:cd05918  125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGgC---LCIPSEEDRLNDLAGFINRLRVTWAFL 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1368 VPPLLQLFidEPgvAACGSLRRLFSGGEALPAELRNRVLQRlpaVALHNRYGPTETAINVTHWQCRAeDGERSPIGRPLG 1447
Cdd:cd05918  202 TPSVARLL--DP--EDVPSLRTLVLGGEALTQSDVDTWADR---VRLINAYGPAECTIAATVSPVVP-STDPRNIGRPLG 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1448 nVVCRVLDAEFN--LLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPF------SAAGERLYRTGDRARWNADGVLE 1519
Cdd:cd05918  274 -ATCWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLE 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1520 YLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV----IREGVAGSQLV--------------GYYTGAVGAEAEAE 1581
Cdd:cd05918  353 YVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVevvkPKDGSSSPQLVafvvldgsssgsgdGDSLFLEPSDEFRA 432
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15597620 1582 QNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05918  433 LVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
1143-1623 1.48e-118

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 385.67  E-value: 1.48e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd17656    3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLTQAHLFERLPGAEGVTPICLDSLkldnwpSQAPGLHL----HGDNLAYVIYTSGSTGQPKGVGNTHAALAER 1298
Cdd:cd17656   83 DSGVRVVLTQRHLKSKLSFNKSTILLEDPSI------SQEDTSNIdyinNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1299 LQWmQATYTLD--GDDVLmQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFI 1376
Cdd:cd17656  157 LHF-EREKTNInfSDKVL-QFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1377 DE----PGVAACgsLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAInVTHWQCRAED--GERSPIGRPLGNVV 1450
Cdd:cd17656  235 SErefiNRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAeiPELPPIGKPISNTW 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1451 CRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSaAGERLYRTGDRARWNADGVLEYLGRLDQQVKL 1530
Cdd:cd17656  312 IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD-PNERMYRTGDLARYLPDGNIEFLGRADHQVKI 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1531 RGFRIEPEEIQARLLAQPGVAQAVVVIREGVAG-SQLVGYYTgavgaeAEAEQN-QRLRAALQAELPEYMVPTQLMRLAQ 1608
Cdd:cd17656  391 RGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGeKYLCAYFV------MEQELNiSQLREYLAKQLPEYMIPSFFVPLDQ 464
                        490
                 ....*....|....*
gi 15597620 1609 MPLGPSGKLDTRALP 1623
Cdd:cd17656  465 LPLTPNGKVDRKALP 479
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1132-1623 2.30e-118

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 383.83  E-value: 2.30e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:cd17645    2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1212 YPSERLAYMLADSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNT 1291
Cdd:cd17645   82 YPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMIE 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1292 HAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPL 1371
Cdd:cd17645  126 HHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGA 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1372 LQLFIDEPGVaacgSLRRLFSGGEALPAELRNrvlqrlpAVALHNRYGPTETAINVTHWQCRAEDGErSPIGRPLGNVVC 1451
Cdd:cd17645  206 AEQFMQLDNQ----SLRVLLTGGDKLKKIERK-------GYKLVNNYGPTENTVVATSFEIDKPYAN-IPIGKPIDNTRV 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1452 RVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLR 1531
Cdd:cd17645  274 YILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1532 GFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQ-LVGYYTGAVGAEAEAeqnqrLRAALQAELPEYMVPTQLMRLAQMP 1610
Cdd:cd17645  353 GYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYVTAPEEIPHEE-----LREWLKNDLPDYMIPTYFVHLKALP 427
                        490
                 ....*....|...
gi 15597620 1611 LGPSGKLDTRALP 1623
Cdd:cd17645  428 LTANGKVDRKALP 440
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
2188-2689 3.04e-116

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 379.19  E-value: 3.04e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2188 LHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2267
Cdd:cd05918    1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2268 PEYPLERLQYMIEDSGVRLLLShaalfealgelpagvarwcleedgpaldaedpaplaalSGPQHQAYLIYTSGSTGKPK 2347
Cdd:cd05918   81 PSHPLQRLQEILQDTGAKVVLT--------------------------------------SSPSDAAYVIFTSGSTGKPK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2348 GVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLraqgqwGAEEIC-----ELIRAEGV 2422
Cdd:cd05918  123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI------PSEEDRlndlaGFINRLRV 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2423 SILGFTPSYGSQLaqwlesQGRQLP-VRMCITGGEALTgehlQRIRQAFAP-ASFFNAYGPTETVVMplaCLAPERLEEG 2500
Cdd:cd05918  197 TWAFLTPSVARLL------DPEDVPsLRTLVLGGEALT----QSDVDTWADrVRLINAYGPAECTIA---ATVSPVVPST 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2501 AASVpIGSVVGARvAYILDAD--LALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPF------AAEGGRLYRTGD 2572
Cdd:cd05918  264 DPRN-IGRPLGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGD 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2573 LVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEH-PQVREALVLAL---DSPSGKQLAGYVASA----------- 2637
Cdd:cd05918  342 LVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkDGSSSPQLVAFVVLDgsssgsgdgds 421
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2638 -VAEQDEDAQAALREaLKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05918  422 lFLEPSDEFRALVAE-LRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1729-2155 1.94e-115

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 375.06  E-value: 1.94e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1729 VPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQ 1808
Cdd:cd19538    2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1809 DfsaldRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDR 1888
Cdd:cd19538   82 I-----KEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1889 ESPLEPLPVQYLDYSVWQREWLESGERQ-----RQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAER 1963
Cdd:cd19538  157 APELAPLPVQYADYALWQQELLGDESDPdsliaRQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQ 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1964 VRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQT 2043
Cdd:cd19538  237 LLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKET 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2044 VIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMcnvqrWEFQQTRQ----LAGMTVEYIANDARATKFDLNLEVTDL-- 2117
Cdd:cd19538  317 NLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIM-----LALQNTPQpsldLPGLEAKLELRTVGSAKFDLTFELREQyn 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 15597620 2118 ---DQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19538  392 dgtPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3718-4230 4.00e-115

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 374.73  E-value: 4.00e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:cd12115    4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3798 PTQRLTRIVELSRTLVLVCTqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvysgPQNLAYVIYTSGSTGLP 3877
Cdd:cd12115   84 PPERLRFILEDAQARLVLTD-------------------------------------------PDDLAYVIYTSGSTGRP 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3878 KGVMVEQAGMLNN-QLSKVPYLELDENDVIAQTaSQSFDISVWQFLAAPLFGARVAIVPNAVAhdpqgLLAHVGEQGITV 3956
Cdd:cd12115  121 KGVAIEHRNAAAFlQWAAAAFSAEELAGVLAST-SICFDLSVFELFGPLATGGKVVLADNVLA-----LPDLPAAAEVTL 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIQGMLaeERQAL-DGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAEcsddvaffrvdlASTESTYLP- 4034
Cdd:cd12115  195 INTVPSAAAELL--RHDALpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE------------DTTYSTVAPv 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4035 ---------IGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGD 4105
Cdd:cd12115  261 ppgasgevsIGRPLANTQAYVL----DRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGD 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4106 LARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQE-GANGKYLVGYLVPgetprssaDSPAGLm 4184
Cdd:cd12115  336 LVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAAGERRLVAYIVA--------EPGAAG- 406
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620 4185 veqgaWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd12115  407 -----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3723-4230 1.10e-114

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 373.51  E-value: 1.10e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3723 VAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRL 3802
Cdd:cd05945    1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3803 TRIVELSRTLVLVCtqacreqalalfdelgcvdrprllvwdeiqqgegAEHDpqvysgpqnLAYVIYTSGSTGLPKGVMV 3882
Cdd:cd05945   81 REILDAAKPALLIA----------------------------------DGDD---------NAYIIFTSGSTGRPKGVQI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3883 EQAGMLN--NQLskVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESV 3960
Cdd:cd05945  118 SHDNLVSftNWM--LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVST 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3961 PSLIQGMLAEE---RQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVD-LASTESTYLPIG 4036
Cdd:cd05945  196 PSFAAMCLLSPtftPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTpEVLDGYDRLPIG 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4037 SPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPfgapGERLYRTGDLARRRADGVLE 4116
Cdd:cd05945  276 YAKPGAKLVIL----DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLF 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4117 YVGRIDHQVKIRGFRIELGEIEARLHERADVREA-AVAVQEGANGKYLVGYLVPGETprssadSPAGLMVEqgawferIK 4195
Cdd:cd05945  348 YRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAvVVPKYKGEKVTELIAFVVPKPG------AEAGLTKA-------IK 414
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620 4196 QQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05945  415 AELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
1143-1623 1.91e-114

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 372.89  E-value: 1.91e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVG-PDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML 1221
Cdd:cd17648    2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1222 ADSGVELLLTQAhlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKG-------VGNTHAA 1294
Cdd:cd17648   82 EDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGvlvehgsVVNLRTS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1295 LAERlqwmqatYTLD--GDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLL 1372
Cdd:cd17648  126 LSER-------YFGRdnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1373 QLFidepGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALhNRYGPTETAINVTHWQCRAEDGERSPIGRPLGNVVCR 1452
Cdd:cd17648  199 QQY----DLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLII-NAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCY 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1453 VLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGE-------RLYRTGDRARWNADGVLEYLGRLD 1525
Cdd:cd17648  274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQErargrnaRLYKTGDLVRWLPSGELEYLGRND 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1526 QQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQ------LVGYYTGAVGAEAEAEqnqrLRAALQAELPEYMV 1599
Cdd:cd17648  354 FQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLPEPGHVPESD----LLSFLRAKLPRYMV 429
                        490       500
                 ....*....|....*....|....
gi 15597620 1600 PTQLMRLAQMPLGPSGKLDTRALP 1623
Cdd:cd17648  430 PARLVRLEGIPVTINGKLDVRALP 453
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
675-1097 4.33e-114

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 370.99  E-value: 4.33e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  675 LPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRI--DERGEFAWQ 752
Cdd:cd19540    2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  753 FVDLaalaeheRAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACG 832
Cdd:cd19540   82 VVDV-------TEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  833 GQPADLAPLELHYAEFAAWQRQWLD-----AGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALA 907
Cdd:cd19540  155 GRAPDWAPLPVQYADYALWQRELLGdeddpDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  908 RAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAR 987
Cdd:cd19540  235 ARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  988 EATLGAQANQDLPFDQVLAACG----QGGQ-LFQVLFNHQQRDLSALrRLPGLLADELPWHSREAKFDLQLQ-----SEE 1057
Cdd:cd19540  315 ETDLAAFAHQDVPFERLVEALNpprsTARHpLFQVMLAFQNTAAATL-ELPGLTVEPVPVDTGVAKFDLSFTlterrDAD 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 15597620 1058 DARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19540  394 GAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1132-1622 4.84e-114

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 370.87  E-value: 4.84e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:cd17653    1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1212 YPSERLAYMLADSGVELLltqahlferlpgaegvtpICLDSlkldnwpsqapglhlhGDNLAYVIYTSGSTGQPKGVGNT 1291
Cdd:cd17653   81 LPSARIQAILRTSGATLL------------------LTTDS----------------PDDLAYIIFTSGSTGIPKGVMVP 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1292 HAALAERLQWMQAT-YTLDGDDVLmQKAPVSFDVSVWECFWPLVTGCRLVLAAPgehrdPARLVELVRQfgVTTLHFVPP 1370
Cdd:cd17653  127 HRGVLNYVSQPPARlDVGPGSRVA-QVLSIAFDACIGEIFSTLCNGGTLVLADP-----SDPFAHVART--VDALMSTPS 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 LLQLFIDEPgvaaCGSLRRLFSGGEALPAELRNRvlqRLPAVALHNRYGPTETAINVTHwqCRAEDGERSPIGRPLGNVV 1450
Cdd:cd17653  199 ILSTLSPQD----FPNLKTIFLGGEAVPPSLLDR---WSPGRRLYNAYGPTECTISSTM--TELLPGQPVTIGKPIPNST 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1451 CRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAaGERLYRTGDRARWNADGVLEYLGRLDQQVKL 1530
Cdd:cd17653  270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWP-GSRMYRTGDYGRWTEDGGLEFLGREDNQVKV 348
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1531 RGFRIEPEEIQARLLA-QPGVAQAVVVIREGvagsQLVGYYTGAVGAEAeaeqnqRLRAALQAELPEYMVPTQLMRLAQM 1609
Cdd:cd17653  349 RGFRINLEEIEEVVLQsQPEVTQAAAIVVNG----RLVAFVTPETVDVD------GLRSELAKHLPSYAVPDRIIALDSF 418
                        490
                 ....*....|...
gi 15597620 1610 PLGPSGKLDTRAL 1622
Cdd:cd17653  419 PLTANGKVDRKAL 431
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1138-1622 9.84e-114

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 370.81  E-value: 9.84e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1138 LAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERL 1217
Cdd:cd05945    1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1218 AYMLADSGVELLLTQahlferlpgaegvtpicldslkldnwpsqapglhlhGDNLAYVIYTSGSTGQPKGVGNTHAALAE 1297
Cdd:cd05945   81 REILDAAKPALLIAD------------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1298 RLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFID 1377
Cdd:cd05945  125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1378 EPG--VAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERS---PIGRPLGNVVCR 1452
Cdd:cd05945  205 SPTftPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYdrlPIGYAKPGAKLV 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1453 VLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPfsaaGERLYRTGDRARWNADGVLEYLGRLDQQVKLRG 1532
Cdd:cd05945  285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNG 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1533 FRIEPEEIQARLLAQPGVAQAVVVIR-EGVAGSQLVGYYTGavGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPL 1611
Cdd:cd05945  361 YRIELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFVVP--KPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPL 438
                        490
                 ....*....|.
gi 15597620 1612 GPSGKLDTRAL 1622
Cdd:cd05945  439 NANGKIDRKAL 449
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3727-4230 1.24e-113

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 370.26  E-value: 1.24e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd17650    1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRTLVLVcTQacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvysgPQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd17650   81 EDSGAKLLL-TQ------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRN 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIA-QTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQ 3965
Cdd:cd17650  118 VAHAAHAWRREYELDSFPVRLlQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIR 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3966 GM---LAEERQALDGLRwMLPTGEAMPPELARQWLkrYPRIG----LVNAYGPAECSDDVAFFRVDLAST-ESTYLPIGS 4037
Cdd:cd17650  198 PVmayVYRNGLDLSAMR-LLIVGSDGCKAQDFKTL--AARFGqgmrIINSYGVTEATIDSTYYEEGRDPLgDSANVPIGR 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4038 PTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgAPGERLYRTGDLARRRADGVLEY 4117
Cdd:cd17650  275 PLPNTAMYVL----DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVEL 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4118 VGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPGETPRSSAdspaglmveqgawferIKQ 4196
Cdd:cd17650  350 LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGeARLCAYVVAAATLNTAE----------------LRA 413
                        490       500       510
                 ....*....|....*....|....*....|....
gi 15597620 4197 QLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd17650  414 FLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3718-4230 1.40e-113

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 371.49  E-value: 1.40e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:cd05918    4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3798 PTQRLTRIVELSRTLVLVCtqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLP 3877
Cdd:cd05918   84 PLQRLQEILQDTGAKVVLT------------------------------------------SSPSDAAYVIFTSGSTGKP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3878 KGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNavaHDPQGLLAHVGEQ-GITV 3956
Cdd:cd05918  122 KGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSE---EDRLNDLAGFINRlRVTW 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIqGMLaeERQALDGLRWMLPTGEAMPPELARQWLkryPRIGLVNAYGPAECSDDVAFFRVDLASTESTylpIG 4036
Cdd:cd05918  199 AFLTPSVA-RLL--DPEDVPSLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAECTIAATVSPVVPSTDPRN---IG 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4037 SPTdNNRLYLLGAGADDafELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPF------GAPGERLYRTGDLARRR 4110
Cdd:cd05918  270 RPL-GATCWVVDPDNHD--RLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYN 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4111 ADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAV----QEGANGKYLVGYLVPGETPRSSADSPAGLMVE 4186
Cdd:cd05918  347 PDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEP 426
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 4187 QGAWFE---RIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05918  427 SDEFRAlvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
2189-2690 5.17e-113

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 368.42  E-value: 5.17e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2189 HGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2268
Cdd:cd17645    1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2269 EYPLERLQYMIEDSGVRLLLShaalfealgelpagvarwcleedgpalDAEDpaplaalsgpqhQAYLIYTSGSTGKPKG 2348
Cdd:cd17645   81 DYPGERIAYMLADSSAKILLT---------------------------NPDD------------LAYVIYTSGSTGLPKG 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2349 VAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARV-VLRAQGQWGAEEICELIRAEGVSIlGF 2427
Cdd:cd17645  122 VMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALhVVPSERRLDLDALNDYFNQEGITI-SF 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2428 TPSYGSQLAQWLESQGrqlpVRMCITGGEALtgehlQRIRQAfaPASFFNAYGPTETVVMplACLAPERLEEGaaSVPIG 2507
Cdd:cd17645  201 LPTGAAEQFMQLDNQS----LRVLLTGGDKL-----KKIERK--GYKLVNNYGPTENTVV--ATSFEIDKPYA--NIPIG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2508 SVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVGR 2587
Cdd:cd17645  266 KPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVP-GERMYRTGDLAKFLPDGNIEFLGR 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2588 IDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVasaVAEQDEDAqaalrEALKTHLKQQLPDYMV 2666
Cdd:cd17645  345 LDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGrKYLVAYV---TAPEEIPH-----EELREWLKNDLPDYMI 416
                        490       500
                 ....*....|....*....|....
gi 15597620 2667 PAHLLLLASLPLTANGKLDRRALP 2690
Cdd:cd17645  417 PTYFVHLKALPLTANGKVDRKALP 440
AMP-binding pfam00501
AMP-binding enzyme;
1134-1531 8.20e-113

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 366.64  E-value: 8.20e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1134 LERQLAQSAERVALEWDGG-SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1213 PSERLAYMLADSGVELLLTQAHL-FERLPGAEG-----VTPICLDSL-----------KLDNWPSQAPGLHLHGDNLAYV 1275
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkLEELLEALGklevvKLVLVLDRDpvlkeeplpeeAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1276 IYTSGSTGQPKGVGNTHAALAERLQWMQATYT----LDGDDVLMQKAPVSFDVSV-WECFWPLVTGCRLVLAAPGEHRDP 1350
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1351 ARLVELVRQFGVTTLHFVPPLLQLFID--EPGVAACGSLRRLFSGGEALPAELRNRVLQRLPaVALHNRYGPTETAINVT 1428
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFG-GALVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1429 HWQCRAEDGERSP-IGRPLGNVVCRVLDAEF-NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADpfsaageRLYRT 1506
Cdd:pfam00501  320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYRT 392
                          410       420
                   ....*....|....*....|....*
gi 15597620   1507 GDRARWNADGVLEYLGRLDQQVKLR 1531
Cdd:pfam00501  393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1130-1630 1.11e-112

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 367.60  E-value: 1.11e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:COG0318    1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1210 PDYPSERLAYMLADSGVELLLTqahlferlpgaegvtpicldslkldnwpsqapglhlhgdnlAYVIYTSGSTGQPKGVG 1289
Cdd:COG0318   81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1290 NTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFW-PLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFV 1368
Cdd:COG0318  120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1369 PPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPL 1446
Cdd:COG0318  197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1447 GNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvADPFsaagerlYRTGDRARWNADGVLEYLGRLDQ 1526
Cdd:COG0318  276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIVGRKKD 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1527 QVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMR 1605
Cdd:COG0318  348 MIISGGENVYPAEVEEVLAAHPGVAEAAVVgVPDEKWGERVVAFVVLRPGAELDAEE---LRAFLRERLARYKVPRRVEF 424
                        490       500
                 ....*....|....*....|....*
gi 15597620 1606 LAQMPLGPSGKLDTRALPEPVWQQR 1630
Cdd:COG0318  425 VDELPRTASGKIDRRALRERYAAGA 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
2200-2690 5.06e-112

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 365.95  E-value: 5.06e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVG-PEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYM 2278
Cdd:cd17648    1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2279 IEDSGVRLLLShaalfealgelpagvarwcleedgpaldaedpaplaalsGPQHQAYLIYTSGSTGKPKGVAVSHGEIAM 2358
Cdd:cd17648   81 LEDTGARVVIT---------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2359 HCAAVIECFGMRAEDCE--LHFYSINFDAASERLLAPLLCGAR-VVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQL 2435
Cdd:cd17648  122 LRTSLSERYFGRDNGDEavLFFSNYVFDFFVEQMTLALLNGQKlVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2436 aqwleSQGRQLPVRMCITGGEALTGEHLQRIRQAFaPASFFNAYGPTETVVMPLACLAP--ERLEEGaasvpIGSVVGAR 2513
Cdd:cd17648  202 -----DLARLPHLKRVDAAGEEFTAPVFEKLRSRF-AGLIINAYGPTETTVTNHKRFFPgdQRFDKS-----LGRPVRNT 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2514 VAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEG-------GRLYRTGDLVRLCDNGQVEYVG 2586
Cdd:cd17648  271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLG 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2587 RIDHQVKIRGFRIELGEIEARLLEHPQVREALVLA------LDSPSGKQLAGYV---ASAVAEQDedaqaalreaLKTHL 2657
Cdd:cd17648  351 RNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkedasqAQSRIQKYLVGYYlpePGHVPESD----------LLSFL 420
                        490       500       510
                 ....*....|....*....|....*....|...
gi 15597620 2658 KQQLPDYMVPAHLLLLASLPLTANGKLDRRALP 2690
Cdd:cd17648  421 RAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
11-564 6.07e-112

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 365.67  E-value: 6.07e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   11 LVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGV 89
Cdd:COG0318    1 LADLLRRAAARHPDRPALVF------GGRRLTYAELDARARRLAAAlRALGVGPGDRVALLLPNSPEFVVAFLAALRAGA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   90 IAVPAYPpesarRHHQERLLSIIADAEPRLVLTtadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvrpehi 169
Cdd:COG0318   75 VVVPLNP-----RLTAEELAYILEDSGARALVT----------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  170 AFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPRYfleRP 249
Cdd:COG0318  103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLL-PRF---DP 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  250 VRWLEAISQYGGTV-SGGPDFAYRLCservAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAAsrfdasSFFACYG 328
Cdd:COG0318  179 ERVLELIERERVTVlFGVPTMLARLL----RHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGV------RIVEGYG 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  329 LAEATLFVTGgqrgqgipalavdgealarnRIAEGEGSVLMCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAH 408
Cdd:COG0318  249 LTETSPVVTV--------------------NPEDPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMK 307
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  409 GYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------VPSAR 477
Cdd:COG0318  308 GYWNDPEATAEAF--RDG--WLRTGDLGRLDeDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHpgvaeaavvgVPDEK 383
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  478 KG-RVAAFAVTVDGEEgigiaaeigrgvqksVPAQELIDSIRQAVAeAYQeAPKVVALLnpGALPKTSSGKLQRSACRLR 556
Cdd:COG0318  384 WGeRVVAFVVLRPGAE---------------LDAEELRAFLRERLA-RYK-VPRRVEFV--DELPRTASGKIDRRALRER 444

                 ....*...
gi 15597620  557 LEDGSLDS 564
Cdd:COG0318  445 YAAGALEA 452
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
2200-2689 1.15e-111

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 365.83  E-value: 1.15e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd12114    1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLSHaalfeaLGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd12114   81 ADAGARLVLTD------GPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWG-AEEICELIRAEGVSILGFTPSYGSQLAQW 2438
Cdd:cd12114  155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdPAHWAELIERHGVTLWNSVPALLEMLLDV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 LESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTET----VVMPLaclapERLEEGAASVPIGSVVGAR 2513
Cdd:cd12114  235 LEAAQALLPsLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEAsiwsIYHPI-----DEVPPDWRSIPYGRPLANQ 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2514 VAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPfaaEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVK 2593
Cdd:cd12114  310 RYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2594 IRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVasavaEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLL 2673
Cdd:cd12114  387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFV-----VPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIAL 461
                        490
                 ....*....|....*.
gi 15597620 2674 ASLPLTANGKLDRRAL 2689
Cdd:cd12114  462 EALPLTANGKVDRAAL 477
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
2200-2689 2.89e-111

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 363.33  E-value: 2.89e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd17650    1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLshaalfealgelpagvarwcleedgpaLDAEDPaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd17650   81 EDSGAKLLL---------------------------TQPEDL------------AYVIYTSGTTGKPKGVMVEHRNVAHA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCE-LHFYSINFDAASERLLAPLLCGARVVLRAQG-QWGAEEICELIRAEGVSILGFTPSYGSQLAQ 2437
Cdd:cd17650  122 AHAWRREYELDSFPVRlLQMASFSFDVFAGDFARSLLNGGTLVICPDEvKLDPAALYDLILKSRITLMESTPALIRPVMA 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2438 WLESQGRQLP-VRMCITGGEALTGEH----LQRIRQAfapASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGA 2512
Cdd:cd17650  202 YVYRNGLDLSaMRLLIVGSDGCKAQDfktlAARFGQG---MRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPN 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2513 RVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAeGGRLYRTGDLVRLCDNGQVEYVGRIDHQV 2592
Cdd:cd17650  279 TAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAP-GERMYRTGDLARWRADGNVELLGRVDHQV 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2593 KIRGFRIELGEIEARLLEHPQVREALVLALDSPSG-KQLAGYVasaVAEQDEDAqAALREalktHLKQQLPDYMVPAHLL 2671
Cdd:cd17650  358 KIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGeARLCAYV---VAAATLNT-AELRA----FLAKELPSYMIPSYYV 429
                        490
                 ....*....|....*...
gi 15597620 2672 LLASLPLTANGKLDRRAL 2689
Cdd:cd17650  430 QLDALPLTPNGKVDRRAL 447
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3717-4231 4.90e-111

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 362.64  E-value: 4.90e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:cd17645    2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3797 HPTQRLTRIVELSRTLVLVctqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGL 3876
Cdd:cd17645   82 YPGERIAYMLADSSAKILL-------------------------------------------TNPDDLAYVIYTSGSTGL 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3877 PKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITV 3956
Cdd:cd17645  119 PKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 lesvpSLIQGMLAEERQALD--GLRWMLPTGEAmppelarqwLKRYPRIG--LVNAYGPAECSDDVAFFRVDlasTESTY 4032
Cdd:cd17645  199 -----SFLPTGAAEQFMQLDnqSLRVLLTGGDK---------LKKIERKGykLVNNYGPTENTVVATSFEID---KPYAN 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4033 LPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgAPGERLYRTGDLARRRAD 4112
Cdd:cd17645  262 IPIGKPIDNTRVYIL----DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPD 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4113 GVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPgetprssadspaglmvEQGAWF 4191
Cdd:cd17645  337 GNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVlAKEDADGRKYLVAYVTA----------------PEEIPH 400
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15597620 4192 ERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17645  401 EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3727-4231 3.99e-110

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 361.41  E-value: 3.99e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd17656    2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRTLVLVctqACREQALALFDELGCVdrprLLVWDEIQQGEGAEHDPQVYSgpQNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd17656   82 LDSGVRVVL---TQRHLKSKLSFNKSTI----LLEDPSISQEDTSNIDYINNS--DDLLYIIYTSGTTGKPKGVQLEHKN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLeSVPSLIQG 3966
Cdd:cd17656  153 MVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAEERQAL----DGLRWMLPTGEA-MPPELARQWLKRYpRIGLVNAYGPAEcSDDVAFFRVDLASTESTYLPIGSPTDN 4041
Cdd:cd17656  232 FIFSEREFInrfpTCVKHIITAGEQlVITNEFKEMLHEH-NVHLHNHYGPSE-THVVTTYTINPEAEIPELPPIGKPISN 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4042 NRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgAPGERLYRTGDLARRRADGVLEYVGRI 4121
Cdd:cd17656  310 TWIYIL----DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRA 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4122 DHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPgetprssadspaglmvEQGAWFERIKQQLRA 4200
Cdd:cd17656  385 DHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGeKYLCAYFVM----------------EQELNISQLREYLAK 448
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15597620 4201 DLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17656  449 QLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
2199-2690 6.64e-110

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 361.02  E-value: 6.64e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2199 SPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYM 2278
Cdd:cd17656    1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2279 IEDSGVRLLLSHAAL-----FEALGELPagvarwcleeDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSH 2353
Cdd:cd17656   81 MLDSGVRVVLTQRHLksklsFNKSTILL----------EDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEH 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2354 GEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARV-VLRAQGQWGAEEICELIRAEGVSILGFTPSYG 2432
Cdd:cd17656  151 KNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2433 SQLAQWLESQGRqLP--VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPErlEEGAASVPIGSVV 2510
Cdd:cd17656  231 KFIFSEREFINR-FPtcVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPE--AEIPELPPIGKPI 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2511 GARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEgGRLYRTGDLVRLCDNGQVEYVGRIDH 2590
Cdd:cd17656  308 SNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPN-ERMYRTGDLARYLPDGNIEFLGRADH 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2591 QVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVASAVAEQDEDaqaalreaLKTHLKQQLPDYMVPAH 2669
Cdd:cd17656  387 QVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELNISQ--------LREYLAKQLPEYMIPSF 458
                        490       500
                 ....*....|....*....|.
gi 15597620 2670 LLLLASLPLTANGKLDRRALP 2690
Cdd:cd17656  459 FVPLDQLPLTPNGKVDRKALP 479
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1726-2174 8.38e-110

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 359.72  E-value: 8.38e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1726 EQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFP-SVDGVPVQRVHGDGGLH 1804
Cdd:pfam00668    2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1805 MDWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAF 1884
Cdd:pfam00668   82 LEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1885 LDDRESPLEPLPvQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERV 1964
Cdd:pfam00668  162 LKGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1965 RRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTV 2044
Cdd:pfam00668  241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2045 IDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQ----TRQLAGMTVEYIANDARATKFDLNLEVTDLDQR 2120
Cdd:pfam00668  321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDsqeeEFQLSELDLSVSSVIEEEAKYDLSLTASERGGG 400
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15597620   2121 LGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLL 2174
Cdd:pfam00668  401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
24-554 6.71e-107

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 357.42  E-value: 6.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    24 ERLALRFLA-EDDGEGVVLSY--RDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESA 100
Cdd:NF040633   43 DRVCIRFWDySESREGTAVEYtrAEVNTRIKAVAARLQQVGKPGDRVAILANNSPEYIFGFLGALYAGMVPVPLYDPNEP 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   101 rrHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEH------------ 168
Cdd:NF040633  123 --GHADHLRAVLADSGPTVVLTNKTSAPAVRAHFADLPAAERPRILSVDSLPDSLAESWVNPMATIEGqpllapagtdps 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   169 --IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFsGVPCVLMSPRYFL 246
Cdd:NF040633  201 ddTAFLQYTSGSTRTPAGVVLTNRSIVTNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAFVTIL-GLEFELMSPRDFI 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   247 ERPVRWLEAISQYGGTV---SGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSF 323
Cdd:NF040633  280 QQPKRWVDQLSRREDDVnvyTVVPNFALELAARYANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTAL 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   324 FACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSV-----LMCCGRSQPEHAVLIVDAASGEVLGDDNVGE 398
Cdd:NF040633  360 RPSYGLAEASLLVTTPQTEERPLFTYFDREALAEGRAVEVAEDSenavpFASNGQVVRPQVLAIVDPETGQELPDGTVGE 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   399 IWAAGPSIAHGYWRNPEASAKAF-------VERDGRT-------WLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQD 464
Cdd:NF040633  440 IWVHGDNMAAGYLDREEETAETFrntlgerLAENSRAegapednWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQD 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   465 IERTVESEVPSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAqELIDSIRQAVAEAYQEAPKVVALLNPGALPKTS 544
Cdd:NF040633  520 IEATVQEASDHIRPDSVAAFAVPGDDVEKLVILAERDDEADESGDA-EAIEAIRAAVTSAHGVVPADIRIVAPGEIARSS 598
                         570
                  ....*....|
gi 15597620   545 SGKLQRSACR 554
Cdd:NF040633  599 SGKIARRVNA 608
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3717-4230 6.21e-106

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 347.37  E-value: 6.21e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:cd17653    1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3797 HPTQRLTRIVELSRTLVLVCTqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGL 3876
Cdd:cd17653   81 LPSARIQAILRTSGATLLLTT-----------------------------------------DSPDDLAYIIFTSGSTGI 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3877 PKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVaivpnaVAHDPQGLLAHVGeQGITV 3956
Cdd:cd17653  120 PKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL------VLADPSDPFAHVA-RTVDA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIQgMLaeERQALDGLRWMLPTGEAMPPELARQWLkryPRIGLVNAYGPAECSDDVAFFRVdlasTESTYLPIG 4036
Cdd:cd17653  193 LMSTPSILS-TL--SPQDFPNLKTIFLGGEAVPPSLLDRWS---PGRRLYNAYGPTECTISSTMTEL----LPGQPVTIG 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4037 SPTDNNRLYLLGAGAddafELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGaPGERLYRTGDLARRRADGVLE 4116
Cdd:cd17653  263 KPIPNSTCYILDADL----QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDGGLE 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4117 YVGRIDHQVKIRGFRIELGEIEAR-LHERADVREAAVAVQEGAngkyLVGYLVPgetprSSADSpaglmveqgawfERIK 4195
Cdd:cd17653  338 FLGREDNQVKVRGFRINLEEIEEVvLQSQPEVTQAAAIVVNGR----LVAFVTP-----ETVDV------------DGLR 396
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620 4196 QQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd17653  397 SELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
9-553 3.06e-105

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 351.10  E-value: 3.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFLA-EDDGEGVV--LSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCL 85
Cdd:NF038337    4 SSVVSLLRERAGLQPDDVAFRYTDyEQDWAGVTetLTWAQLYRRTLNVAHEVRRHGTTGDRAVILAPQGLPYIVAFLGAM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAVPAYPPESARrhHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAwdePQVR 165
Cdd:NF038337   84 QAGLIAVPLSVPQPGS--HDERVSAVLADTSPSVVLTTSAAAAAVAEYLHRPDTGAVPAVIEIDSLDLDGPNS---PSIR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 ---PEHIAFLQYTSGSTALPKGVQVSHGNLVAN-EVLIRRGF----GIGA-DDVIVSWLPLYHDMGLIGGLLQPIFSGVP 236
Cdd:NF038337  159 isdAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNfQQLMAAYFpdtnGVAPrDTTIVSWLPFYHDMGLVLGVIAPILGGYR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   237 CVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAAS 316
Cdd:NF038337  239 SELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAVRKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPY 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   317 RFDASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALAR---NRIAEGEGSVLMCCGRSQPEhAVLIVDAASGEVLGD 393
Cdd:NF038337  319 NFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEPEKLSEgsaQRCEARTGSPLLSYGTPTSP-TVRIVDPDTCIECPA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   394 DNVGEIWAAGPSIAHGYWRNPEASAKAF----VERDGRT----WLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDI 465
Cdd:NF038337  398 GTVGEIWVHGDNVAEGYWQKPEETRRTFggvlANPSPGTpegpWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDI 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   466 ERTVEsevpSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKV----VALLNPGALP 541
Cdd:NF038337  478 ESTVQ----EITGGRVAAISVPVDETEKLVTIIELKKRGDSDEEAMRKLDAVKNNVTAAISRSHGLnvadLVLVPPGSIP 553
                         570
                  ....*....|..
gi 15597620   542 KTSSGKLQRSAC 553
Cdd:NF038337  554 TTTSGKIRRAAC 565
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3727-4230 3.56e-104

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 344.25  E-value: 3.56e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:cd12114    1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 E-LSRTLVLVCtqacreqalaLFDELGCVDRPRLLVWDEIQQGEGAEHDPQVySGPQNLAYVIYTSGSTGLPKGVMVEQA 3885
Cdd:cd12114   81 AdAGARLVLTD----------GPDAQLDVAVFDVLILDLDALAAPAPPPPVD-VAPDDLAYVIFTSGSTGTPKGVMISHR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3886 GMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQ 3965
Cdd:cd12114  150 AALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3966 gMLAE----ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDN 4041
Cdd:cd12114  230 -MLLDvleaAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLAN 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4042 NRLYLLGAGADDafelVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPfgaPGERLYRTGDLARRRADGVLEYVGRI 4121
Cdd:cd12114  309 QRYRVLDPRGRD----CPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRR 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4122 DHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPgeTPRSSADSPAGLmveqgawferiKQQLRAD 4201
Cdd:cd12114  382 DGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVP--DNDGTPIAPDAL-----------RAFLAQT 448
                        490       500
                 ....*....|....*....|....*....
gi 15597620 4202 LPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd12114  449 LPAYMIPSRVIALEALPLTANGKVDRAAL 477
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
2188-2691 4.55e-103

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 339.86  E-value: 4.55e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2188 LHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2267
Cdd:COG0318    1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2268 PEYPLERLQYMIEDSGVRLLLShaalfealgelpagvarwcleedgpaldaedpaplaalsgpqhqAYLIYTSGSTGKPK 2347
Cdd:COG0318   81 PRLTAEELAYILEDSGARALVT--------------------------------------------ALILYTSGTTGRPK 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2348 GVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAA-SERLLAPLLCGARVVLRAQgqWGAEEICELIRAEGVSILG 2426
Cdd:COG0318  117 GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLF 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2427 FTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVvmPLACLAPERLEEgAASVP 2505
Cdd:COG0318  195 GVPTMLARLLRHPEFARYDLSsLRLVVSGGAPLPPELLERFEERFGVR-IVEGYGLTETS--PVVTVNPEDPGE-RRPGS 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2506 IGSVV-GARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVpdpfaaegGRLYRTGDLVRLCDNGQVEY 2584
Cdd:COG0318  271 VGRPLpGVEVR-IVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR--------DGWLRTGDLGRLDEDGYLYI 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2585 VGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP-SGKQLAGYVasaVAEQDEDAQAalrEALKTHLKQQLPD 2663
Cdd:COG0318  342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEkWGERVVAFV---VLRPGAELDA---EELRAFLRERLAR 415
                        490       500
                 ....*....|....*....|....*...
gi 15597620 2664 YMVPAHLLLLASLPLTANGKLDRRALPA 2691
Cdd:COG0318  416 YKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3727-4231 7.75e-102

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 336.68  E-value: 7.75e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGI-DQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRI 3805
Cdd:cd17648    1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3806 VELSRTLVLVctqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVMVEQA 3885
Cdd:cd17648   81 LEDTGARVVI-------------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHG 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3886 GMLN--NQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSL 3963
Cdd:cd17648  118 SVVNlrTSLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3964 IQGMlaeERQALDGLRWMLPTGEAMPPELARQWLKRYP-RIglVNAYGPAECS--DDVAFFRVDLASTEStylpIGSPTD 4040
Cdd:cd17648  198 LQQY---DLARLPHLKRVDAAGEEFTAPVFEKLRSRFAgLI--INAYGPTETTvtNHKRFFPGDQRFDKS----LGRPVR 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4041 NNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGE-------RLYRTGDLARRRADG 4113
Cdd:cd17648  269 NTKCYVL----NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQErargrnaRLYKTGDLVRWLPSG 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4114 VLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG------KYLVGYLVPGETPRSSADspaglmveq 4187
Cdd:cd17648  345 ELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQaqsriqKYLVGYYLPEPGHVPESD--------- 415
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 15597620 4188 gawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17648  416 ------LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
2191-2689 3.10e-100

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 331.20  E-value: 3.10e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2191 LFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:cd17653    2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2271 PLERLQYMIEDSGVRLLLShaalfealgelpagvarwcleedgpaldaedpaplaaLSGPQHQAYLIYTSGSTGKPKGVA 2350
Cdd:cd17653   82 PSARIQAILRTSGATLLLT-------------------------------------TDSPDDLAYIIFTSGSTGIPKGVM 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2351 VSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQgqwgAEEICELIRAegVSILGFTPS 2430
Cdd:cd17653  125 VPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP----SDPFAHVART--VDALMSTPS 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2431 YGSQLAQwlesqgRQLP-VRMCITGGEALTgehlQRIRQAFAP-ASFFNAYGPTETVVmplaCLAPERLEEGAAsVPIGS 2508
Cdd:cd17653  199 ILSTLSP------QDFPnLKTIFLGGEAVP----PSLLDRWSPgRRLYNAYGPTECTI----SSTMTELLPGQP-VTIGK 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2509 VVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaAEGGRLYRTGDLVRLCDNGQVEYVGRI 2588
Cdd:cd17653  264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGRE 342
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2589 DHQVKIRGFRIELGEIEAR-LLEHPQVREALVLAldspSGKQLAGYVASAVAEQDedaqaALREALKTHlkqqLPDYMVP 2667
Cdd:cd17653  343 DNQVKVRGFRINLEEIEEVvLQSQPEVTQAAAIV----VNGRLVAFVTPETVDVD-----GLRSELAKH----LPSYAVP 409
                        490       500
                 ....*....|....*....|..
gi 15597620 2668 AHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd17653  410 DRIIALDSFPLTANGKVDRKAL 431
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1729-2155 7.77e-97

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 321.25  E-value: 7.77e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1729 VPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVD-GVPVQRVHGDGGLHMDW 1807
Cdd:cd19539    2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSALDRDSRQQhLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDD 1887
Cdd:cd19539   82 RDLSDPDSDRERR-LEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1888 RESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLlELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRF 1967
Cdd:cd19539  161 PAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEPT-ALPTDRPRPAGFPYPGADLRFELDAELVAALREL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1968 NAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDG 2047
Cdd:cd19539  240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2048 QSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCLTY 2127
Cdd:cd19539  320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGY 399
                        410       420
                 ....*....|....*....|....*...
gi 15597620 2128 SRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19539  400 ATSLFDEETIQGFLADYLQVLRQLLANP 427
AMP-binding pfam00501
AMP-binding enzyme;
2192-2595 4.65e-96

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 318.49  E-value: 4.65e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2192 FAARVAASPQAPAL-TFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2271 PLERLQYMIEDSGVRLLL-----SHAALFEALGELPAGVARWCLEEDGP---------ALDAEDPAPLAALSGPQHQAYL 2336
Cdd:pfam00501   81 PAEELAYILEDSGAKVLItddalKLEELLEALGKLEVVKLVLVLDRDPVlkeeplpeeAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2337 IYTSGSTGKPKGVAVSHGEIAMHCAAVIEC----FGMRAEDCELHFYSINFDAASER-LLAPLLCGARVVLRAQG-QWGA 2410
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFpALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2411 EEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVVmpl 2489
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSsLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTG--- 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2490 ACLAPERLEEGAASVP-IGSVVGARVAYILDAD-LALVPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaeggRL 2567
Cdd:pfam00501  317 VVTTPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GW 389
                          410       420
                   ....*....|....*....|....*...
gi 15597620   2568 YRTGDLVRLCDNGQVEYVGRIDHQVKIR 2595
Cdd:pfam00501  390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
2196-2689 5.98e-96

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 319.58  E-value: 5.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2196 VAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2275
Cdd:cd05945    1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2276 QYMIEDSGVRLLLShaalfealgelpagvarwcleedgpaldaeDPAPLAalsgpqhqaYLIYTSGSTGKPKGVAVSHGE 2355
Cdd:cd05945   81 REILDAAKPALLIA------------------------------DGDDNA---------YIIFTSGSTGRPKGVQISHDN 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2356 IAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGA------RVVLRAQGQWGAEeicelIRAEGVSILGFTP 2429
Cdd:cd05945  122 LVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGAtlvpvpRDATADPKQLFRF-----LAEHGITVWVSTP 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2430 SYgsqLAQWLESQGR---QLP-VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVmplACLA---PERLEEGAA 2502
Cdd:cd05945  197 SF---AAMCLLSPTFtpeSLPsLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATV---AVTYievTPEVLDGYD 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2503 SVPIGSVV-GARvAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaEGGRLYRTGDLVRLCDNGQ 2581
Cdd:cd05945  271 RLPIGYAKpGAK-LVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD----EGQRAYRTGDLVRLEADGL 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2582 VEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasavaEQDEDAQAALREALKTHLKQQ 2660
Cdd:cd05945  346 LFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFV-----VPKPGAEAGLTKAIKAELAER 420
                        490       500
                 ....*....|....*....|....*....
gi 15597620 2661 LPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05945  421 LPPYMIPRRFVYLDELPLNANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
3719-4128 8.77e-94

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 311.94  E-value: 8.77e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3719 FEAQVAAHPQRIAASCLE-QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3798 PTQRLTRIVELSR-TLVLVCTQACREQALALFDELG------CVDRPRLLVWDEIQQGEGAEHDPQVYS---GPQNLAYV 3867
Cdd:pfam00501   81 PAEELAYILEDSGaKVLITDDALKLEELLEALGKLEvvklvlVLDRDPVLKEEPLPEEAKPADVPPPPPpppDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3868 IYTSGSTGLPKGVMVEQAGMLNNQLS----KVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNAVAHDP 3942
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLaGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3943 QGLLAHVGEQGITVLESVPSLIQGMLA---EERQALDGLRWMLPTGEAMPPELARQWLKRYPRiGLVNAYGPAECSdDVA 4019
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagaPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETT-GVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4020 FFRVDLASTESTYLPIGSPTDNNRLYLLGagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPhpfgapgER 4099
Cdd:pfam00501  319 TTPLPLDEDLRSLGSVGRPLPGTEVKIVD---DETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-------DG 388
                          410       420
                   ....*....|....*....|....*....
gi 15597620   4100 LYRTGDLARRRADGVLEYVGRIDHQVKIR 4128
Cdd:pfam00501  389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
676-1115 3.04e-92

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 308.88  E-value: 3.04e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    676 PQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFL-ERDGAALQRIDERGEFAWQFV 754
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFELEII 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    755 DLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQ 834
Cdd:pfam00668   86 DISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    835 PADLAPLElHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAA 914
Cdd:pfam00668  166 PLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    915 LDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQ 994
Cdd:pfam00668  245 KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAE 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    995 ANQDLPFDQVLAACGQ-----GGQLFQVLFNHQ----QRDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDArGRLTL 1065
Cdd:pfam00668  325 PHQGYPFGDLVNDLRLprdlsRHPLFDPMFSFQnylgQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERG-GGLTI 403
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 15597620   1066 NFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIALVDAEQAAHL 1115
Cdd:pfam00668  404 KIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
674-1097 4.61e-92

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 307.65  E-value: 4.61e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  674 DLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQF 753
Cdd:cd19538    1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  754 VdlaalAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGG 833
Cdd:cd19538   81 E-----IKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  834 QPADLAPLELHYAEFAAWQRQWLDAGEG-----ARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALAR 908
Cdd:cd19538  156 EAPELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQ 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  909 AIREAALDHEASVFMWLLAAFQALLHRhSGQGE-IRIGVPSANRQRLETQGLVGFFINTLVLR----GTPRarqpFAALL 983
Cdd:cd19538  236 QLLQLAKDNNVTLFMVLQAGFAALLTR-LGAGTdIPIGSPVAGRNDDSLEDLVGFFVNTLVLRtdtsGNPS----FRELL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  984 GEAREATLGAQANQDLPFDQVLAACGQGGQ-----LFQVLF---NHQQRDLSalrrLPGLLADELPWHSREAKFDL--QL 1053
Cdd:cd19538  311 ERVKETNLEAYEHQDIPFERLVEALNPTRSrsrhpLFQIMLalqNTPQPSLD----LPGLEAKLELRTVGSAKFDLtfEL 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620 1054 QSEEDARGRLTLN--FDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19538  387 REQYNDGTPNGIEgfIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
135-559 8.00e-92

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 311.16  E-value: 8.00e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   135 AQLSAANAPQLLCVDQLDPAvaEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGAD-DVIVS 213
Cdd:PRK07768  122 APVLEEKGIRVLTVADLLAA--DPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVS 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   214 WLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQ-RLDLSGWR 292
Cdd:PRK07768  200 WLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKPgAFDLSSLR 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   293 VAFSGSEPIRQDSLERFAEkfAASRF--DASSFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIA----EGEGS 366
Cdd:PRK07768  280 FALNGAEPIDPADVEDLLD--AGARFglRPEAILPAYGMAEATLAVSFSPCGAGLVVDEVDADLLAALRRAvpatKGNTR 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   367 VLMCCGRSQPEHAVLIVDaASGEVLGDDNVGEIWAAGPSIAHGYwrNPEASAKAFVERDGrtWLRTGDLGFLRD-GELFV 445
Cdd:PRK07768  358 RLATLGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGY--LTMDGFIPAQDADG--WLDTGDLGYLTEeGEVVV 432
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   446 TGRLKDMLIVRGHNLYPQDIERTVESeVPSARKGRVAAFAVTVD-GEEGIGIAAEigrgvQKSVPAQELIDSIRQAVAEA 524
Cdd:PRK07768  433 CGRVKDVIIMAGRNIYPTDIERAAAR-VEGVRPGNAVAVRLDAGhSREGFAVAVE-----SNAFEDPAEVRRIRHQVAHE 506
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 15597620   525 YQEA----PKVVALLNPGALPKTSSGKLQRSACRLRLED 559
Cdd:PRK07768  507 VVAEvgvrPRNVVVLGPGSIPKTPSGKLRRANAAELVTP 545
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3247-3699 2.41e-91

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 306.18  E-value: 2.41e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3247 IEDVYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRT 3326
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3327 RIEFLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSA 3406
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3407 LGESRPANLPTPPRYRDYIAWLQR----QDLEQSRRWWSESLRGFERPTLVPSDRpflREHAGESggmIVGDRYT-RLDA 3481
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDY---ARPADRS---FKGDRLSfTLDE 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3482 ADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPvgMPEMQRTVGLFINSIPLRVQMpAAGQrcTV 3561
Cdd:pfam00668  235 DTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SPDIERMVGMFVNTLPLRIDP-KGGK--TF 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3562 REWLNRLFERNLELREHEHLPLVAIQESSELPKGQ---PLFDSLFVFENAPVEVSVLDrAQSLNAS----SDSGRTHTNF 3634
Cdd:pfam00668  310 SELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPRDLsrhPLFDPMFSFQNYLGQDSQEE-EFQLSELdlsvSSVIEEEAKY 388
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620   3635 PLTVVCYP-GDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALADGFHGELEALPLLGEDERDFLL 3699
Cdd:pfam00668  389 DLSLTASErGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1728-2154 6.04e-91

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 304.18  E-value: 6.04e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1728 PVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDW 1807
Cdd:cd20483    1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSalDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDD 1887
Cdd:cd20483   81 IDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1888 R-ESPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGN---EHPLLELpGDRPRPPVQSHQGDLYRFDLSPELAER 1963
Cdd:cd20483  159 RdLATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipdASKLLPF-AKAERPPVKDYERSTVEATLDKELLAR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1964 VRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQT 2043
Cdd:cd20483  238 MKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTT 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2044 VIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQ------RWEFQQTRqlagMTvEYIANDARaTKFDLNLEVT-D 2116
Cdd:cd20483  318 CLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgkfpEYDTGDFK----FT-DYDHYDIP-TACDIALEAEeD 391
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597620 2117 LDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGD 2154
Cdd:cd20483  392 PDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
676-1097 5.38e-90

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 301.22  E-value: 5.38e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  676 PQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERD-GAALQRIDERGEFAWQFV 754
Cdd:cd19539    3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  755 DLAALAEHERAAAAAQRREAEAQqPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQ 834
Cdd:cd19539   83 DLSDPDSDRERRLEELLRERESR-GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  835 PADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPvLELATDHPRTARQASPAARYSLRVDEALARAIREAA 914
Cdd:cd19539  162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  915 LDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQ 994
Cdd:cd19539  241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  995 ANQDLPFDQVLAACG-----QGGQLFQVLFNHQQRDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGrLTLNFDY 1069
Cdd:cd19539  321 RHQELPFQQLVAELPvdrdaGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTG-LRGSLGY 399
                        410       420
                 ....*....|....*....|....*...
gi 15597620 1070 AADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19539  400 ATSLFDEETIQGFLADYLQVLRQLLANP 427
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3718-4233 7.88e-90

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 301.73  E-value: 7.88e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:COG0318    4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3798 PTQRLTRIVELSRTLVLVCtqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvysgpqnlAYVIYTSGSTGLP 3877
Cdd:COG0318   84 TAEELAYILEDSGARALVT------------------------------------------------ALILYTSGTTGRP 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3878 KGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNavaHDPQGLLAHVGEQGITV 3956
Cdd:COG0318  116 KGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLaGATLVLLPR---FDPERVLELIERERVTV 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPAECSDDVAFFRVDLASTESTyl 4033
Cdd:COG0318  193 LFGVPTMLARLLRHPEFArydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPG-- 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4034 PIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapgERLYRTGDLARRRADG 4113
Cdd:COG0318  270 SVGRPLPGVEVRIV----DEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR--------DGWLRTGDLGRLDEDG 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4114 VLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSAdspaglmveqgawfE 4192
Cdd:COG0318  338 YLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVvGVPDEKWGERVVAFVVLRPGAELDA--------------E 403
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15597620 4193 RIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:COG0318  404 ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1730-2155 1.35e-86

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 291.53  E-value: 1.35e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQD 1809
Cdd:cd20484    3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1810 FSALDRDSRQQHLQTladsEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRE 1889
Cdd:cd20484   83 ISSLKESEIIAYLRE----KAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1890 SPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNA 1969
Cdd:cd20484  159 PTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFAR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1970 ARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQS 2049
Cdd:cd20484  239 SQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2050 HQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQrwEFQQTRQL--------AGMTVEYIANDARATKFDLNLEVTDLDQRL 2121
Cdd:cd20484  319 HAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQ--NFLQSTSLqqflaeyqDVLSIEFVEGIHQEGEYELVLEVYEQEDRF 396
                        410       420       430
                 ....*....|....*....|....*....|....
gi 15597620 2122 GCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd20484  397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1731-1976 1.42e-86

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 283.85  E-value: 1.42e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1731 LSYSQQRMWFLwqlEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQDF 1810
Cdd:COG4908    1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1811 SALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRES 1890
Cdd:COG4908   78 SALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1891 PLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFNAA 1970
Cdd:COG4908  158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                 ....*.
gi 15597620 1971 RGLTMF 1976
Cdd:COG4908  238 HGATVN 243
AMP-binding pfam00501
AMP-binding enzyme;
15-456 4.98e-86

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 289.60  E-value: 4.98e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     15 LRRRAVQEPERLALrflaeDDGEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:pfam00501    1 LERQAARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGlRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     94 AYPpesarRHHQERLLSIIADAEPRLVLTTADLREPLLqmNAQLSAANAPQL-LCVDQLDPAVAEAWDE----------- 161
Cdd:pfam00501   76 LNP-----RLPAEELAYILEDSGAKVLITDDALKLEEL--LEALGKLEVVKLvLVLDRDPVLKEEPLPEeakpadvpppp 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    162 -PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVAN----EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVP 236
Cdd:pfam00501  149 pPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANvlsiKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    237 CVLMSPRYFLeRPVRWLEAISQYGGTVSGG-PDFAYRLcserVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAa 315
Cdd:pfam00501  229 VVLPPGFPAL-DPAALLELIERYKVTVLYGvPTLLNML----LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG- 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    316 srfdaSSFFACYGLAEATLFVTGGQRGqgipalavdgealarnriaEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDN 395
Cdd:pfam00501  303 -----GALVNGYGLTETTGVVTTPLPL-------------------DEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGE 358
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620    396 VGEIWAAGPSIAHGYWRNPEASAKAFVERDgrtWLRTGDLG-FLRDGELFVTGRLKDMLIVR 456
Cdd:pfam00501  359 PGELCVRGPGVMKGYLNDPELTAEAFDEDG---WYRTGDLGrRDEDGYLEIVGRKKDQIKLG 417
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1729-2155 1.04e-85

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 288.59  E-value: 1.04e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1729 VPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTF--PSVDGVPVQRVHGDGGLHMD 1806
Cdd:cd19532    2 EPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1807 WQDFSalDRDSRQQHLQTLadseAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAfld 1886
Cdd:cd19532   82 HVQIS--DEAEVEEEFERL----KNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1887 dreSPLEPLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEH---PLLELPGDRPRPPVQSHQGDLYRFDLSPELAER 1963
Cdd:cd19532  153 ---QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPeplPLLPFAKVKSRPPLTRYDTHTAERRLDAALAAR 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1964 VRRfnAARGL--TMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVR 2041
Cdd:cd19532  230 IKE--ASRKLrvTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETR 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2042 QTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVqRWEFQQTRQLAGMTVEYI-ANDARaTKFDLNLEVTDLDQR 2120
Cdd:cd19532  308 DKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINY-RQGVAESRPFGDCELEGEeFEDAR-TPYDLSLDIIDNPDG 385
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15597620 2121 lGCCLTYS--RDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19532  386 -DCLLTLKvqSSLYSEEDAELLLDSYVNLLEAFARDP 421
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
868-1734 8.13e-84

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 306.22  E-value: 8.13e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    868 WRERLgDTAPVLELATDHPRTARQASPAARYSLRVDEAlarairEAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVP 947
Cdd:TIGR03443    2 WSERL-DNPTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    948 SANRQRletqglvgffinTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAAC------GQGGQLFQVLFNH 1021
Cdd:TIGR03443   75 SNKSGR------------PFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIqaakklERTPPLFRLAFQD 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1022 QQrDLSALRRLPGLLADelpwhsreakFDLQLQSEEdarGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCL 1101
Cdd:TIGR03443  143 AP-DNQQTTYSTGSTTD----------LTVFLTPSS---PELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPI 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1102 GDIALVDAEQAAHLA------EWG------------SAPCEPARAWLPELLERQLAQSAERvalewdggSLGYAELHARA 1163
Cdd:TIGR03443  209 GKVSLITPSQKSLLPdptkdlDWSgfrgaihdifadNAEKHPDRTCVVETPSFLDPSSKTR--------SFTYKQINEAS 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1164 NRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERL-----------------AYMLADSGV 1226
Cdd:TIGR03443  281 NILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQtiylsvakpraliviekAGTLDQLVR 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1227 ELLLTQAHLFERLP-------GA------EGVTPICL---DSLKldnwpSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGN 1290
Cdd:TIGR03443  361 DYIDKELELRTEIPalalqddGSlvggslEGGETDVLapyQALK-----DTPTGVVVGPDSNPTLSFTSGSEGIPKGVLG 435
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1291 THAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPP 1370
Cdd:TIGR03443  436 RHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPA 515
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1371 LLQLFIDEpGVAACGSLRRLFSGGEALPAE--LRnrvLQRL-PAVALHNRYGPTETAINVTHWQ--CRAEDG-------E 1438
Cdd:TIGR03443  516 MGQLLSAQ-ATTPIPSLHHAFFVGDILTKRdcLR---LQTLaENVCIVNMYGTTETQRAVSYFEipSRSSDStflknlkD 591
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1439 RSPIGRPLGNVVCRVLDAEFNLLPAGVA--GELCIGGLGLARGYLGRPALSAERFVADPFSAAGE--------------- 1501
Cdd:TIGR03443  592 VMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkperef 671
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1502 ------RLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQ-LVGY----- 1569
Cdd:TIGR03443  672 wlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPtLVSYivpqd 751
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1570 -------YTGAVGAEAEAEQNQR-----------LRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQRE 1631
Cdd:TIGR03443  752 ksdeleeFKSEVDDEESSDPVVKglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLA 831
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1632 HVEPR----------TELQRRIAAIWSEVL--GLPRVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELE 1699
Cdd:TIGR03443  832 AVAKNrsasaadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIK 911
                          970       980       990
                   ....*....|....*....|....*....|....*
gi 15597620   1700 AFCEQVRAAQAAGRTDSHGAIRRIDREQPVPLSYS 1734
Cdd:TIGR03443  912 GFAKEVDRLKKGEELADEGDSEIEEEETVLELDYA 946
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
8-560 1.44e-82

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 284.17  E-value: 1.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    8 PTTLVQALRRRAvqepERLALRFLA--EDDGEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGC 84
Cdd:cd05906    9 PRTLLELLLRAA----ERGPTKGITyiDADGSEEFQSYQDLLEDARRLAAGlRQLGLRPGDSVILQFDDNEDFIPAFWAC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   85 LYAGVIAVP-----AYPPESARRHHQERLLSIIADAeprLVLTTADLREPLLqmnaqlsAANAPQLLCVDQLD-----PA 154
Cdd:cd05906   85 VLAGFVPAPltvppTYDEPNARLRKLRHIWQLLGSP---VVLTDAELVAEFA-------GLETLSGLPGIRVLsieelLD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  155 VAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSG 234
Cdd:cd05906  155 TAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  235 VPCVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFA 314
Cdd:cd05906  235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  315 ASRFDASSFFACYGLAEAtlfVTGGQRGQGIPALAVDGEalarnriaegegSVLMCCGRSQPEHAVLIVDaASGEVLGDD 394
Cdd:cd05906  315 PYGLPPDAIRPAFGMTET---CSGVIYSRSFPTYDHSQA------------LEFVSLGRPIPGVSMRIVD-DEGQLLPEG 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  395 NVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVP 474
Cdd:cd05906  379 EVGRLQVRGPVVTKGYYNNPEANAEAFTE-DG--WFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVE-EVP 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  475 SARKGRVAAFAVTVDGEEGIGIA----AEIGRGVQKSvpaqELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQR 550
Cdd:cd05906  455 GVEPSFTAAFAVRDPGAETEELAiffvPEYDLQDALS----ETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQR 530
                        570
                 ....*....|
gi 15597620  551 SACRLRLEDG 560
Cdd:cd05906  531 SKLKAAFEAG 540
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2786-3232 2.82e-77

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 265.74  E-value: 2.82e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2786 VQGDSALTPIQH--WFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAF-RQVDGE---WLAQHRPL 2859
Cdd:pfam00668    1 VQDEYPLSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEpvqVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2860 R-EQELLWHVPVQSFDECAELFAKA--QRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQ 2936
Cdd:pfam00668   81 ElEIIDISDLSESEEEEAIEAFIQRdlQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2937 FAEGAEPALPAKTSaFRDWAGRLQAYAGSESLREELGWWQARLGG--QPVEWPCDRPQGDNREALAESVSLRLDPQrTRQ 3014
Cdd:pfam00668  161 LLKGEPLPLPPKTP-YKDYAEWLQQYLQSEDYQKDAAYWLEQLEGelPVLQLPKDYARPADRSFKGDRLSFTLDED-TEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3015 LLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREalfdDIDLTRSVGWFTSAYPLRLTPAQSP--GESIK 3092
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP----SPDIERMVGMFVNTLPLRIDPKGGKtfSELIK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3093 AIKEQLR-AVPHKGLGYGVLRYLADPAVRQAMAALPTAPITF-NYLGQfdQSFADALFQPLDQPTGPIHDEQApLPNELS 3170
Cdd:pfam00668  315 RVQEDLLsAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQ--DSQEEEFQLSELDLSVSSVIEEE-AKYDLS 391
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620   3171 VDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQL 3232
Cdd:pfam00668  392 LTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
674-1097 6.17e-77

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 263.50  E-value: 6.17e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  674 DLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFA-WQ 752
Cdd:cd19066    1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFrIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  753 FVDLAALAEHERAAAAAQRREAEAqqPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACG 832
Cdd:cd19066   81 IIDLRNLADPEARLLELIDQIQQT--IYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  833 GQPAdLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIRE 912
Cdd:cd19066  159 QKPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLRE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  913 AALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLG 992
Cdd:cd19066  238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  993 AQANQDLPFDQVLAACGQGGQ-----LFQVLFNHQQRDLSaLRRLPGLLADELPWHSRE-AKFDLQLQSEEDARGRLTLN 1066
Cdd:cd19066  318 AIEHQRVPFIELVRHLGVVPEapkhpLFEPVFTFKNNQQQ-LGKTGGFIFTTPVYTSSEgTVFDLDLEASEDPDGDLLLR 396
                        410       420       430
                 ....*....|....*....|....*....|.
gi 15597620 1067 FDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19066  397 LEYSRGVYDERTIDRFAERYMTALRQLIENP 427
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1730-2155 2.44e-76

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 261.75  E-value: 2.44e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTF-PSVDGVPVQRVHGDGGLHMDWQ 1808
Cdd:cd19543    3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLQVVLKDRKLPWREL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1809 DFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDR 1888
Cdd:cd19543   83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1889 ESPLEPlPVQYLDYSvwqrEWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERVRRFN 1968
Cdd:cd19543  163 PPSLPP-VRPYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1969 AARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANR---IrPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVI 2045
Cdd:cd19543  238 RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRpaeL-PGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2046 DGQSHQDLP--------------FDHLVealqpprsaaynpLFQVMCNVQRWEFQQTRQlaGMTVEYIANdARATKFDLN 2111
Cdd:cd19543  317 ELREHEYVPlyeiqawsegkqalFDHLL-------------VFENYPVDESLEEEQDED--GLRITDVSA-EEQTNYPLT 380
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 15597620 2112 LEVTdLDQRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19543  381 VVAI-PGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1728-2155 1.08e-75

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 260.03  E-value: 1.08e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1728 PVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGdgglHMDW 1807
Cdd:cd19066    1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLD----KTVR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSALD---RDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAF 1884
Cdd:cd19066   77 FRIEIIDlrnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1885 LDDRESPLePLPVQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSPELAERV 1964
Cdd:cd19066  157 ERQKPTLP-PPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1965 RRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTV 2044
Cdd:cd19066  236 REVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2045 IDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQ--QTRQLAGMTVEYiaNDARATKFDLNLEVT-DLDQRL 2121
Cdd:cd19066  316 REAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQlgKTGGFIFTTPVY--TSSEGTVFDLDLEASeDPDGDL 393
                        410       420       430
                 ....*....|....*....|....*....|....
gi 15597620 2122 GCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19066  394 LLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
3440-4337 1.51e-75

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 280.03  E-value: 1.51e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3440 WSESLrgfERPTLVPSDRPFLREHAGESggmivgdrytrLDAADGARLRELAQRYQLTVNTFAQ--AAWALTLRRFSGER 3517
Cdd:TIGR03443    2 WSERL---DNPTLSVLPHDYLRPANNRL-----------VEATYSLQLPSAEVTAGGGSTPFIIllAAFAALVYRLTGDE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3518 DVLFGVTVA--GRPvgmpemqrtvglFINSIPLRVQMPAAGQRCTVrewlNRLFERNL--------ELREHehlplvaIQ 3587
Cdd:TIGR03443   68 DIVLGTSSNksGRP------------FVLRLNITPELSFLQLYAKV----SEEEKEGAsdigvpfdELSEH-------IQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3588 ESSELPKGQPLFDslFVFENAPvevsvldraqslNASSDSGRTHTNFPLTVVCYPG-DDLGLHLSYDQRYFEAPTVERLL 3666
Cdd:TIGR03443  125 AAKKLERTPPLFR--LAFQDAP------------DNQQTTYSTGSTTDLTVFLTPSsPELELSIYYNSLLFSSDRITIVA 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3667 GEFKRLLLALADGFHGELEALPLLGEDERDFL------LDGCnrsardypleqGYV----RLFEAQVAAHPQR------- 3729
Cdd:TIGR03443  191 DQLAQLLSAASSNPDEPIGKVSLITPSQKSLLpdptkdLDWS-----------GFRgaihDIFADNAEKHPDRtcvvetp 259
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3730 --IAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTriVE 3807
Cdd:TIGR03443  260 sfLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQT--IY 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3808 LS----RTLVLVCTQACREQALALF--DELGCVDR-PRL-------LVWDEIQQGEGAEHDPQ---------VYSGPQNL 3864
Cdd:TIGR03443  338 LSvakpRALIVIEKAGTLDQLVRDYidKELELRTEiPALalqddgsLVGGSLEGGETDVLAPYqalkdtptgVVVGPDSN 417
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3865 AYVIYTSGSTGLPKGV-------------MVEQAGmlnnqlskvpyleLDENDV------IAQTASQSfDISVWQFLAAP 3925
Cdd:TIGR03443  418 PTLSFTSGSEGIPKGVlgrhfslayyfpwMAKRFG-------------LSENDKftmlsgIAHDPIQR-DMFTPLFLGAQ 483
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3926 LfgarvaIVPNAVAHDPQGLLAH-VGEQGITVLESVPSLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIG 4004
Cdd:TIGR03443  484 L------LVPTADDIGTPGRLAEwMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVC 557
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4005 LVNAYGPAECSDDVAFFRVDLASTESTYL-------PIGSPTDNnrLYLLGAGADDAFELVPLGAVGELCVAGTGVGRGY 4077
Cdd:TIGR03443  558 IVNMYGTTETQRAVSYFEIPSRSSDSTFLknlkdvmPAGKGMKN--VQLLVVNRNDRTQTCGVGEVGEIYVRAGGLAEGY 635
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4078 VGDPLRTAQAFVPHPFGAPGE---------------------RLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGE 4136
Cdd:TIGR03443  636 LGLPELNAEKFVNNWFVDPSHwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGE 715
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4137 IEARLHERADVREAAVAVQEGANG-KYLVGYLVP-----------GETPRSSADSP-AGLMVEQGAWFERIKQQLRADLP 4203
Cdd:TIGR03443  716 IDTHLSQHPLVRENVTLVRRDKDEePTLVSYIVPqdksdeleefkSEVDDEESSDPvVKGLIKYRKLIKDIREYLKKKLP 795
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4204 DYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQNQAYQAPRN-------ELEETLARIWAEVL--KVERVGVFDNFF 4274
Cdd:TIGR03443  796 SYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeeftETEREIRDLWLELLpnRPATISPDDSFF 875
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   4275 ELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESLapseiseQKAERLNDLMS 4337
Cdd:TIGR03443  876 DLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRL-------KKGEELADEGD 931
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
29-560 5.77e-75

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 260.50  E-value: 5.77e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   29 RFLAEDDGEGVVlSYRDLDLRARS-IAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPayppesarrhhqer 107
Cdd:cd05908    5 IFILGDKKEKFV-SYRHLREEALGyLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVP-------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  108 lLSIIADAEPRLvlttadlrepllQMNAQLSAANAPQLLCVDqldpavaEAWDEpqvRPEHIAFLQYTSGSTALPKGVQV 187
Cdd:cd05908   70 -VSIGSNEEHKL------------KLNKVWNTLKNPYLITEE-------EVLCE---LADELAFIQFSSGSTGDPKGVML 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  188 SHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQYGGTVSGGP 267
Cdd:cd05908  127 THENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSP 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  268 DFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSFFACYGLAEATLFVTG--------- 338
Cdd:cd05908  207 NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEASVGASLpkaqspfkt 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  339 ---GQRGQ--GIPALAVDGEalarnriaEGEGSVLMCCGRSQPEHAVLIVDAASgEVLGDDNVGEIWAAGPSIAHGYWRN 413
Cdd:cd05908  287 itlGRRHVthGEPEPEVDKK--------DSECLTFVEVGKPIDETDIRICDEDN-KILPDGYIGHIQIRGKNVTPGYYNN 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  414 PEASAKAFVErDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKGRVAAFAV--TVDGE 491
Cdd:cd05908  358 PEATAKVFTD-DG--WLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAE-ELEGVELGRVVACGVnnSNTRN 433
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  492 EGIGIAAEIGRGVQKSVPAQELIDSIRQavaeaYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDG 560
Cdd:cd05908  434 EEIFCFIEHRKSEDDFYPLGKKIKKHLN-----KRGGWQINEVLPIRRIPKTTSGKVKRYELAQRYQSG 497
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1133-1626 1.56e-74

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 259.44  E-value: 1.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1133 LLER--QLAQS-AERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK04813    4 IIETieEFAQTqPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVELLLTQAHLferLPGAEGVTPICLDSLKlDNWPSQAP---GLHLHGDNLAYVIYTSGSTGQPK 1286
Cdd:PRK04813   84 VSSPAERIEMIIEVAKPSLIIATEEL---PLEILGIPVITLDELK-DIFATGNPydfDHAVKGDDNYYIIFTSGTTGKPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1287 GVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLH 1366
Cdd:PRK04813  160 GVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1367 FVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAE---DGERSP 1441
Cdd:PRK04813  240 STPSFADMCLLDPSFNEehLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEmldQYKRLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1442 IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvadpFSAAGERLYRTGDRARWNaDGVLEYL 1521
Cdd:PRK04813  320 IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAGYLE-DGLLFYQ 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1522 GRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV--IREG-VagSQLVGYY-TGAVGAEAEAEQNQRLRAALQAELPEY 1597
Cdd:PRK04813  395 GRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVpyNKDHkV--QYLIAYVvPKEEDFEREFELTKAIKKELKERLMEY 472
                         490       500
                  ....*....|....*....|....*....
gi 15597620  1598 MVPTQLMRLAQMPLGPSGKLDTRALPEPV 1626
Cdd:PRK04813  473 MIPRKFIYRDSLPLTPNGKIDRKALIEEV 501
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3727-4230 1.57e-74

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 259.44  E-value: 1.57e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:PRK04813   16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3807 ELSRTLVLVCTqacreqALALFDELGCvdrpRLLVWDEIQQGEGAEHDPQV---YSGPQNlAYVIYTSGSTGLPKGVMVE 3883
Cdd:PRK04813   96 EVAKPSLIIAT------EELPLEILGI----PVITLDELKDIFATGNPYDFdhaVKGDDN-YYIIFTSGTTGKPKGVQIS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3884 QAGMLN-----NQLSKVPylelDENDVIAQtASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLE 3958
Cdd:PRK04813  165 HDNLVSftnwmLEDFALP----EGPQFLNQ-APYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3959 SVPSLIQ-GMLAEE--RQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSddVAFFRVDLasTE---STY 4032
Cdd:PRK04813  240 STPSFADmCLLDPSfnEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEAT--VAVTSIEI--TDemlDQY 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4033 --LPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpFGAPGERLYRTGDLARRr 4110
Cdd:PRK04813  316 krLPIGYAKPDSPLLII----DEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGDAGYL- 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4111 ADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAaVAVQEGANGK--YLVGYLVPGETPrssadspaglmveqg 4188
Cdd:PRK04813  387 EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESA-VVVPYNKDHKvqYLIAYVVPKEED--------------- 450
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 15597620  4189 awFER-------IKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK04813  451 --FERefeltkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
3251-3678 1.84e-74

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 256.22  E-value: 1.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3251 YPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEF 3330
Cdd:cd19536    2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3331 LDWSelPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFM-MSNHHILIDAWCRGLLMNDFFEIYSALGE 3409
Cdd:cd19536   82 LDLT--PLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 SRPANLPTPPRYRDYIAWLQRQDL-EQSRRWWSESLRGFERPTLvpsdrPFLREhagESGGMIVGDRYTRLDAADGARLR 3488
Cdd:cd19536  160 YKPLSLPPAQPYRDFVAHERASIQqAASERYWREYLAGATLATL-----PALSE---AVGGGPEQDSELLVSVPLPVRSR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3489 ELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAgqrcTVREWLNRL 3568
Cdd:cd19536  232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEE----TVEDLLKRA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3569 FERNLELREHEHLPLVAIQESSElpkGQPLFDSLFVFENAPvevsvLDRAQSLNASSDSGRTHTNFPLTVVCYP------ 3642
Cdd:cd19536  308 QEQELESLSHEQVPLADIQRCSE---GEPLFDSIVNFRHFD-----LDFGLPEWGSDEGMRRGLLFSEFKSNYDvnlsvl 379
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597620 3643 --GDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALAD 3678
Cdd:cd19536  380 pkQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELAT 417
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
3250-3679 2.01e-74

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 255.31  E-value: 2.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3250 VYPLTPMQEGLLLHTLLEPGTGIYYMQdrYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGE-TMLQVIHKPGRTRI 3328
Cdd:cd19542    1 IYPCTPMQEGMLLSQLRSPGLYFNHFV--FDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEgTFLQVVLKSLDPPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3329 EFLDwselpedGHEERLQALHKREREAGFdLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSAlg 3408
Cdd:cd19542   79 EEVE-------TDEDSLDALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3409 esrpANLPTPPRYRDYIAWLQRQDLEQSRRWWSESLRGFERPTLvpsdrPFLREHAGesggmivGDRYTRLDAADGARLR 3488
Cdd:cd19542  149 ----QLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAF-----PSLSPKRP-------AERSLSSTRRSLAKLE 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3489 ELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPaagQRCTVREWLNRL 3568
Cdd:cd19542  213 AFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLD---PDWTVLDLLRQL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3569 FERNLELREHEHLPLVAIQESSELPKGQPLFDSLFVFENAPvEVSVLDRAQSLNASSDSGRTHTNFPLTV-VCYPGDDLG 3647
Cdd:cd19542  290 QQQYLRSLPHQHLSLREIQRALGLWPSGTLFNTLVSYQNFE-ASPESELSGSSVFELSAAEDPTEYPVAVeVEPSGDSLK 368
                        410       420       430
                 ....*....|....*....|....*....|..
gi 15597620 3648 LHLSYDQRYFEAPTVERLLGEFKRLLLALADG 3679
Cdd:cd19542  369 VSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
678-922 1.08e-73

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 247.26  E-value: 1.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  678 SAAQQRLWLtwqIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLA 757
Cdd:COG4908    2 SPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  758 ALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPAD 837
Cdd:COG4908   79 ALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  838 LAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDH 917
Cdd:COG4908  159 LPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAH 238

                 ....*
gi 15597620  918 EASVF 922
Cdd:COG4908  239 GATVN 243
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
1132-1626 6.73e-73

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 254.68  E-value: 6.73e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:TIGR01734    4 EAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1212 YPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWP---SQApglhLHGDNLAYVIYTSGSTGQPKGV 1288
Cdd:TIGR01734   84 IPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPvsfDHA----VKGDDNYYIIYTSGSTGNPKGV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1289 GNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFV 1368
Cdd:TIGR01734  160 QISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVST 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1369 PPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAE---DGERSPIG 1443
Cdd:TIGR01734  240 PSFVDMCLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEildQYPRLPIG 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1444 --RPLGNVvcRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvadpFSAAGERLYRTGDRARWNaDGVLEYL 1521
Cdd:TIGR01734  320 faKPDMNL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEGQPAYRTGDAGTIT-DGQLFYQ 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1522 GRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIR----EGVAgsQLVGYytgAVGAEAEAEQNQRLRAALQAEL--- 1594
Cdd:TIGR01734  393 GRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKynkdHKVE--YLIAA---IVPETEDFEKEFQLTKAIKKELkks 467
                          490       500       510
                   ....*....|....*....|....*....|...
gi 15597620   1595 -PEYMVPTQLMRLAQMPLGPSGKLDTRALPEPV 1626
Cdd:TIGR01734  468 lPAYMIPRKFIYRDQLPLTANGKIDRKALAEEV 500
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1922-2784 7.05e-73

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 271.55  E-value: 7.05e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1922 WKAQLGNEhPLLELPGDRPRPPVQSHQGDLYRFDLSPELAErvrrfnAARGLTMFMTMTATLAALLYRYSGQQDLRIGAP 2001
Cdd:TIGR03443    2 WSERLDNP-TLSVLPHDYLRPANNRLVEATYSLQLPSAEVT------AGGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2002 VANRIRPesegligaflntQVLRCRLDGQMSVGELLEQVRQTVIDGQSHQDLPFDHLVEALQPP-RSAAYNPLFQVMCnV 2080
Cdd:TIGR03443   75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAkKLERTPPLFRLAF-Q 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2081 QRWEFQQTRQLAGMTveyiandaraTKFDLNLEVTDLDQRLGccLTYSRDLFDEPRIARMAGHWQNLLEALLGDPQRRIA 2160
Cdd:TIGR03443  142 DAPDNQQTTYSTGST----------TDLTVFLTPSSPELELS--IYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2161 ELPLFAaEERKQLLLAGTA--GEAGLQDTLHGLFAARVAASPQAP----ALTFAG-----QTLSYAELDARSNRLARVLR 2229
Cdd:TIGR03443  210 KVSLIT-PSQKSLLPDPTKdlDWSGFRGAIHDIFADNAEKHPDRTcvveTPSFLDpssktRSFTYKQINEASNILAHYLL 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2230 SHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLshaaLFEALGELPAGVARWCL 2309
Cdd:TIGR03443  289 KTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALI----VIEKAGTLDQLVRDYID 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2310 EE------------------DGPALDAEDP---APLAALS--------GPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHC 2360
Cdd:TIGR03443  365 KElelrteipalalqddgslVGGSLEGGETdvlAPYQALKdtptgvvvGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYF 444
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2361 AAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGAE-EICELIRAEGVSILGFTPSYGsqlaQWL 2439
Cdd:TIGR03443  445 PWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPgRLAEWMAKYGATVTHLTPAMG----QLL 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2440 ESQG-RQLP-VRMCITGGEALTGEHLQRIrQAFAPASFF-NAYGPTET------VVMPLACLAPERLEEGAASVPIGsvV 2510
Cdd:TIGR03443  521 SAQAtTPIPsLHHAFFVGDILTKRDCLRL-QTLAENVCIvNMYGTTETqravsyFEIPSRSSDSTFLKNLKDVMPAG--K 597
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2511 GarvayILDADLALVPQ---------GATGELYVGGAGLARGYHERPALSAERFVPDPFAAEG----------------- 2564
Cdd:TIGR03443  598 G-----MKNVQLLVVNRndrtqtcgvGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkperefw 672
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2565 ----GRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGY------ 2633
Cdd:TIGR03443  673 lgprDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRrDKDEEPTLVSYivpqdk 752
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2634 ---VASAVAEQDEDAQA-----------ALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPAL--- 2696
Cdd:TIGR03443  753 sdeLEEFKSEVDDEESSdpvvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQlaa 832
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2697 -----NRQAYEAPRSVLEQQLAGVWREVL-NV-ERVGLGDNFFELGGDSILSIQVVSRAR-QLGIHFSPRDLFQHQTVQS 2768
Cdd:TIGR03443  833 vaknrSASAADEEFTETEREIRDLWLELLpNRpATISPDDSFFDLGGHSILATRMIFELRkKLNVELPLGLIFKSPTIKG 912
                          970
                   ....*....|....*..
gi 15597620   2769 LAA-VARHSQASQAEQG 2784
Cdd:TIGR03443  913 FAKeVDRLKKGEELADE 929
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1272-1618 8.25e-71

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 242.58  E-value: 8.25e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1272 LAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPgehRDPA 1351
Cdd:cd04433    2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1352 RLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPaVALHNRYGPTETAINVTH 1429
Cdd:cd04433   79 AALELIEREKVTILLGVPTLLARLLKAPESAGydLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1430 WQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvadpfsaaGERLYRTGDR 1509
Cdd:cd04433  158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1510 ARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQnqrLRA 1588
Cdd:cd04433  230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGERVVAVVVLRPGADLDAEE---LRA 306
                        330       340       350
                 ....*....|....*....|....*....|
gi 15597620 1589 ALQAELPEYMVPTQLMRLAQMPLGPSGKLD 1618
Cdd:cd04433  307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
676-1097 4.12e-69

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 240.82  E-value: 4.12e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  676 PQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLER--DGAALQRIDERGEFAWQF 753
Cdd:cd19532    3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDpeDGEPMQGVLASSPLRLEH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  754 VDlaalaeHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAeacgG 833
Cdd:cd19532   83 VQ------ISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN----G 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  834 QPadLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLEL---ATDHPRTARQASPAARYSLRVDEALARAI 910
Cdd:cd19532  153 QP--LLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAARI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  911 REAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREAT 990
Cdd:cd19532  231 KEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  991 LGAQANQDLPFDQVLAACG---QGGQ--LFQVLFNHQQRDLSAlRRLPGLLADELPWHSREAKFDLQLQSEEDARGRLTL 1065
Cdd:cd19532  311 YAALAHSRVPFDVLLDELGvprSATHspLFQVFINYRQGVAES-RPFGDCELEGEEFEDARTPYDLSLDIIDNPDGDCLL 389
                        410       420       430
                 ....*....|....*....|....*....|..
gi 15597620 1066 NFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19532  390 TLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
168-549 5.06e-69

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 237.18  E-value: 5.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  168 HIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdMGLIGGLLQPIFSGVPCVLMSPRyfle 247
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPKF---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  248 RPVRWLEAISQYGGTVSGGPDFAYRLCserVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAAsrfdasSFFACY 327
Cdd:cd04433   76 DPEAALELIEREKVTILLGVPTLLARL---LKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVNGY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  328 GLAEATLFVTGGQrgqgipalavdgealarnriAEGEGSVLMCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIA 407
Cdd:cd04433  147 GLTETGGTVATGP--------------------PDDDARKPGSVGRPVPGVEVRIVDPD-GGELPPGEIGELVVRGPSVM 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  408 HGYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARkgRVAAFAV 486
Cdd:cd04433  206 KGYWNNPEATAAVD--EDG--WYRTGDLGRLDeDGYLYIVGRLKDMIKSGGENVYPAEVEAVLL-GHPGVA--EAAVVGV 278
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  487 TvDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAeAYQEaPKVVALLNpgALPKTSSGKLQ 549
Cdd:cd04433  279 P-DPEWGERVVAVVVLRPGADLDAEELRAHVRERLA-PYKV-PRRVVFVD--ALPRTASGKID 336
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3250-3678 5.18e-69

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 240.72  E-value: 5.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3250 VYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMlQVIHKPGRTRIE 3329
Cdd:cd19531    1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPV-QVILPPLPLPLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3330 FLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGE 3409
Cdd:cd19531   80 VVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 SRPANLPTPP-RYRDYIAW----LQRQDLEQSRRWWSESLRGfERPTL-VPSD--RPFLREHAgesggmivGDRYT-RLD 3480
Cdd:cd19531  160 GRPSPLPPLPiQYADYAVWqrewLQGEVLERQLAYWREQLAG-APPVLeLPTDrpRPAVQSFR--------GARVRfTLP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3481 AADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPvgMPEMQRTVGLFINSIPLRVQMpaAGQRcT 3560
Cdd:cd19531  231 AELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRN--RAELEGLIGFFVNTLVLRTDL--SGDP-T 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3561 VREWLNRLFERNLELREHEHLP---LVAiqessEL-----PKGQPLFDSLFVFENAPVEVSVLDraqSLNASS-DSGRTH 3631
Cdd:cd19531  306 FRELLARVRETALEAYAHQDLPfekLVE-----ALqperdLSRSPLFQVMFVLQNAPAAALELP---GLTVEPlEVDSGT 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 3632 TNFPLTVVCYPGDD-LGLHLSYDQRYFEAPTVERLLGEFKRLLLALAD 3678
Cdd:cd19531  378 AKFDLTLSLTETDGgLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVA 425
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
3250-3676 1.40e-67

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 236.44  E-value: 1.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3250 VYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIE 3329
Cdd:cd19547    1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3330 FLDWSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGE 3409
Cdd:cd19547   81 LLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 SRPANLPTPPRYRDYIAWLQRQDL--EQSRRWWSESLRGFErPT---LVPSDRpflrehAGESGGMI--VGDRYTRLdaa 3482
Cdd:cd19547  161 GREPQLSPCRPYRDYVRWIRARTAqsEESERFWREYLRDLT-PSpfsTAPADR------EGEFDTVVheFPEQLTRL--- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3483 dgarLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAGqrcTVR 3562
Cdd:cd19547  231 ----VNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQ---TVT 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3563 EWLNRLFERNLELREHEHLPLVAIQE--SSELPKGQPLFDSLFVFENAPvEVSVLDRAQSLNASSDSGRTHTNFPLTVVC 3640
Cdd:cd19547  304 GLLETIHRDLATTAAHGHVPLAQIKSwaSGERLSGGRVFDNLVAFENYP-EDNLPGDDLSIQIIDLHAQEKTEYPIGLIV 382
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15597620 3641 YPGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLAL 3676
Cdd:cd19547  383 LPLQKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQL 418
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
11-554 1.89e-67

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 237.46  E-value: 1.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   11 LVQALRRRAVQEPERLALRFLaeddgeGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGV 89
Cdd:cd05936    1 LADLLEEAARRFPDKTALIFM------GRKLTYRELDALAEAFAAGLQNLgVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   90 IAVPAYPPESARRhhqerLLSIIADAEPRLVLTTADLREpllqmnaQLSAANAPQLlcvdqldpavaeawdEPQVRPEHI 169
Cdd:cd05936   75 VVVPLNPLYTPRE-----LEHILNDSGAKALIVAVSFTD-------LLAAGAPLGE---------------RVALTPEDV 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  170 AFLQYTSGSTALPKGVQVSHGNLVANEVLIRR--GFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPRYfle 247
Cdd:cd05936  128 AVLQYTSGTTGVPKGAMLTHRNLVANALQIKAwlEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLI-PRF--- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  248 RPVRWLEAISQYGGTV-SGGPDfayrLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffac 326
Cdd:cd05936  204 RPIGVLKEIRKHRVTIfPGVPT----MYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEG------ 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  327 YGLAEATlfvtggqrgqgiPALAVdgealarNRIAEG--EGSVlmccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGP 404
Cdd:cd05936  274 YGLTETS------------PVVAV-------NPLDGPrkPGSI----GIPLPGTEVKIVDDD-GEELPPGEVGELWVRGP 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  405 SIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------V 473
Cdd:cd05936  330 QVMKGYWNRPEETAEAF--VDG--WLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHpavaeaavvgV 405
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  474 PSARKG-RVAAFAVTVDGEegigiaaeigrgvqkSVPAQELIDSIRQAVAeAYqEAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd05936  406 PDPYSGeAVKAFVVLKEGA---------------SLTEEEIIAFCREQLA-GY-KVPRQVEFRD--ELPKSAVGKILRRE 466

                 ..
gi 15597620  553 CR 554
Cdd:cd05936  467 LR 468
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1130-1622 4.01e-67

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 236.69  E-value: 4.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:cd05936    1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1210 PDYPSERLAYMLADSGVELLLTqAHLFERLpgaegvtpicldslkLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVG 1289
Cdd:cd05936   81 PLYTPRELEHILNDSGAKALIV-AVSFTDL---------------LAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1290 NTHAALAERLQWMQATY--TLDGDDVLMQKAPV--SFDVSVwECFWPLVTGCRLVLaapgEHR-DPARLVELVRQFGVTT 1364
Cdd:cd05936  145 LTHRNLVANALQIKAWLedLLEGDDVVLAALPLfhVFGLTV-ALLLPLALGATIVL----IPRfRPIGVLKEIRKHRVTI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1365 LHFVPPLLQLFIDEPGVAACG--SLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTETAiNVTHwqCRAEDGERSP- 1441
Cdd:cd05936  220 FPGVPTMYIALLNAPEFKKRDfsSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETS-PVVA--VNPLDGPRKPg 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1442 -IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlyRTGDRARWNADGVLEY 1520
Cdd:cd05936  296 sIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDEDGYFFI 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1521 LGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMV 1599
Cdd:cd05936  368 VDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGEAVKAFVVLKEGASLTEEE---IIAFCREQLAGYKV 444
                        490       500
                 ....*....|....*....|...
gi 15597620 1600 PTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05936  445 PRQVEFRDELPKSAVGKILRREL 467
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
3250-3679 7.67e-67

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 233.34  E-value: 7.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3250 VYPLTPMQEGLLLHTLLEPGTGIYYMqdRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPgrtriE 3329
Cdd:cd19545    1 IYPCTPLQEGLMALTARQPGAYVGQR--VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKE-----S 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3330 FLDWSELPEdgheerLQALHKREREAGFDLLeQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSAlge 3409
Cdd:cd19545   74 PISWTESTS------LDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 srpANLPTPPRYRDYIAWLQRQDLEQSRRWWSESLRGferptLVPSDRPFLrehagesggmIVGDRYTRLDAADGARLRE 3489
Cdd:cd19545  144 ---EPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAG-----LDPAVFPPL----------PSSRYQPRPDATLEHSISL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3490 LAQ-RYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLFINSIPLRVQmpaAGQRCTVREWLNRL 3568
Cdd:cd19545  206 PSSaSSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVR---IDPEQSVEDFLQTV 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3569 FERNLELREHEHLPLVAIQESSELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTVVCYP-GDDLG 3647
Cdd:cd19545  283 QKDLLDMIPFEHTGLQNIRRLGPDARAACNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFSSYGLTLECQLsGSGLR 362
                        410       420       430
                 ....*....|....*....|....*....|..
gi 15597620 3648 LHLSYDQRYFEAPTVERLLGEFKRLLLALADG 3679
Cdd:cd19545  363 VRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
1130-1622 4.33e-66

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 235.06  E-value: 4.33e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1210 PDYPSERLAYMLADSGVELLLTQAHLFERL-----------------------PGAEGVTPICLDSLKldNWPSQAPGLH 1266
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTSSERLDLLhpalpgchdlrtliivgdpahasEGHPGEEPASWPKLL--ALGDADPPHP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1267 LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAapgE 1346
Cdd:TIGR03098  160 VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH---D 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1347 HRDPARLVELVRQFGVTTLHFVPPL-LQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTEtAI 1425
Cdd:TIGR03098  237 YLLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AF 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1426 NVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGERLYR 1505
Cdd:TIGR03098  316 RSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1506 T----GDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEA 1580
Cdd:TIGR03098  396 LavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAIVLVVTPPGGEELDR 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 15597620   1581 EQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:TIGR03098  476 AA---LLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
676-1097 4.85e-66

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 232.21  E-value: 4.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  676 PQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVD 755
Cdd:cd20484    3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  756 LAALAEHERAAAAAQRREAeaqqPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQP 835
Cdd:cd20484   83 ISSLKESEIIAYLREKAKE----PFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  836 ADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAAL 915
Cdd:cd20484  159 PTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFAR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  916 DHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQA 995
Cdd:cd20484  239 SQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  996 NQDLPF-----DQVLAACGQGGQLFQVLF---NHQQRdlSALRRLPGLLADELPW------HsREAKFDLQLQS-EEDAr 1060
Cdd:cd20484  319 HAAYPFpamvrDLNIPRSQANSPVFQVAFfyqNFLQS--TSLQQFLAEYQDVLSIefvegiH-QEGEYELVLEVyEQED- 394
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15597620 1061 gRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd20484  395 -RFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK12316 PRK12316
peptide synthase; Provisional
23-975 5.43e-65

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 248.33  E-value: 5.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    23 PERLALRFLAEDdgegvvLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpesar 101
Cdd:PRK12316  525 PEAPALAFGEET------LDYAELNRRANRLAHALIERGVGPDVLVgVAMERSIEMVVALLAILKAGGAYVPLDP----- 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   102 RHHQERLLSIIADAEPRLVLTTADLrEPLLQMNAQLsaanapQLLCVDQLDPAVAEAWDEP---QVRPEHIAFLQYTSGS 178
Cdd:PRK12316  594 EYPAERLAYMLEDSGVQLLLSQSHL-GRKLPLAAGV------QVLDLDRPAAWLEGYSEENpgtELNPENLAYVIYTSGS 666
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   179 TALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPRYFLErPVRWLEAISQ 258
Cdd:PRK12316  667 TGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKLVELINR 744
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   259 YGGTVSGGPDFAYR--LCSERVAE-SALQRLDLSGwrvafsgsEPIRQDSLERFAEKFAASRfdassFFACYGLAEATLF 335
Cdd:PRK12316  745 EGVDTLHFVPSMLQafLQDEDVAScTSLRRIVCSG--------EALPADAQEQVFAKLPQAG-----LYNLYGPTEAAID 811
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   336 VTggqrgqgipalavdgealARNRIAEGEGSVLMccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPE 415
Cdd:PRK12316  812 VT------------------HWTCVEEGGDSVPI--GRPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHGRPG 870
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   416 ASAKAFVER---DGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKGRVAAfavtVDGE 491
Cdd:PRK12316  871 LTAERFVPSpfvAGERMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLL-EHPWVREAAVLA----VDGK 945
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   492 EGIG-IAAEIGRGVQKSVPAQELIDSIRQAVAEAYqeapkvvaLLNPGALPKTSSGKLQRSAcrLRLEDGSldsyalfpg 570
Cdd:PRK12316  946 QLVGyVVLESEGGDWREALKAHLAASLPEYMVPAQ--------WLALERLPLTPNGKLDRKA--LPAPEAS--------- 1006
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   571 lQAVQEAQPPAGDDEllARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSlGVALDLRQLFEAPTLQAFsA 650
Cdd:PRK12316 1007 -VAQQGYVAPRNALE--RTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSL-A 1081
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   651 TVARQLAAGLPAEAPMAHlprgvDLPQSAAQQrlWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRT 730
Cdd:PRK12316 1082 LVAKAGQATAADQGPASG-----EVALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRL 1154
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   731 RFLERDGAALQRIDER--GEFAWQfvdlaalaEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHH 808
Cdd:PRK12316 1155 RFREEDGGWQQAYAAPqaGEVLWQ--------RQAASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHH 1226
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   809 IVADGWSLNLLLDEFSRLYAEACGGQPAdlaplelHYAEFAAW-QRQWLDAGEGARQLAYWRERLGDTAPvlELATDHPR 887
Cdd:PRK12316 1227 LVVDGVSWRILLEDLQRAYADLDADLPA-------RTSSYQAWaRRLHEHAGARAEELDYWQAQLEDAPH--ELPCENPD 1297
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   888 TARQASPAARYSLRVD-EALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRL-ETQGL---VGF 962
Cdd:PRK12316 1298 GALENRHERKLELRLDaERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLfEDIDLsrtVGW 1377
                         970
                  ....*....|...
gi 15597620   963 FINTLVLRGTPRA 975
Cdd:PRK12316 1378 FTSLFPVRLTPAA 1390
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1132-1622 5.91e-64

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 230.38  E-value: 5.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDG-----GSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYV 1206
Cdd:COG0365   13 NCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1207 PLDPDYPSERLAYMLADSGVELLLTQAHLFER----------------LPGAEGVtpICLD----SLKLDNW-------- 1258
Cdd:COG0365   93 PVFPGFGAEALADRIEDAEAKVLITADGGLRGgkvidlkekvdealeeLPSLEHV--IVVGrtgaDVPMEGDldwdella 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1259 --PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA-LAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFW-PLV 1334
Cdd:COG0365  171 aaSAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYgPLL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1335 TGCRLVL--AAPGeHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACG----SLRRLFSGGEALPAELRNRVLQR 1408
Cdd:COG0365  251 NGATVVLyeGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydlsSLRLLGSAGEPLNPEVWEWWYEA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1409 LpAVALHNRYGPTET----AINVTHWQCRAedGErspIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGG--LGLARGYLG 1482
Cdd:COG0365  330 V-GVPIVDGWGQTETggifISNLPGLPVKP--GS---MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWN 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1483 RPalsaERFvADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA 1562
Cdd:COG0365  404 DP----ERY-RETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV---GVP 475
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 1563 ----GSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:COG0365  476 deirGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
2187-2691 1.65e-63

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 227.74  E-value: 1.65e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2187 TLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL 2266
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2267 DPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVA--RWCLEEDGPALDAEDPAPLAALSGPQHQ----------- 2333
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHdlRTLIIVGDPAHASEGHPGEEPASWPKLLalgdadpphpv 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2334 -----AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLraQGQW 2408
Cdd:TIGR03098  161 idsdmAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVL--HDYL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2409 GAEEICELIRAEGVSILGFTPSYGSQLAQ--WLESQGRQLpvRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETvv 2486
Cdd:TIGR03098  239 LPRDVLKALEKHGITGLAAVPPLWAQLAQldWPESAAPSL--RYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEA-- 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2487 MPLACLAPERLEEGAASvpIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGR 2566
Cdd:TIGR03098  315 FRSTYLPPEEVDRRPDS--IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELH 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2567 LYRT----GDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP-SGKQLAgyvasAVAEQ 2641
Cdd:TIGR03098  393 LPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPtLGQAIV-----LVVTP 467
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 15597620   2642 DEDAQAAlREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPA 2691
Cdd:TIGR03098  468 PGGEELD-RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
34-549 3.96e-63

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 225.55  E-value: 3.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   34 DDGEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESAR--RHHqerlls 110
Cdd:cd05911    4 DADTGKELTYAQLRTLSRRLAAGlRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADelAHQ------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  111 iIADAEPRLVLTTADLREPLLQMNAQLS--------AANAPQLLCVDQLDPAV--AEAWDEPQVR---PEHIAFLQYTSG 177
Cdd:cd05911   78 -LKISKPKVIFTDPDGLEKVKEAAKELGpkdkiivlDDKPDGVLSIEDLLSPTlgEEDEDLPPPLkdgKDDTAAILYSSG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  178 STALPKGVQVSHGNLVANEVLIRRGFG--IGADDVIVSWLPLYHDMGLIGGLLQPIFsGVPcVLMSPRYFlerPVRWLEA 255
Cdd:cd05911  157 TTGLPKGVCLSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLN-GAT-VIIMPKFD---SELFLDL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  256 ISQYGGTVSG-GPDFAYRLcservAESA-LQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASsffacYGLAEAT 333
Cdd:cd05911  232 IEKYKITFLYlVPPIAAAL-----AKSPlLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQG-----YGMTETG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  334 LFVTggqrgqgipaLAVDGEalarnriaEGEGSvlmcCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRN 413
Cdd:cd05911  302 GILT----------VNPDGD--------DKPGS----VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNN 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  414 PEASAKAFVErDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIErTVESEVPsarkgRVAAFAVtvdgee 492
Cdd:cd05911  360 PEATKETFDE-DG--WLHTGDIGYFDeDGYLYIVDRKKELIKYKGFQVAPAELE-AVLLEHP-----GVADAAV------ 424
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  493 gIGIAAEIG---------RGVQKSVPAQELIDSIRQAVAEAYQeapkvvalLNPG-----ALPKTSSGKLQ 549
Cdd:cd05911  425 -IGIPDEVSgelprayvvRKPGEKLTEKEVKDYVAKKVASYKQ--------LRGGvvfvdEIPKSASGKIL 486
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
676-1096 1.39e-61

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 219.44  E-value: 1.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  676 PQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVD 755
Cdd:cd20483    3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  756 LAALAEHERAAAAAQRREAEAqqPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLY-AEACGGQ 834
Cdd:cd20483   83 LSEAADPEAALDQLVRNLRRQ--ELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdALRAGRD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  835 PADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRERLGD---TAPVLELATDHPRTARQASpAARYSLRVDEALARAIR 911
Cdd:cd20483  161 LATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipdASKLLPFAKAERPPVKDYE-RSTVEATLDKELLARMK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  912 EAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATL 991
Cdd:cd20483  240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  992 GAQANQDLPFDQVLAACG-----QGGQLFQVLFNHQqrdlsalrrLPGLLA-------DELPWHSREAK--FDLQLQSEE 1057
Cdd:cd20483  320 EAYEHSAVPFDYIVDALDvprstSHFPIGQIAVNYQ---------VHGKFPeydtgdfKFTDYDHYDIPtaCDIALEAEE 390
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 15597620 1058 DARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAED 1096
Cdd:cd20483  391 DPDGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIRD 429
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1134-1618 1.55e-61

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 219.40  E-value: 1.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1134 LERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYP 1213
Cdd:cd17631    1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1214 SERLAYMLADSGVELLLtqahlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHA 1293
Cdd:cd17631   81 PPEVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1294 ALAERLQWMQATYTLDGDDVLMQKAPVsFDVSVWECFWP--LVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPPL 1371
Cdd:cd17631  122 NLLWNAVNALAALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLVPTM 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1372 LQLFIDEPGVA--ACGSLRRLFSGGEALPAELRNRVLQRlpAVALHNRYGPTETAINVThwQCRAEDGERSP--IGRPLG 1447
Cdd:cd17631  198 IQALLQHPRFAttDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVT--FLSPEDHRRKLgsAGRPVF 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1448 NVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlyRTGDRARWNADGVLEYLGRLDQQ 1527
Cdd:cd17631  274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDM 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1528 VKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQL 1603
Cdd:cd17631  346 IISGGENVYPAEVEDVLYEHPAVAEVAVI---GVPdekwGEAVVAVVVPRPGAELDEDE---LIAHCRERLARYKIPKSV 419
                        490
                 ....*....|....*
gi 15597620 1604 MRLAQMPLGPSGKLD 1618
Cdd:cd17631  420 EFVDALPRNATGKIL 434
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
4-930 2.34e-61

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 234.37  E-value: 2.34e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    4 AFELPTTLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFF 82
Cdd:COG1020  471 PYPADATLHELFEAQAARTPDAVAVVF------GDQSLTYAELNARANRLAHHlRALGVGPGDLVGVCLERSLEMVVALL 544
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   83 GCLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLVLTTADLREPLlqmnaqlsAANAPQLLCVDQLDPAVAEAW 159
Cdd:COG1020  545 AVLKAGAAYVPldpAYP--------AERLAYMLEDAGARLVLTQSALAARL--------PELGVPVLALDALALAAEPAT 608
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  160 D-EPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPCV 238
Cdd:COG1020  609 NpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATLV 687
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  239 LMSPRYFLErPVRWLEAISQYGGTVSGGPDFAYRLCSERVAEsalqrlDLSGWRVAFSGSEPIRQDSLERFAEKFAASRF 318
Cdd:COG1020  688 LAPPEARRD-PAALAELLARHRVTVLNLTPSLLRALLDAAPE------ALPSLRLVLVGGEALPPELVRRWRARLPGARL 760
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  319 dassfFACYGLAEATLFVTggqrgqgipALAVDGEALARNRIAegegsvlmcCGRSQPEHAVLIVDAAsGEVLGDDNVGE 398
Cdd:COG1020  761 -----VNLYGPTETTVDST---------YYEVTPPDADGGSVP---------IGRPIANTRVYVLDAH-LQPVPVGVPGE 816
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  399 IWAAGPSIAHGYWRNPEASAKAFVE----RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVeSEV 473
Cdd:COG1020  817 LYIGGAGLARGYLNRPELTAERFVAdpfgFPGARLYRTGDLArWLPDGNLEFLGRADDQVKIRGFRIELGEIEAAL-LQH 895
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  474 PSarkgrVAAFAVTVDGEEGIG--IAAEIGRGVQKSVPAQELidsiRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRS 551
Cdd:COG1020  896 PG-----VREAVVVAREDAPGDkrLVAYVVPEAGAAAAAALL----RLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  552 acrlrledgsldsyALFPGLQAVQEAQPPAGDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLG 631
Cdd:COG1020  967 --------------ALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  632 VALDLRQLFEAPTLQAFSATVARQLAAGLPAEAPMAHLPRGvdLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDE 711
Cdd:COG1020 1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLP--PLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  712 AALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPLLRVS 791
Cdd:COG1020 1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  792 LVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGARQLAYWRER 871
Cdd:COG1020 1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALA 1270
                        890       900       910       920       930
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  872 LGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQ 930
Cdd:COG1020 1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
2191-2689 2.90e-61

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 222.68  E-value: 2.90e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2191 LFAARVAASPQAPALTFAG-----QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVP 2265
Cdd:COG0365   14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2266 LDPEYPLERLQYMIEDSGVRLLLSHAALF-------------EALGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQ- 2331
Cdd:COG0365   94 VFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkekvdEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAAs 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2332 -----------HQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAEDceLHFY-----------SInfdaase 2388
Cdd:COG0365  174 aefepeptdadDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGD--VFWCtadigwatghsYI------- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2389 rLLAPLLCGARVVL--RAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP---VRMCITGGEALTGEHL 2463
Cdd:COG0365  245 -VYGPLLNGATVVLyeGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlssLRLLGSAGEPLNPEVW 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2464 QRIRQAF-APasFFNAYGPTETVVMPLACLAPERLEEGAASVPigsVVGARVAyILDADLALVPQGATGELYVGGA--GL 2540
Cdd:COG0365  324 EWWYEAVgVP--IVDGWGQTETGGIFISNLPGLPVKPGSMGKP---VPGYDVA-VVDEDGNPVPPGEEGELVIKGPwpGM 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2541 ARGYHERPALSAERFvpdpFAAEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVL 2620
Cdd:COG0365  398 FRGYWNDPERYRETY----FGRFPG-WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2621 ALDSPSGKQ-LAGYVasaVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:COG0365  473 GVPDEIRGQvVKAFV---VLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1725-2155 3.46e-61

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 218.50  E-value: 3.46e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1725 REQPVPLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLH 1804
Cdd:cd19546    1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1805 MDWQDFSALDRDsrqqhLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAF 1884
Cdd:cd19546   81 PELPVVPATEEE-----LPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGAR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1885 LDDRESPLEPLPVQYLDYSVWQREWLeSGERQR------QLDYWKAQLGNEHPLLELPGDRPRPPVQSHQGDLYRFDLSP 1958
Cdd:cd19546  156 REGRAPERAPLPLQFADYALWERELL-AGEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1959 ELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRI-RPESEGLIGAFLNTQVLRCRLDGQMSVGELL 2037
Cdd:cd19546  235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELL 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2038 EQVRQTVIDGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNV-----QRWEfqqTRQLAGMTVEYIANDARATKFDLNL 2112
Cdd:cd19546  315 GRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVrdddnDPWD---APELPGLRTSPVPLGTEAMELDLSL 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 15597620 2113 EVTDLDQRLGC------CLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19546  392 ALTERRNDDGDpdgldgSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
691-1097 4.92e-61

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 217.46  E-value: 4.92e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  691 DPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFL-ERDGAALQRIDERGEFAWQFVDLAALAEHERAAAAA 769
Cdd:cd19543   18 DPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRELDLSHLSEAEQEAELE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  770 QRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLElHYAEFA 849
Cdd:cd19543   98 ALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVR-PYRDYI 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  850 AW-QRQWLDAGEgarqlAYWRERLG---DTAPvleLATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWL 925
Cdd:cd19543  177 AWlQRQDKEAAE-----AYWREYLAgfeEPTP---LPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVV 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  926 LAAFQALLHRHSGQGEIRIGVPSANRQrLETQGL---VGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFD 1002
Cdd:cd19543  249 QGAWALLLSRYSGRDDVVFGTTVSGRP-AELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHEYVPLY 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1003 QVLAACGQGGQLFQ--VLFNHQQRDLSALRRLPGLLADELPWHSREA-KFDLQLQSEEDarGRLTLNFDYAADLFDEASI 1079
Cdd:cd19543  328 EIQAWSEGKQALFDhlLVFENYPVDESLEEEQDEDGLRITDVSAEEQtNYPLTVVAIPG--EELTIKLSYDAEVFDEATI 405
                        410
                 ....*....|....*...
gi 15597620 1080 RRFAAQYLELLRQVAEDP 1097
Cdd:cd19543  406 ERLLGHLRRVLEQVAANP 423
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
2191-2689 4.10e-60

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 216.28  E-value: 4.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2191 LFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:cd05936    4 LLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2271 PLERLQYMIEDSGVRLLLSHAAlFEALGELPAGVARWcleedgPALDAEDPaplaalsgpqhqAYLIYTSGSTGKPKGVA 2350
Cdd:cd05936   84 TPRELEHILNDSGAKALIVAVS-FTDLLAAGAPLGER------VALTPEDV------------AVLQYTSGTTGVPKGAM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2351 VSHGEIAMHCAAVIECFGMRAEDCELH------FYSINFDAAserLLAPLLCGARVVL--RAQgqwgAEEICELIRAEGV 2422
Cdd:cd05936  145 LTHRNLVANALQIKAWLEDLLEGDDVVlaalplFHVFGLTVA---LLLPLALGATIVLipRFR----PIGVLKEIRKHRV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2423 SILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVvmPLACLAPERLEEGA 2501
Cdd:cd05936  218 TIFPGVPTMYIALLNAPEFKKRDFSsLRLCISGGAPLPVEVAERFEELTG-VPIVEGYGLTETS--PVVAVNPLDGPRKP 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2502 ASV--PIGSVvgarVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVpdpfaaeGGRLyRTGDLVRLCDN 2579
Cdd:cd05936  295 GSIgiPLPGT----EVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-------DGWL-RTGDIGYMDED 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2580 GQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaVAEQDEdaqAALREALKTHLK 2658
Cdd:cd05936  363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpDPYSGEAVKAFV---VLKEGA---SLTEEEIIAFCR 436
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15597620 2659 QQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05936  437 EQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1730-2155 5.13e-60

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 214.16  E-value: 5.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGLHMDWQD 1809
Cdd:cd19533    3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1810 FSAlDRDSRQQHLQTLADSEAHrPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDDRE 1889
Cdd:cd19533   83 LSG-DPDPEGAAQQWMQEDLRK-PLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1890 SPLEPLPvQYLDYSVWQREWLESGERQRQLDYWKAQLGNEHPLLELpgdRPRPPVQSHQGDLYRFDLSPELAERVRRFNA 1969
Cdd:cd19533  161 APPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL---ARRAPGRSLAFLRRTAELPPELTRTLLEAAE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1970 ARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVIDGQS 2049
Cdd:cd19533  237 AHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2050 HQDLPFDHLVEALQppRSAAYNPLFQVMCNVQRWEFQQTRQLAGMTVEYIANDARAtkfDLNLEVTDLD--QRLGCCLTY 2127
Cdd:cd19533  317 HQRYRYEDLRRDLG--LTGELHPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTN---DLSIFVYDRDdeSGLRIDFDA 391
                        410       420
                 ....*....|....*....|....*...
gi 15597620 2128 SRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19533  392 NPALYSGEDLARHQERLLRLLEEAAADP 419
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
162-560 1.10e-59

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 216.56  E-value: 1.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   162 PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVAN-EVLIRRGFGIGADDVIVSWLPLYHDMGLIGgLLQPIFSGVPCVLM 240
Cdd:PRK05851  147 TPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNlRGLNARVGLDAATDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   241 SPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLC---SERVAEsalqrLDLSGWRVAFSGSEPIRQDSLERFAEKFAASR 317
Cdd:PRK05851  226 PTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIgkyARRVSD-----VDLGALRVALNGGEPVDCDGFERFATAMAPFG 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   318 FDASSFFACYGLAEATLFVTGGQRGQGipaLAVDgealarnriaegegSVLMCCGRSQPEHAVL----------IVDAAS 387
Cdd:PRK05851  301 FDAGAAAPSYGLAESTCAVTVPVPGIG---LRVD--------------EVTTDDGSGARRHAVLgnpipgmevrISPGDG 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   388 GEVLGDDNVGEIWAAGPSIAHGYWrnpeasAKAFVERDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIER 467
Cdd:PRK05851  364 AAGVAGREIGEIEIRGASMMSGYL------GQAPIDPDD--WFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIER 435
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   468 tVESEVPSARKGRVAAFAvTVDG--EEGIGIAAEIgRGVQKSVPAQELIdsirQAVAEAYQEAPKVVALLNPGALPKTSS 545
Cdd:PRK05851  436 -VAAQVRGVREGAVVAVG-TGEGsaRPGLVIAAEF-RGPDEAGARSEVV----QRVASECGVVPSDVVFVAPGSLPRTSS 508
                         410
                  ....*....|....*
gi 15597620   546 GKLQRSACRLRLEDG 560
Cdd:PRK05851  509 GKLRRLAVKRSLEAA 523
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2198-2689 2.73e-59

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 214.76  E-value: 2.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2198 ASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQy 2277
Cdd:PRK04813   14 TQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIE- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2278 MIEDSgvrlllSHAALFEALGELPAGVarwcleEDGPALDAEDPAPLAALSGP---QHQ------AYLIYTSGSTGKPKG 2348
Cdd:PRK04813   93 MIIEV------AKPSLIIATEELPLEI------LGIPVITLDELKDIFATGNPydfDHAvkgddnYYIIFTSGTTGKPKG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2349 VAVSHgeiamhcaaviecfgmraeDCELHF---------------------YSinFDAaSERLLAPLLC--GARVVLRAQ 2405
Cdd:PRK04813  161 VQISH-------------------DNLVSFtnwmledfalpegpqflnqapYS--FDL-SVMDLYPTLAsgGTLVALPKD 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2406 GQWGAEEICELIRAEGVSILGFTPSYgSQLAQWLES-QGRQLP----VRMCitgGEALTGEHLQRIRQAFAPASFFNAYG 2480
Cdd:PRK04813  219 MTANFKQLFETLPQLPINVWVSTPSF-ADMCLLDPSfNEEHLPnlthFLFC---GEELPHKTAKKLLERFPSATIYNTYG 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2481 PTE-TVVMPLACLAPERLEEGAaSVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdp 2559
Cdd:PRK04813  295 PTEaTVAVTSIEITDEMLDQYK-RLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF---- 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2560 FAAEGGRLYRTGDLVRLcDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDsPSGK--QLAGYVAsa 2637
Cdd:PRK04813  370 FTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYN-KDHKvqYLIAYVV-- 445
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597620  2638 VAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK04813  446 PKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
3251-3677 3.92e-59

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 211.88  E-value: 3.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3251 YPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEF 3330
Cdd:cd19066    2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3331 LDWSELpeDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGES 3410
Cdd:cd19066   82 IDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3411 RPANLPTPPRYRDYIAWLQRQ----DLEQSRRWWSESLRGFERPTLVPSDRPFLREhAGESGGMIVgdryTRLDAADGAR 3486
Cdd:cd19066  160 KPTLPPPVGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQV-ASYEVLTLE----FFLRSEETKR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3487 LRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPvGMPEMqRTVGLFINSIPLRVQMPAAGqrcTVREWLN 3566
Cdd:cd19066  235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP-DEAVE-DTIGLFLNLLPLRIDTSPDA---TFPELLK 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3567 RLFERNLELREHEHLPLVAIQESS----ELPKGqPLFDSLFVFENAPVEVSVLDrAQSLNASSDSGRTHTNFPLTVVCYP 3642
Cdd:cd19066  310 RTKEQSREAIEHQRVPFIELVRHLgvvpEAPKH-PLFEPVFTFKNNQQQLGKTG-GFIFTTPVYTSSEGTVFDLDLEASE 387
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15597620 3643 G--DDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALA 3677
Cdd:cd19066  388 DpdGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
14-562 1.39e-58

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 214.59  E-value: 1.39e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   14 ALRRRAVQEPERLALRFLAEDdGEGVVLSYRDLD---------LRARSIAAalqahaqlGDRAVLLFPSGPDYVAAFFGC 84
Cdd:COG0365   14 CLDRHAEGRGDKVALIWEGED-GEERTLTYAELRrevnrfanaLRALGVKK--------GDRVAIYLPNIPEAVIAMLAC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   85 LYAGVIAVPAYP---PESarrhhqerLLSIIADAEPRLVLTTADLREP--LLQMNAQLSAA--NAPQL---LCVDQLDPA 154
Cdd:COG0365   85 ARIGAVHSPVFPgfgAEA--------LADRIEDAEAKVLITADGGLRGgkVIDLKEKVDEAleELPSLehvIVVGRTGAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  155 VAEA----WDE-----------PQVRPEHIAFLQYTSGSTALPKGVQVSHGN-LVANEVLIRRGFGIGADDVI-----VS 213
Cdd:COG0365  157 VPMEgdldWDEllaaasaefepEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFwctadIG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  214 WLplyhdMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCsERVAESALQRLDLSGWRV 293
Cdd:COG0365  237 WA-----TGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRAL-MKAGDEPLKKYDLSSLRL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  294 AFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEatlfvTGGQRGQGIPALAVDgealarnriaegEGSvlmcCGR 373
Cdd:COG0365  311 LGSAGEPLNPEVWEWWYEAVGVPIVDG------WGQTE-----TGGIFISNLPGLPVK------------PGS----MGK 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  374 SQPEHAVLIVDAAsGEVLGDDNVGEIWAAG--PSIAHGYWRNPEASAKAFVERDGRTWlRTGDLGFL-RDGELFVTGRLK 450
Cdd:COG0365  364 PVPGYDVAVVDED-GNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGRFPGWY-RTGDGARRdEDGYFWILGRSD 441
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  451 DMLIVRGHNLYPQDIERTVES-----E-----VPSARKG-RVAAFAVTVDGEEgigiaaeigrgvqksvPAQELIDSIRQ 519
Cdd:COG0365  442 DVINVSGHRIGTAEIESALVShpavaEaavvgVPDEIRGqVVKAFVVLKPGVE----------------PSDELAKELQA 505
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620  520 AVAE---AYqEAPKVVALLNpgALPKTSSGKLQRSACRLRLEDGSL 562
Cdd:COG0365  506 HVREelgPY-AYPREIEFVD--ELPKTRSGKIMRRLLRKIAEGRPL 548
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2792-3028 2.64e-57

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 199.88  E-value: 2.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2792 LTPIQHWFFDLpLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRP-----LREQELLW 2866
Cdd:COG4908    1 LSPAQKRFLFL-EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPdadlpLEVVDLSA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2867 HVPVQSFDECAELFAK-AQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPAL 2945
Cdd:COG4908   80 LPEPEREAELEELVAEeASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2946 PAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGGQP--VEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApAAY 3023
Cdd:COG4908  160 PELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPpvLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA-KAH 238

                 ....*
gi 15597620 3024 RTQVN 3028
Cdd:COG4908  239 GATVN 243
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
2334-2685 2.92e-57

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 203.29  E-value: 2.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2334 AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRaqGQWGAEEI 2413
Cdd:cd04433    3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDPEAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2414 CELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVVMPLACL 2492
Cdd:cd04433   81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVATGP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2493 APERLEegaASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfaaEGGrLYRTGD 2572
Cdd:cd04433  160 PDDDAR---KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDG-WYRTGD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2573 LVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLAGYVasavaeQDEDAQAALRE 2651
Cdd:cd04433  229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEwGERVVAVV------VLRPGADLDAE 302
                        330       340       350
                 ....*....|....*....|....*....|....
gi 15597620 2652 ALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLD 2685
Cdd:cd04433  303 ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1130-1628 6.37e-57

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 208.50  E-value: 6.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVELLLTQ-------AHLFERLPGAEGV--------TPICLDSLKLDNW----PSQAPGLHLHGD 1270
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLVDsefvpllAAILPQLPTVRTVivegdgpaAPLAPEVGEYEELlaaaSDTFDFPDIDEN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1271 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFDVSVWE-CFWPLVTGCRLVLaaPGEHrD 1349
Cdd:PRK06187  168 DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGlPYLALMAGAKQVI--PRRF-D 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1350 PARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNrYGPTET---- 1423
Cdd:PRK06187  244 PENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLREFKEKFGIDLVQG-YGMTETspvv 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1424 AINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPA--GVAGELCIGGLGLARGYLGRPALSAERFVADpfsaage 1501
Cdd:PRK06187  323 SVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDGG------- 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1502 rLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAE 1577
Cdd:PRK06187  396 -WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI---GVPdekwGERPVAVVVLKPGAT 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15597620  1578 AEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQ 1628
Cdd:PRK06187  472 LDAKE---LRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAE 519
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1-560 7.34e-57

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 208.12  E-value: 7.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAfelPTTLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLD---------LRARSIAAalqahaqlGDR-AVLL 70
Cdd:PRK06187    1 MQDY---PLTIGRILRHGARKHPDKEAVYF------DGRRTTYAELDervnrlanaLRALGVKK--------GDRvAVFD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    71 FPSgPDYVAAFFGCLYAGVIAVPA---YPPEsarrhhqeRLLSIIADAEPRLVLTTADLREPLLQMNAQL---------- 137
Cdd:PRK06187   64 WNS-HEYLEAYFAVPKIGAVLHPInirLKPE--------EIAYILNDAEDRVVLVDSEFVPLLAAILPQLptvrtviveg 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   138 ---SAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSW 214
Cdd:PRK06187  135 dgpAAPLAPEVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVI 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   215 LPLYHDMGLigGL-LQPIFSGVPCVLmsPRYFLERPVrwLEAISQYGGTVSGG-PDFAYRLCSERVAesalQRLDLSGWR 292
Cdd:PRK06187  215 VPMFHVHAW--GLpYLALMAGAKQVI--PRRFDPENL--LDLIETERVTFFFAvPTIWQMLLKAPRA----YFVDFSSLR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   293 VAFSGSEPIRQDSLERFAEKFAAsrfdasSFFACYGLAEATlfvtggqrgqgiPALAV---DGEALARNRIAegeGSVlm 369
Cdd:PRK06187  285 LVIYGGAALPPALLREFKEKFGI------DLVQGYGMTETS------------PVVSVlppEDQLPGQWTKR---RSA-- 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   370 ccGRSQPEHAVLIVDAAsGEVLGDDN--VGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVT 446
Cdd:PRK06187  342 --GRPLPGVEARIVDDD-GDELPPDGgeVGEIIVRGPWLMQGYWNRPEATAETI--DGG--WLHTGDVGYIdEDGYLYIT 414
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   447 GRLKDMLIVRGHNLYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGEEgigiaaeigrgvqksVPAQELID 515
Cdd:PRK06187  415 DRIKDVIISGGENIYPRELEDALYGHpavaevavigVPDEKWGeRPVAVVVLKPGAT---------------LDAKELRA 479
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 15597620   516 SIRQAVAeAYQeAPKVVALLNpgALPKTSSGKLQRSACRLRLEDG 560
Cdd:PRK06187  480 FLRGRLA-KFK-LPKRIAFVD--ELPRTSVGKILKRVLREQYAEG 520
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
15-550 9.56e-57

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 205.15  E-value: 9.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   15 LRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:cd17631    1 LRRRARRHPDRTALVF------GGRSLTYAELDERVNRLAHAlRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 AYPpesarRHHQERLLSIIADAEPRLVLttadlrepllqmnaqlsaanapqllcvdqldpavaeawDEPqvrpehiAFLQ 173
Cdd:cd17631   75 LNF-----RLTPPEVAYILADSGAKVLF--------------------------------------DDL-------ALLM 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  174 YTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMspRYFleRPVRWL 253
Cdd:cd17631  105 YTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL--RKF--DPETVL 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  254 EAISQYGGTVSGG-PDFAYRLCservAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAAsrfdassFFACYGLAEA 332
Cdd:cd17631  181 DLIERHRVTSFFLvPTMIQALL----QHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVK-------FVQGYGMTET 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  333 TlfvtggqrgqgiPALAVDGEALARNRIaegeGSvlmcCGRSQPEHAVLIVDaASGEVLGDDNVGEIWAAGPSIAHGYWR 412
Cdd:cd17631  250 S------------PGVTFLSPEDHRRKL----GS----AGRPVFFVEVRIVD-PDGREVPPGEVGEIVVRGPHVMAGYWN 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  413 NPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------VPSARKG-R 480
Cdd:cd17631  309 RPEATAAAF--RDG--WFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHpavaevavigVPDEKWGeA 384
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  481 VAAFAVTVDGEEgigiaaeigrgvqksVPAQELIDSIRQAVAeAYQeAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd17631  385 VVAVVVPRPGAE---------------LDEDELIAHCRERLA-RYK-IPKSVEFVD--ALPRNATGKILK 435
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
3864-4226 9.88e-57

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 201.74  E-value: 9.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3864 LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNavaHDPQ 3943
Cdd:cd04433    2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3944 GLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRyPRIGLVNAYGPAECSDDVAF 4020
Cdd:cd04433   79 AALELIEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTVAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4021 FRVDLASTESTylPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgapGERL 4100
Cdd:cd04433  158 GPPDDDARKPG--SVGRPVPGVEVRIV----DPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGW 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4101 YRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGetPRSSADS 4179
Cdd:cd04433  224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVvGVPDPEWGERVVAVVVLR--PGADLDA 301
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 4180 paglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLD 4226
Cdd:cd04433  302 ------------EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1150-1556 3.68e-56

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 205.14  E-value: 3.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1150 DGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELL 1229
Cdd:cd05911    7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1230 LTQAHLFER-LPGAEGVTP----ICLDSL--------KLDNWPSQAPG------LHLHGDNLAYVIYTSGSTGQPKGVGN 1290
Cdd:cd05911   87 FTDPDGLEKvKEAAKELGPkdkiIVLDDKpdgvlsieDLLSPTLGEEDedlpppLKDGKDDTAAILYSSGTTGLPKGVCL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1291 THAALAERLqwMQATYTLDG----DDVLMqkAPVSFDVS--VWECFWPLVTGCRLVLaapgeHR--DPARLVELVRQFGV 1362
Cdd:cd05911  167 SHRNLIANL--SQVQTFLYGndgsNDVIL--GFLPLYHIygLFTTLASLLNGATVII-----MPkfDSELFLDLIEKYKI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1363 TTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHwqcrAEDGERS 1440
Cdd:cd05911  238 TFLYLVPPIAAALAKSPLLDKydLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV----NPDGDDK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1441 P--IGRPLGNVVCRVLDAEFN-LLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGV 1517
Cdd:cd05911  314 PgsVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGY 386
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 15597620 1518 LEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:cd05911  387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVI 425
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
3087-3240 7.26e-56

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 192.10  E-value: 7.26e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3087 PGESIKAIKEQLRAVPHKGLGYGVLRYLADPAvrQAMAALPTAPITFNYLGQFDQSFADALFQPLDQPTGPIHDEQAPLP 3166
Cdd:TIGR01720    2 LGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPE--EKLAASPQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRP 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620   3167 NELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHCLEDGAGGLTPSDFPLAQLSQAQLDAL 3240
Cdd:TIGR01720   80 YALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
3253-3499 4.65e-55

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 193.72  E-value: 4.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3253 LTPMQEGLLLhtlLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMlQVIHKPGRTRIEFLD 3332
Cdd:COG4908    1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPV-QRIDPDADLPLEVVD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3333 WSELPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESRP 3412
Cdd:COG4908   77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3413 ANLPTPPR-YRDYIAWLQRQ----DLEQSRRWWSESLRGFERPTLVPSD--RPFLREHAGESggmivgdRYTRLDAADGA 3485
Cdd:COG4908  157 PPLPELPIqYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDrpRPAVQTFRGAT-------LSFTLPAELTE 229
                        250
                 ....*....|....
gi 15597620 3486 RLRELAQRYQLTVN 3499
Cdd:COG4908  230 ALKALAKAHGATVN 243
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
3252-3677 5.42e-55

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 199.91  E-value: 5.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3252 PLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIEFL 3331
Cdd:cd19539    3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3332 DwsELPEDGHEERLQALHKREREA-GFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGES 3410
Cdd:cd19539   83 D--LSDPDSDRERRLEELLRERESrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3411 RPANLPTPP-RYRDYIAWLQRQD----LEQSRRWWSESLRGFErPTLVPSDRPflrehAGESGGMIVGDRYTRLDAADGA 3485
Cdd:cd19539  161 PAAPLPELRqQYKEYAAWQREALaaprAAELLDFWRRRLRGAE-PTALPTDRP-----RPAGFPYPGADLRFELDAELVA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3486 RLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRpvGMPEMQRTVGLFINSIPLRVQMPAAGqrcTVREWL 3565
Cdd:cd19539  235 ALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGR--NHPRFESTVGFFVNLLPLRVDVSDCA---TFRDLI 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3566 NRLFERNLELREHEHLP---LVAIQESSELPKGQPLFDSLFVFENAPVEvsVLDRAQSLNASSDSG-RTHTNFPLTV-VC 3640
Cdd:cd19539  310 ARVRKALVDAQRHQELPfqqLVAELPVDRDAGRHPLVQIVFQVTNAPAG--ELELAGGLSYTEGSDiPDGAKFDLNLtVT 387
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15597620 3641 YPGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALA 3677
Cdd:cd19539  388 EEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLL 424
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
675-1097 8.58e-55

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 199.13  E-value: 8.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  675 LPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFV 754
Cdd:cd19533    2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  755 DLaaLAEHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQ 834
Cdd:cd19533   82 DL--SGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  835 PADLAPL---------ELHYAEFAAWQrqwldagegaRQLAYWRERLGDTAPVLELAtdhPRTARQASPAARYSLRVDEA 905
Cdd:cd19533  160 PAPPAPFgsfldlveeEQAYRQSERFE----------RDRAFWTEQFEDLPEPVSLA---RRAPGRSLAFLRRTAELPPE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  906 LARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGE 985
Cdd:cd19533  227 LTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  986 AREATLGAQANQDLPFDQVLAACGQGGQ---LFQVLFNHQ--QRDLsalrRLPGLLADELPwHSREAKFDLQLQ-SEEDA 1059
Cdd:cd19533  307 VSRELRSLLRHQRYRYEDLRRDLGLTGElhpLFGPTVNYMpfDYGL----DFGGVVGLTHN-LSSGPTNDLSIFvYDRDD 381
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597620 1060 RGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19533  382 ESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1130-1624 2.09e-54

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 200.90  E-value: 2.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK07656    7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVELLLTQAHLF-------ERLPGAEGVTpICLD------SLKLDNWPS---------QAPGlhL 1267
Cdd:PRK07656   87 TRYTADEAAYILARGDAKALFVLGLFLgvdysatTRLPALEHVV-ICETeeddphTEKMKTFTDflaagdpaeRAPE--V 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1268 HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFDVSVWECFW--PLVTGCRLVlaaPG 1345
Cdd:PRK07656  164 DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATIL---PL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1346 EHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC--GSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTET 1423
Cdd:PRK07656  240 PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEdlSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1424 AINVTHwqCRAEDGERSP---IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaag 1500
Cdd:PRK07656  320 SGVTTF--NRLDDDRKTVagtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW---- 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1501 erLYrTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQL--VG--YYTGAVGA 1576
Cdd:PRK07656  394 --LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI---GVPDERLgeVGkaYVVLKPGA 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 15597620  1577 EAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK07656  468 ELTEEE---LIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
3250-3647 2.12e-54

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 197.66  E-value: 2.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3250 VYPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGRTRIE 3329
Cdd:cd19544    1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3330 FLDWSelPEDGHEERLQALHKREReAGFDLlEQPPfhlrLIRL------GEARYWFMMSNHHILIDAWCRGLLMNdffEI 3403
Cdd:cd19544   81 ELTLD--PGDDALAQLRARFDPRR-YRLDL-RQAP----LLRAhvaedpANGRWLLLLLFHHLISDHTSLELLLE---EI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3404 ySALGESRPANLPTPPRYRDYIAWLQRQ-DLEQSRRWWSESLRGFERPTLvpsdrPFLREHAGESGGMIVGDRYTrLDAA 3482
Cdd:cd19544  150 -QAILAGRAAALPPPVPYRNFVAQARLGaSQAEHEAFFREMLGDVDEPTA-----PFGLLDVQGDGSDITEARLA-LDAE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3483 DGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGvTV-AGRPVGMPEMQRTVGLFINSIPLRVQMpaagQRCTV 3561
Cdd:cd19544  223 LAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTLPLRVRL----GGRSV 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3562 REWLNRLFERNLELREHEHLPLVAIQESSELPKGQPLFDSLFVFENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTV-Vc 3640
Cdd:cd19544  298 REAVRQTHARLAELLRHEHASLALAQRCSGVPAPTPLFSALLNYRHSAAAAAAAALAAWEGIELLGGEERTNYPLTLsV- 376

                 ....*..
gi 15597620 3641 ypgDDLG 3647
Cdd:cd19544  377 ---DDLG 380
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2791-3214 2.25e-53

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 195.32  E-value: 2.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2791 ALTPIQHWFFDLPLAR--REHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHV 2868
Cdd:cd19066    3 PLSPMQRGMWFLKKLAtdPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEII 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2869 PVQSFDEC-----AELFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQfAEGAEP 2943
Cdd:cd19066   83 DLRNLADPearllELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDA-AERQKP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2944 ALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGG--QPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApA 3021
Cdd:cd19066  162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGlpPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA-R 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3022 AYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREalfdDIDLTRSVGWFTSAYPLRL--TPAQSPGESIKAIKEQLR 3099
Cdd:cd19066  241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP----DEAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQSR 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3100 AVPHKGLGYGVLRYLADPAVRQAmAALPTAPITFNYLGQFDQSfadaLFQPLDQPTGPIH--DEQAP--LPNELSVDGQv 3175
Cdd:cd19066  317 EAIEHQRVPFIELVRHLGVVPEA-PKHPLFEPVFTFKNNQQQL----GKTGGFIFTTPVYtsSEGTVfdLDLEASEDPD- 390
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 15597620 3176 ygGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHC 3214
Cdd:cd19066  391 --GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
35-550 5.17e-53

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 196.38  E-value: 5.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   35 DGEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPPESARRhhqerlls 110
Cdd:cd05926    9 PGSTPALTYADLAELVDDLARQLAALgIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPlnpAYKKAEFEF-------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  111 IIADAEPRLVLTTADLREPLLQMNAQLSAA------------NAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGS 178
Cdd:cd05926   81 YLADLGSKLVLTPKGELGPASRAASKLGLAilelaldvgvliRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  179 TALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGvPCVLMSPRYfleRPVRWLEAISQ 258
Cdd:cd05926  161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAG-GSVVLPPRF---SASTFWPDVRD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  259 YGGT-VSGGPDFAYRLCS--ERVAESALQRLdlsgwRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLF 335
Cdd:cd05926  237 YNATwYTAVPTIHQILLNrpEPNPESPPPKL-----RFIRSCSASLPPAVLEALEATFGAPVLEA------YGMTEAAHQ 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  336 VTGgqrgqgipalavdgealarNRIAEGE---GSVlmccGRSQ-PEhaVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYW 411
Cdd:cd05926  306 MTS-------------------NPLPPGPrkpGSV----GKPVgVE--VRILDED-GEILPPGVVGEICLRGPNVTRGYL 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  412 RNPEASAKAFvERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVES--EVPSArkgrvAAFAVTV 488
Cdd:cd05926  360 NNPEANAEAA-FKDG--WFRTGDLGYLdADGYLFLTGRIKELINRGGEKISPLEVDGVLLShpAVLEA-----VAFGVPD 431
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  489 D--GEEgigIAAEIGRGVQKSVPAQELIDSIRQAVAeAYqEAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd05926  432 EkyGEE---VAAAVVLREGASVTEEELRAFCRKHLA-AF-KVPKKVYFVD--ELPKTATGKIQR 488
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
9-549 2.59e-52

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 195.56  E-value: 2.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFLaeddgeGVVLSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLY 86
Cdd:PRK08314   10 TSLFHNLEVSARRYPDKTAIVFY------GRAISYRELLEEAERLAGylQQECGVRKGDRVLLYMQNSPQFVIAYYAILR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    87 AGVIAVPAYPPESArrhhqERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANA-----------------PQLLCV- 148
Cdd:PRK08314   84 ANAVVVPVNPMNRE-----EELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVivaqysdylpaepeiavPAWLRAe 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   149 ---DQLDPAVAEAWDEP----------QVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWL 215
Cdd:PRK08314  159 pplQALAPGGVVAWKEAlaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   216 PLYHDMGLIGGLLQPIFSGVPCVLMSpryflerpvRW-----LEAISQYGGTVSGGP-----DFayrLCSERVAESalqr 285
Cdd:PRK08314  239 PLFHVTGMVHSMNAPIYAGATVVLMP---------RWdreaaARLIERYRVTHWTNIptmvvDF---LASPGLAER---- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   286 lDLSGWRVAFSGSEPIRQDSLERFAEKFAAsrfdasSFFACYGLAEATLFVTGGQRGQ------GIPALAVDgealARnr 359
Cdd:PRK08314  303 -DLSSLRYIGGGGAAMPEAVAERLKELTGL------DYVEGYGLTETMAQTHSNPPDRpklqclGIPTFGVD----AR-- 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   360 iaegegsvlmccgrsqpehavlIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFL- 438
Cdd:PRK08314  370 ----------------------VIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEIDGKRFFRTGDLGRMd 427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   439 RDGELFVTGRLKDMLIVRGHNLYPQDIERTV-------ESEV---PSARKG-RVAAFAVTVDGEEGigiaaeigrgvqkS 507
Cdd:PRK08314  428 EEGYFFITDRLKRMINASGFKVWPAEVENLLykhpaiqEACViatPDPRRGeTVKAVVVLRPEARG-------------K 494
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 15597620   508 VPAQELIDSIRQAVAeAYqEAPKVVALLNpgALPKTSSGKLQ 549
Cdd:PRK08314  495 TTEEEIIAWAREHMA-AY-KYPRIVEFVD--SLPKSGSGKIL 532
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
2185-2689 3.85e-52

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 194.25  E-value: 3.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2185 QDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYV 2264
Cdd:PRK06187    5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2265 PLDPEYPLERLQYMIEDSGVRLLL---SHAALFEALGELPAGVARWCLEEDGPA-------------LDAEDPAPLAALS 2328
Cdd:PRK06187   85 PINIRLKPEEIAYILNDAEDRVVLvdsEFVPLLAAILPQLPTVRTVIVEGDGPAaplapevgeyeelLAAASDTFDFPDI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2329 GPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLraQGQW 2408
Cdd:PRK06187  165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVI--PRRF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2409 GAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVvm 2487
Cdd:PRK06187  243 DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFsSLRLVIYGGAALPPALLREFKEKFG-IDLVQGYGMTETS-- 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2488 PLACLAPERLEEGAASVPIGSV------VGARvayILDADLALVP--QGATGELYVGGAGLARGYHERPALSAERFVPDp 2559
Cdd:PRK06187  320 PVVSVLPPEDQLPGQWTKRRSAgrplpgVEAR---IVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG- 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2560 faaeggrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaV 2638
Cdd:PRK06187  396 -------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDEKWGERPVAVV---V 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15597620  2639 AEQDEDAQAalrEALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK06187  466 LKPGATLDA---KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
1153-1622 4.52e-52

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 192.30  E-value: 4.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ 1232
Cdd:cd17654   16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 AHLferlpgaegvtpiclDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDD 1312
Cdd:cd17654   96 KEL---------------DNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1313 VLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVE-LVRQFGVTTLHFVPPLLQLF----IDEPGVAACGSL 1387
Cdd:cd17654  161 ILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFgsqsIKSTVLSATSSL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1388 RRLFSGGEALPAELRNRVL-QRLPAVALHNRYGPTETAINVTHWQCRAEDGErSPIGRPLGNVVCRVLDAEFNllpaGVA 1466
Cdd:cd17654  241 RVLALGGEPFPSLVILSSWrGKGNRTRIFNIYGITEVSCWALAYKVPEEDSP-VQLGSPLLGTVIEVRDQNGS----EGT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1467 GELCIGglGLARGYlgrpalsaerFVADPFSAAGERLYRTGDRARwNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLA 1546
Cdd:cd17654  316 GQVFLG--GLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 1547 QPGVAQAVVVIREgvaGSQLVGYYtgaVGAEAEAEQNQRLRAALQA--ELPEYMVptqlmRLAQMPLGPSGKLDTRAL 1622
Cdd:cd17654  383 CLGVESCAVTLSD---QQRLIAFI---VGESSSSRIHKELQLTLLSshAIPDTFV-----QIDKLPLTSHGKVDKSEL 449
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
2195-2686 1.73e-51

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 190.13  E-value: 1.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2195 RVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLER 2274
Cdd:cd17631    4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2275 LQYMIEDSGVRLLLshaalfealgelpagvarwcleedgpaldaEDPAplaalsgpqhqaYLIYTSGSTGKPKGVAVSHG 2354
Cdd:cd17631   84 VAYILADSGAKVLF------------------------------DDLA------------LLMYTSGTTGRPKGAMLTHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2355 EIAMHCAAVIECFGMRAEDCELHFYSI-NFDAASERLLAPLLCGARVVLRAqgQWGAEEICELIRAEGVSILGFTPSYGS 2433
Cdd:cd17631  122 NLLWNAVNALAALDLGPDDVLLVVAPLfHIGGLGVFTLPTLLRGGTVVILR--KFDPETVLDLIERHRVTSFFLVPTMIQ 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2434 QLAQWLESQGRQLP-VRMCITGGEALTgEHLQRIRQAFAPAsFFNAYGPTETVvmPLAC-LAPERLEE--GAASVPigsV 2509
Cdd:cd17631  200 ALLQHPRFATTDLSsLRAVIYGGAPMP-ERLLRALQARGVK-FVQGYGMTETS--PGVTfLSPEDHRRklGSAGRP---V 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2510 VGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfaaEGGrLYRTGDLVRLCDNGQVEYVGRID 2589
Cdd:cd17631  273 FFVEVR-IVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-------RDG-WFHTGDLGRLDEDGYLYIVDRKK 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2590 HQVKIRGFRIELGEIEARLLEHPQVREALVLALdsPSGKQlaGYVASAVAEQDEDAQAALrEALKTHLKQQLPDYMVPAH 2669
Cdd:cd17631  344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGV--PDEKW--GEAVVAVVVPRPGAELDE-DELIAHCRERLARYKIPKS 418
                        490
                 ....*....|....*..
gi 15597620 2670 LLLLASLPLTANGKLDR 2686
Cdd:cd17631  419 VEFVDALPRNATGKILK 435
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
1143-1622 1.76e-51

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 190.19  E-value: 1.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKG-VGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML 1221
Cdd:cd05941    1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1222 ADSGVELLLtqahlferlpgaegvtpicldslkldnwpsqapglhlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQW 1301
Cdd:cd05941   81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1302 MQATYTLDGDDVLMQKAP---VSFDVSVWECfwPLVTGCRLVL-----AAPGEHRDPARLVELVrqFGVTTL-------- 1365
Cdd:cd05941  121 LVDAWRWTEDDVLLHVLPlhhVHGLVNALLC--PLFAGASVEFlpkfdPKEVAISRLMPSITVF--MGVPTIytrllqyy 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1366 HFVPPLLQLFIdepgVAACGSLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTETAINVThwqCRAeDGERSP--IG 1443
Cdd:cd05941  197 EAHFTDPQFAR----AAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMALS---NPL-DGERRPgtVG 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1444 RPLGNVVCRVLDAEFN-LLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLG 1522
Cdd:cd05941  268 MPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILG 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1523 RL-DQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQNqrLRAALQAELPEY 1597
Cdd:cd05941  341 RSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVI---GVPdpdwGERVVAVVVLRAGAAALSLEE--LKEWAKQRLAPY 415
                        490       500
                 ....*....|....*....|....*
gi 15597620 1598 MVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05941  416 KRPRRLILVDELPRNAMGKVNKKEL 440
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1143-1620 2.20e-51

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 192.41  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:PRK07798   18 DRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1223 DSGVELLLTQ-------AHLFERLPGA--------EGVTPICLDSLKLDNWPSQAPGLHL----HGDNLaYVIYTSGSTG 1283
Cdd:PRK07798   98 DSDAVALVYErefaprvAEVLPRLPKLrtlvvvedGSGNDLLPGAVDYEDALAAGSPERDfgerSPDDL-YLLYTGGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1284 QPKGV----GNTHAALAERLQWMQATYTLDGDDVLMQKA----PVSFDVS-------VWECFWPLVTGCRLVLAaPGEHR 1348
Cdd:PRK07798  177 MPKGVmwrqEDIFRVLLGGRDFATGEPIEDEEELAKRAAagpgMRRFPAPplmhgagQWAAFAALFSGQTVVLL-PDVRF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1349 DPARLVELVRQFGVTTLHFV-----PPLLQLfIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTET 1423
Cdd:PRK07798  256 DADEVWRTIEREKVNVITIVgdamaRPLLDA-LEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSET 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1424 AINVTHwqcRAEDGERSPIGRPLG-NVVCRVLDAEFNLLPAGvagelcIGGLG-LAR------GYLGRPALSAERFvadp 1495
Cdd:PRK07798  335 GFGGSG---TVAKGAVHTGGPRFTiGPRTVVLDEDGNPVEPG------SGEIGwIARrghiplGYYKDPEKTAETF---- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1496 FSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYT 1571
Cdd:PRK07798  402 PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV---GVPderwGQEVVAVVQ 478
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 15597620  1572 GAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTR 1620
Cdd:PRK07798  479 LREGARPDLAE---LRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
2194-2619 1.72e-50

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 189.34  E-value: 1.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2194 ARVAAS-PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2272
Cdd:PRK07656   12 ARAARRfGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2273 ERLQYMIEDSGVRLLLSHAAL----FEALGELPAGVARWCLEEDGPA------------LDAEDPAPLAALSGPQHQAYL 2336
Cdd:PRK07656   92 DEAAYILARGDAKALFVLGLFlgvdYSATTRLPALEHVVICETEEDDphtekmktftdfLAAGDPAERAPEVDPDDVADI 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2337 IYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED---CELHFYSiNF--DAAserLLAPLLCGARVVLraQGQWGAE 2411
Cdd:PRK07656  172 LFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylAANPFFH-VFgyKAG---VNAPLMRGATILP--LPVFDPD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2412 EICELIRAEGVSILGFTPS-YGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVvmPLA 2490
Cdd:PRK07656  246 EVFRLIETERITVLPGPPTmYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEAS--GVT 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2491 CLAPerLEEGAASVP--IG-SVVGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaegGRL 2567
Cdd:PRK07656  324 TFNR--LDDDRKTVAgtIGtAIAGVENK-IVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD------GWL 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597620  2568 YrTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALV 2619
Cdd:PRK07656  395 H-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAV 445
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
38-550 2.63e-50

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 188.60  E-value: 2.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   38 GVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR-HHQerllsiIADA 115
Cdd:cd05904   30 GRALTYAELERRVRRLAAGlAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEiAKQ------VKDS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  116 EPRLVLTTADLREPLLQMNAQL---------SAANAPQLLCVDQLDPAVaeawdePQVRPEHIAFLQYTSGSTALPKGVQ 186
Cdd:cd05904  104 GAKLAFTTAELAEKLASLALPVvlldsaefdSLSFSDLLFEADEAEPPV------VVIKQDDVAALLYSSGTTGRSKGVM 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  187 VSHGNLVANEVLIRRGFGIGA--DDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPRYFLErpvRWLEAISQYGgtVS 264
Cdd:cd05904  178 LTHRNLIAMVAQFVAGEGSNSdsEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVM-PRFDLE---ELLAAIERYK--VT 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  265 GGPdFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRfdassFFACYGLAEATlfvtggqrgqG 344
Cdd:cd05904  252 HLP-VVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVD-----LGQGYGMTEST----------G 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  345 IPALAVDGEALARNRiaegeGSvlmcCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVEr 424
Cdd:cd05904  316 VVAMCFAPEKDRAKY-----GS----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK- 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  425 DGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEvPSarkgrVAAFAVT--VDGEEGIGIAAEIG 501
Cdd:cd05904  386 EG--WLHTGDLCYIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSH-PE-----ILDAAVIpyPDEEAGEVPMAFVV 457
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  502 RGVQKSVPAQELIDSIrqavaeAYQEAP--KV--VALLNpgALPKTSSGKLQR 550
Cdd:cd05904  458 RKPGSSLTEDEIMDFV------AKQVAPykKVrkVAFVD--AIPKSPSGKILR 502
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
37-563 5.70e-50

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 189.10  E-value: 5.70e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   37 EGVVLSYRDLDLRARSIAAALQAHAQ--LGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSIIAD 114
Cdd:cd05905   11 EATTLTWGKLLSRAEKIAAVLQKKVGlkPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDIS-----QQLGFLLGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  115 AEPRLVLTT-ADLREPLLQMNAQLSAANAPQLLcvdqLDPAVAEAWDEPQ--------------VRPEHIAFLQYTSGST 179
Cdd:cd05905   86 CKVRVALTVeACLKGLPKKLLKSKTAAEIAKKK----GWPKILDFVKIPKskrsklkkwgphppTRDGDTAYIEYSFSSD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  180 ALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQY 259
Cdd:cd05905  162 GSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTLSQY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  260 GGTVSggpdfayrLCSERVAESALQRL------------DLSGWR---VAFsgSEPIRQDSLERFAEKFAA----SRFDA 320
Cdd:cd05905  242 KVRDA--------YVKLRTLHWCLKDLsstlaslknrdvNLSSLRmcmVPC--ENRPRISSCDSFLKLFQTlglsPRAVS 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  321 SSFFACYGLAEATLFVTGGQRGQGIpalaVDGEALARNRIA-EGEGS----VLMCCGRSQPEHAVLIVDAASGEVLGDDN 395
Cdd:cd05905  312 TEFGTRVNPFICWQGTSGPEPSRVY----LDMRALRHGVVRlDERDKpnslPLQDSGKVLPGAQVAIVNPETKGLCKDGE 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  396 VGEIWAAGPSIAHGYWRNP-EASAKAFVERDGRT--------WLRTGDLGFLRDGE-----------LFVTGRLKDMLIV 455
Cdd:cd05905  388 IGEIWVNSPANASGYFLLDgETNDTFKVFPSTRLstgitnnsYARTGLLGFLRPTKctdlnveehdlLFVVGSIDETLEV 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  456 RGHNLYPQDIERTVESEVPSarKGRVAAFAVTvdgeEGIGIAAEigrgvQKSVPAQELID---SIRQAVAEAYQEAPKVV 532
Cdd:cd05905  468 RGLRHHPSDIEATVMRVHPY--RGRCAVFSIT----GLVVVVAE-----QPPGSEEEALDlvpLVLNAILEEHQVIVDCV 536
                        570       580       590
                 ....*....|....*....|....*....|.
gi 15597620  533 ALLNPGALPKTSSGKLQRSACRLRLEDGSLD 563
Cdd:cd05905  537 ALVPPGSLPKNPLGEKQRMEIRQAFLAGKLH 567
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
1153-1624 7.05e-50

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 187.13  E-value: 7.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ 1232
Cdd:cd05926   14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 -----------AHLFERLPGAEGVTPIC---LDSLKLDNWPS----QAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA 1294
Cdd:cd05926   94 kgelgpasraaSKLGLAILELALDVGVLiraPSAESLSNLLAdkknAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRN 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1295 LAERLQWMQATYTLDGDDVLMQKAPVsFDVS--VWECFWPLVTGCRLVLAApgehR-DPARLVELVRQFGVTTLHFVPPL 1371
Cdd:cd05926  174 LAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVRDYNATWYTAVPTI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1372 LQLFIDEPG---VAACGSLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTETAINVTHWQCRAedGERSP--IGRPL 1446
Cdd:cd05926  249 HQILLNRPEpnpESPPPKLRFIRSCSASLPPAVLEA-LEATFGAPVLEAYGMTEAAHQMTSNPLPP--GPRKPgsVGKPV 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1447 GNVVcRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQ 1526
Cdd:cd05926  326 GVEV-RILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYLDADGYLFLTGRIKE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1527 QVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMR 1605
Cdd:cd05926  398 LINRGGEKISPLEVDGVLLSHPAVLEAVAFgVPDEKYGEEVAAAVVLREGASVTEEE---LRAFCRKHLAAFKVPKKVYF 474
                        490
                 ....*....|....*....
gi 15597620 1606 LAQMPLGPSGKLDTRALPE 1624
Cdd:cd05926  475 VDELPKTATGKIQRRKVAE 493
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
671-1097 9.44e-50

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 184.99  E-value: 9.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  671 RGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRI--DERGE 748
Cdd:cd19546    1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldADAAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  749 FAWQFVdlaalaeHERAAAAAQRREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYA 828
Cdd:cd19546   81 PELPVV-------PATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  829 EACGGQPADLAPLELHYAEFAAWQRQWLdAGEGAR------QLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRV 902
Cdd:cd19546  154 ARREGRAPERAPLPLQFADYALWERELL-AGEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  903 DEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRL-ETQGLVGFFINTLVLRGTPRARQPFAA 981
Cdd:cd19546  233 DAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  982 LLGEAREATLGAQANQDLPFDQVLAACGQGGQ-----LFQVLFNHQQRDLSALR--RLPGLLADELPWHSREAKFDLQL- 1053
Cdd:cd19546  313 LLGRVREAVREARRHQDVPFERLAELLALPPSadrhpVFQVALDVRDDDNDPWDapELPGLRTSPVPLGTEAMELDLSLa 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 1054 ----QSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19546  393 lterRNDDGDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3716-4230 1.29e-49

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 185.46  E-value: 1.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3716 VRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:cd05936    2 ADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3796 GHPTQRLTRIVELSRTLVLVCTQAcreqalalFDELgcvdrprllvwdeIQQGEGAEHDPQVysGPQNLAYVIYTSGSTG 3875
Cdd:cd05936   82 LYTPRELEHILNDSGAKALIVAVS--------FTDL-------------LAAGAPLGERVAL--TPEDVAVLQYTSGTTG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3876 LPKGVMVEQAGMLNNQLSKVPYLE--LDENDVI----------AQTASqsfdisvwqFLAAPLFGARVAIVPNAvahDPQ 3943
Cdd:cd05936  139 VPKGAMLTHRNLVANALQIKAWLEdlLEGDDVVlaalplfhvfGLTVA---------LLLPLALGATIVLIPRF---RPI 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3944 GLLAHVGEQGITVLESVPSLIQGML-AEERQALD--GLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPAECSDDVAF 4020
Cdd:cd05936  207 GVLKEIRKHRVTIFPGVPTMYIALLnAPEFKKRDfsSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAV 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4021 FRVDLASTESTylpIGSP---TDNnRLYllgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapg 4097
Cdd:cd05936  286 NPLDGPRKPGS---IGIPlpgTEV-KIV------DDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-------- 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4098 ERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVP----GETP 4173
Cdd:cd05936  348 DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAV-----------VG--VPdpysGEAV 414
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620 4174 RssadspAGLMVEQGAWF--ERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05936  415 K------AFVVLKEGASLteEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3739-4231 1.30e-49

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 186.95  E-value: 1.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRltRIVELSrtlvlvctq 3818
Cdd:cd17647   21 FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--QNIYLG--------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3819 acreqalalfdelgcVDRPRLLVWDEiqqgegaehDPQVYSGPQNLAYVIYTSGSTGLPKGVmveqagmLNNQLSKVPYL 3898
Cdd:cd17647   90 ---------------VAKPRGLIVIR---------AAGVVVGPDSNPTLSFTSGSEGIPKGV-------LGRHFSLAYYF 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3899 E-------LDENDVIAQTASQSFDiSVWQFLAAPLF-GARVaIVPNAVAHDPQGLLAH-VGEQGITVLESVPSLIQGMLA 3969
Cdd:cd17647  139 PwmakrfnLSENDKFTMLSGIAHD-PIQRDMFTPLFlGAQL-LVPTQDDIGTPGRLAEwMAKYGATVTHLTPAMGQLLTA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3970 EERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYL-------PIGSPTDNn 4042
Cdd:cd17647  217 QATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSDPTFLknlkdvmPAGRGMLN- 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4043 rLYLLGAGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPG---------------------ERLY 4101
Cdd:cd17647  296 -VQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLY 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4102 RTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANG-KYLVGYLVPGETP------- 4173
Cdd:cd17647  375 RTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEePTLVSYIVPRFDKpddesfa 454
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 4174 ------RSSADSPAGLMVEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd17647  455 qedvpkEVSTDPIVKGLIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
3717-4232 1.69e-49

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 186.53  E-value: 1.69e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:TIGR03098    4 HLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3797 HPTQRLTRIVELSRTLVLVcTQACREQALALFDElGCVDRPRLLV------------------WDEIQQGEGAehDPQVY 3858
Cdd:TIGR03098   84 LKAEQVAHILADCNVRLLV-TSSERLDLLHPALP-GCHDLRTLIIvgdpahaseghpgeepasWPKLLALGDA--DPPHP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3859 SGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVaivpnaV 3938
Cdd:TIGR03098  160 VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV------V 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3939 AHD---PQGLLAHVGEQGITVLESVPSL-IQ-GMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAE 4013
Cdd:TIGR03098  234 LHDyllPRDVLKALEKHGITGLAAVPPLwAQlAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4014 CsddvafFRvdlasteSTYLP----------IGSPTDNNRLYLLGagaDDAFELVPlGAVGELCVAGTGVGRGYVGDPLR 4083
Cdd:TIGR03098  314 A------FR-------STYLPpeevdrrpdsIGKAIPNAEVLVLR---EDGSECAP-GEEGELVHRGALVAMGYWNDPEK 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4084 TAQAFVPHPFGAPGERLYRT----GDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGA 4158
Cdd:TIGR03098  377 TAERFRPLPPFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfGVPDPT 456
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620   4159 NGKYLVGYLVPgetPRSSADSPAGLMVEqgawferikqqLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:TIGR03098  457 LGQAIVLVVTP---PGGEELDRAALLAE-----------CRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3726-4227 5.20e-49

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 182.81  E-value: 5.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3726 HPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDpghptQRLTRi 3805
Cdd:cd17631    8 HPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN-----FRLTP- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3806 velsrtlvlvctqacREQALALFDElgcvdRPRLLVWDeiqqgegaehdpqvysgpqnLAYVIYTSGSTGLPKGVMVEQA 3885
Cdd:cd17631   82 ---------------PEVAYILADS-----GAKVLFDD--------------------LALLMYTSGTTGRPKGAMLTHR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3886 GMLNNQLSKVPYLELDENDViaqtasqsfdisvwQFLAAPLF---------------GARVAIVPnavAHDPQGLLAHVG 3950
Cdd:cd17631  122 NLLWNAVNALAALDLGPDDV--------------LLVVAPLFhigglgvftlptllrGGTVVILR---KFDPETVLDLIE 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3951 EQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYPRIglVNAYGPAECSDDVAFFRVDLAs 4027
Cdd:cd17631  185 RHRVTSFFLVPTMIQALLQHPRFAttdLSSLRAVIYGGAPMPERLLRALQARGVKF--VQGYGMTETSPGVTFLSPEDH- 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4028 tESTYLPIGSPTDNNRLYLLGAGADDafelVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgapGERLYRTGDLA 4107
Cdd:cd17631  262 -RRKLGSAGRPVFFVEVRIVDPDGRE----VPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--------RDGWFHTGDLG 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4108 RRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVP----GETPRS--SADSPA 4181
Cdd:cd17631  329 RLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAV-----------IG--VPdekwGEAVVAvvVPRPGA 395
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620 4182 GLMVEQgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDR 4227
Cdd:cd17631  396 ELDEDE------LIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1144-1622 3.01e-48

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 182.57  E-value: 3.01e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1144 RVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLAD 1223
Cdd:cd05959   20 KTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLED 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1224 SGVELLLTQAHLFERLPGA--------------EGVTPICLDSLKLDNWPSQAPGLH---LHGDNLAYVIYTSGSTGQPK 1286
Cdd:cd05959  100 SRARVVVVSGELAPVLAAAltksehtlvvlivsGGAGPEAGALLLAELVAAEAEQLKpaaTHADDPAFWLYSSGSTGRPK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1287 GVGNTHAAlaerLQWMQATYT-----LDGDDVLMQKAPVSFDVSVWE-CFWPLVTGCRLVLAApgEHRDPARLVELVRQF 1360
Cdd:cd05959  180 GVVHLHAD----IYWTAELYArnvlgIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMP--ERPTPAAVFKRIRRY 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1361 GVTTLHFVPPLLQLFIDEPGVAACG--SLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTEtainVTHWQC--RAED 1436
Cdd:cd05959  254 RPTVFFGVPTLYAAMLAAPNLPSRDlsSLRLCVSAGEALPAEVGER-WKARFGLDILDGIGSTE----MLHIFLsnRPGR 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1437 GERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVadpfsaaGErLYRTGDRARWNADG 1516
Cdd:cd05959  329 VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-WTRTGDKYVRDDDG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1517 VLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELP 1595
Cdd:cd05959  401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLA 480
                        490       500
                 ....*....|....*....|....*..
gi 15597620 1596 EYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05959  481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
2203-2689 5.34e-48

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 181.80  E-value: 5.34e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2203 PALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDS 2282
Cdd:cd05959   21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2283 GVRLLLSHAALFEALGELPAG---------VARWCLEEDGPALDAEDPAPLA-----ALSGPQHQAYLIYTSGSTGKPKG 2348
Cdd:cd05959  101 RARVVVVSGELAPVLAAALTKsehtlvvliVSGGAGPEAGALLLAELVAAEAeqlkpAATHADDPAFWLYSSGSTGRPKG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2349 VAVSHGEIAMHC-AAVIECFGMRAEDCELH----FYSINFDAAserLLAPLLCGARVVLRAqGQWGAEEICELIRAEGVS 2423
Cdd:cd05959  181 VVHLHADIYWTAeLYARNVLGIREDDVCFSaaklFFAYGLGNS---LTFPLSVGATTVLMP-ERPTPAAVFKRIRRYRPT 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2424 ILGFTPS-YGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVVMPLACLaPERLEEGAA 2502
Cdd:cd05959  257 VFFGVPTlYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG-LDILDGIGSTEMLHIFLSNR-PGRVRYGTT 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2503 SVPigsVVGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVpdpfaaegGRLYRTGDLVRLCDNGQV 2582
Cdd:cd05959  335 GKP---VPGYEVE-LRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ--------GEWTRTGDKYVRDDDGFY 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2583 EYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGkqLAGYVASAVAEQDEDAQAALREALKTHLKQQLP 2662
Cdd:cd05959  403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG--LTKPKAFVVLRPGYEDSEALEEELKEFVKDRLA 480
                        490       500
                 ....*....|....*....|....*..
gi 15597620 2663 DYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05959  481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
8-554 8.72e-48

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 181.26  E-value: 8.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     8 PTTLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLY 86
Cdd:PRK07656    4 WMTLPELLARAARRFGDKEAYVF------GDQRLTYAELNARVRRAAAALAALgIGKGDRVAIWAPNSPHWVIAALGALK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    87 AGVIAVP---AYPPESARrhhqerllSIIADAEPRLVLTTADLREPLLQMNAQL-------------SAANAPQLLCVDQ 150
Cdd:PRK07656   78 AGAVVVPlntRYTADEAA--------YILARGDAKALFVLGLFLGVDYSATTRLpalehvviceteeDDPHTEKMKTFTD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   151 LDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQP 230
Cdd:PRK07656  150 FLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   231 IFSGVpCVLMSPRYfleRPVRWLEAISQYGGTVSGGPDFAYR--LCSERVAESalqrlDLSGWRVAFSGSEPIRQDSLER 308
Cdd:PRK07656  230 LMRGA-TILPLPVF---DPDEVFRLIETERITVLPGPPTMYNslLQHPDRSAE-----DLSSLRLAVTGAASMPVALLER 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   309 FAEKfaasrFDASSFFACYGLAEATLFVTGGQRGQGipalavdgealaRNRIAegeGSvlmcCGRSQPEHAVLIVDaASG 388
Cdd:PRK07656  301 FESE-----LGVDIVLTGYGLSEASGVTTFNRLDDD------------RKTVA---GT----IGTAIAGVENKIVN-ELG 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   389 EVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAfVERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIER 467
Cdd:PRK07656  356 EEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-IDADG--WLHTGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEE 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   468 -------TVESEV---PSARKGRVA-AFAVTVDGEEgigiaaeigrgvqksVPAQELIDSIRQAVAEaYQeAPKVVALLN 536
Cdd:PRK07656  433 vlyehpaVAEAAVigvPDERLGEVGkAYVVLKPGAE---------------LTEEELIAYCREHLAK-YK-VPRSIEFLD 495
                         570
                  ....*....|....*...
gi 15597620   537 pgALPKTSSGKLQRSACR 554
Cdd:PRK07656  496 --ELPKNATGKVLKRALR 511
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
1153-1625 1.27e-47

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 181.18  E-value: 1.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLadsGVellltq 1232
Cdd:cd17647   20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYL---GV------ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 ahlferlpgaegVTPICLDSLkldnwpsQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDD 1312
Cdd:cd17647   91 ------------AKPRGLIVI-------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEND 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1313 VLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEpGVAACGSLRRLFS 1392
Cdd:cd17647  152 KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQ-ATTPFPKLHHAFF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1393 GGEALPAE--LRnrvLQRL-PAVALHNRYGPTETAINVTHWQCRAEDGERS---------PIGRPLGNVVCRVLDA--EF 1458
Cdd:cd17647  231 VGDILTKRdcLR---LQTLaENVRIVNMYGTTETQRAVSYFEVPSRSSDPTflknlkdvmPAGRGMLNVQLLVVNRndRT 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1459 NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAG---------------------ERLYRTGDRARWNADGV 1517
Cdd:cd17647  308 QICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLYRTGDLGRYLPNGD 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1518 LEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQ-LVGYY-------------TGAVGAEAEAEQ- 1582
Cdd:cd17647  388 CECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPtLVSYIvprfdkpddesfaQEDVPKEVSTDPi 467
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 1583 ----------NQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEP 1625
Cdd:cd17647  468 vkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
2209-2664 1.67e-47

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 179.72  E-value: 1.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2209 GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL 2288
Cdd:cd05911    8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2289 SHAALFEA----------------LGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVS 2352
Cdd:cd05911   88 TDPDGLEKvkeaakelgpkdkiivLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2353 HGEIAMHCAAVIECFG--MRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQwgAEEICELIRAEGVSILGFTPS 2430
Cdd:cd05911  168 HRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFD--SELFLDLIEKYKITFLYLVPP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2431 YGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVvmPLACLAPERlEEGAASVpiGSV 2509
Cdd:cd05911  246 IAAALAKSPLLDKYDLSsLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETG--GILTVNPDG-DDKPGSV--GRL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2510 V-GARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRI 2588
Cdd:cd05911  321 LpNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYLYIVDRK 393
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2589 DHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGyvASAVAEQDEDAQAalrEALKTHLKQQLPDY 2664
Cdd:cd05911  394 KELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPR--AYVVRKPGEKLTE---KEVKDYVAKKVASY 464
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
2200-2689 2.06e-47

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 179.82  E-value: 2.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2200 PQAPALTFAGQT--LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQY 2277
Cdd:cd05926    1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2278 MIEDSGVRLLL---------SHAA--LFEALGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQ----AYLIYTSGS 2342
Cdd:cd05926   81 YLADLGSKLVLtpkgelgpaSRAAskLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLpddlALILHTSGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2343 TGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELH---FYSINFDAASerLLAPLLCGARVVL----RAQGQWGaeeice 2415
Cdd:cd05926  161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVvmpLFHVHGLVAS--LLSTLAAGGSVVLpprfSASTFWP------ 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2416 LIRAEGVSILGFTPSYGSQLAQWLESQGRQLP--VRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETV-VMPLACL 2492
Cdd:cd05926  233 DVRDYNATWYTAVPTIHQILLNRPEPNPESPPpkLRFIRSCSASLPPAVLEALEATFG-APVLEAYGMTEAAhQMTSNPL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2493 APERLEEGaaSVPIGsvVGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGD 2572
Cdd:cd05926  312 PPGPRKPG--SVGKP--VGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGD 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2573 LVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQlagyVASAVaeQDEDAQAALRE 2651
Cdd:cd05926  380 LGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpDEKYGEE----VAAAV--VLREGASVTEE 453
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15597620 2652 ALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05926  454 ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1161-1622 3.47e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 178.02  E-value: 3.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1161 ARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGA----YVPLDPDYPSERLAYMLADSGVELLLTQAHLF 1236
Cdd:cd05922    1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1237 ERLPGAEGVTPICLDSLKLDNWP---SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDV 1313
Cdd:cd05922   81 DRLRDALPASPDPGTVLDADGIRaarASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHrdPARLVELVRQFGVTTLHFVPP----LLQLFIDEPGVAacgSLRR 1389
Cdd:cd05922  161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPStyamLTRLGFDPAKLP---SLRY 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1390 LFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGEL 1469
Cdd:cd05922  236 LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1470 CIGGLGLARGYLGRPALSAERfvadpfSAAGERLYrTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPG 1549
Cdd:cd05922  316 VHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 1550 VAQAVVVIREGVAGSQLVGYYTGAVGAEAEAeqnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05922  389 IIEAAAVGLPDPLGEKLALFVTAPDKIDPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
64-550 4.94e-47

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 176.90  E-value: 4.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesarrHHQERLLS-IIADAEPRLVLTTADLrepllqmnaqlsaana 142
Cdd:cd05935   26 GDRVGICLQNSPQYVIAYFAIWRANAVVVPINP------MLKERELEyILNDSGAKVAVVGSEL---------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  143 pqllcvdqldpavaeawdepqvrpEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMG 222
Cdd:cd05935   84 ------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  223 LIGGLLQPIFSGVPCVLMSpryflerpvRW-----LEAISQYGGTVSGGpdfAYRLCSERVAESALQRLDLSGWRVAFSG 297
Cdd:cd05935  140 FVGSLNTAVYVGGTYVLMA---------RWdretaLELIEKYKVTFWTN---IPTMLVDLLATPEFKTRDLSSLKVLTGG 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  298 SEPIRQDSLERFAEKFAASrfdassFFACYGLAEATLFVTGGQRG------QGIPALAVDgealarnriaegegsvlmcc 371
Cdd:cd05935  208 GAPMPPAVAEKLLKLTGLR------FVEGYGLTETMSQTHTNPPLrpklqcLGIP*FGVD-------------------- 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  372 grsqpehaVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFL-RDGELFVTGRLK 450
Cdd:cd05935  262 --------ARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMdEEGYFFFVDRVK 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  451 DMLIVRGHNLYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGEEGigiaaeigrgvqkSVPAQELIDSIRQ 519
Cdd:cd05935  334 RMINVSGFKVWPAEVEAKLYKHpai*evcvisVPDERVGeEVKAFIVLRPEYRG-------------KVTEEDIIEWARE 400
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15597620  520 AVAeAYqEAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd05935  401 QMA-AY-KYPREVEFVD--ELPRSASGKILW 427
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3740-4230 8.11e-47

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 176.89  E-value: 8.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIveLSRTLVLVCTQA 3819
Cdd:cd17654   18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTV--MKKCHVSYLLQN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3820 CREQALALFDElgcvdrprllvwdeiqqgegAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLE 3899
Cdd:cd17654   96 KELDNAPLSFT--------------------PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3900 LDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQgLLAHV--GEQGITVLESVPSLIQGMLAEERQ---- 3973
Cdd:cd17654  156 ITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPS-KLADIlfKRHRITVLQATPTLFRRFGSQSIKstvl 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3974 -ALDGLRWMLPTGEAMPPE-LARQWLKRYPRIGLVNAYGPAECSDDVAFFRVdlASTESTyLPIGSPTdnnrlyllgaga 4051
Cdd:cd17654  235 sATSSLRVLALGGEPFPSLvILSSWRGKGNRTRIFNIYGITEVSCWALAYKV--PEEDSP-VQLGSPL------------ 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4052 ddafelvpLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRaDGVLEYVGRIDHQVKIRGFR 4131
Cdd:cd17654  300 --------LGTVIEVRDQNGSEGTGQVFLGGLNRVCILDDEVTVPKGTMRATGDFVTVK-DGELFFLGRKDSQIKRRGKR 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4132 IELGEIEARLHERADVREAAVAVQegaNGKYLVGYLVpgeTPRSSAdspaglmveqgawfeRIKQQLRADL------PDY 4205
Cdd:cd17654  371 INLDLIQQVIESCLGVESCAVTLS---DQQRLIAFIV---GESSSS---------------RIHKELQLTLlsshaiPDT 429
                        490       500
                 ....*....|....*....|....*
gi 15597620 4206 MVplhwlVLDRMPLNANGKLDRKAL 4230
Cdd:cd17654  430 FV-----QIDKLPLTSHGKVDKSEL 449
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3746-4230 9.53e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 176.86  E-value: 9.53e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3746 RRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAG----YLPLDPGHPTQRLTRIVEL-SRTLVLVctqac 3820
Cdd:cd05922    1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADaGGRIVLA----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3821 rEQALALFDELGCVDRPRLLVWDEIQQGEGAEHD-PQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLE 3899
Cdd:cd05922   76 -DAGAADRLRDALPASPDPGTVLDADGIRAARASaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3900 LDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAhdPQGLLAHVGEQGITVLESVPSLIQgMLAE---ERQALD 3976
Cdd:cd05922  155 ITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYA-MLTRlgfDPAKLP 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3977 GLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTylPIGSPTDNNRLYLLGagaDDAFE 4056
Cdd:cd05922  232 SLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPG--SIGLAIPGGEFEILD---DDGTP 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4057 LVPlGAVGELCVAGTGVGRGYVGDPLRTAQAfvphpfGAPGERLYrTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGE 4136
Cdd:cd05922  307 TPP-GEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTE 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4137 IEARLHERADVREAAVAVQEGANGKYLVGYLVpgetpRSSADSPAGLMVeqgawferikqQLRADLPDYMVPLHWLVLDR 4216
Cdd:cd05922  379 IEAAARSIGLIIEAAAVGLPDPLGEKLALFVT-----APDKIDPKDVLR-----------SLAERLPPYKVPATVRVVDE 442
                        490
                 ....*....|....
gi 15597620 4217 MPLNANGKLDRKAL 4230
Cdd:cd05922  443 LPLTASGKVDYAAL 456
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
2201-2689 3.24e-46

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 174.79  E-value: 3.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2201 QAPALTFAGQTLSYAELDARSNRLARVL-RSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:cd05941    1 DRIAIVDDGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2280 EDSGVRLLLShaalfealgelpagvarwcleedgPALdaedpaplaalsgpqhqayLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd05941   81 TDSEPSLVLD------------------------PAL-------------------ILYTSGTTGRPKGVVLTHANLAAN 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECFGMRAEDCELHFYSIN-----FDAaserLLAPLLCGARVVLraQGQWGAEEICELIRAEGVSILGFTPSYGSQ 2434
Cdd:cd05941  118 VRALVDAWRWTEDDVLLHVLPLHhvhglVNA----LLCPLFAGASVEF--LPKFDPKEVAISRLMPSITVFMGVPTIYTR 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2435 LAQWLESQGRQL---------PVRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETvVMPLAC-LAPERLeEGAASV 2504
Cdd:cd05941  192 LLQYYEAHFTDPqfaraaaaeRLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEI-GMALSNpLDGERR-PGTVGM 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2505 PIGSVvgarVAYILDADLA-LVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVE 2583
Cdd:cd05941  269 PLPGV----QARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYW 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2584 YVGRI-DHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSgkqlAGYVASAVAEQDEDAQAALREALKTHLKQQLP 2662
Cdd:cd05941  338 ILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD----WGERVVAVVVLRAGAAALSLEELKEWAKQRLA 413
                        490       500
                 ....*....|....*....|....*..
gi 15597620 2663 DYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05941  414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
42-466 4.03e-46

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 173.61  E-value: 4.03e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     42 SYRDLDLRARSIAAA--LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPPEsarrhhqeRLLSIIADAE 116
Cdd:TIGR01733    1 TYRELDERANRLARHlrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPldpAYPAE--------RLAFILEDAG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    117 PRLVLTTADLREPLLQMNAqlsAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANE 196
Cdd:TIGR01733   73 ARLLLTDSALASRLAGLVL---PVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    197 VLIRRGFGIGADDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLMSPRYFLERPVRWLEAISQYGGTV-SGGPDFAYRLCS 275
Cdd:TIGR01733  150 AWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVlNLTPSLLALLAA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    276 ErvAESALQRLdlsgwRVAFSGSEPIRQDSLERFAEKFAASRfdassFFACYGLAEATLFVTggqrgqgipALAVDGEAL 355
Cdd:TIGR01733  229 A--LPPALASL-----RLVILGGEALTPALVDRWRARGPGAR-----LINLYGPTETTVWST---------ATLVDPDDA 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    356 ARNriaegegsVLMCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVE-----RDGRTWL 430
Cdd:TIGR01733  288 PRE--------SPVPIGRPLANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPdpfagGDGARLY 358
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 15597620    431 RTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIE 466
Cdd:TIGR01733  359 RTGDLVRYLpDGNLEFLGRIDDQVKIRGYRIELGEIE 395
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2219-2689 1.72e-45

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 173.01  E-value: 1.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2219 ARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGA----YVPLDPEYPLERLQYMIEDSGVRLLLSHAALF 2294
Cdd:cd05922    1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2295 E--ALGELPAGVARWCLEEDGpALDAEDPAPLAALSGPQhQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAE 2372
Cdd:cd05922   81 DrlRDALPASPDPGTVLDADG-IRAARASAPAHEVSHED-LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2373 DCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGaEEICELIRAEGVSILGFTPSYGSQLAQwLESQGRQLP-VRMC 2451
Cdd:cd05922  159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLD-DAFWEDLREHGATGLAGVPSTYAMLTR-LGFDPAKLPsLRYL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2452 ITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVmPLACLAPERLEE--GAASVPIGsvvGARVaYILDADLALVPQGA 2529
Cdd:cd05922  237 TQAGGRLPQETIARLRELLPGAQVYVMYGQTEATR-RMTYLPPERILEkpGSIGLAIP---GGEF-EILDDDGTPTPPGE 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2530 TGELYVGGAGLARGYHERPALSAErfvpdpfAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLL 2609
Cdd:cd05922  312 PGEIVHRGPNVMKGYWNDPPYRRK-------EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAAR 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2610 EHPQVREALVLALDSPSGKQLAgyvASAVAEQDEDAQAALRealktHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05922  385 SIGLIIEAAAVGLPDPLGEKLA---LFVTAPDKIDPKDVLR-----SLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
24-550 2.76e-45

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 172.09  E-value: 2.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   24 ERLALRflaeDDGEgvVLSYRDLDLRARSIAAA--LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP--PES 99
Cdd:cd05941    1 DRIAIV----DDGD--SITYADLVARAARLANRllALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPsyPLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  100 ARRHhqerllsIIADAEPRLVLttadlrepllqmnaqlsaanapqllcvdqlDPAVaeawdepqvrpehiafLQYTSGST 179
Cdd:cd05941   75 ELEY-------VITDSEPSLVL------------------------------DPAL----------------ILYTSGTT 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  180 ALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPryF---LERPVRWLEAI 256
Cdd:cd05941  102 GRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPK--FdpkEVAISRLMPSI 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  257 S-------------QYGGTVSGGPDFAYRLCSERVaesalqrldlsgwRVAFSGSEPIRQDSLERFAEKFAAS---Rfda 320
Cdd:cd05941  180 TvfmgvptiytrllQYYEAHFTDPQFARAAAAERL-------------RLMVSGSAALPVPTLEEWEAITGHTlleR--- 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  321 ssffacYGLAEATLFVTGGQRGQGIPalavdgealarnriaegeGSVlmccGRSQPEHAVLIVDAASGEVLGDDNVGEIW 400
Cdd:cd05941  244 ------YGMTEIGMALSNPLDGERRP------------------GTV----GMPLPGVQARIVDEETGEPLPRGEVGEIQ 295
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  401 AAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFLR-DGELFVTGRLKDMLI-VRGHNLYPQDIERTVEsEVPSARK 478
Cdd:cd05941  296 VRGPSVFKEYWNKPEATKEEFTD-DG--WFKTGDLGVVDeDGYYWILGRSSVDIIkSGGYKVSALEIERVLL-AHPGVSE 371
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  479 grVAAFAVTvDGEEGIGIAAEI-GRGVQKSVPAQELIDSIRQAVAeAYQeAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd05941  372 --CAVIGVP-DPDWGERVVAVVvLRAGAAALSLEELKEWAKQRLA-PYK-RPRRLILVD--ELPRNAMGKVNK 437
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
8-466 4.60e-45

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 175.29  E-value: 4.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    8 PTTLVQALRRRAVQEPERLALRFLaeDDGEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLY 86
Cdd:COG1022   10 ADTLPDLLRRRAARFPDRVALREK--EDGIWQSLTWAEFAERVRALAAGlLALGVKPGDRVAILSDNRPEWVIADLAILA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   87 AGVIAVPAYPPESArrhhqERLLSIIADAEPRLVLT-TADLREPLLQMNAQLSA------------ANAPQLLCVDQL-- 151
Cdd:COG1022   88 AGAVTVPIYPTSSA-----EEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSlrhivvldprglRDDPRLLSLDELla 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  152 -------DPAVAEAWDepQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLI 224
Cdd:COG1022  163 lgrevadPAELEARRA--AVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  225 GGLLQpIFSGVpCVlmsprYFLERPvrwlEAISQYGGTVsgGPDFayrLCS-----ERVAESALQRLDLSGW--RVAFsg 297
Cdd:COG1022  241 VSYYA-LAAGA-TV-----AFAESP----DTLAEDLREV--KPTF---MLAvprvwEKVYAGIQAKAEEAGGlkRKLF-- 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  298 sepirqDSLERFAEKFAASRFD--ASSFF--ACYGLAEATLF-----VTGGQrgqgIPALAVDGEALARN---------- 358
Cdd:COG1022  303 ------RWALAVGRRYARARLAgkSPSLLlrLKHALADKLVFsklreALGGR----LRFAVSGGAALGPElarffralgi 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  359 RIAEG----EGSVLMCCgrsQPEHAVLIvdAASG------EV-LGDDnvGEIWAAGPSIAHGYWRNPEASAKAFVErDGr 427
Cdd:COG1022  373 PVLEGygltETSPVITV---NRPGDNRI--GTVGpplpgvEVkIAED--GEILVRGPNVMKGYYKNPEATAEAFDA-DG- 443
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15597620  428 tWLRTGDLGFLR-DGELFVTGRLKDMLIVR-GHNLYPQDIE 466
Cdd:COG1022  444 -WLHTGDIGELDeDGFLRITGRKKDLIVTSgGKNVAPQPIE 483
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1144-1617 4.61e-45

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 171.11  E-value: 4.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1144 RVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLAD 1223
Cdd:cd05919    1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1224 SGVELLLTqahlferlpgaegvtpicldslkldnwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAAL---AERlq 1300
Cdd:cd05919   81 CEARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPllfADA-- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1301 WMQATYTLDGDDVLMQKAPVSFDVSVWECFW-PLVTGCRLVLAApgEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEP 1379
Cdd:cd05919  123 MAREALGLTPGDRVFSSAKMFFGYGLGNSLWfPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDSC 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1380 GV--AACGSLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTETAInvTHWQCRAEDGERSPIGRPLGNVVCRVLDAE 1457
Cdd:cd05919  201 AGspDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGH--IFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1458 FNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvadpfsaAGErLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEP 1537
Cdd:cd05919  278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1538 EEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGK 1616
Cdd:cd05919  350 VEVESLIIQHPAVAEAAVVaVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429

                 .
gi 15597620 1617 L 1617
Cdd:cd05919  430 L 430
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1126-1622 5.02e-45

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 173.58  E-value: 5.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1126 ARAW-LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGA 1204
Cdd:PRK08316    8 ARRQtIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1205 YVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEG----VTPICLDSLKL----------DNW----PSQAPGLH 1266
Cdd:PRK08316   88 HVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALAllpvDTLILSLVLGGreapggwldfADWaeagSVAEPDVE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1267 LHGDNLAYVIYTSGSTGQPKGVGNTHAALAErlQWMQATYTLD--GDDVLMQKAPV----SFDVSVWECFWplVTGCRLV 1340
Cdd:PRK08316  168 LADDDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVAGDmsADDIPLHALPLyhcaQLDVFLGPYLY--VGATNVI 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1341 LAAPgehrDPARLVELVRQFGVTTLhFVPP-----LLQlfidEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVA 1413
Cdd:PRK08316  244 LDAP----DPELILRTIEAERITSF-FAPPtvwisLLR----HPDFDTrdLSSLRKGYYGASIMPVEVLKELRERLPGLR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1414 LHNRYGPTEtaINVTHWQCRAEDGERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERF 1491
Cdd:PRK08316  315 FYNCYGQTE--IAPLATVLGPEEHLRRPgsAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1492 VADPFsaagerlyRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLVGYYT 1571
Cdd:PRK08316  393 RGGWF--------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI---GLPDPKWIEAVT 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  1572 GAV----GAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK08316  462 AVVvpkaGATVTEDE---LIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3736-4237 6.44e-45

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 174.14  E-value: 6.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVGIDQPVALLaergldlLGMIV-------GSFKAGAGYLPLDPGHPTQRLTRIVEL 3808
Cdd:COG0365   37 ERTLTYAELRREVNRFANALRALGVKKGDRVAIY-------LPNIPeaviamlACARIGAVHSPVFPGFGAEALADRIED 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3809 SRTLVLVCTQACR------------EQALA---------LFDELGC-VDRPRLLVWDEIQQGEGAEHDPqVYSGPQNLAY 3866
Cdd:COG0365  110 AEAKVLITADGGLrggkvidlkekvDEALEelpslehviVVGRTGAdVPMEGDLDWDELLAAASAEFEP-EPTDADDPLF 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3867 VIYTSGSTGLPKGVMVEQAGMLNNQLSKVPY-LELDENDVIAQTASQSFDISVWQFLAAPL-FGARVAIVPNAVAH-DPQ 3943
Cdd:COG0365  189 ILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTADIGWATGHSYIVYGPLlNGATVVLYEGRPDFpDPG 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3944 GLLAHVGEQGITVLESVPSLIQGMLAE-----ERQALDGLRWMLPTGEAMPPELARQWLKRyprIG--LVNAYGpaecsd 4016
Cdd:COG0365  269 RLWELIEKYGVTVFFTAPTAIRALMKAgdeplKKYDLSSLRLLGSAGEPLNPEVWEWWYEA---VGvpIVDGWG------ 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4017 dvaffrvdlaSTEsTYLPIGSPTDNNRLY-------LLGAGA---DDAFELVPLGAVGELCVAGTGVG--RGYVGDPLRT 4084
Cdd:COG0365  340 ----------QTE-TGGIFISNLPGLPVKpgsmgkpVPGYDVavvDEDGNPVPPGEEGELVIKGPWPGmfRGYWNDPERY 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4085 AQAFVPHPFGapgerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYL 4163
Cdd:COG0365  409 RETYFGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVvGVPDEIRGQVV 483
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 4164 VGYLV--PGETPrssadSPAglMVeqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQ 4237
Cdd:COG0365  484 KAFVVlkPGVEP-----SDE--LA------KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
2203-2689 8.43e-45

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 170.34  E-value: 8.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2203 PALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDS 2282
Cdd:cd05919    2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2283 GVRLLLSHAAlfealgelpagvarwcleedgpalDAedpaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAMHCAA 2362
Cdd:cd05919   82 EARLVVTSAD------------------------DI---------------AYLLYSSGTTGPPKGVMHAHRDPLLFADA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2363 V-IECFGMRAEDCELHFYSINFD-AASERLLAPLLCGARVVLrAQGQWGAEEICELIRAEGVSILGFTPS-YGSQLAQWL 2439
Cdd:cd05919  123 MaREALGLTPGDRVFSSAKMFFGyGLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVLYGVPTfYANLLDSCA 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2440 ESQGRQLPVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVVMPLaCLAPERLEEGAASVPigsVVGARVAyILD 2519
Cdd:cd05919  202 GSPDALRSLRLCVSAGEALPRGLGERWMEHFG-GPILDGIGATEVGHIFL-SNRPGAWRLGSTGRP---VPGYEIR-LVD 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2520 ADLALVPQGATGELYVGGAGLARGYHERPALSAERFVpdpfaaegGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRI 2599
Cdd:cd05919  276 EEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWV 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2600 ELGEIEARLLEHPQVREALVLALDSPSGkqLAGYVASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLT 2679
Cdd:cd05919  348 SPVEVESLIIQHPAVAEAAVVAVPESTG--LSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRT 425
                        490
                 ....*....|
gi 15597620 2680 ANGKLDRRAL 2689
Cdd:cd05919  426 ATGKLQRFKL 435
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
2212-2689 4.71e-44

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 167.90  E-value: 4.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSha 2291
Cdd:cd05972    1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2292 alfealgelpagvarwcleedgpalDAEDPaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRA 2371
Cdd:cd05972   79 -------------------------DAEDP------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2372 EDCelhFYSINFDA----ASERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP 2447
Cdd:cd05972  122 DDI---HWNIADPGwakgAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2448 VRMCITGGEALTGEHLQRIRQAFAPaSFFNAYGPTETVVMPLACLAPErLEEGAASVPIGsvvGARVAyILDADLALVPQ 2527
Cdd:cd05972  199 LRLVVSAGEPLNPEVIEWWRAATGL-PIRDGYGQTETGLTVGNFPDMP-VKPGSMGRPTP---GYDVA-IIDDDGRELPP 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2528 GATGELYV--GGAGLARGYHERPALSAERFVPDpfaaeggrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIE 2605
Cdd:cd05972  273 GEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2606 ARLLEHPQVREALVLALDSPS-GKQLAGYVasaVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKL 2684
Cdd:cd05972  345 SALLEHPAVAEAAVVGSPDPVrGEVVKAFV---VLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421

                 ....*
gi 15597620 2685 DRRAL 2689
Cdd:cd05972  422 RRVEL 426
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1156-1623 7.78e-44

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 167.08  E-value: 7.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTqahl 1235
Cdd:cd05934    6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 ferlpgaegvtpicldslkldnwpsqapglhlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLM 1315
Cdd:cd05934   82 -----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1316 QKAPVSF-DVSVWECFWPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVP-PLLQLFIDEPGVAACGSLRRLFSG 1393
Cdd:cd05934  127 TVLPLFHiNAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGaMLSYLLAQPPSPDDRAHRLRAAYG 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1394 GEALPAELRnRVLQRLpAVALHNRYGPTETAINVThwqcRAEDGERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCI 1471
Cdd:cd05934  204 APNPPELHE-EFEERF-GVRLLEGYGMTETIVGVI----GPRDEPRRPgsIGRPAPGYEVRIVDDDGQELPAGEPGELVI 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1472 ---GGLGLARGYLGRPALSAERFvadpfsAAGerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQP 1548
Cdd:cd05934  278 rglRGWGFFKGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHP 349
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 1549 GVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALP 1623
Cdd:cd05934  350 AVREAAVVaVPDEVGEDEVKAVVVLRPGETLDPEE---LFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1139-1626 8.84e-44

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 168.24  E-value: 8.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1139 AQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGvgpdvRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLA 1218
Cdd:PRK07787   11 AAADIADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1219 YMLADSGVELLLTQAhlferlPGAEGVTPICLDSLKLDNWPSQAPGlhlHGDNLAYVIYTSGSTGQPKGVGNTHAALAER 1298
Cdd:PRK07787   86 HILADSGAQAWLGPA------PDDPAGLPHVPVRLHARSWHRYPEP---DPDAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1299 LQWMQATYTLDGDDVLMQKAPVsFDVSvwecfwplvtgcRLVLAAPGEHRDPARLVELVR----------QFGVTTLHFV 1368
Cdd:PRK07787  157 LDALAEAWQWTADDVLVHGLPL-FHVH------------GLVLGVLGPLRIGNRFVHTGRptpeayaqalSEGGTLYFGV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1369 PPLLQLFIDEPGVA-ACGSLRRLFSGGEALPAElrnrVLQRLPAVALH---NRYGPTETAINVThwqCRAeDGERSP--I 1442
Cdd:PRK07787  224 PTVWSRIAADPEAArALRGARLLVSGSAALPVP----VFDRLAALTGHrpvERYGMTETLITLS---TRA-DGERRPgwV 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1443 GRPLGNVVCRVLDAEFNLLPAGVA--GELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEY 1520
Cdd:PRK07787  296 GLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHRI 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1521 LGRLDQQ-VKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAeqnqrLRAALQAELP 1595
Cdd:PRK07787  369 VGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVV---GVPdddlGQRIVAYVVGADDVAADE-----LIDFVAQQLS 440
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  1596 EYMVPTQLMRLAQMPLGPSGKLDTRALPEPV 1626
Cdd:PRK07787  441 VHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
PRK12467 PRK12467
peptide synthase; Provisional
11-875 9.82e-44

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 178.05  E-value: 9.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    11 LVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGV 89
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVF------GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVgVAVERSVEMIVALLAVLKAGG 3170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    90 IAVP---AYPpesarrhhQERLLSIIADAEPRLVLTTADLREpllqmnaQLSAANAPQLLCVDQLDP-AVAEAWDEPQVR 165
Cdd:PRK12467 3171 AYVPldpEYP--------RERLAYMIEDSGVKLLLTQAHLLE-------QLPAPAGDTALTLDRLDLnGYSENNPSTRVM 3235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDmGLIGGLLQPIFSGVPCVLMSPRyf 245
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFD-GAQERFLWTLICGGCLVVRDND-- 3312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   246 LERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDlsgwRVAFSGsEPIRQDSLERFAEKFAASrfdasSFFA 325
Cdd:PRK12467 3313 LWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLD----IYVFGG-EAVPPAAFEQVKRKLKPR-----GLTN 3382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   326 CYGLAEATLFVTggqrgqgipALAVDGEALArnriaegeGSVLMCCGRSQPEHAVLIVDAASGEV-LGddNVGEIWAAGP 404
Cdd:PRK12467 3383 GYGPTEAVVTVT---------LWKCGGDAVC--------EAPYAPIGRPVAGRSIYVLDGQLNPVpVG--VAGELYIGGV 3443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   405 SIAHGYWRNPEASAKAFV----ERDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKG 479
Cdd:PRK12467 3444 GLARGYHQRPSLTAERFVadpfSGSGGRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEARLL-QHPSVREA 3522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   480 RVAAfavtVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEaYQEAPKVVALlnpGALPKTSSGKLQRSAcrlrLED 559
Cdd:PRK12467 3523 VVLA----RDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPD-YMVPAQLLVL---AAMPLGPNGKVDRKA----LPD 3590
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   560 gsldsyalfPGLQAVQEAQPPAGDDEllARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQL 639
Cdd:PRK12467 3591 ---------PDAKGSREYVAPRSEVE--QQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDL 3659
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   640 FEAPTLQAFSATVArqlaaglpaeapmahlprGVDLPQSAAqqrlwltwqidpqsaaynipgglrlrgeLDEAALRASFQ 719
Cdd:PRK12467 3660 MSAPTIAELAGYSP------------------LGDVPVNLL----------------------------LDLNRLETGFP 3693
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   720 RLVERHEALRTRFlerDGAALQRIdergefawqfvdlaalaeheraaaaaqrreaeaqqpfdlekgpllrvslvrLDEQE 799
Cdd:PRK12467 3694 ALFCRHEGLGTVF---DYEPLAVI---------------------------------------------------LEGDR 3719
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   800 HQLWVTLHHIVADGWslnllldefsrlyaeacggQPADLAPLELHYAEFAAWQRQWLDA--------GEGARQLAYWRER 871
Cdd:PRK12467 3720 HVLGLTCRHLLDDGW-------------------QDTSLQAMAVQYADYILWQQAKGPYgllgwslgGTLARLVAELLER 3780

                  ....
gi 15597620   872 LGDT 875
Cdd:PRK12467 3781 EGES 3784
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
19-552 2.68e-43

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 166.27  E-value: 2.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   19 AVQEPERLALrflaedDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLF-PSGPDYVAAFFGCLYAGVIAVP---A 94
Cdd:cd05945    1 AAANPDRPAV------VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYgHKSPDAIAAFLAALKAGHAYVPldaS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   95 YPPEsarrhhqeRLLSIIADAEPRLVLTTADlrepllqmnaqlsaanapqllcvdqlDPAvaeawdepqvrpehiaFLQY 174
Cdd:cd05945   75 SPAE--------RIREILDAAKPALLIADGD--------------------------DNA----------------YIIF 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  175 TSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHD---MGLIGGLLqpifSGVPCVLMsPRYFLERPVR 251
Cdd:cd05945  105 TSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDlsvMDLYPALA----SGATLVPV-PRDATADPKQ 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  252 WLEAISQYGGTV-SGGPDFAyRLC--SERVAESALQRLDLsgwrVAFSGsEPIRQDSLERFAEKFAASRFdassfFACYG 328
Cdd:cd05945  180 LFRFLAEHGITVwVSTPSFA-AMCllSPTFTPESLPSLRH----FLFCG-EVLPHKTARALQQRFPDARI-----YNTYG 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  329 LAEATLFVTggqrgqgipALAVDGEALARNriaegeGSVLMccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAH 408
Cdd:cd05945  249 PTEATVAVT---------YIEVTPEVLDGY------DRLPI--GYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSK 310
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  409 GYWRNPEASAKAFVERDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKgrvaafAVT 487
Cdd:cd05945  311 GYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALR-QVPGVKE------AVV 383
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  488 V---DGEEGIGIAAEIgrgVQKSVPAQELIDSIRQAVAE---AYQEAPKVVALlnpGALPKTSSGKLQRSA 552
Cdd:cd05945  384 VpkyKGEKVTELIAFV---VPKPGAEAGLTKAIKAELAErlpPYMIPRRFVYL---DELPLNANGKIDRKA 448
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
1156-1622 2.82e-43

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 166.08  E-value: 2.82e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHL 1235
Cdd:TIGR01923    2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1236 FErlpgaEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLM 1315
Cdd:TIGR01923   82 EE-----KDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1316 QKAPVsFDVS----VWECfwpLVTGCRLVLaapgeHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGvaACGSLRRLF 1391
Cdd:TIGR01923  157 LSLPL-YHISglsiLFRW---LIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEGG--HNENLRKIL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1392 SGGEALPAELRNRVLQRlpAVALHNRYGPTETAINVThwQCRAED-GERSPIGRPLGNVVCRVLDAEfnllPAGVaGELC 1470
Cdd:TIGR01923  226 LGGSAIPAPLIEEAQQY--GLPIYLSYGMTETCSQVT--TATPEMlHARPDVGRPLAGREIKIKVDN----KEGH-GEIM 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1471 IGGLGLARGYLGRPALSAERFVADPFsaagerlyRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGV 1550
Cdd:TIGR01923  297 VKGANLMKGYLYQGELTPAFEQQGWF--------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGI 368
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   1551 AQAVVVIREGVA-GSQLVGYytgaVGAEAEAEQNQrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:TIGR01923  369 QEAVVVPKPDAEwGQVPVAY----IVSESDISQAK-LIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3717-4230 3.86e-43

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 167.67  E-value: 3.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:PRK06187   10 RILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3797 HPTQRLTRIVELSRTLVLVCTQACREQALALFDELGCV-------------DRPRLLVWDEIQQGEgAEHDPQVYSGPQN 3863
Cdd:PRK06187   90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVrtvivegdgpaapLAPEVGEYEELLAAA-SDTFDFPDIDEND 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3864 LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIaqtasqsfdisvwqFLAAPLF--------------GA 3929
Cdd:PRK06187  169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVY--------------LVIVPMFhvhawglpylalmaGA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3930 RVAIVPnavAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEER---QALDGLRWMLPTGEAMPPELARQWLKRYpRIGLV 4006
Cdd:PRK06187  235 KQVIPR---RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRayfVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4007 NAYGPAECSDDVAFFRVDLASTESTYLPI--GSPTDNNRLYLLgagaDDAFELVP--LGAVGELCVAGTGVGRGYVGDPL 4082
Cdd:PRK06187  311 QGYGMTETSPVVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIV----DDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4083 RTAQAFVPhpfGapgerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGK 4161
Cdd:PRK06187  387 ATAETIDG---G-----WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAViGVPDEKWGE 458
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  4162 YLVGYLV--PGETPrsSADSpaglmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK06187  459 RPVAVVVlkPGATL--DAKE--------------LRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2209-2690 4.55e-43

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 165.16  E-value: 4.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2209 GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL 2288
Cdd:cd05934    1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2289 ShaalfealgelpagvarwcleedgpaldaeDPAplaalsgpqhqaYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFG 2368
Cdd:cd05934   81 V------------------------------DPA------------SILYTSGTTGPPKGVVITHANLTFAGYYSARRFG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2369 MRAED---CELHFYSINFDAASerLLAPLLCGARVVLR----AQGQWGAeeicelIRAEGVSI---LGFTPSYgsQLAQW 2438
Cdd:cd05934  119 LGEDDvylTVLPLFHINAQAVS--VLAALSVGATLVLLprfsASRFWSD------VRRYGATVtnyLGAMLSY--LLAQP 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 LESQGRQLPVRmCITGGEALTGEHlQRIRQAFApASFFNAYGPTETVVmplaCLAPERLEEGAASvPIGSVVGARVAYIL 2518
Cdd:cd05934  189 PSPDDRAHRLR-AAYGAPNPPELH-EEFEERFG-VRLLEGYGMTETIV----GVIGPRDEPRRPG-SIGRPAPGYEVRIV 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2519 DADLALVPQGATGELYV---GGAGLARGYHERPALSAERFvpdpfaaEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIR 2595
Cdd:cd05934  261 DDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-------RNG-WFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2596 GFRIELGEIEARLLEHPQVREALVLALDSP-SGKQLAGYVasavaeQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLA 2674
Cdd:cd05934  333 GENISSAEVERAILRHPAVREAAVVAVPDEvGEDEVKAVV------VLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVD 406
                        490
                 ....*....|....*.
gi 15597620 2675 SLPLTANGKLDRRALP 2690
Cdd:cd05934  407 DLPKTPTEKVAKAQLR 422
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
2195-2653 1.31e-42

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 166.65  E-value: 1.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2195 RVAASPQAPALTFA------GQTLSYAELDARSNRLARVLRSHGvGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2268
Cdd:cd05931    2 RAAARPDRPAYTFLddeggrEETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2269 EYP---LERLQYMIEDSGVRLLLSHAALFEALGE----LPAGVARWCLEEDGPALDAEDPAPLAALsGPQHQAYLIYTSG 2341
Cdd:cd05931   81 PTPgrhAERLAAILADAGPRVVLTTAAALAAVRAfaasRPAAGTPRLLVVDLLPDTSAADWPPPSP-DPDDIAYLQYTSG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2342 STGKPKGVAVSHGEIAMHCAAVIECFGMRAE-----------DCELHFYsinfdaaserLLAPLLCGARVVL-------R 2403
Cdd:cd05931  160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGdvvvswlplyhDMGLIGG----------LLTPLYSGGPSVLmspaaflR 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2404 AQGQWgaeeiCELIRAEGVSIlGFTPSYGSQL-AQWLESQgrQLP------VRMCITGGEALTGEHLQRIRQAFAPA--- 2473
Cdd:cd05931  230 RPLRW-----LRLISRYRATI-SAAPNFAYDLcVRRVRDE--DLEgldlssWRVALNGAEPVRPATLRRFAEAFAPFgfr 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2474 --SFFNAYGPTETVVM----------PLACLAPERLEEGAASVPI-----------GSVVGARVAYILDAD-LALVPQGA 2529
Cdd:cd05931  302 peAFRPSYGLAEATLFvsggppgtgpVVLRVDRDALAGRAVAVAAddpaarelvscGRPLPDQEVRIVDPEtGRELPDGE 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2530 TGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGRLyRTGDLVRLCDnGQVEYVGRIDHQVKIRGFRIELGEIEARLL 2609
Cdd:cd05931  382 VGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWL-RTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATAE 459
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 2610 E-HPQVREALV--LALDSPSGKQLAGyVASAVAEQDEDAQAALREAL 2653
Cdd:cd05931  460 EaHPALRPGCVaaFSVPDDGEERLVV-VAEVERGADPADLAAIAAAI 505
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
1156-1622 1.38e-42

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 164.21  E-value: 1.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHL 1235
Cdd:cd05969    3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 FERLpgaegvTPicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAErlQWMQATYTLD--GDDV 1313
Cdd:cd05969   83 YERT------DP----------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIF--YYFTGKYVLDlhPDDI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKA-PVSFDVSVWECFWPLVTGCRLVLAapGEHRDPARLVELVRQFGVTTLHFVPPLLQLFI---DEPGVA-ACGSLR 1388
Cdd:cd05969  133 YWCTAdPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMkegDELARKyDLSSLR 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1389 RLFSGGEALPAELRNRVLQRLpAVALHNRYGPTET-AINVTHWQCraEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAG 1467
Cdd:cd05969  211 FIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETgSIMIANYPC--MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKG 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1468 ELCI--GGLGLARGYLGRPALSAERFVadpfsaagERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:cd05969  288 ILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALM 359
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 1546 AQPGVAQAVVVIREG-VAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05969  360 EHPAVAEAGVIGKPDpLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1153-1556 1.57e-42

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 163.80  E-value: 1.57e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ 1232
Cdd:cd05935    1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 AHLferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDD 1312
Cdd:cd05935   81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1313 VLMQKAPVsFDVS--VWECFWPLVTGCRLVLAAPGEhRDPARlvELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLR 1388
Cdd:cd05935  127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATPEFKTrdLSSLK 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1389 RLFSGGEALPAELRNRVLQrLPAVALHNRYGPTETaINVTHWQCRAEDgERSPIGRPLGNVVCRVLDAEFNL-LPAGVAG 1467
Cdd:cd05935  203 VLTGGGAPMPPAVAEKLLK-LTGLRFVEGYGLTET-MSQTHTNPPLRP-KLQCLGIP*FGVDARVIDIETGReLPPNEVG 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1468 ELCIGGLGLARGYLGRPALSAERFVADpfsaAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQ 1547
Cdd:cd05935  280 EIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355

                 ....*....
gi 15597620 1548 PGVAQAVVV 1556
Cdd:cd05935  356 PAI*EVCVI 364
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1150-1556 1.62e-42

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 165.49  E-value: 1.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1150 DGGSLGYAELHARANRLAHYLRDKGVGP-DVrVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVEL 1228
Cdd:cd05904   29 TGRALTYAELERRVRRLAAGLAKRGGRKgDV-VLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1229 LLTQAHLFERLPGAeGVTPICLDSLKLDNW----------PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTH---AAL 1295
Cdd:cd05904  108 AFTTAELAEKLASL-ALPVVLLDSAEFDSLsfsdllfeadEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHrnlIAM 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1296 AERLQWMQATyTLDGDDVLMqkapvsfdvsvweCFWPL-----VTGCRLVLAAPGE------HRDPARLVELVRQFGVTT 1364
Cdd:cd05904  187 VAQFVAGEGS-NSDSEDVFL-------------CVLPMfhiygLSSFALGLLRLGAtvvvmpRFDLEELLAAIERYKVTH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1365 LHFVPPLLQLFIDEPGVAAC--GSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTE-TAINVTHWQCRAEDGERSP 1441
Cdd:cd05904  253 LPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFAPEKDRAKYGS 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1442 IGRPLGNVVCRVLDAEFNL-LPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEY 1520
Cdd:cd05904  333 VGRLVPNVEAKIVDPETGEsLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGDLCYIDEDGYLFI 405
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15597620 1521 LGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:cd05904  406 VDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
40-554 2.28e-42

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 163.40  E-value: 2.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   40 VLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyPPESARRHHqerlLSIIADAEPR 118
Cdd:cd05919   10 SVTYGQLHDGANRLGSAlRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVI-NPLLHPDDY----AYIARDCEAR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  119 LVLTTADlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvrpeHIAFLQYTSGSTALPKGVQVSHGNLVAN-EV 197
Cdd:cd05919   85 LVVTSAD------------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFaDA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  198 LIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRyflERPVRWLEAISQYGGTV-SGGPDFAYRLcse 276
Cdd:cd05919  123 MAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW---PTAERVLATLARFRPTVlYGVPTFYANL--- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  277 rVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFaasrfdassffacyglaeatlfvtGGQRGQGIPALAVdGEALA 356
Cdd:cd05919  197 -LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF------------------------GGPILDGIGATEV-GHIFL 250
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  357 RNRIAEGE-GSvlmcCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDL 435
Cdd:cd05919  251 SNRPGAWRlGS----TGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--NGG--WYRTGDK 321
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  436 gFLRDGELFVT--GRLKDMLIVRGHNLYPQDIERTVeSEVPSARKgrvAAFAVTVDGEEGIGIAAEIgrgVQKS--VPAQ 511
Cdd:cd05919  322 -FCRDADGWYThaGRADDMLKVGGQWVSPVEVESLI-IQHPAVAE---AAVVAVPESTGLSRLTAFV---VLKSpaAPQE 393
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 15597620  512 ELIDSIRQAVAE--AYQEAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05919  394 SLARDIHRHLLErlSAHKVPRRIAFVD--ELPRTATGKLQRFKLR 436
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
1272-1622 2.56e-42

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 159.80  E-value: 2.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1272 LAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFDVS----VWECFWplvTGCRLVLAapgEH 1347
Cdd:cd17630    2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPL-YHVGglaiLVRSLL---AGAELVLL---ER 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1348 RDPARLVELvrQFGVTTLHFVPPLLQLFIDEP-GVAACGSLRRLFSGGEALPAELRNRVLQRlpAVALHNRYGPTETAIN 1426
Cdd:cd17630   75 NQALAEDLA--PPGVTHVSLVPTQLQRLLDSGqGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETASQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1427 VTHWqcRAEDGERSPIGRPLGNVVCRVLDAefnllpagvaGELCIGGLGLARGYLGRPalsaerfVADPFSAAGerLYRT 1506
Cdd:cd17630  151 VATK--RPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEFNEDG--WFTT 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1507 GDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAeq 1582
Cdd:cd17630  210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV---GVPdeelGQRPVAVIVGRGPADPAE-- 284
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 15597620 1583 nqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd17630  285 ---LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2213-2689 3.03e-42

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 162.99  E-value: 3.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2213 SYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRlllshaa 2292
Cdd:cd05971    8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2293 lfealgelpagvarwCLEEDGpaldAEDPaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGM--R 2370
Cdd:cd05971   81 ---------------ALVTDG----SDDP------------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLfpR 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2371 AEDCelhFYSiNFDAA-----SERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPS-------YGSQLAQW 2438
Cdd:cd05971  130 DGDL---YWT-PADWAwigglLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkmmrqQGEQLKHA 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2439 lesqgrQLPVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGsvvGARVAyIL 2518
Cdd:cd05971  206 ------QVKLRAIATGGESLGEELLGWAREQFG-VEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIP---GHRVA-IV 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2519 DADLALVPQGATGELYV--GGAGLARGYHERPALSAERFVpdpfaaegGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRG 2596
Cdd:cd05971  275 DDNGTPLPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMA--------GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSG 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2597 FRIELGEIEARLLEHPQVREALVLALDSP-SGKQLAGYVASAVAEQDEDaqaALREALKTHLKQQLPDYMVPAHLLLLAS 2675
Cdd:cd05971  347 YRIGPAEIEECLLKHPAVLMAAVVGIPDPiRGEIVKAFVVLNPGETPSD---ALAREIQELVKTRLAAHEYPREIEFVNE 423
                        490
                 ....*....|....
gi 15597620 2676 LPLTANGKLDRRAL 2689
Cdd:cd05971  424 LPRTATGKIRRREL 437
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
2210-2692 3.26e-42

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 165.00  E-value: 3.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS 2289
Cdd:cd17647   19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 HAAlfealgelpAGVarwcleedgpaldaedpaplaaLSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGM 2369
Cdd:cd17647   99 IRA---------AGV----------------------VVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2370 RAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGA-EEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPV 2448
Cdd:cd17647  148 SENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTpGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHH 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2449 RMCItgGEALTGEHLQRIrQAFAP-ASFFNAYGPTET------VVMPLACLAPERLEEGAASVPIGSvvgarvaYILDAD 2521
Cdd:cd17647  228 AFFV--GDILTKRDCLRL-QTLAEnVRIVNMYGTTETqravsyFEVPSRSSDPTFLKNLKDVMPAGR-------GMLNVQ 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2522 LALVPQ---------GATGELYVGGAGLARGYHERPALSAERFVPDPFAAEG---------------------GRLYRTG 2571
Cdd:cd17647  298 LLVVNRndrtqicgiGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLYRTG 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2572 DLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYV--------------AS 2636
Cdd:cd17647  378 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRrDKDEEPTLVSYIvprfdkpddesfaqED 457
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2637 AVAEQDEDAQAA-------LREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAP 2692
Cdd:cd17647  458 VPKEVSTDPIVKgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1086-1617 3.68e-42

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 166.21  E-value: 3.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1086 YLELLRQVAEDPQRCLG----DIALVDAEQAAHLAEWgsAPCEPARAWLP--------ELLERQLAQSAERVALEWDGG- 1152
Cdd:cd17634    1 YETKYRQSINDPDTFWGeagkILDWITPYQKVKNTSF--APGAPSIKWFEdatlnlaaNALDRHLRENGDRTAIIYEGDd 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 -----SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVE 1227
Cdd:cd17634   79 tsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1228 LLLTQAHLFER------LPGAE-----GVTP----ICLDSLKLD---------NWPSQ---APGLH----LHGDNLAYVI 1276
Cdd:cd17634  159 LLITADGGVRAgrsvplKKNVDdalnpNVTSvehvIVLKRTGSDidwqegrdlWWRDLiakASPEHqpeaMNAEDPLFIL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1277 YTSGSTGQPKGVGNTHAALAERLQW-MQATYTLDGDDVLMQKAPVSFDVS-VWECFWPLVTGCRLVL--AAPgEHRDPAR 1352
Cdd:cd17634  239 YTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPAR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1353 LVELVRQFGVTTLHFVPPLLQLFIDEPGVAACG----SLRRLFSGGEAL---PAELRNRVL--QRLPAValhNRYGPTET 1423
Cdd:cd17634  318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdrsSLRILGSVGEPInpeAYEWYWKKIgkEKCPVV---DTWWQTET 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1424 AINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGL--GLARGYLGRPalsaERFVADPFSAAgE 1501
Cdd:cd17634  395 GGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTF-K 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1502 RLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEA 1580
Cdd:cd17634  470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgIPHAIKGQAPYAYVVLNHGVEPSP 549
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 15597620 1581 EQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:cd17634  550 ELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1730-2155 3.88e-42

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 161.71  E-value: 3.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMwfLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTF--PSVDGVPVQRVHGDggLHMDW 1807
Cdd:cd19542    3 PCTPMQEGM--LLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKS--LDPPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSaldrdSRQQHLQTLADSEAHRPFdLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLDD 1887
Cdd:cd19542   79 EEVE-----TDEDSLDALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1888 RESPLEplpvQYLDYsvwqrewLESGERQRQLDYWKAQLGNEHPLLElpgdrprPPVQSHQGDLYRFDLSPELAERVRRF 1967
Cdd:cd19542  153 PAPPFS----DYISY-------LQSQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAF 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1968 NAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANR--IRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVI 2045
Cdd:cd19542  215 CASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYL 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2046 DGQSHQDLPFDHLVEALQPPRSAaynPLFQVMCNVQRWEFQQTRQLAGMTVEYIANDARATKFDLNLEVTDLDQRLGCCL 2125
Cdd:cd19542  295 RSLPHQHLSLREIQRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSL 371
                        410       420       430
                 ....*....|....*....|....*....|
gi 15597620 2126 TYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19542  372 AYSTSVLSEEQAEELLEQFDDILEALLANP 401
PRK12316 PRK12316
peptide synthase; Provisional
18-658 4.29e-42

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 172.83  E-value: 4.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    18 RAVQEPERLALRFLAEDdgegvvLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYP 96
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEK------LTYAELNRRANRLAHALIARGVGPEVLVgIAMERSAEMMVGLLAVLKAGGAYVPLDP 4633
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    97 pesarRHHQERLLSIIADAEPRLVLTTADLREpllqmnaQLSAANAPQLLCVDQLDPAVAEAWDEPQVR--PEHIAFLQY 174
Cdd:PRK12316 4634 -----EYPRERLAYMMEDSGAALLLTQSHLLQ-------RLPIPDGLASLALDRDEDWEGFPAHDPAVRlhPDNLAYVIY 4701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   175 TSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDmGLIGGLLQPIFSGVPCVLMSPRYFLerPVRWLE 254
Cdd:PRK12316 4702 TSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGASVVIRDDSLWD--PERLYA 4778
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   255 AISQYGGTVSGGPDFAYRLcserVAESALQRLDLSGWRVAFSGSEPIRQDSLERfaekfAASRFDASSFFACYGLAEATL 334
Cdd:PRK12316 4779 EIHEHRVTVLVFPPVYLQQ----LAEHAERDGEPPSLRVYCFGGEAVAQASYDL-----AWRALKPVYLFNGYGPTETTV 4849
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   335 FVTggqrgqgipalavdgeaLARNRIAEGEGSVLMCCGRSQPEHAVLIVDAaSGEVLGDDNVGEIWAAGPSIAHGYWRNP 414
Cdd:PRK12316 4850 TVL-----------------LWKARDGDACGAAYMPIGTPLGNRSGYVLDG-QLNPLPVGVAGELYLGGEGVARGYLERP 4911
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   415 EASAKAFV-----ERDGRTWlRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKgrvaAFAVTV 488
Cdd:PRK12316 4912 ALTAERFVpdpfgAPGGRLY-RTGDLARYRaDGVIDYLGRVDHQVKIRGFRIELGEIEARLR-EHPAVRE----AVVIAQ 4985
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   489 DGEEGIGIAAEI----GRGVQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSAcrLRLEDGSLds 564
Cdd:PRK12316 4986 EGAVGKQLVGYVvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKA--LPQPDASL-- 5061
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   565 yalfpglqaVQEAQPPAgDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFEAPT 644
Cdd:PRK12316 5062 ---------LQQAYVAP-RSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPT 5131
                         650
                  ....*....|....
gi 15597620   645 LQAFSATVARQLAA 658
Cdd:PRK12316 5132 LAAFVELAAAAGSG 5145
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1730-2154 4.32e-42

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 161.20  E-value: 4.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFpsvdgvpvqrVHGDGGLHMDWQD 1809
Cdd:cd19537    3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRY----------VPRDGGLRRSYSS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1810 FSaldrdSRQQHLQTL-ADSEAHRPFDLESGPLLRVCMVKmaereHYLVVTLHHIVTEGWAMDIFARELGALYEAFlddr 1888
Cdd:cd19537   73 SP-----PRVQRVDTLdVWKEINRPFDLEREDPIRVFISP-----DTLLVVMSHIICDLTTLQLLLREVSAAYNGK---- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1889 esPLEPLPVQYLDYSVWQREwlesgERQRQLDYWKAQLGNeHPLLELPgdrPRPPVQSHQGDLYRFDLSPELAERVRRFN 1968
Cdd:cd19537  139 --LLPPVRREYLDSTAWSRP-----ASPEDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFS 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1969 AARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPESEGLIGAFLNTQVLRCRLD--GQMSVGELLEQVRQTVID 2046
Cdd:cd19537  208 TSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAVRRSSQA 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2047 GQSHQdLPFDHLVEALQPPRSAAYNPLFQVMcnV---QRWEFQQTRQLAGMTVEYIAndARATKFDLNLEVTDL-DQRLG 2122
Cdd:cd19537  288 ALAHA-IPWHQLLEHLGLPPDSPNHPLFDVM--VtfhDDRGVSLALPIPGVEPLYTW--AEGAKFPLMFEFTALsDDSLL 362
                        410       420       430
                 ....*....|....*....|....*....|..
gi 15597620 2123 CCLTYSRDLFDEPRIARMAGHWQNLLEALLGD 2154
Cdd:cd19537  363 LRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
PRK06178 PRK06178
acyl-CoA synthetase; Validated
2180-2651 5.30e-42

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 165.21  E-value: 5.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2180 GEAGLQDTLHglfaARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKA 2259
Cdd:PRK06178   31 GERPLTEYLR----AWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2260 GGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALG--------------------------ELPAGVARWCLEEDG 2313
Cdd:PRK06178  107 GAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEqvraetslrhvivtsladvlpaeptlPLPDSLRAPRLAAAG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2314 -----PALDA---EDPAPLAALSGPqhqAYLIYTSGSTGKPKGVAVSHGEIAMHCAA-VIECFGMRAEDCELHFYSInFD 2384
Cdd:PRK06178  187 aidllPALRActaPVPLPPPALDAL---AALNYTGGTTGMPKGCEHTQRDMVYTAAAaYAVAVVGGEDSVFLSFLPE-FW 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2385 AASER--LLAPLLCGARVVLRAqgQWGAEEICELIRAEGVSILGFTPSYGSQL---AQWLESQGRQLPVRMCITGGEALT 2459
Cdd:PRK06178  263 IAGENfgLLFPLFSGATLVLLA--RWDAVAFMAAVERYRVTRTVMLVDNAVELmdhPRFAEYDLSSLRQVRVVSFVKKLN 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2460 GEHLQRIRQAFAPASFFNAYGPTET-----------------VVMPLACLAPerleegaasVPigsvvGARVAyILDADL 2522
Cdd:PRK06178  341 PDYRQRWRALTGSVLAEAAWGMTEThtcdtftagfqdddfdlLSQPVFVGLP---------VP-----GTEFK-ICDFET 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2523 -ALVPQGATGELYVGGAGLARGYHERPALSAERFVpdpfaaeGGRLyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIEL 2601
Cdd:PRK06178  406 gELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWL-HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFP 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620  2602 GEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAEQDEDAqAALRE 2651
Cdd:PRK06178  478 SEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA-AALQA 526
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
1153-1617 6.15e-42

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 162.16  E-value: 6.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ 1232
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 AHLFERLPGAEgvtpicldslkldnwpsqapglhlhGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDD 1312
Cdd:cd05903   81 ERFRQFDPAAM-------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1313 VLMQKAPVS-FDVSVWECFWPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPPLLQLFID--EPGVAACGSLRR 1389
Cdd:cd05903  136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNavEEAGEPLSRLRT 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1390 LFSGGEALPAELRNRVLQRLPAVALhNRYGPTETAINVThwqcRAEDGERSPI----GRPLGNVVCRVLDAEFNLLPAGV 1465
Cdd:cd05903  213 FVCGGATVPRSLARRAAELLGAKVC-SAYGSTECPGAVT----SITPAPEDRRlytdGRPLPGVEIKVVDDTGATLAPGV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1466 AGELCIGGLGLARGYLGRPALSAErfvadpfsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:cd05903  288 EGELLSRGPSVFLGYLDRPDLTAD--------AAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 1546 AQPGVAQAVVVI----REGVAGSQLVGYYTGA-VGAEAEAEQNQRLRAALQaELPEymvptQLMRLAQMPLGPSGKL 1617
Cdd:cd05903  360 GHPGVIEAAVVAlpdeRLGERACAVVVTKSGAlLTFDELVAYLDRQGVAKQ-YWPE-----RLVHVDDLPRTPSGKV 430
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
2212-2693 6.22e-42

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 162.29  E-value: 6.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHA 2291
Cdd:cd05969    1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2292 ALFEalgelpagvarwcleedgpALDAEDPaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRA 2371
Cdd:cd05969   81 ELYE-------------------RTDPEDP------------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2372 EDCELH----------FYSInfdaaserlLAPLLCGARVVLrAQGQWGAEEICELIRAEGVSILGFTPS-------YGSQ 2434
Cdd:cd05969  130 DDIYWCtadpgwvtgtVYGI---------WAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTairmlmkEGDE 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2435 LAQW--LESqgrqlpVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGA 2512
Cdd:cd05969  200 LARKydLSS------LRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAA 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2513 rvayILDADLALVPQGATGELYV--GGAGLARGYHERPALSAERFVpdpfaaegGRLYRTGDLVRLCDNGQVEYVGRIDH 2590
Cdd:cd05969  273 ----VVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADD 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2591 QVKIRGFRIELGEIEARLLEHPQVREALVLALDSPsgkqLAGYVASA--VAEQDEDAQAALREALKTHLKQQLPDYMVPA 2668
Cdd:cd05969  341 IIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP----LRGEIIKAfiSLKEGFEPSDELKEEIINFVRQKLGAHVAPR 416
                        490       500
                 ....*....|....*....|....*
gi 15597620 2669 HLLLLASLPLTANGKLDRRALPAPD 2693
Cdd:cd05969  417 EIEFVDNLPKTRSGKIMRRVLKAKE 441
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
23-552 7.95e-42

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 161.93  E-value: 7.95e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRFlaeddgEGVVLSYRDLD---------LRARSIAAalqahaqlGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:cd05930    1 PDAVAVVD------GDQSLTYAELDaranrlaryLRERGVGP--------GDLVAVLLERSLEMVVAILAVLKAGAAYVP 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 ---AYPPEsarrhhqeRLLSIIADAEPRLVLTTADlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvrpeHIA 170
Cdd:cd05930   67 ldpSYPAE--------RLAYILEDSGAKLVLTDPD------------------------------------------DLA 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  171 FLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPRYFLErPV 250
Cdd:cd05930   97 YVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEEVRKD-PE 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  251 RWLEAISQYGGTVSGGPDFAYRLCservaESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRfdassFFACYGLA 330
Cdd:cd05930  175 ALADLLAEEGITVLHLTPSLLRLL-----LQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGAR-----LVNLYGPT 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  331 EATLFVTGGQrgqgipalaVDGEALARNRIaegegsvlmCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGY 410
Cdd:cd05930  245 EATVDATYYR---------VPPDDEEDGRV---------PIGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGY 305
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  411 WRNPEASAKAFVE---RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVeSEVPSarkgrVAAFAV 486
Cdd:cd05930  306 LNRPELTAERFVPnpfGPGERMYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL-LAHPG-----VREAAV 379
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  487 TV--DGEEGIGIAAEIgrgvqksVPAQE---LIDSIRQAVAEAYQEA--PKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd05930  380 VAreDGDGEKRLVAYV-------VPDEGgelDEEELRAHLAERLPDYmvPSAFVVLD--ALPLTPNGKVDRKA 443
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
1154-1622 1.37e-41

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 160.97  E-value: 1.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQA 1233
Cdd:cd05972    1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAErlQWMQATYTLD--GD 1311
Cdd:cd05972   81 ------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLG--HIPTAAYWLGlrPD 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1312 DVLMQKAPVSFDVSVWECFW-PLVTGCRLVLAApGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVA-ACGSLRR 1389
Cdd:cd05972  123 DIHWNIADPGWAKGAWSSFFgPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSyKFSHLRL 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1390 LFSGGEALPAELRNRVLQRLpAVALHNRYGPTETA--INVTHWQcraeDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAG 1467
Cdd:cd05972  202 VVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGltVGNFPDM----PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEG 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1468 ELCI--GGLGLARGYLGRPALSAERFVADpfsaagerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:cd05972  277 DIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 1546 AQPGVAQAVVVIR-EGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05972  349 EHPAVAEAAVVGSpDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
2211-2634 1.84e-40

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 157.54  E-value: 1.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2211 TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSh 2290
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2291 aalfealgelpagVARWcleedgpalDAEDPAPLaalsgPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMR 2370
Cdd:cd05903   80 -------------PERF---------RQFDPAAM-----PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2371 AEDCEL------HFysINFDAAserLLAPLLCGARVVLraQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGR 2444
Cdd:cd05903  133 PGDVFLvaspmaHQ--TGFVYG---FTLPLLLGAPVVL--QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGE 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2445 QLP-VRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETvvmPLACLAPERLEEGAASVPIGSVV-GARVAyILDADL 2522
Cdd:cd05903  206 PLSrLRTFVCGGATVPRSLARRAAELLG-AKVCSAYGSTEC---PGAVTSITPAPEDRRLYTDGRPLpGVEIK-VVDDTG 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2523 ALVPQGATGELYVGGAGLARGYHERPALSAErfvpdpfAAEGGrLYRTGDLVRLCDNGQVEYVGRiDHQVKIR-GFRIEL 2601
Cdd:cd05903  281 ATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEG-WFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPV 351
                        410       420       430
                 ....*....|....*....|....*....|....
gi 15597620 2602 GEIEARLLEHPQVREALVLAL-DSPSGKQLAGYV 2634
Cdd:cd05903  352 LEVEDLLLGHPGVIEAAVVALpDERLGERACAVV 385
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
2186-2620 3.06e-40

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 160.65  E-value: 3.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2186 DTLHGLFAARVAASPQAPALTF----AGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGG 2261
Cdd:COG1022   11 DTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2262 AYVPLDPEYPLERLQYMIEDSGVRLLL----SHAA-LFEALGELPAGVARWCLEEDGPALD---------------AEDP 2321
Cdd:COG1022   91 VTVPIYPTSSAEEVAYILNDSGAKVLFvedqEQLDkLLEVRDELPSLRHIVVLDPRGLRDDprllsldellalgreVADP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2322 APLAALS---GPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHF-------------------Y 2379
Cdd:COG1022  171 AELEARRaavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplahvfertvsyyalaagA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2380 SINFDAASERLLA------P-LLCG---------ARVVLRAQGQ---------WGAE--EICELIRAEGVSI-LGFTPSY 2431
Cdd:COG1022  251 TVAFAESPDTLAEdlrevkPtFMLAvprvwekvyAGIQAKAEEAgglkrklfrWALAvgRRYARARLAGKSPsLLLRLKH 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2432 gsQLAQWL------ESQGRQLpvRMCITGGEALtGEHLQRirqafapasFFNA--------YGPTETVVmPLACLAPERl 2497
Cdd:COG1022  331 --ALADKLvfsklrEALGGRL--RFAVSGGAAL-GPELAR---------FFRAlgipvlegYGLTETSP-VITVNRPGD- 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2498 eegaasVPIGSV------VGARVAyildadlalvpqgATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTG 2571
Cdd:COG1022  395 ------NRIGTVgpplpgVEVKIA-------------EDGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTG 448
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15597620 2572 DLVRLCDNGQVEYVGRIDHQVKIR-GFRIELGEIEARLLEHPQVREALVL 2620
Cdd:COG1022  449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1130-1556 4.03e-40

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 160.27  E-value: 4.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVAL-EWDGG---SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAY 1205
Cdd:COG1022   13 LPDLLRRRAARFPDRVALrEKEDGiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1206 VPLDPDYPSERLAYMLADSGVELLL--TQAHL------FERLPGAEGVtpICLDSLKLDNWPS--------------QAP 1263
Cdd:COG1022   93 VPIYPTSSAEEVAYILNDSGAKVLFveDQEQLdkllevRDELPSLRHI--VVLDPRGLRDDPRllsldellalgrevADP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1264 GL------HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVS--FDvSVWECFWpLVT 1335
Cdd:COG1022  171 AElearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAhvFE-RTVSYYA-LAA 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1336 GCRLVLAapgehRDPARLVELVRQFGVTTLHFVPPLL--------QLFIDEPGV-------------------------- 1381
Cdd:COG1022  249 GATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWekvyagiqAKAEEAGGLkrklfrwalavgrryararlagksps 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1382 -------------------AACGS-LRRLFSGGEALPAELrNRVLQRLpAVALHNRYGPTETA--INVTHwqcraeDGER 1439
Cdd:COG1022  324 lllrlkhaladklvfsklrEALGGrLRFAVSGGAALGPEL-ARFFRAL-GIPVLEGYGLTETSpvITVNR------PGDN 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1440 SP--IGRPLGNVVCRVldAEfnllpagvAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGV 1517
Cdd:COG1022  396 RIgtVGPPLPGVEVKI--AE--------DGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDIGELDEDGF 458
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15597620 1518 LEYLGRLDQQVKLR-GFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:COG1022  459 LRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
PRK08316 PRK08316
acyl-CoA synthetase; Validated
2185-2666 1.39e-39

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 157.02  E-value: 1.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2185 QDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYV 2264
Cdd:PRK08316   10 RQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2265 PLDpeYPL--ERLQYMIEDSGVRLLLSHAALFE----ALGELPAGVARWCLEEDGPALDA------------EDPAPLAA 2326
Cdd:PRK08316   90 PVN--FMLtgEELAYILDHSGARAFLVDPALAPtaeaALALLPVDTLILSLVLGGREAPGgwldfadwaeagSVAEPDVE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2327 LSGPQhQAYLIYTSGSTGKPKGVAVSHGE-IAMHCAAVIECfGMRAEDCELHFYSINFDAASERLLAP-LLCGARVVLRA 2404
Cdd:PRK08316  168 LADDD-LAQILYTSGTESLPKGAMLTHRAlIAEYVSCIVAG-DMSADDIPLHALPLYHCAQLDVFLGPyLYVGATNVILD 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2405 QGQwgAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTE 2483
Cdd:PRK08316  246 APD--PELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLsSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2484 tvVMPLA-CLAPERLEEGAASVPIGSV-VGARvayILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfa 2561
Cdd:PRK08316  324 --IAPLAtVLGPEEHLRRPGSAGRPVLnVETR---VVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF------ 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2562 aEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPsgKQLAGYVASAVAEQ 2641
Cdd:PRK08316  393 -RGG-WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP--KWIEAVTAVVVPKA 468
                         490       500
                  ....*....|....*....|....*
gi 15597620  2642 DEDAQAalrEALKTHLKQQLPDYMV 2666
Cdd:PRK08316  469 GATVTE---DELIAHCRARLAGFKV 490
PRK07798 PRK07798
acyl-CoA synthetase; Validated
2187-2687 1.43e-39

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 157.35  E-value: 1.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2187 TLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL 2266
Cdd:PRK07798    4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2267 DPEYPLERLQYMIEDSGVRLLLSHAAL----FEALGELPaGVARWCLEEDGPALDAEDPA-----PLAALSGPQHQA--- 2334
Cdd:PRK07798   84 NYRYVEDELRYLLDDSDAVALVYEREFaprvAEVLPRLP-KLRTLVVVEDGSGNDLLPGAvdyedALAAGSPERDFGers 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2335 ----YLIYTSGSTGKPKGVAVSHGEI---AMHCAAVIEcfGMRAEDCELHFYSINFDAASERLLAP-------------- 2393
Cdd:PRK07798  163 pddlYLLYTGGTTGMPKGVMWRQEDIfrvLLGGRDFAT--GEPIEDEEELAKRAAAGPGMRRFPAPplmhgagqwaafaa 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2394 LLCGARVVLRAQGQWGAEEICELIRAEGVSILGFT-PSYGSQLAQWLESQGR-QLP-VRMCITGGEALTGEHLQRIRQAF 2470
Cdd:PRK07798  241 LFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPyDLSsLFAIASGGALFSPSVKEALLELL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2471 APASFFNAYGPTETVVMPLACLAPERLEEGAASVPIgsvvGARVAyILDADLALVPQGAtgelyvGGAG-LAR------G 2543
Cdd:PRK07798  321 PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTI----GPRTV-VLDEDGNPVEPGS------GEIGwIARrghiplG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2544 YHERPALSAERFvpdpFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALD 2623
Cdd:PRK07798  390 YYKDPEKTAETF----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVP 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  2624 SPS-GKQLAgyvasAVAEQDEDAQAALrEALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRR 2687
Cdd:PRK07798  466 DERwGQEVV-----AVVQLREGARPDL-AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3718-4230 2.86e-39

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 155.83  E-value: 2.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:PRK07656   10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3798 PTQRLTRIVELSRTLVLVCTQACREQALALFDELGCVDR-------------PRLLVWDE-IQQGEGAEHDPQVysGPQN 3863
Cdd:PRK07656   90 TADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHvviceteeddphtEKMKTFTDfLAAGDPAERAPEV--DPDD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3864 LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDEND--VIAQTASQSFDISVwQFLAAPLFGARVAIVPnavAHD 3941
Cdd:PRK07656  168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDryLAANPFFHVFGYKA-GVNAPLMRGATILPLP---VFD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3942 PQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDV 4018
Cdd:PRK07656  244 PDEVFRLIETERITVLPGPPTMYNSLLQHPDRSaedLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVT 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4019 AFFR-----VDLASTestylpIGSPTDN--NRLyllgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPH 4091
Cdd:PRK07656  324 TFNRldddrKTVAGT------IGTAIAGveNKI------VNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4092 PFgapgerLYrTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPG 4170
Cdd:PRK07656  392 GW------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAViGVPDERLGEVGKAYVVLK 464
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4171 ETPRSSADSpagLMveqgAWFERikqqlraDLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK07656  465 PGAELTEEE---LI----AYCRE-------HLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
23-552 3.59e-39

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 154.76  E-value: 3.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRFlaeddgEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesar 101
Cdd:cd12116    1 PDATAVRD------DDRSLSYAELDERANRLAARlRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDP----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  102 RHHQERLLSIIADAEPRLVLTTADLREPLlqmnaqlSAANAPQLLCVDQLDPAVAEAWdePQVRPEHIAFLQYTSGSTAL 181
Cdd:cd12116   70 DYPADRLRYILEDAEPALVLTDDALPDRL-------PAGLPVLLLALAAAAAAPAAPR--TPVSPDDLAYVIYTSGSTGR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  182 PKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLMSPryflerpvrwleaisqygG 261
Cdd:cd12116  141 PKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIAPR------------------E 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  262 TVSGGPDFAYRLCSERV----AESALQRLDL-SGWR-----VAFSGSEPIRQDSLERFAEKfaasrfdASSFFACYGLAE 331
Cdd:cd12116  202 TQRDPEALARLIEAHSItvmqATPATWRMLLdAGWQgraglTALCGGEALPPDLAARLLSR-------VGSLWNLYGPTE 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  332 ATLFVTggqrgqgipalavdgealaRNRIAEGEGSVLMccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYW 411
Cdd:cd12116  275 TTIWST-------------------AARVTAAAGPIPI--GRPLANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYL 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  412 RNPEASAKAFVE----RDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIErTVESEVPSarkgrVAAFAV 486
Cdd:cd12116  333 GRPALTAERFVPdpfaGPGSRLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHRIELGEIE-AALAAHPG-----VAQAAV 406
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  487 TVDGEEG-IGIAAEIGRGVQKSVPAQELidsiRQAVAEA--YQEAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd12116  407 VVREDGGdRRLVAYVVLKAGAAPDAAAL----RAHLRATlpAYMVPSAFVRLD--ALPLTANGKLDRKA 469
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
64-552 3.69e-39

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 154.29  E-value: 3.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQerllsIIADAEPRLVLTTAdlrepllqmnaqlsaanap 143
Cdd:cd05907   30 GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAY-----ILNDSEAKALFVED------------------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  144 qllcvdqldpavaeawdepqvrPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGL 223
Cdd:cd05907   86 ----------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFER 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  224 IGGLLQPIFSGVpCVlmsprYFLERPVRWLEAISQYGGTV-SGGPDFAYRLCSE--RVAESALQRL-----DLSGWRVAF 295
Cdd:cd05907  144 RAGLYVPLLAGA-RI-----YFASSAETLLDDLSEVRPTVfLAVPRVWEKVYAAikVKAVPGLKRKlfdlaVGGRLRFAA 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  296 SGSEPIrQDSLERFAEKFAASRFDAssffacYGLAEATlfvtggqrgqgiPALAVDgeALARNRIAEgEGSVLMCCgrsq 375
Cdd:cd05907  218 SGGAPL-PAELLHFFRALGIPVYEG------YGLTETS------------AVVTLN--PPGDNRIGT-VGKPLPGV---- 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  376 pehavlivdaasgEV-LGDDnvGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLG-FLRDGELFVTGRLKDML 453
Cdd:cd05907  272 -------------EVrIADD--GEILVRGPNVMLGYYKNPEATAEALDA-DG--WLHTGDLGeIDEDGFLHITGRKKDLI 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  454 IVR-GHNLYPQDIERTVESEVPSAR-------KGRVAAFaVTVDGEEGIGIAAEIG---RGVQKSVPAQELIDSIRQAVA 522
Cdd:cd05907  334 ITSgGKNISPEPIENALKASPLISQavvigdgRPFLVAL-IVPDPEALEAWAEEHGiayTDVAELAANPAVRAEIEAAVE 412
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15597620  523 EAYQEAP-----KVVALL------NPGALpkTSSGKLQRSA 552
Cdd:cd05907  413 AANARLSryeqiKKFLLLpepftiENGEL--TPTLKLKRPV 451
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
2187-2621 1.04e-38

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 155.21  E-value: 1.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2187 TLHGLFAARVAASPQAPALT------FAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAG 2260
Cdd:PRK13295   25 TINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2261 GAYVPLDPEYPLERLQYMIEDSGVRLLL--------SHAALFEAL-GELPAGVARWCLEEDGP------------ALDAE 2319
Cdd:PRK13295  105 AVLNPLMPIFRERELSFMLKHAESKVLVvpktfrgfDHAAMARRLrPELPALRHVVVVGGDGAdsfeallitpawEQEPD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2320 DPAPLAALS-GPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELhfysinfdAASER--------- 2389
Cdd:PRK13295  185 APAILARLRpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIL--------MASPMahqtgfmyg 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2390 LLAPLLCGARVVLraQGQWGAEEICELIRAEGVSI-LGFTPsYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIR 2467
Cdd:PRK13295  257 LMMPVMLGATAVL--QDIWDPARAAELIRTEGVTFtMASTP-FLTDLTRAVKESGRPVSsLRTFLCAGAPIPGALVERAR 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2468 QAFApASFFNAYGPTETVVMPLACL--APERleegaASVPIGSVV-GARVAyILDADLALVPQGATGELYVGGAGLARGY 2544
Cdd:PRK13295  334 AALG-AKIVSAWGMTENGAVTLTKLddPDER-----ASTTDGCPLpGVEVR-VVDADGAPLPAGQIGRLQVRGCSNFGGY 406
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2545 HERPALSAErfvpdpfAAEGgrLYRTGDLVRLCDNGQVEYVGRiDHQVKIRGFR-IELGEIEARLLEHPQVREALVLA 2621
Cdd:PRK13295  407 LKRPQLNGT-------DADG--WFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAIVA 474
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3740-4230 1.08e-38

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 154.06  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQA 3819
Cdd:cd05959   31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3820 CREQ---ALALFDELGCV---------DRPRLLVWDEIqqGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGM 3887
Cdd:cd05959  111 LAPVlaaALTKSEHTLVVlivsggagpEAGALLLAELV--AAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADI 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3888 L-NNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPL-FGARVAIVPNAVAhdPQGLLAHVGEQGITVLESVPSLIQ 3965
Cdd:cd05959  189 YwTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLsVGATTVLMPERPT--PAAVFKRIRRYRPTVFFGVPTLYA 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3966 GMLAEER---QALDGLRWMLPTGEAMPPELARQWLKRYpriGL--VNAYGPAE-----CSDDVAffRVDLASTestylpi 4035
Cdd:cd05959  267 AMLAAPNlpsRDLSSLRLCVSAGEALPAEVGERWKARF---GLdiLDGIGSTEmlhifLSNRPG--RVRYGTT------- 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4036 GSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapGErLYRTGDLARRRADGVL 4115
Cdd:cd05959  335 GKPVPGYEVELR----DEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-WTRTGDKYVRDDDGFY 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4116 EYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKY-LVGYLVpgetPRSSADSPAGLmveqgawFERI 4194
Cdd:cd05959  403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTkPKAFVV----LRPGYEDSEAL-------EEEL 471
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15597620 4195 KQQLRADLPDYMVPlHWLV-LDRMPLNANGKLDRKAL 4230
Cdd:cd05959  472 KEFVKDRLAPYKYP-RWIVfVDELPKTATGKIQRFKL 507
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1156-1622 1.75e-38

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 151.82  E-value: 1.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAhl 1235
Cdd:cd05971    9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 ferlpgaegvtpicldslkldnwpsqapglhlhGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTL--DGDDV 1313
Cdd:cd05971   87 ---------------------------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLfpRDGDL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKAPVS-----FDVSVWECFWPLVtgcrlVLAAPGEHRDPARLVELVRQFGVTTLhFVPP-LLQLF--IDEPGVAACG 1385
Cdd:cd05971  134 YWTPADWAwigglLDVLLPSLYFGVP-----VLAHRMTKFDPKAALDLMSRYGVTTA-FLPPtALKMMrqQGEQLKHAQV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1386 SLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTETAINVTHwqCRA----EDGErspIGRPLGNVVCRVLDAEFNLL 1461
Cdd:cd05971  208 KLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGN--CSAlfpiKPGS---MGKPIPGHRVAIVDDNGTPL 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1462 PAGVAGELCIgglglaR--------GYLGRPALSAERFVADPFsaagerlyRTGDRARWNADGVLEYLGRLDQQVKLRGF 1533
Cdd:cd05971  282 PPGEVGEIAV------ElpdpvaflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGY 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1534 RIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLG 1612
Cdd:cd05971  348 RIGPAEIEECLLKHPAVLMAAVVgIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
                        490
                 ....*....|
gi 15597620 1613 PSGKLDTRAL 1622
Cdd:cd05971  428 ATGKIRRREL 437
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
64-554 2.17e-38

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 152.21  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAG----VIAVPAYPPESARRHHqerllSIIADAEPRLVLTTADLREPLlqmNAQLSA 139
Cdd:cd05922   18 GERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLR-----YLVADAGGRIVLADAGAADRL---RDALPA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  140 ANAPQLlcVDQLDPAVAEAWDEPQVRPEH--IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPL 217
Cdd:cd05922   90 SPDPGT--VLDADGIRAARASAPAHEVSHedLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  218 YHDMGLiGGLLQPIFSGVPCVLmSPRYFLERPVrwLEAISQYGGT-VSGGPDFAYRLCSERVAESALQRLdlsgwRVAFS 296
Cdd:cd05922  168 SYDYGL-SVLNTHLLRGATLVL-TNDGVLDDAF--WEDLREHGATgLAGVPSTYAMLTRLGFDPAKLPSL-----RYLTQ 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  297 GSEPIRQDSLERFAEKFAASRfdassFFACYGLAEATLFVTggqrgqgipalavdgeALARNRIAEGEGSVlmccGRSQP 376
Cdd:cd05922  239 AGGRLPQETIARLRELLPGAQ-----VYVMYGQTEATRRMT----------------YLPPERILEKPGSI----GLAIP 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  377 EHAVLIVDaASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKafvERDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIV 455
Cdd:cd05922  294 GGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRK---EGRGGGVLHTGDLARRDeDGFLFIVGRRDRMIKL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  456 RGHNLYPQDIERTVESevpSARKGRVAAFAVTVDGEEGIGIAAEigrgvqksVPAQELIDSIRQAVAEAYqEAPKVVALL 535
Cdd:cd05922  370 FGNRISPTEIEAAARS---IGLIIEAAAVGLPDPLGEKLALFVT--------APDKIDPKDVLRSLAERL-PPYKVPATV 437
                        490       500
                 ....*....|....*....|
gi 15597620  536 NP-GALPKTSSGKLQRSACR 554
Cdd:cd05922  438 RVvDELPLTASGKVDYAALR 457
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3736-4231 2.59e-38

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 150.90  E-value: 2.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLV 3815
Cdd:cd05934    1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3816 CTqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqvysgpqnLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKV 3895
Cdd:cd05934   81 VD----------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSA 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3896 PYLELDENDVIaQTASQSFDIS--VWQFLAAPLFGARVAIVPnavAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQ 3973
Cdd:cd05934  115 RRFGLGEDDVY-LTVLPLFHINaqAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPS 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3974 ALDG---LR-WMlptGEAMPPELARQWLKRYPrIGLVNAYGPAECSDDVAFFRVDLASTEStylpIGSPTDNNRLYLLGa 4049
Cdd:cd05934  191 PDDRahrLRaAY---GAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGPRDEPRRPGS----IGRPAPGYEVRIVD- 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4050 gaDDAFElVPLGAVGELCV---AGTGVGRGYVGDPLRTAQAFvPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVK 4126
Cdd:cd05934  262 --DDGQE-LPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW-------FHTGDLGYRDADGFFYFVDRKKDMIR 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4127 IRGFRIELGEIEARLHERADVREAAVavqegangkylvgYLVPGETprSSADSPAGLMVEQGAWF--ERIKQQLRADLPD 4204
Cdd:cd05934  331 RRGENISSAEVERAILRHPAVREAAV-------------VAVPDEV--GEDEVKAVVVLRPGETLdpEELFAFCEGQLAY 395
                        490       500
                 ....*....|....*....|....*..
gi 15597620 4205 YMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:cd05934  396 FKVPRYIRFVDDLPKTPTEKVAKAQLR 422
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
3251-3677 3.56e-38

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 150.60  E-value: 3.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3251 YPLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMlQVIHKPGRTRIEF 3330
Cdd:cd19533    2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPY-QWIDPYTPVPIRH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3331 LDWSELPEDghEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGES 3410
Cdd:cd19533   81 IDLSGDPDP--EGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3411 RPANLPTPPRYRDYIawLQRQDLEQSRRW------WSESLRGFERPTLVpSDRPFLREHAGESGGMIVGDRYTRldaadg 3484
Cdd:cd19533  159 RPAPPAPFGSFLDLV--EEEQAYRQSERFerdrafWTEQFEDLPEPVSL-ARRAPGRSLAFLRRTAELPPELTR------ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3485 aRLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRpVGMPEMQrTVGLFINSIPLRVQMpAAGQrcTVREW 3564
Cdd:cd19533  230 -TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR-LGAAARQ-TPGMVANTLPLRLTV-DPQQ--TFAEL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3565 LNRLFERNLELREHEHLPLVAI-QESSELPKGQPLFDSLfvfenapVEVSVLDRAQSLNASSDSGRTHTNFP---LTVVC 3640
Cdd:cd19533  304 VAQVSRELRSLLRHQRYRYEDLrRDLGLTGELHPLFGPT-------VNYMPFDYGLDFGGVVGLTHNLSSGPtndLSIFV 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 15597620 3641 YP---GDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALA 3677
Cdd:cd19533  377 YDrddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAA 416
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
172-550 4.62e-38

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 148.19  E-value: 4.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  172 LQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYfleRPVR 251
Cdd:cd05917    7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSF---DPLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  252 WLEAISQYGGTVSGG-----------PDFAyrlcservaesalqRLDLSGWRVAFSGSEPIRQDSLERFAEKFaasrfDA 320
Cdd:cd05917   84 VLEAIEKEKCTALHGvptmfiaelehPDFD--------------KFDLSSLRTGIMAGAPCPPELMKRVIEVM-----NM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  321 SSFFACYGLAEATLFVTGGQRGQGIPAlavdgealarnRIaegeGSVlmccGRSQPEHAVLIVDAASGEVLGDDNVGEIW 400
Cdd:cd05917  145 KDVTIAYGMTETSPVSTQTRTDDSIEK-----------RV----NTV----GRIMPHTEAKIVDPEGGIVPPVGVPGELC 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  401 AAGPSIAHGYWRNPEASAKAFverDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIE-------RTVESE 472
Cdd:cd05917  206 IRGYSVMKGYWNDPEKTAEAI---DGDGWLHTGDLAVMdEDGYCRIVGRIKDMIIRGGENIYPREIEeflhthpKVSDVQ 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  473 V---PSARKGR-VAAFavtVDGEEGIGIAAEigrgvqksvpaqELIDSIRQAVaeAYQEAPKVValLNPGALPKTSSGKL 548
Cdd:cd05917  283 VvgvPDERYGEeVCAW---IRLKEGAELTEE------------DIKAYCKGKI--AHYKVPRYV--FFVDEFPLTVSGKI 343

                 ..
gi 15597620  549 QR 550
Cdd:cd05917  344 QK 345
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1132-1631 4.74e-38

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 152.45  E-value: 4.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPD 1211
Cdd:PRK06188   16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1212 YPSERLAYMLADSGVELLLTQAHLF--------ERLPGAEGVTPICLDSLKLDNW-------PSQAPGLHLHGDnLAYVI 1276
Cdd:PRK06188   96 GSLDDHAYVLEDAGISTLIVDPAPFveralallARVPSLKHVLTLGPVPDGVDLLaaaakfgPAPLVAAALPPD-IAGLA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1277 YTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWecFWP-LVTGCRLVLAApgeHRDPARLVE 1355
Cdd:PRK06188  175 YTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF--FLPtLLRGGTVIVLA---KFDPAEVLR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1356 LVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEAL-PAELRNRVLQRLPAVALHnrYGPTETAINVTHW-- 1430
Cdd:PRK06188  250 AIEEQRITATFLVPTMIYALLDHPDLRTrdLSSLETVYYGASPMsPVRLAEAIERFGPIFAQY--YGQTEAPMVITYLrk 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1431 --QCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvadpfsaAGERLyRTGD 1508
Cdd:PRK06188  328 rdHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGWL-HTGD 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1509 RARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLVGYYTGAV----GAEAEAEQnq 1584
Cdd:PRK06188  400 VAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVI---GVPDEKWGEAVTAVVvlrpGAAVDAAE-- 474
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 15597620  1585 rLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQRE 1631
Cdd:PRK06188  475 -LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRG 520
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1730-2155 5.54e-38

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 149.91  E-value: 5.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVD-GVPVQRVHGDGGLHMDWQ 1808
Cdd:cd19536    3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1809 DFSALdrDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHY-LVVTLHHIVTEGWAMDIFARELGALYEAFLDd 1887
Cdd:cd19536   83 DLTPL--EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLE- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1888 rESPLEPLPVQ-YLDYSVWQREWLESGERQRqldYWKAQLGNehplleLPGDRPRPPVQSHQGDLYR---FDLSPELAER 1963
Cdd:cd19536  160 -YKPLSLPPAQpYRDFVAHERASIQQAASER---YWREYLAG------ATLATLPALSEAVGGGPEQdseLLVSVPLPVR 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1964 VRRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRIRPES--EGLIGAFLNTQVLRCRLDGQmSVGELLEQVR 2041
Cdd:cd19536  230 SRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTgaERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQ 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2042 QTVIDGQSHQDLPfdhlVEALQppRSAAYNPLFQVMCNVQRWEFQQTRQLAG---MTVEYIANDARATKFDLNLEVTDLD 2118
Cdd:cd19536  309 EQELESLSHEQVP----LADIQ--RCSEGEPLFDSIVNFRHFDLDFGLPEWGsdeGMRRGLLFSEFKSNYDVNLSVLPKQ 382
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15597620 2119 QRLGCCLTYSRDLFDEPRIARMAGHWQNLLEALLGDP 2155
Cdd:cd19536  383 DRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
64-550 6.95e-38

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 149.75  E-value: 6.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesARRhhQERLLSIIADAEPRLVLTtadlrepllqmnaqlsaanap 143
Cdd:cd05934   28 GDRVALMLDNCPEFLFAWFALAKLGAVLVPINT---ALR--GDELAYIIDHSGAQLVVV--------------------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  144 qllcvdqlDPAVaeawdepqvrpehiafLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGL 223
Cdd:cd05934   82 --------DPAS----------------ILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQ 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  224 IGGLLQPIFSGVPCVLMsPRYfleRPVRWLEAISQYGGTVS---GGPdFAYRLCSERVAESALQRLdlsgwRVAFSGseP 300
Cdd:cd05934  138 AVSVLAALSVGATLVLL-PRF---SASRFWSDVRRYGATVTnylGAM-LSYLLAQPPSPDDRAHRL-----RAAYGA--P 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  301 IRQDSLERFAEKFAASRFDAssffacYGLAEaTLFVTGGQRGQGIPAlavdgealarnriaegegsvlMCCGRSQPEHAV 380
Cdd:cd05934  206 NPPELHEEFEERFGVRLLEG------YGMTE-TIVGVIGPRDEPRRP---------------------GSIGRPAPGYEV 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  381 LIVDAaSGEVLGDDNVGEI---WAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVR 456
Cdd:cd05934  258 RIVDD-DGQELPAGEPGELvirGLRGWGFFKGYYNMPEATAEAM--RNG--WFHTGDLGYRDaDGFFYFVDRKKDMIRRR 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  457 GHNLYPQDIERTVESeVPSARkgRVAAFAVTVD-GEEGIgIAAEIGRGVQKSVPAqELIDSIRQAVaeAYQEAPKVVALL 535
Cdd:cd05934  333 GENISSAEVERAILR-HPAVR--EAAVVAVPDEvGEDEV-KAVVVLRPGETLDPE-ELFAFCEGQL--AYFKVPRYIRFV 405
                        490
                 ....*....|....*
gi 15597620  536 NpgALPKTSSGKLQR 550
Cdd:cd05934  406 D--DLPKTPTEKVAK 418
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
6-552 1.29e-37

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 152.11  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     6 ELPTT-------LVQALRRRAVQEPERLALRFLAEDdgegvvLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDY 77
Cdd:PRK06710   14 EIPSTisydiqpLHKYVEQMASRYPEKKALHFLGKD------ITFSVFHDKVKRFANYLQKLgVEKGDRVAIMLPNCPQA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    78 VAAFFGCLYAGVIAVPAYP--------------------------PESARRHHQERLLSIIADAEPRLVLTTADLREPLL 131
Cdd:PRK06710   88 VIGYYGTLLAGGIVVQTNPlytereleyqlhdsgakvilcldlvfPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   132 Q---MNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVL-IRRGFG-IG 206
Cdd:PRK06710  168 QkkqSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMgVQWLYNcKE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   207 ADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPRYFLERPvrwLEAISQYGGTV-SGGPDFAYRLCSERVaesaLQR 285
Cdd:PRK06710  248 GEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI-PKFDMKMV---FEAIKKHKVTLfPGAPTIYIALLNSPL----LKE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   286 LDLSGWRVAFSGSEPIRQDSLERFaekfaaSRFDASSFFACYGLAEATlfvtggqrgqgiPAlaVDGEALARNRIAegeG 365
Cdd:PRK06710  320 YDISSIRACISGSAPLPVEVQEKF------ETVTGGKLVEGYGLTESS------------PV--THSNFLWEKRVP---G 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   366 SVlmccGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKafVERDGrtWLRTGDLGFL-RDGELF 444
Cdd:PRK06710  377 SI----GVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAA--VLQDG--WLHTGDVGYMdEDGFFY 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   445 VTGRLKDMLIVRGHNLYPQDIERTV-ESE---------VPSARKGR-VAAFAVTVDGEEGigiaaeigrgvqksvpAQEL 513
Cdd:PRK06710  449 VKDRKKDMIVASGFNVYPREVEEVLyEHEkvqevvtigVPDPYRGEtVKAFVVLKEGTEC----------------SEEE 512
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 15597620   514 IDSIRQAVAEAYQeAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:PRK06710  513 LNQFARKYLAAYK-VPKVYEFRD--ELPKTTVGKILRRV 548
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
15-552 1.40e-37

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 150.50  E-value: 1.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   15 LRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:cd17646    4 VAEQAARTPDAPAVVD------EGRTLTYRELDERANRLAHLLRARgVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 ---AYPPEsarrhhqeRLLSIIADAEPRLVLTTADLREPLlqmnaqlsAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIA 170
Cdd:cd17646   78 ldpGYPAD--------RLAYMLADAGPAVVLTTADLAARL--------PAGGDVALLGDEALAAPPATPPLVPPRPDNLA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  171 FLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPRyfLERPV 250
Cdd:cd17646  142 YVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARPG--GHRDP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  251 RWL-EAISQYGGTVSggpDFAYRLCSERVAESALQRLDlsGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGL 329
Cdd:cd17646  219 AYLaALIREHGVTTC---HFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNL------YGP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  330 AEATLFVTGGQrgqgipalaVDGEAlarnriaeGEGSVLMccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHG 409
Cdd:cd17646  288 TEAAIDVTHWP---------VRGPA--------ETPSVPI--GRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARG 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  410 YWRNPEASAKAFVE---RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVesevpsARKGRVAAFA 485
Cdd:cd17646  348 YLGRPALTAERFVPdpfGPGSRMYRTGDLArWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAAL------AAHPAVTHAV 421
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  486 VTVDGEEGIG---IAAEIGRGVQKSVPAQELidsiRQAVAEAYQEA--PKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd17646  422 VVARAAPAGAarlVGYVVPAAGAAGPDTAAL----RAHLAERLPEYmvPAAFVVLD--ALPLTANGKLDRAA 487
PRK08316 PRK08316
acyl-CoA synthetase; Validated
10-559 2.62e-37

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 150.47  E-value: 2.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAG 88
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVF------GDRSWTYAELDAAVnRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    89 VIAVPA----YPPESARrhhqerllsIIADAEPRLVLTTADLRePLLQMNAQLSAANAPQLLCV-----------DQLDP 153
Cdd:PRK08316   86 AVHVPVnfmlTGEELAY---------ILDHSGARAFLVDPALA-PTAEAALALLPVDTLILSLVlggreapggwlDFADW 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   154 AVAEAWDEPQVRP--EHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPI 231
Cdd:PRK08316  156 AEAGSVAEPDVELadDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   232 FSGVPCVLM-SPryfleRPVRWLEAISQYGGT-----------VSGGPDFAYRlcservaesalqrlDLSGWRVAFSGSE 299
Cdd:PRK08316  236 YVGATNVILdAP-----DPELILRTIEAERITsffapptvwisLLRHPDFDTR--------------DLSSLRKGYYGAS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   300 PIRQDSLERFAEKFAASRfdassFFACYGLAEatlfvtggqrgqgIPALAVdgeALARNRIAEGEGSvlmcCGRsqpehA 379
Cdd:PRK08316  297 IMPVEVLKELRERLPGLR-----FYNCYGQTE-------------IAPLAT---VLGPEEHLRRPGS----AGR-----P 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   380 VL-----IVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDML 453
Cdd:PRK08316  347 VLnvetrVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF--RGG--WFHSGDLGVMdEEGYITVVDRKKDMI 421
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   454 IVRGHNLYPQDIERTVE-----SEV-----PSARKGR-VAAFAVTVDGEEgigiaaeigrgvqksVPAQELIDSIRQAVA 522
Cdd:PRK08316  422 KTGGENVASREVEEALYthpavAEVaviglPDPKWIEaVTAVVVPKAGAT---------------VTEDELIAHCRARLA 486
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 15597620   523 eAYQeAPKVVALLNpgALPKTSSGKLQRSACRLRLED 559
Cdd:PRK08316  487 -GFK-VPKRVIFVD--ELPRNPSGKILKRELRERYAG 519
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
64-554 2.70e-37

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 149.83  E-value: 2.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPA---YPPESAR---RHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQL 137
Cdd:cd05959   54 EERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlLTPDDYAyylEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  138 SAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRG-FGIGADDVIVSWLP 216
Cdd:cd05959  134 GAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAK 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  217 LYHDMGLIGGLLQPIFSGVPCVLMSPRyflERPVRWLEAISQYGGTV-SGGPD-FAYRLCSERVAESALQRLdlsgwRVA 294
Cdd:cd05959  214 LFFAYGLGNSLTFPLSVGATTVLMPER---PTPAAVFKRIRRYRPTVfFGVPTlYAAMLAAPNLPSRDLSSL-----RLC 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  295 FSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEAT-LFVTggqrgqgipalavdgealarNRiaegEGSV-LMCCG 372
Cdd:cd05959  286 VSAGEALPAEVGERWKARFGLDILDG------IGSTEMLhIFLS--------------------NR----PGRVrYGTTG 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  373 RSQPEHAVLIVDAASGEVlGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVErdgrTWLRTGDlGFLR--DGELFVTGRLK 450
Cdd:cd05959  336 KPVPGYEVELRDEDGGDV-ADGEPGELYVRGPSSATMYWNNRDKTRDTFQG----EWTRTGD-KYVRddDGFYTYAGRAD 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  451 DMLIVRGHNLYPQDIERTV-------ESEVPSA----RKGRVAAFAVTVDGEEGIGIAAEigrgvqksvpaqELIDSIRQ 519
Cdd:cd05959  410 DMLKVSGIWVSPFEVESALvqhpavlEAAVVGVededGLTKPKAFVVLRPGYEDSEALEE------------ELKEFVKD 477
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620  520 AVAeAYQeAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05959  478 RLA-PYK-YPRWIVFVD--ELPKTATGKIQRFKLR 508
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1130-1618 3.80e-37

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 150.58  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK06178   35 LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVELLLTQ---AHLFERLPGAEGVTPICLDSLK-------------------------------L 1255
Cdd:PRK06178  115 PLFREHELSYELNDAGAEVLLALdqlAPVVEQVRAETSLRHVIVTSLAdvlpaeptlplpdslraprlaaagaidllpaL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1256 DNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAerlqWMQATYTL-----DGDDVLMQKAPVsfdvsvwecF 1330
Cdd:PRK06178  195 RACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV----YTAAAAYAvavvgGEDSVFLSFLPE---------F 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1331 W----------PLVTGCRLVLAApgehR-DPARLVELVRQFGVT-TLHFVPPLLQLfIDEPGVAA--CGSLR--RLFSGG 1394
Cdd:PRK06178  262 WiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTrTVMLVDNAVEL-MDHPRFAEydLSSLRqvRVVSFV 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1395 EALPAELRNRVLQRLPAVALHNRYGPTETAINVTH---WQCRAEDGERSPI--GRPLGNVVCRVLDAEFN-LLPAGVAGE 1468
Cdd:PRK06178  337 KKLNPDYRQRWRALTGSVLAEAAWGMTETHTCDTFtagFQDDDFDLLSQPVfvGLPVPGTEFKICDFETGeLLPLGAEGE 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1469 LCIGGLGLARGYLGRPALSAERFVadpfsaagERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQP 1548
Cdd:PRK06178  417 IVVRTPSLLKGYWNKPEATAEALR--------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  1549 GVAQAVVVIR--EGvAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPtQLMRLAQMPLGPSGKLD 1618
Cdd:PRK06178  489 AVLGSAVVGRpdPD-KGQVPVAFVQLKPGADLTAAA---LQAWCRENMAVYKVP-EIRIVDALPMTATGKVR 555
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2212-2661 4.25e-37

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 147.66  E-value: 4.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHA 2291
Cdd:cd05973    1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2292 ALFEALgelpagvarwcleEDGPALdaedpaplaalsgpqhqayLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRA 2371
Cdd:cd05973   81 ANRHKL-------------DSDPFV-------------------MMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRP 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2372 EDCelhFYSINFDAASERL----LAPLLCGARVVLRAqGQWGAEEICELIRAEGVSILGFTPS-YGSQLAQWLESQGR-Q 2445
Cdd:cd05973  129 EDS---FWNAADPGWAYGLyyaiTGPLALGHPTILLE-GGFSVESTWRVIERLGVTNLAGSPTaYRLLMAAGAEVPARpK 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2446 LPVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTEtVVMPLA-CLAPER-LEEGAASVPigsVVGARVAyILDADLA 2523
Cdd:cd05973  205 GRLRRVSSAGEPLTPEVIRWFDAALG-VPIHDHYGQTE-LGMVLAnHHALEHpVHAGSAGRA---MPGWRVA-VLDDDGD 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2524 LVPQGATGELyvggaglARGYHERPALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGE 2603
Cdd:cd05973  279 ELGPGEPGRL-------AIDIANSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFD 351
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620 2604 IEARLLEHPQVREALVLALDSP-SGKQLAGYVasaVAEQDEDAQAALREALKTHLKQQL 2661
Cdd:cd05973  352 VESALIEHPAVAEAAVIGVPDPeRTEVVKAFV---VLRGGHEGTPALADELQLHVKKRL 407
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1140-1616 4.45e-37

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 149.26  E-value: 4.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1140 QSAERVALEWDGGS-LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLA 1218
Cdd:PRK07514   14 ADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1219 YMLADSGVELLLTQAHLFERL-PGAEGVTPICLDSLKLDNWPS------QAPGLHL----HGDNLAYVIYTSGSTGQPKG 1287
Cdd:PRK07514   94 YFIGDAEPALVVCDPANFAWLsKIAAAAGAPHVETLDADGTGSlleaaaAAPDDFEtvprGADDLAAILYTSGTTGRSKG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1288 VGNTHAALAERLQWMQATYTLDGDDVLMQKAP--------VSFDVSvwecfwpLVTGCRLVLAApgeHRDPARLVELVRQ 1359
Cdd:PRK07514  174 AMLSHGNLLSNALTLVDYWRFTPDDVLIHALPifhthglfVATNVA-------LLAGASMIFLP---KFDPDAVLALMPR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1360 fgVTTLHFVPPLLQLFIDEPGV--AACGSLRRLFSGGEALPAELRNRVLQRLPAVALHnRYGPTETAINVTHwqcrAEDG 1437
Cdd:PRK07514  244 --ATVMMGVPTFYTRLLQEPRLtrEAAAHMRLFISGSAPLLAETHREFQERTGHAILE-RYGMTETNMNTSN----PYDG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1438 ERSP--IGRPLGNVVCRVLDAEFNL-LPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNA 1514
Cdd:PRK07514  317 ERRAgtVGFPLPGVSLRVTDPETGAeLPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1515 DGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQnqrLRAAL 1590
Cdd:PRK07514  390 RGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI---GVPhpdfGEGVTAVVVPKPGAALDEAA---ILAAL 463
                         490       500
                  ....*....|....*....|....*.
gi 15597620  1591 QAELPEYMVPTQLMRLAQMPLGPSGK 1616
Cdd:PRK07514  464 KGRLARFKQPKRVFFVDELPRNTMGK 489
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1138-1631 1.14e-36

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 148.95  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1138 LAQSAER----VALEWDGGSLGYAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:PRK08314   16 LEVSARRypdkTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1213 PSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPI-CL------------DSLKLDNW-----PSQA------------ 1262
Cdd:PRK08314   96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLrHVivaqysdylpaePEIAVPAWlraepPLQAlapggvvawkea 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1263 ------PGLHLHG-DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFDVSVWECFW--PL 1333
Cdd:PRK08314  176 laaglaPPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTGMVHSMnaPI 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1334 VTGCRLVLaAPGEHRDPARlvELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRvLQRLPA 1411
Cdd:PRK08314  255 YAGATVVL-MPRWDREAAA--RLIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMPEAVAER-LKELTG 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1412 VALHNRYGPTETaINVTHW--------QCraedgerspIGRPLGNVVCRVLDAE-FNLLPAGVAGELCIGGLGLARGYLG 1482
Cdd:PRK08314  331 LDYVEGYGLTET-MAQTHSnppdrpklQC---------LGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1483 RPALSAERFVadpfSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGV------------ 1550
Cdd:PRK08314  401 RPEATAEAFI----EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIqeacviatpdpr 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1551 ----AQAVVVIREGvagsqlvgyYTGAVGAEaeaeqnqRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPV 1626
Cdd:PRK08314  477 rgetVKAVVVLRPE---------ARGKTTEE-------EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQE 540

                  ....*
gi 15597620  1627 WQQRE 1631
Cdd:PRK08314  541 KARAA 545
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
2187-2619 1.49e-36

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 147.77  E-value: 1.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2187 TLHGLFAARVAASPQAPALTFA--GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYV 2264
Cdd:cd05904    6 PLDSVSFLFASAHPSRPALIDAatGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2265 PLDPEYPLERLQYMIEDSGVRLLLSHAALFE----------ALGELPAGvarwCLEEDGPALDAEDPAPLAALSGPQHQA 2334
Cdd:cd05904   86 TANPLSTPAEIAKQVKDSGAKLAFTTAELAEklaslalpvvLLDSAEFD----SLSFSDLLFEADEAEPPVVVIKQDDVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2335 YLIYTSGSTGKPKGVAVSHGE-IAMHCAAV-IECFGMRAEDCEL------HFYSINFdaaseRLLAPLLCGARVVlrAQG 2406
Cdd:cd05904  162 ALLYSSGTTGRSKGVMLTHRNlIAMVAQFVaGEGSNSDSEDVFLcvlpmfHIYGLSS-----FALGLLRLGATVV--VMP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2407 QWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETV 2485
Cdd:cd05904  235 RFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSsLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2486 VMPLACLAPERLEEGAASVpiGSVVGARVAYILDAD-LALVPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaeg 2564
Cdd:cd05904  315 GVVAMCFAPEKDRAKYGSV--GRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE------ 386
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620 2565 GRLyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALV 2619
Cdd:cd05904  387 GWL-HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
2211-2689 1.59e-36

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 146.46  E-value: 1.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2211 TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSH 2290
Cdd:cd17654   16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2291 AalfealgelpagvarwclEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMR 2370
Cdd:cd17654   96 K------------------ELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2371 AEDCeLHFYSIN-FDAASERLLAPLLCGArVVLRAQGQWGAEEIC---ELIRAEGVSILGFTPS----YGSQLAQWlESQ 2442
Cdd:cd17654  158 SEDI-LFLTSPLtFDPSVVEIFLSLSSGA-TLLIVPTSVKVLPSKladILFKRHRITVLQATPTlfrrFGSQSIKS-TVL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2443 GRQLPVRMCITGGEALTGEHLQR-IRQAFAPASFFNAYGPTETVVMPLAclapERLEEGAASVPIGSVVGARVAYILDad 2521
Cdd:cd17654  235 SATSSLRVLALGGEPFPSLVILSsWRGKGNRTRIFNIYGITEVSCWALA----YKVPEEDSPVQLGSPLLGTVIEVRD-- 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2522 laLVPQGATGELYVGGagLARGYherpalsaerFVPDPFAAEGGRLYRTGDLVRLcDNGQVEYVGRIDHQVKIRGFRIEL 2601
Cdd:cd17654  309 --QNGSEGTGQVFLGG--LNRVC----------ILDDEVTVPKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINL 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2602 GEIEARLLEHPQVrEALVLALdSPSGKQLAGYVasavaeqDEDAQAALREALKTHLKQ--QLPDYMVpahllLLASLPLT 2679
Cdd:cd17654  374 DLIQQVIESCLGV-ESCAVTL-SDQQRLIAFIV-------GESSSSRIHKELQLTLLSshAIPDTFV-----QIDKLPLT 439
                        490
                 ....*....|
gi 15597620 2680 ANGKLDRRAL 2689
Cdd:cd17654  440 SHGKVDKSEL 449
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1109-1624 1.98e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 148.15  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1109 AEQAAHLAEWGSAPCEPARAwlpellerqLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERS 1188
Cdd:PRK07788   39 LRLAADIRRYGPFAGLVAHA---------ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1189 PQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAE-------------------GVTPIC 1249
Cdd:PRK07788  110 RGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPpdlgrlrawggnpdddepsGSTDET 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1250 LDSLKLDNWPSQAPGLHLHGdnlAYVIYTSGSTGQPKGVGNTH----AALAERLQWMqatyTLDGDDVLMQKAPVsFDVS 1325
Cdd:PRK07788  190 LDDLIAGSSTAPLPKPPKPG---GIVILTSGTTGTPKGAPRPEpsplAPLAGLLSRV----PFRAGETTLLPAPM-FHAT 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1326 VWECF---WPLvtGCRLVLaapgeHR--DPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA----CGSLRRLFSGGEA 1396
Cdd:PRK07788  262 GWAHLtlaMAL--GSTVVL-----RRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLakydTSSLKIIFVSGSA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1397 LPAELRNRVLQRLPAVaLHNRYGPTETAINVThwqCRAEDGERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGL 1474
Cdd:PRK07788  335 LSPELATRALEAFGPV-LYNLYGSTEVAFATI---ATPEDLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1475 GLARGYLGrpalsaerfVADPFSAAGerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAV 1554
Cdd:PRK07788  411 FPFEGYTD---------GRDKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAA 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  1555 VVireGVA----GSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK07788  480 VI---GVDdeefGQRLRAFVVKAPGAALDEDA---IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1130-1622 2.19e-36

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 147.60  E-value: 2.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAI----CAErspqLLVGLLAIVKAGGAY 1205
Cdd:COG1021   27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVqlpnVAE----FVIVFFALFRAGAIP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1206 VPLdpdYPSER---LAYMLADSGVELLLTQAH------------LFERLPGAEGV-------TPICLDSLklDNWPSQAP 1263
Cdd:COG1021  103 VFA---LPAHRraeISHFAEQSEAVAYIIPDRhrgfdyralareLQAEVPSLRHVlvvgdagEFTSLDAL--LAAPADLS 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1264 GLHLHGDNLAYVIYTSGSTGQPKGVGNTHA-------ALAERLQwmqatytLDGDDVLMQKAPVS--FDVSVWECFWPLV 1334
Cdd:COG1021  178 EPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylysvrASAEICG-------LDADTVYLAALPAAhnFPLSSPGVLGVLY 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1335 TGCRLVLAAPGehrDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGV--AACGSLRRLFSGGEALPAELRNRVLQRLPAv 1412
Cdd:COG1021  251 AGGTVVLAPDP---SPDTAFPLIERERVTVTALVPPLALLWLDAAERsrYDLSSLRVLQVGGAKLSPELARRVRPALGC- 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1413 ALHNRYGPTETAINVThwqcRAEDGE---RSPIGRPL--GNVVcRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALS 1487
Cdd:COG1021  327 TLQQVFGMAEGLVNYT----RLDDPEeviLTTQGRPIspDDEV-RIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHN 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1488 AERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLv 1567
Cdd:COG1021  402 ARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV---AMPDEYL- 470
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1568 GYYTGAV----GAEAEAEQnqrLRAALQA-ELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:COG1021  471 GERSCAFvvprGEPLTLAE---LRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
2187-2689 2.83e-36

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 146.32  E-value: 2.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2187 TLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL 2266
Cdd:cd05920   16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2267 DPEYPLERLQYMIEDSGVRLLLshaalfealgelpagVARwcleedgpALDAEDPAPLA---ALSGPQhQAYLIYTSGST 2343
Cdd:cd05920   96 LPSHRRSELSAFCAHAEAVAYI---------------VPD--------RHAGFDHRALArelAESIPE-VALFLLSGGTT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2344 GKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSI--NFDAASERLLAPLLCGARVVLRAQGQwgAEEICELIRAEG 2421
Cdd:cd05920  152 GTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAahNFPLACPGVLGTLLAGGRVVLAPDPS--PDAAFPLIEREG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2422 VSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPaSFFNAYGPTETVVMPLACLAPERLEEG 2500
Cdd:cd05920  230 VTVTALVPALVSLWLDAAASRRADLSsLRLLQVGGARLSPALARRVPPVLGC-TLQQVFGMAEGLLNYTRLDDPDEVIIH 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2501 AASVPIGSVVGARVAyilDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNG 2580
Cdd:cd05920  309 TQGRPMSPDDEIRVV---DEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDG 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2581 QVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaVAEQDEDAQAALREALKthlKQ 2659
Cdd:cd05920  379 YLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMpDELLGERSCAFV---VLRDPPPSAAQLRRFLR---ER 452
                        490       500       510
                 ....*....|....*....|....*....|
gi 15597620 2660 QLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05920  453 GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1121-1624 4.67e-36

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 146.83  E-value: 4.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1121 APCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVK 1200
Cdd:PRK06155   14 DPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAW 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1201 AGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAE-GVTPI----CLDSLKLDNWP------------SQAP 1263
Cdd:PRK06155   94 LGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADpGDLPLpavwLLDAPASVSVPagwstaplppldAPAP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1264 GLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFDVSVWECFWP-LVTGCRLVLa 1342
Cdd:PRK06155  174 AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPL-FHTNALNAFFQaLLAGATYVL- 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1343 apGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGeaLPAELRNRVLQRLpAVALHNRYGP 1420
Cdd:PRK06155  252 --EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESdrAHRVRVALGPG--VPAALHAAFRERF-GVDLLDGYGS 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1421 TET--AINVTHwqcraedGERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGG---LGLARGYLGRPALSAErfva 1493
Cdd:PRK06155  327 TETnfVIAVTH-------GSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE---- 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1494 dpfsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVgyyTG 1572
Cdd:PRK06155  396 ----AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAaAVFPVPSELGEDEVM---AA 468
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597620  1573 AVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK06155  469 VVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
9-560 4.81e-36

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 147.45  E-value: 4.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRFLaeddgeGVVLSYRDLD-LRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYA 87
Cdd:PRK05605   32 TTLVDLYDNAVARFGDRPALDFF------GATTTYAELGkQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    88 GVIAV---PAYPPESARRH---HQERLLSI---IADAEPRLVLTTA-------DLRE--PLLQ-------------MNAQ 136
Cdd:PRK05605  106 GAVVVehnPLYTAHELEHPfedHGARVAIVwdkVAPTVERLRRTTPletivsvNMIAamPLLQrlalrlpipalrkARAA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   137 LSAAnAPQLLCVDQL----DPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIR---RGFGIGaDD 209
Cdd:PRK05605  186 LTGP-APGTVPWETLvdaaIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKawvPGLGDG-PE 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   210 VIVSWLPLYHDMGL-IGGLLQPIFSGVPCVLMSPRYFL------ERPVRWLEAIsqyggtvsggPDFAYRLcserVAESA 282
Cdd:PRK05605  264 RVLAALPMFHAYGLtLCLTLAVSIGGELVLLPAPDIDLildamkKHPPTWLPGV----------PPLYEKI----AEAAE 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   283 LQRLDLSGWRVAFSGSEPIRQDSLERFaEKFAASRfdassFFACYGLAEATlfvtggqrgqgiPALAvdGEALARNRIAe 362
Cdd:PRK05605  330 ERGVDLSGVRNAFSGAMALPVSTVELW-EKLTGGL-----LVEGYGLTETS------------PIIV--GNPMSDDRRP- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   363 geGSVlmccGRSQPEHAVLIVDAAS-GEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVerDGrtWLRTGDLGFL-RD 440
Cdd:PRK05605  389 --GYV----GVPFPDTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL--DG--WFRTGDVVVMeED 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   441 GELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKGRVAAFAvTVDGEEGIGIAAEIGRGVqkSVPAQELIDSIRQA 520
Cdd:PRK05605  459 GFIRIVDRIKELIITGGFNVYPAEVEEVLR-EHPGVEDAAVVGLP-REDGSEEVVAAVVLEPGA--ALDPEGLRAYCREH 534
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 15597620   521 VAeAYQeAPKVVALLNpgALPKTSSGKLQRSACRLRLEDG 560
Cdd:PRK05605  535 LT-RYK-VPRRFYHVD--ELPRDQLGKVRRREVREELLEK 570
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
2212-2689 5.71e-36

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 144.16  E-value: 5.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHA 2291
Cdd:cd05935    2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2292 ALfEALGELPagvarwcleedgpaldaedpaplaalsgpqhqayliYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRA 2371
Cdd:cd05935   82 EL-DDLALIP------------------------------------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2372 ED----CELHFYSINFDAAserLLAPLLCGARVVLraQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP 2447
Cdd:cd05935  125 SDvilaCLPLFHVTGFVGS---LNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLS 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2448 -VRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETvvMPLACLAP-ERLEEGAASVPIgSVVGARVAYIldADLALV 2525
Cdd:cd05935  200 sLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTET--MSQTHTNPpLRPKLQCLGIP*-FGVDARVIDI--ETGREL 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2526 PQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIE 2605
Cdd:cd05935  274 PPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2606 ARLLEHPQVREALVLALDSPSgkqlAGYVASAVAEQDEDAQA-ALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKL 2684
Cdd:cd05935  350 AKLYKHPAI*EVCVISVPDER----VGEEVKAFIVLRPEYRGkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425

                 ....*
gi 15597620 2685 DRRAL 2689
Cdd:cd05935  426 LWRLL 430
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
1156-1556 7.63e-36

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 144.28  E-value: 7.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQahl 1235
Cdd:cd05907    8 WAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE--- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 ferlpgaegvtpicldslkldnwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLM 1315
Cdd:cd05907   85 --------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1316 QKAPVS--FDVSVWECFwPLVTGCRLVLAapgehRDPARLVELVRQFGVTTLHFVP----------------PLLQLFID 1377
Cdd:cd05907  133 SFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPrvwekvyaaikvkavpGLKRKLFD 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1378 epgVAACGSLRRLFSGGEALPAELrNRVLQRLpAVALHNRYGPTET--AINVTHWQCRAEDgersPIGRPLGNVVCRVld 1455
Cdd:cd05907  207 ---LAVGGRLRFAASGGAPLPAEL-LHFFRAL-GIPVYEGYGLTETsaVVTLNPPGDNRIG----TVGKPLPGVEVRI-- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1456 aefnllpaGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRL-DQQVKLRGFR 1534
Cdd:cd05907  276 --------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKN 340
                        410       420
                 ....*....|....*....|..
gi 15597620 1535 IEPEEIQARLLAQPGVAQAVVV 1556
Cdd:cd05907  341 ISPEPIENALKASPLISQAVVI 362
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
3729-4230 7.96e-36

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 144.14  E-value: 7.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3729 RIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPghptqRLTRivel 3808
Cdd:cd05919    1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP-----LLHP---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3809 srtlvlvctqacREQALALFDElgcvdRPRLLVWDEiqqgegaehdpqvysgpQNLAYVIYTSGSTGLPKGVMVEQAG-M 3887
Cdd:cd05919   72 ------------DDYAYIARDC-----EARLVVTSA-----------------DDIAYLLYSSGTTGPPKGVMHAHRDpL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3888 LNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNAVahDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:cd05919  118 LFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAvGASAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYAN 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3967 MLAE---ERQALDGLRWMLPTGEAMPPELARQWLKRYPrIGLVNAYGpaeCSDDVAFF---RVDLASTESTYLPIgsPTD 4040
Cdd:cd05919  196 LLDScagSPDALRSLRLCVSAGEALPRGLGERWMEHFG-GPILDGIG---ATEVGHIFlsnRPGAWRLGSTGRPV--PGY 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4041 NNRLyllgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapgERLYRTGDLARRRADGVLEYVGR 4120
Cdd:cd05919  270 EIRL------VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGR 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4121 IDHQVKIRGFRIELGEIEARLHERADVREAA-VAVQEGANGKYLVGYLVPgETPRSSadspaglmveQGAWFERIKQQLR 4199
Cdd:cd05919  336 ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAvVAVPESTGLSRLTAFVVL-KSPAAP----------QESLARDIHRHLL 404
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15597620 4200 ADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05919  405 ERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1269-1620 1.16e-35

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 141.75  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1269 GDNLaYVIYTSGSTGQPKGV----GNTHAALAERLQWMQATYTLD----------GDDVLMQKAPVSFDVSVWECFWPLV 1334
Cdd:cd05924    3 ADDL-YILYTGGTTGMPKGVmwrqEDIFRMLMGGADFGTGEFTPSedahkaaaaaAGTVMFPAPPLMHGTGSWTAFGGLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1335 TGCRLVLaaPGEHRDPARLVELVRQFGVTTLHFV-----PPLLQLfIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRL 1409
Cdd:cd05924   82 GGQTVVL--PDDRFDPEEVWRTIEKHKVTSMTIVgdamaRPLIDA-LRDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1410 PAVALHNRYGPTETAINVTHwQCRAEDGERSPIGRPLGNVVcrVLDAEFNLLPAGVAGELCIGGLGL-ARGYLGRPALSA 1488
Cdd:cd05924  159 PNITLVDAFGSSETGFTGSG-HSAGSGPETGPFTRANPDTV--VLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1489 ERFVadpfSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GS 1564
Cdd:cd05924  236 ETFP----EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV---GRPderwGQ 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 1565 QLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTR 1620
Cdd:cd05924  309 EVVAVVQLREGAGVDLEE---LREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1154-1617 1.26e-35

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 143.43  E-value: 1.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQA 1233
Cdd:cd05973    1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaegvtpicldslklDNWPSQAPGLHLHgdnlayvIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDV 1313
Cdd:cd05973   81 ----------------------ANRHKLDSDPFVM-------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKAPVSFDVSVWECFW-PLVTGCRLVLAAPGehRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC---GSLRR 1389
Cdd:cd05973  132 FWNAADPGWAYGLYYAITgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPArpkGRLRR 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1390 LFSGGEALPAELRNRVLQRLpAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGEL 1469
Cdd:cd05973  210 VSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRL 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1470 CI----GGLGLARGYLGRPAlsaerfvadpfSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:cd05973  289 AIdianSPLMWFRGYQLPDT-----------PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALI 357
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 1546 AQPGVAQAVVVIR-EGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:cd05973  358 EHPAVAEAAVIGVpDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3737-4225 1.47e-35

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 144.28  E-value: 1.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVC 3816
Cdd:cd05911    9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3817 TQACREQALALFDELGCVDR------------PRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQ 3884
Cdd:cd05911   89 DPDGLEKVKEAAKELGPKDKiivlddkpdgvlSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3885 AGMLNN-QLSKVPYLELDENDVIAQTASQSFDIS-VWQFLAAPLFGARVAIVPNAvahDPQGLLAHVGEQGITVLESVPS 3962
Cdd:cd05911  169 RNLIANlSQVQTFLYGNDGSNDVILGFLPLYHIYgLFTTLASLLNGATVIIMPKF---DSELFLDLIEKYKITFLYLVPP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3963 LIQgMLAE----ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVA---FFRVDLASTestylpi 4035
Cdd:cd05911  246 IAA-ALAKspllDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSV------- 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4036 GSPTDNNRLYLLGagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRADGVL 4115
Cdd:cd05911  318 GRLLPNVEAKIVD---DDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4116 EYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVPGETprsSADSPAGLMV-EQGAWF--E 4192
Cdd:cd05911  388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV-----------IG--IPDEV---SGELPRAYVVrKPGEKLteK 451
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15597620 4193 RIKQQLRADLPDYmvplHWL-----VLDRMPLNANGKL 4225
Cdd:cd05911  452 EVKDYVAKKVASY----KQLrggvvFVDEIPKSASGKI 485
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
23-553 1.57e-35

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 143.95  E-value: 1.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRflaedDGEGVvLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPPE 98
Cdd:cd12114    1 PDATAVI-----CGDGT-LTYGELAERARRVAGALKAAgVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPvdiDQPAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   99 sarrhhqeRLLSIIADAEPRLVLTTADLrepllqmnaqlsAANAPQLLCVDQLDPAVAEAWDEPQVR---PEHIAFLQYT 175
Cdd:cd12114   75 --------RREAILADAGARLVLTDGPD------------AQLDVAVFDVLILDLDALAAPAPPPPVdvaPDDLAYVIFT 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  176 SGSTALPKGVQVSHGNlVANEVL-IRRGFGIGADDVIVSWLPLYHDMGL--IGGLLQpifSGVPCVLmsPRYFLER-PVR 251
Cdd:cd12114  135 SGSTGTPKGVMISHRA-ALNTILdINRRFAVGPDDRVLALSSLSFDLSVydIFGALS---AGATLVL--PDEARRRdPAH 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  252 WLEAISQYGGTV-SGGPDFAYRLCSERVAESALqrldLSGWRVAFSGSEPIRQDSLERFAEKFAASRfdassFFACYGLA 330
Cdd:cd12114  209 WAELIERHGVTLwNSVPALLEMLLDVLEAAQAL----LPSLRLVLLSGDWIPLDLPARLRALAPDAR-----LISLGGAT 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  331 EATLFVTGGQRGQGIPALAV--DGEALARNRIAegegsvlmccgrsqpehavlIVDaASGEVLGDDNVGEIWAAGPSIAH 408
Cdd:cd12114  280 EASIWSIYHPIDEVPPDWRSipYGRPLANQRYR--------------------VLD-PRGRDCPDWVPGELWIGGRGVAL 338
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  409 GYWRNPEASAKAFVE-RDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsevpsaRKGRVAAFAV 486
Cdd:cd12114  339 GYLGDPELTAARFVThPDGERLYRTGDLGRYRpDGTLEFLGRRDGQVKVRGYRIELGEIEAALQ------AHPGVARAVV 412
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  487 TVDGEEgiGIAAEIGRGVQKSVPAQELIDSIRQAVAE---AYQEAPKVVALlnpGALPKTSSGKLQRSAC 553
Cdd:cd12114  413 VVLGDP--GGKRLAAFVVPDNDGTPIAPDALRAFLAQtlpAYMIPSRVIAL---EALPLTANGKVDRAAL 477
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
15-552 1.90e-35

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 144.02  E-value: 1.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   15 LRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:cd17651    1 FERQAARTPDAPALVA------EGRRLTYAELDRRANRLAHRLRARGVGPGDLVaLCARRSAELVVALLAILKAGAAYVP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 ---AYPPEsarrhhqeRLLSIIADAEPRLVLTTADLREpllqmnaQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIA 170
Cdd:cd17651   75 ldpAYPAE--------RLAFMLADAGPVLVLTHPALAG-------ELAVELVAVTLLDQPGAAAGADAEPDPALDADDLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  171 FLQYTSGSTALPKGVQVSHG---NLVANEvliRRGFGIGADDVIVSWLPLYHDMGligglLQPIFSGVPC---------- 237
Cdd:cd17651  140 YVIYTSGSTGRPKGVVMPHRslaNLVAWQ---ARASSLGPGARTLQFAGLGFDVS-----VQEIFSTLCAgatlvlppee 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  238 VLMSPRYFLerpvRWLEAisqYGGTVSGGPDFAYRLCSERVAESALQRLDLsgwRVAFSGSEPIRQDSLERfaEKFAASR 317
Cdd:cd17651  212 VRTDPPALA----AWLDE---QRISRVFLPTVALRALAEHGRPLGVRLAAL---RYLLTGGEQLVLTEDLR--EFCAGLP 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  318 FDAssFFACYGLAEATlFVTggqrgqgipALAVDGEALARNRIAEgegsvlmcCGRSQPEHAVLIVDAAsGEVLGDDNVG 397
Cdd:cd17651  280 GLR--LHNHYGPTETH-VVT---------ALSLPGDPAAWPAPPP--------IGRPIDNTRVYVLDAA-LRPVPPGVPG 338
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  398 EIWAAGPSIAHGYWRNPEASAKAFVE---RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVesev 473
Cdd:cd17651  339 ELYIGGAGLARGYLNRPELTAERFVPdpfVPGARMYRTGDLArWLPDGELEFLGRADDQVKIRGFRIELGEIEAAL---- 414
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  474 psARKGRVAAFAVTVDgEEGIG---IAAEIGRGVQKSVPAQELIDSIRQAVAEAYqeAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd17651  415 --ARHPGVREAVVLAR-EDRPGekrLVAYVVGDPEAPVDAAELRAALATHLPEYM--VPSAFVLLD--ALPLTPNGKLDR 487

                 ..
gi 15597620  551 SA 552
Cdd:cd17651  488 RA 489
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
34-550 1.97e-35

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 143.35  E-value: 1.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   34 DDGEGVVLSYRDLDLRARSIAA-ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesarRHHQERLLSII 112
Cdd:cd05914    1 LYYGGEPLTYKDLADNIAKFALlLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILA-----EFTADEVHHIL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  113 ADAEPRLVLTTadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEHIAFLQYTSGSTALPKGVQVSHGNL 192
Cdd:cd05914   76 NHSEAKAIFVS-----------------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNI 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  193 VANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSpryflERPVRWLEAISQYGGTVSGGPDFAYR 272
Cdd:cd05914  115 VSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLD-----KIPSAKIIALAFAQVTPTLGVPVPLV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  273 LcsERVAESALQ-RLDLSG--WRVAfsgsEPIRQDSLERFAEKFAASRFDASSFFACYGLAEATLFVTGGQRGQGIPALa 349
Cdd:cd05914  190 I--EKIFKMDIIpKLTLKKfkFKLA----KKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTIGFPYT- 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  350 vdgealarnrIAEG--EGSVLMCcgRSQPEHAVLivdAASGEVLGDDNV-----------GEIWAAGPSIAHGYWRNPEA 416
Cdd:cd05914  263 ----------IGYGmtETAPIIS--YSPPNRIRL---GSAGKVIDGVEVridspdpatgeGEIIVRGPNVMKGYYKNPEA 327
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  417 SAKAFVErDGrtWLRTGDLG-FLRDGELFVTGRLKDMLIV-RGHNLYPQDIERTV-------ESEVPSARKGRVAAFAVT 487
Cdd:cd05914  328 TAEAFDK-DG--WFHTGDLGkIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKInnmpfvlESLVVVQEKKLVALAYID 404
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  488 VDGEEgigiaaeigrgvQKSVPAQELIDSIRQAVAEAY-QEAP---KVVAL-LNPGALPKTSSGKLQR 550
Cdd:cd05914  405 PDFLD------------VKALKQRNIIDAIKWEVRDKVnQKVPnykKISKVkIVKEEFEKTPKGKIKR 460
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
3252-3678 2.11e-35

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 142.56  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3252 PLTPMQEGL-LLHTLlEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMlQVIHKPGRTRIEf 3330
Cdd:cd19540    3 PLSFAQQRLwFLNRL-DGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPY-QVVLPAAEARPD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3331 LDWSELPEDGHEERLQALhkreREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSA-LGE 3409
Cdd:cd19540   80 LTVVDVTEDELAARLAEA----ARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAArRAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 SRPANLPTPPRYRDYIAWlQR-----QDLEQSR-----RWWSESLRGF-ERPTLvPSDRPflR-EHAGESGGMIvgdrYT 3477
Cdd:cd19540  156 RAPDWAPLPVQYADYALW-QRellgdEDDPDSLaarqlAYWRETLAGLpEELEL-PTDRP--RpAVASYRGGTV----EF 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3478 RLDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRpvGMPEMQRTVGLFINSIPLRVQmpAAGQ 3557
Cdd:cd19540  228 TIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGR--GDEALDDLVGMFVNTLVLRTD--VSGD 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3558 RcTVREWLNRLFERNLELREHEHLP---LVAIQESSELPKGQPLFDSLFVFENAPVEVSVLDRaqsLNAS-SDSGRTHTN 3633
Cdd:cd19540  304 P-TFAELLARVRETDLAAFAHQDVPferLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPG---LTVEpVPVDTGVAK 379
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15597620 3634 FPLTVVCYP-----GDDLGLH--LSYDQRYFEAPTVERLLGEFKRLLLALAD 3678
Cdd:cd19540  380 FDLSFTLTErrdadGAPAGLTgeLEYATDLFDRSTAERLADRFVRVLEAVVA 431
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
2210-2664 2.64e-35

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 142.73  E-value: 2.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLs 2289
Cdd:cd05907    4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 haalfealgelpagvarwcleedgpaldAEDPAPLAALsgpqhqaylIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGM 2369
Cdd:cd05907   83 ----------------------------VEDPDDLATI---------IYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2370 RAEDCELHF--YSINFdaasER---LLAPLLCGARVVLRAQGQWGAEEICEL--------------IRAEGVSILGftPS 2430
Cdd:cd05907  126 TEGDRHLSFlpLAHVF----ERragLYVPLLAGARIYFASSAETLLDDLSEVrptvflavprvwekVYAAIKVKAV--PG 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2431 YGSQLAQWLeSQGRqlpVRMCITGGEALTGEHLQRIRQAFAPasFFNAYGPTET--VVmplACLAPERLEEGaaSVpiGS 2508
Cdd:cd05907  200 LKRKLFDLA-VGGR---LRFAASGGAPLPAELLHFFRALGIP--VYEGYGLTETsaVV---TLNPPGDNRIG--TV--GK 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2509 V---VGARVAyildadlalvpqgATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYV 2585
Cdd:cd05907  267 PlpgVEVRIA-------------DDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHIT 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2586 GRI-DHQVKIRGFRIELGEIEARLLEHPQVREALVL--------ALDSPSGKQLAGYVAS--------AVAEQDEDAQAA 2648
Cdd:cd05907  327 GRKkDLIITSGGKNISPEPIENALKASPLISQAVVIgdgrpflvALIVPDPEALEAWAEEhgiaytdvAELAANPAVRAE 406
                        490
                 ....*....|....*.
gi 15597620 2649 LREALKtHLKQQLPDY 2664
Cdd:cd05907  407 IEAAVE-AANARLSRY 421
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
40-550 2.73e-35

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 142.52  E-value: 2.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   40 VLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpeSARRHhqeRLLSIIADAEPR 118
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALgVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP--FFREH---ELAFILRRAKAK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  119 LVLTTADLRepllQMNaqlsaanapqllcvdqldpavaeawdePQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVL 198
Cdd:cd05903   76 VFVVPERFR----QFD---------------------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQ 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  199 IRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSpryfLERPVRWLEAISQYGGTVSGG-PDFAYRLCseR 277
Cdd:cd05903  125 YAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD----IWDPDKALALMREHGVTFMMGaTPFLTDLL--N 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  278 VAESALQRldLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVTGGQRGQGIPALAVDGEALAR 357
Cdd:cd05903  199 AVEEAGEP--LSRLRTFVCGGATVPRSLARRAAELLGAKVCSA------YGSTECPGAVTSITPAPEDRRLYTDGRPLPG 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  358 NRIAegegsvlmccgrsqpehavlIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVErdgrTWLRTGDLGF 437
Cdd:cd05903  271 VEIK--------------------VVDDT-GATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPE----GWFRTGDLAR 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  438 L-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGEEgIGIAAeigrgvq 505
Cdd:cd05903  326 LdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHpgvieaavvaLPDERLGeRACAVVVTKSGAL-LTFDE------- 397
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 15597620  506 ksvpAQELIDsiRQAVAEAYqeAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd05903  398 ----LVAYLD--RQGVAKQY--WPERLVHVD--DLPRTPSGKVQK 432
PRK09088 PRK09088
acyl-CoA synthetase; Validated
1156-1617 2.89e-35

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 143.41  E-value: 2.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHL 1235
Cdd:PRK09088   25 YAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1236 FERLPGAEGVTPIC--LDSLKLDNWPSQAPglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDV 1313
Cdd:PRK09088  105 AAGRTDVEDLAAFIasADALEPADTPSIPP------ERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSS 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1314 LMQKAPVSFDVSvwecfwpLVTGCRLVLAAPGEHR-----DPAR-LVELVRQ-FGVTTLHFVPPLLQLFIDEPGV--AAC 1384
Cdd:PRK09088  179 FLCDAPMFHIIG-------LITSVRPVLAVGGSILvsngfEPKRtLGRLGDPaLGITHYFCVPQMAQAFRAQPGFdaAAL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1385 GSLRRLFSGGEALPAE-LRNRVLQRLPAValhNRYGPTE--TAINVThWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLL 1461
Cdd:PRK09088  252 RHLTALFTGGAPHAAEdILGWLDDGIPMV---DGFGMSEagTVFGMS-VDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDC 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1462 PAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQ 1541
Cdd:PRK09088  328 PAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIE 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  1542 ARLLAQPGVAQAVVVireGVAGSQL--VGYYTgAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK09088  401 AVLADHPGIRECAVV---GMADAQWgeVGYLA-IVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL 474
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
38-554 3.52e-35

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 144.81  E-value: 3.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    38 GVVLSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYPPESARrhHQER----- 107
Cdd:PRK08974   46 GEVMTFRKLEERSRAFAAylQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPLYTPRELE--HQLNdsgak 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   108 ---LLSIIADAEPRLVLTTADLREPLLQMNAQLSAANA----------PQLLCVDQLDPAVA--EA--------WDEPQV 164
Cdd:PRK08974  124 aivIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAKGtlvnfvvkyiKRLVPKYHLPDAISfrSAlhkgrrmqYVKPEL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   165 RPEHIAFLQYTSGSTALPKGVQVSHGNLVAN--------EVLIRRGfgigaDDVIVSWLPLYHDMGLIGGLLQPIFSGVP 236
Cdd:PRK08974  204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqakaayGPLLHPG-----KELVVTALPLYHIFALTVNCLLFIELGGQ 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   237 CVLMS-PRYfLERPVRWLeaiSQYGGTVSGGPD--FAYRLCSERVAEsalqrLDLSGWRVAFSGSEPIRQDSLERFAEkf 313
Cdd:PRK08974  279 NLLITnPRD-IPGFVKEL---KKYPFTAITGVNtlFNALLNNEEFQE-----LDFSSLKLSVGGGMAVQQAVAERWVK-- 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   314 aasrFDASSFFACYGLAEATLFVTGgqrgqgipalavdgealARNRIAEGEGSVlmccGRSQPEHAVLIVDAAsGEVLGD 393
Cdd:PRK08974  348 ----LTGQYLLEGYGLTECSPLVSV-----------------NPYDLDYYSGSI----GLPVPSTEIKLVDDD-GNEVPP 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   394 DNVGEIWAAGPSIAHGYWRNPEASAKafVERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVese 472
Cdd:PRK08974  402 GEPGELWVKGPQVMLGYWQRPEATDE--VIKDG--WLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV--- 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   473 vpsARKGRVAAFAVtvdgeegIGIAAEI-GRGVQ-------KSVPAQELIDSIRQAVAeAYQeAPKVVALLNpgALPKTS 544
Cdd:PRK08974  475 ---MLHPKVLEVAA-------VGVPSEVsGEAVKifvvkkdPSLTEEELITHCRRHLT-GYK-VPKLVEFRD--ELPKSN 540
                         570
                  ....*....|
gi 15597620   545 SGKLQRSACR 554
Cdd:PRK08974  541 VGKILRRELR 550
PRK06188 PRK06188
acyl-CoA synthetase; Validated
2191-2692 3.74e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 143.97  E-value: 3.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2191 LFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVG-LALERSlEMVVGLLAILKAGGAYVPLDPE 2269
Cdd:PRK06188   17 LLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVAlLSLNRP-EVLMAIGAAQLAGLRRTALHPL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2270 YPLERLQYMIEDSGVRLLLSHAALF----EALGELPAGVARW---CLEEDGP----ALDAEDPAPLAALSGPQHQAYLIY 2338
Cdd:PRK06188   96 GSLDDHAYVLEDAGISTLIVDPAPFveraLALLARVPSLKHVltlGPVPDGVdllaAAAKFGPAPLVAAALPPDIAGLAY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2339 TSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASerLLAP-LLCGARVVLraQGQWGAEEICELI 2417
Cdd:PRK06188  176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIV--LAKFDPAEVLRAI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2418 RAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTEtVVMPLACLA--- 2493
Cdd:PRK06188  252 EEQRITATFLVPTMIYALLDHPDLRTRDLSsLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTE-APMVITYLRkrd 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2494 -----PERLeeGAASVPIgsvVGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfaaEGGRLy 2568
Cdd:PRK06188  330 hdpddPKRL--TSCGRPT---PGLRVA-LLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGWL- 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2569 RTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaVAEQDEDAQA 2647
Cdd:PRK06188  396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpDEKWGEAVTAVV---VLRPGAAVDA 472
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  2648 A-LREALKTHL------KQ-----QLPdymvpahllllaslpLTANGKLDRRALPAP 2692
Cdd:PRK06188  473 AeLQAHVKERKgsvhapKQvdfvdSLP---------------LTALGKPDKKALRAR 514
PRK06178 PRK06178
acyl-CoA synthetase; Validated
10-466 3.82e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 144.80  E-value: 3.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFLaeddgeGVVLSYRDLD-LRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAG 88
Cdd:PRK06178   34 PLTEYLRAWARERPQRPAIIFY------GHVITYAELDeLSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    89 VIAVPAYPpeSARRHHqerLLSIIADAEPRLVLTTADLREPLLQMNAQLSAAN-----------------------APQL 145
Cdd:PRK06178  108 AVHVPVSP--LFREHE---LSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHvivtsladvlpaeptlplpdslrAPRL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   146 LCVDQLD-----PAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLV---ANEVLIrrGFGIGADDVIVSWLPL 217
Cdd:PRK06178  183 AAAGAIDllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAV--AVVGGEDSVFLSFLPE 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   218 YHDMGLIGGLLQPIFSGVPCVLMSpryflerpvRW-----LEAISQYGGTVSGGP-DFAyrlcSERVAESALQRLDLSGW 291
Cdd:PRK06178  261 FWIAGENFGLLFPLFSGATLVLLA---------RWdavafMAAVERYRVTRTVMLvDNA----VELMDHPRFAEYDLSSL 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   292 RVAFSGS--EPIRQDSLERFAEKFAASRFDASsffacYGLAE---ATLFVTGGQRGqgipalavDGEALARNriaegegs 366
Cdd:PRK06178  328 RQVRVVSfvKKLNPDYRQRWRALTGSVLAEAA-----WGMTEthtCDTFTAGFQDD--------DFDLLSQP-------- 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   367 vlMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLG-FLRDGELFV 445
Cdd:PRK06178  387 --VFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL--RDG--WLHTGDIGkIDEQGFLHY 460
                         490       500
                  ....*....|....*....|.
gi 15597620   446 TGRLKDMLIVRGHNLYPQDIE 466
Cdd:PRK06178  461 LGRRKEMLKVNGMSVFPSEVE 481
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1128-1617 4.82e-35

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 143.96  E-value: 4.82e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1128 AWLPELLERQLAQSAER--VALEWDGGS--LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGG 1203
Cdd:cd05906   10 RTLLELLLRAAERGPTKgiTYIDADGSEefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1204 AYVPLDP----DYPSERLAYM-----LADSGVelLLTQAHLFERLPGAEGVTPICLDSL----KLDNWPSQAPGLHLHGD 1270
Cdd:cd05906   90 VPAPLTVpptyDEPNARLRKLrhiwqLLGSPV--VLTDAELVAEFAGLETLSGLPGIRVlsieELLDTAADHDLPQSRPD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1271 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWEC-FWPLVTGCRLVLAAPGEH-R 1348
Cdd:cd05906  168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEEIlA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1349 DPARLVELVRQFGVTtLHFVPPLL------QLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRL-----PAVALHNR 1417
Cdd:cd05906  248 DPLRWLDLIDRYRVT-ITWAPNFAfallndLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPA 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1418 YGPTETAINVThW--QCRAEDGERSP----IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERF 1491
Cdd:cd05906  327 FGMTETCSGVI-YsrSFPTYDHSQALefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1492 VADPFsaagerlYRTGDRArWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ---AVVVIREGVAGSQL-- 1566
Cdd:cd05906  406 TEDGW-------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAETEEla 477
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597620 1567 VGYYTGAVGAEAEAEQNQRLRAALQAEL---PEYMVPTQlmrLAQMPLGPSGKL 1617
Cdd:cd05906  478 IFFVPEYDLQDALSETLRAIRSVVSREVgvsPAYLIPLP---KEEIPKTSLGKI 528
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
13-552 4.88e-35

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 142.73  E-value: 4.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   13 QALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
Cdd:cd12117    1 ELFEEQAARTPDAVAVVY------GDRSLTYAELNERANRLARRLRAAgVGPGDVVGVLAERSPELVVALLAVLKAGAAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   92 VPAYPpesarRHHQERLLSIIADAEPRLVLTTADLrepllqmnAQLSAANAPQLLCVDQLDPAVAEAWdEPQVRPEHIAF 171
Cdd:cd12117   75 VPLDP-----ELPAERLAFMLADAGAKVLLTDRSL--------AGRAGGLEVAVVIDEALDAGPAGNP-AVPVSPDDLAY 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  172 LQYTSGSTALPKGVQVSHGNlVANEVLIRRGFGIGADDVIVSWLPLYHDMGLI---GGLLqpifSGVPCVLMsPRYFLER 248
Cdd:cd12117  141 VMYTSGSTGRPKGVAVTHRG-VVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFeiwGALL----NGARLVLA-PKGTLLD 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  249 PVRWLEAISQYGGTV----SGgpdfAYRLCSERVAESalqrldLSGWRVAFSGSEPIRQDSLERFAEKFAASRfdassFF 324
Cdd:cd12117  215 PDALGALIAEEGVTVlwltAA----LFNQLADEDPEC------FAGLRELLTGGEVVSPPHVRRVLAACPGLR-----LV 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  325 ACYGLAEATLFVTggqrgqgipALAVDgealarnRIAEGEGSVLMccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGP 404
Cdd:cd12117  280 NGYGPTENTTFTT---------SHVVT-------ELDEVAGSIPI--GRPIANTRVYVLDED-GRPVPPGVPGELYVGGD 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  405 SIAHGYWRNPEASAKAFVE---RDGRTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSarkgr 480
Cdd:cd12117  341 GLALGYLNRPALTAERFVAdpfGPGERLYRTGDLaRWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALR-AHPG----- 414
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  481 VAAFAVTVDGEEGIG--IAAEIgrgvqksVPAQEL-IDSIRQAVAE---AYQeAPKVVALLnpGALPKTSSGKLQRSA 552
Cdd:cd12117  415 VREAVVVVREDAGGDkrLVAYV-------VAEGALdAAELRAFLRErlpAYM-VPAAFVVL--DELPLTANGKVDRRA 482
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1130-1617 4.94e-35

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 144.15  E-value: 4.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEW--DGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVP 1207
Cdd:PRK12583   20 IGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1208 LDPDYPSERLAYMLADSGVELLLT---------QAHLFERLPGAEGVTPICLDSLKLDNW-------PSQAPGL------ 1265
Cdd:PRK12583  100 INPAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGQPGALACERLPELrgvvslaPAPPPGFlawhel 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1266 -----------------HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERlQWMQA-TYTLDGDDVLMqkAPVSFdvsvW 1327
Cdd:PRK12583  180 qargetvsrealaerqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVAeSLGLTEHDRLC--VPVPL----Y 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1328 ECFWPLVT--GCRLVLAA---PGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAE 1400
Cdd:PRK12583  253 HCFGMVLAnlGCMTVGAClvyPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIE 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1401 LRNRVLQRLPAVALHNRYGPTETAiNVTHWQCRAEDGER--SPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLAR 1478
Cdd:PRK12583  333 VMRRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMK 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1479 GYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVir 1558
Cdd:PRK12583  412 GYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF-- 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  1559 eGVA----GSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK12583  483 -GVPdekyGEEIVAWVRLHPGHAASEEE---LREFCKARIAHFKVPRYFRFVDEFPMTVTGKV 541
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
675-1097 5.48e-35

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 141.05  E-value: 5.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  675 LPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERD-GAALQRIDERGEFAWQF 753
Cdd:cd19536    2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  754 VDLAALAEHERAAAAAQRREAEAqqPFDLEKGPLLRVSLVRLDEQEHQLWV-TLHHIVADGWSLNLLLDEFSRLYAEACG 832
Cdd:cd19536   82 LDLTPLEEQLDPLRAYKEETKIR--RFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEILAVYNQLLE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  833 GQPADLAPlELHYAEFAAWQRQWLDAGEGARqlaYWRERLGDtapvLELATDHP-RTARQASPAARYSLRVDEALARAIR 911
Cdd:cd19536  160 YKPLSLPP-AQPYRDFVAHERASIQQAASER---YWREYLAG----ATLATLPAlSEAVGGGPEQDSELLVSVPLPVRSR 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  912 EAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQrLETQG---LVGFFINTLVLRGTpRARQPFAALLGEARE 988
Cdd:cd19536  232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRS-EETTGaerLLGLFLNTLPLRVT-LSEETVEDLLKRAQE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  989 ATLGAQANQDLPfdqvLAA---CGQGGQLFQVLFNHQQRDLSALRRLPGLLADELPW--HSREAKFDLQLQSEEDARGRL 1063
Cdd:cd19536  310 QELESLSHEQVP----LADiqrCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGllFSEFKSNYDVNLSVLPKQDRL 385
                        410       420       430
                 ....*....|....*....|....*....|....
gi 15597620 1064 TLNFDYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19536  386 ELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
3279-3678 7.90e-35

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 140.86  E-value: 7.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3279 YRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETmLQVIHKPGRTRIEFLDWselpeDGHEERLQALHKREREAGFD 3358
Cdd:cd19538   30 IKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVP-YQLILEEDEATPKLEIK-----EVDEEELESEINEAVRYPFD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3359 LLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSA-LGESRPANLPTPPRYRDYIAWlQRQDLEQSR 3437
Cdd:cd19538  104 LSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRArCKGEAPELAPLPVQYADYALW-QQELLGDES 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3438 R----------WWSESLRGFERPTLVPSDRPFLREHAGEsggmivGDRYT-RLDAADGARLRELAQRYQLTVNTFAQAAW 3506
Cdd:cd19538  183 DpdsliarqlaYWKKQLAGLPDEIELPTDYPRPAESSYE------GGTLTfEIDSELHQQLLQLAKDNNVTLFMVLQAGF 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3507 ALTLRRFSGERDVLFGVTVAGRpvGMPEMQRTVGLFINSIPLRVQmpAAGQRcTVREWLNRLFERNLELREHEHLP---L 3583
Cdd:cd19538  257 AALLTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLVLRTD--TSGNP-SFRELLERVKETNLEAYEHQDIPferL 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3584 VAIQESSELPKGQPLFDSLFVFENAPVEVSVLDRAQS--LNASSDSGRTHTNFPLTVVCYPGDDLGLH--LSYDQRYFEA 3659
Cdd:cd19538  332 VEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAklELRTVGSAKFDLTFELREQYNDGTPNGIEgfIEYRTDLFDH 411
                        410
                 ....*....|....*....
gi 15597620 3660 PTVERLLGEFKRLLLALAD 3678
Cdd:cd19538  412 ETIEALAQRYLLLLESAVE 430
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
2198-2664 1.34e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 142.61  E-value: 1.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2198 ASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQY 2277
Cdd:PRK07786   29 MQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2278 MIEDSGVRLLLSHAALfealgelpAGVARwCLEEDGPALD--------------------AEDPAPLAALSGPQHQAYLI 2337
Cdd:PRK07786  109 LVSDCGAHVVVTEAAL--------APVAT-AVRDIVPLLStvvvaggssddsvlgyedllAEAGPAHAPVDIPNDSPALI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2338 -YTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED----CELHFYSInfdAASERLLAPLLCGARVVLRAQGQWGAEE 2412
Cdd:PRK07786  180 mYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSdvgfVGVPLFHI---AGIGSMLPGLLLGAPTVIYPLGAFDPGQ 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2413 ICELIRAEGVSILGFTPsygsqlAQWL------ESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTEtvV 2486
Cdd:PRK07786  257 LLDVLEAEKVTGIFLVP------AQWQavcaeqQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTE--M 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2487 MPLACLaperLEEGAASVPIGSV------VGARVayiLDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpf 2560
Cdd:PRK07786  329 SPVTCM----LLGEDAIRKLGSVgkviptVAARV---VDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF----- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2561 aaEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGkqlaGYVASAVAE 2640
Cdd:PRK07786  397 --AGG-WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW----GEVPVAVAA 469
                         490       500
                  ....*....|....*....|....
gi 15597620  2641 QDEDAQAALREALKTHLKQQLPDY 2664
Cdd:PRK07786  470 VRNDDAALTLEDLAEFLTDRLARY 493
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
1156-1622 1.35e-34

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 142.00  E-value: 1.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHL 1235
Cdd:cd12119   28 YAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDF 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 F-------ERLPGAEGVtpICLDSlKLDNWPSQAPGLH-----LHG-----------DNLAYVI-YTSGSTGQPKGVGNT 1291
Cdd:cd12119  108 LplleaiaPRLPTVEHV--VVMTD-DAAMPEPAGVGVLayeelLAAespeydwpdfdENTAAAIcYTSGTTGNPKGVVYS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1292 HAALAerLQWMQATYT----LDGDDVLMQKAPVsFDVSVWEC-FWPLVTGCRLVLaaPGEHRDPARLVELVRQFGVTTLH 1366
Cdd:cd12119  185 HRSLV--LHAMAALLTdglgLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGVTFAA 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1367 FVPPLLQLFIDEPgvAACG----SLRRLFSGGEALPAELRNRVLQRLpaVALHNRYGPTET----AINVTHWQCRAEDGE 1438
Cdd:cd12119  260 GVPTVWQGLLDHL--EANGrdlsSLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETsplgTVARPPSEHSNLSED 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1439 -----RSPIGRPLGNVVCRVLDAEFNLLPA-GVA-GELCIGGLGLARGYLGRPAlSAERFVADPFsaagerlYRTGDRAR 1511
Cdd:cd12119  336 eqlalRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW-------LRTGDVAT 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1512 WNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEqnqRLR 1587
Cdd:cd12119  408 IDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVI---GVPhpkwGERPLAVVVLKEGATVTAE---ELL 481
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620 1588 AALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd12119  482 EFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1129-1622 2.35e-34

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 140.54  E-value: 2.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1129 WLPELLERQLAQSA----ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGA 1204
Cdd:cd05920   12 WQDEPLGDLLARSAarhpDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1205 YVPLDPDYPSERLAYMLADSGVELLltqahlferlpgaegvtpICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQ 1284
Cdd:cd05920   92 PVLALPSHRRSELSAFCAHAEAVAY------------------IVPDRHAGFDHRALARELAESIPEVALFLLSGGTTGT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1285 PKGVGNTHAALAERL----QWMQatytLDGDDVLMQKAPVS--FDVSVWECFWPLVTGCRLVLAAPGehrDPARLVELVR 1358
Cdd:cd05920  154 PKLIPRTHNDYAYNVrasaEVCG----LDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1359 QFGVTTLHFVPPLLQLFIDEPGV--AACGSLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTETAINVThwqcRAED 1436
Cdd:cd05920  227 REGVTVTALVPALVSLWLDAAASrrADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNYT----RLDD 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1437 GERSPI---GRPL--GNVVcRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRAR 1511
Cdd:cd05920  302 PDEVIIhtqGRPMspDDEI-RVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVR 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1512 WNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREgvagSQLVGYYTGAV----GAEAEAEQnqrLR 1587
Cdd:cd05920  374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMP----DELLGERSCAFvvlrDPPPSAAQ---LR 446
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 15597620 1588 AAL-QAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05920  447 RFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1145-1631 2.52e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 140.81  E-value: 2.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1145 VALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADS 1224
Cdd:PRK08276    3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1225 GVELLLTQAHLFERLPGAEGVTPICLDSLKL-----------DNW---------PSQAPGLHLHgdnlayviYTSGSTGQ 1284
Cdd:PRK08276   83 GAKVLIVSAALADTAAELAAELPAGVPLLLVvagpvpgfrsyEEAlaaqpdtpiADETAGADML--------YSSGTTGR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1285 PKGV------GNTHAALAERLQWMQATYTLDGDDV------LMQKAPVSFDVSVwecfwpLVTGCRLVLAapgEHRDPAR 1352
Cdd:PRK08276  155 PKGIkrplpgLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTAPLRFGMSA------LALGGTVVVM---EKFDAEE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1353 LVELVRQFGVTTLHFVPP----LLQLfidEPGVAA---CGSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTE--- 1422
Cdd:PRK08276  226 ALALIERYRVTHSQLVPTmfvrMLKL---PEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEggg 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1423 -TAINVTHWQCRaedgeRSPIGRPLGNVVcRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAage 1501
Cdd:PRK08276  302 vTVITSEDWLAH-----PGSVGKAVLGEV-RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT--- 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1502 rlyrTGDRARWNADGVLeYL-GRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGA 1576
Cdd:PRK08276  373 ----VGDVGYLDEDGYL-YLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVF---GVPdeemGERVKAVVQPADGA 444
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  1577 EAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQRE 1631
Cdd:PRK08276  445 DAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQ 499
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3706-4230 2.59e-34

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 141.44  E-value: 2.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3706 ARDYpLEQGYVR------LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGM 3779
Cdd:COG1021   13 AARY-REAGYWRgetlgdLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3780 IVGSFKAGAgyLPLD--PGHPTQRLTRIVELSRTLVLVCTQACReqalaLFDELGCVDR-----PRL---LVWDEIQQG- 3848
Cdd:COG1021   92 FFALFRAGA--IPVFalPAHRRAEISHFAEQSEAVAYIIPDRHR-----GFDYRALARElqaevPSLrhvLVVGDAGEFt 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3849 ------EGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDV--IAQTASQSFDISVWQ 3920
Cdd:COG1021  165 sldallAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVylAALPAAHNFPLSSPG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3921 FLAAPLFGARVAIVPNAvahDPQGLLAHVGEQGITVLESVPSLIQGML---AEERQALDGLRWMLPTGEAMPPELARQwl 3997
Cdd:COG1021  245 VLGVLYAGGTVVLAPDP---SPDTAFPLIERERVTVTALVPPLALLWLdaaERSRYDLSSLRVLQVGGAKLSPELARR-- 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3998 kRYPRIG--LVNAYGPAECSddVAFFRVD-----LASTESTylPIgSPTDNNRLyllgagADDAFELVPLGAVGELCVAG 4070
Cdd:COG1021  320 -VRPALGctLQQVFGMAEGL--VNYTRLDdpeevILTTQGR--PI-SPDDEVRI------VDEDGNPVPPGEVGELLTRG 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4071 TGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVkIR-GFRIELGEIEARLHERADVRE 4149
Cdd:COG1021  388 PYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHD 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4150 AA-VAVQEGANGKYLVGYLVP-GETPRSSAdspaglmveqgawferIKQQLRA-DLPDYMVPLHWLVLDRMPLNANGKLD 4226
Cdd:COG1021  460 AAvVAMPDEYLGERSCAFVVPrGEPLTLAE----------------LRRFLRErGLAAFKLPDRLEFVDALPLTAVGKID 523

                 ....
gi 15597620 4227 RKAL 4230
Cdd:COG1021  524 KKAL 527
PLN02246 PLN02246
4-coumarate--CoA ligase
35-560 2.74e-34

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 141.66  E-value: 2.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    35 DGE-GVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVI---AVPAY-PPESARRhhqerl 108
Cdd:PLN02246   44 DGAtGRVYTYADVELLSRRVAAGLHKLgIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttANPFYtPAEIAKQ------ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   109 lsiIADAEPRLVLTTADLREPLlqmnAQLSAANAPQLLCVDQ----------LDPAVAEAWDEPQVRPEHIAFLQYTSGS 178
Cdd:PLN02246  118 ---AKASGAKLIITQSCYVDKL----KGLAEDDGVTVVTIDDppegclhfseLTQADENELPEVEISPDDVVALPYSSGT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   179 TALPKGVQVSHGNL---VANEVlirRG----FGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPRYFLerpVR 251
Cdd:PLN02246  191 TGLPKGVMLTHKGLvtsVAQQV---DGenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIM-PKFEI---GA 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   252 WLEAISQYGGTVsgGPdFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASsffacYGLAE 331
Cdd:PLN02246  264 LLELIQRHKVTI--AP-FVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQG-----YGMTE 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   332 ATlfvtggqrgqgiPALAVdGEALARNRIAEGEGSvlmcCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYW 411
Cdd:PLN02246  336 AG------------PVLAM-CLAFAKEPFPVKSGS----CGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   412 RNPEASAKAfVERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEvPS-------ARKGRVA- 482
Cdd:PLN02246  399 NDPEATANT-IDKDG--WLHTGDIGYIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISH-PSiadaavvPMKDEVAg 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   483 ----AFAVTVDGEEgigiAAEigrgvqksvpaqeliDSIRQAVAEA---YQEAPKVVALlnpGALPKTSSGKLQRSACRL 555
Cdd:PLN02246  475 evpvAFVVRSNGSE----ITE---------------DEIKQFVAKQvvfYKRIHKVFFV---DSIPKAPSGKILRKDLRA 532

                  ....*
gi 15597620   556 RLEDG 560
Cdd:PLN02246  533 KLAAG 537
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
3713-4230 3.01e-34

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 140.77  E-value: 3.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3713 QGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALR-AAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYL 3791
Cdd:PRK06839    2 QGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3792 PLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPqnlaYVI-YT 3870
Cdd:PRK06839   82 PLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESAS----FIIcYT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3871 SGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDViAQTASQSFDISVWQFLAAP-LFGARVAIVPNAVahDPQGLLAHV 3949
Cdd:PRK06839  158 SGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDR-SIVLLPLFHIGGIGLFAFPtLFAGGVIIVPRKF--EPTKALSMI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3950 GEQGITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGlvNAYGPAECSDDVAFFRVDLA 4026
Cdd:PRK06839  235 EKHKVTVVMGVPTIHQALINCskfETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEEDA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4027 STESTylPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgapGERLYRTGDL 4106
Cdd:PRK06839  313 RRKVG--SIGKPVLFCDYELI----DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--------QDGWLCTGDL 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4107 ARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPgetprssadSPAGLMV 4185
Cdd:PRK06839  379 ARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVvGRQHVKWGEIPIAFIVK---------KSSSVLI 449
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 15597620  4186 EqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK06839  450 E-----KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
23-552 4.42e-34

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 138.98  E-value: 4.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRFlaeddgEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPPE 98
Cdd:cd17643    1 PEAVAVVD------EDRRLTYGELDARAnRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPidpAYPVE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   99 sarrhhqeRLLSIIADAEPRLVLTtadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEHIAFLQYTSGS 178
Cdd:cd17643   75 --------RIAFILADSGPSLLLT------------------------------------------DPDDLAYVIYTSGS 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  179 TALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVS-------------WLPLYHdmgliGGLLqpifsgvpcvLMSPRYF 245
Cdd:cd17643  105 TGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLfhsyafdfsvweiWGALLH-----GGRL----------VVVPYEV 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  246 LERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLsgwRVAFSGSEPIRQDSLERFAEKFAASRFDASSFfa 325
Cdd:cd17643  170 ARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLAL---RYVIFGGEALEAAMLRPWAGRFGLDRPQLVNM-- 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  326 cYGLAEATLFVTggqrgqgipalavdGEALARNRIAEGEGSVLmccGRSQPEHAVLIVDaASGEVLGDDNVGEIWAAGPS 405
Cdd:cd17643  245 -YGITETTVHVT--------------FRPLDAADLPAAAASPI---GRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAG 305
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  406 IAHGYWRNPEASAKAFVE----RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVesevpsARKGR 480
Cdd:cd17643  306 VARGYLGRPELTAERFVAnpfgGPGSRMYRTGDLArRLPDGELEYLGRADEQVKIRGFRIELGEIEAAL------ATHPS 379
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  481 VAAFAVTV-DGEEGIG--IAAEIGRGVQKSVPAQelidsIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSA 552
Cdd:cd17643  380 VRDAAVIVrEDEPGDTrlVAYVVADDGAAADIAE-----LRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAA 449
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2210-2656 5.56e-34

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 139.13  E-value: 5.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPeyplerlqymiedsgvrllls 2289
Cdd:cd05910    1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP--------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 haalfealGELPAGVARwCLEEDGPalDAEDPAPLAalsgpQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGM 2369
Cdd:cd05910   60 --------GMGRKNLKQ-CLQEAEP--DAFIGIPKA-----DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2370 RAEDCELHFYSInFDaaserLLAPLLCGARVV----LRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQ 2445
Cdd:cd05910  124 RPGEVDLATFPL-FA-----LFGPALGLTSVIpdmdPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2446 LP-VRMCITGGEALTGEHLQRIRQAFAP-ASFFNAYGPTETvvMPLACLAPERLE-------EGAASVPIGSVVG---AR 2513
Cdd:cd05910  198 LPsLRRVLSAGAPVPIALAARLRKMLSDeAEILTPYGATEA--LPVSSIGSRELLatttaatSGGAGTCVGRPIPgvrVR 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2514 VAYILDADLA------LVPQGATGELYVGGAGLARGYHERPALSAERFVPDPfaaEGGRLYRTGDLVRLCDNGQVEYVGR 2587
Cdd:cd05910  276 IIEIDDEPIAewddtlELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGR 352
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 2588 IDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVAS--AVAEQDEDAQAALREALKTH 2656
Cdd:cd05910  353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVEPlpGTITPRARLEQELRALAKDY 423
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1134-1624 6.90e-34

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 139.61  E-value: 6.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1134 LERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:PRK06839    8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1213 PSERLAYMLADSGVELLLTQ---AHLFERLPGAEGVTP-ICLDSLK--LDNWPSqapGLHLHGDNLAYVI-YTSGSTGQP 1285
Cdd:PRK06839   88 TENELIFQLKDSGTTVLFVEktfQNMALSMQKVSYVQRvISITSLKeiEDRKID---NFVEKNESASFIIcYTSGTTGKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1286 KGvgnthAAL-AERLQW--MQATYTLD--GDDVLMQKAPVsFDVSVWECF-WP-LVTGCRLVLAapgEHRDPARLVELVR 1358
Cdd:PRK06839  165 KG-----AVLtQENMFWnaLNNTFAIDltMHDRSIVLLPL-FHIGGIGLFaFPtLFAGGVIIVP---RKFEPTKALSMIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1359 QFGVTTLHFVPPLLQLFIDEPGVAACG--SLRRLFSGGEALPAELRNRVLQRlpAVALHNRYGPTETAINVthWQCRAED 1436
Cdd:PRK06839  236 KHKVTVVMGVPTIHQALINCSKFETTNlqSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETSPTV--FMLSEED 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1437 GERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAErfvadpfsAAGERLYRTGDRARWNA 1514
Cdd:PRK06839  312 ARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWLCTGDLARVDE 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1515 DGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIRE----GVAGSQLVGYYTGAVGAEAEaeqnqrLRAAL 1590
Cdd:PRK06839  384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKD------VIEHC 457
                         490       500       510
                  ....*....|....*....|....*....|....
gi 15597620  1591 QAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK06839  458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4-660 1.90e-33

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 143.26  E-value: 1.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     4 AFELP-TTLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAF 81
Cdd:PRK10252  452 AVEIPeTTLSALVAQQAAKTPDAPALAD------ARYQFSYREMREQVVALANLLRERgVKPGDSVAVALPRSVFLTLAL 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    82 FGCLYAGVIAVP---AYPPEsarrhhqeRLLSIIADAEPRLVLTTADLRepllqmnAQLSAANAPQLLCVDQLDPAvAEA 158
Cdd:PRK10252  526 HAIVEAGAAWLPldtGYPDD--------RLKMMLEDARPSLLITTADQL-------PRFADVPDLTSLCYNAPLAP-QGA 589
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   159 WDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVpCV 238
Cdd:PRK10252  590 APLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVS-VWEFFWPFIAGA-KL 667
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   239 LMSPRYFLERPVRWLEAISQYGGTVSggpDFAYRLCSERVAESALQRLD--LSGWRVAFSGSEPIRQDSLERFAEKFAAS 316
Cdd:PRK10252  668 VMAEPEAHRDPLAMQQFFAEYGVTTT---HFVPSMLAAFVASLTPEGARqsCASLRQVFCSGEALPADLCREWQQLTGAP 744
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   317 RFDassffaCYGLAEATLFVTggqrgqGIPAlavDGEALARNRiaegegsvlmccGRSQP------EHAVLIVDAASGEV 390
Cdd:PRK10252  745 LHN------LYGPTEAAVDVS------WYPA---FGEELAAVR------------GSSVPigypvwNTGLRILDARMRPV 797
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   391 lGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVE---RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 466
Cdd:PRK10252  798 -PPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDVArWLDDGAVEYLGRSDDQLKIRGQRIELGEID 876
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   467 RTVESeVPSARKGRVAAFAVTVDGEEGiGIAAEIgrgVQKSVPAQEL---IDSIRQAVAEAYQEAPKVVALLNPGALPKT 543
Cdd:PRK10252  877 RAMQA-LPDVEQAVTHACVINQAAATG-GDARQL---VGYLVSQSGLpldTSALQAQLRERLPPHMVPVVLLQLDQLPLS 951
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   544 SSGKLQRSACRLrledgsldsyalfPGLQAVQEAQPPAGDDEllARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVV 623
Cdd:PRK10252  952 ANGKLDRKALPL-------------PELKAQVPGRAPKTGTE--TIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLA 1016
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 15597620   624 AQVRDSLGVALDLRQLFEAPTLQAFSATVA----RQLAAGL 660
Cdd:PRK10252 1017 AQLSRQFARQVTPGQVMVASTVAKLATLLDaeedESRRLGF 1057
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
2192-2621 2.29e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 138.94  E-value: 2.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2192 FAARVAAS--PQAPALTFAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2268
Cdd:PRK08314   14 HNLEVSARryPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2269 EYPLERLQYMIEDSGVRLLLSHAALFE----ALGELPAG---VAR---------------WCLEEdgPALDAEDP----- 2321
Cdd:PRK08314   94 MNREEELAHYVTDSGARVAIVGSELAPkvapAVGNLRLRhviVAQysdylpaepeiavpaWLRAE--PPLQALAPggvva 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2322 ---------APLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHF----------YSIN 2382
Cdd:PRK08314  172 wkealaaglAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVlplfhvtgmvHSMN 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2383 fdaaserllAPLLCGARVVLRAqgQWGAEEICELIRAEGVSILGFTPsygSQLAQWLES---QGRQLPVRMCITGGEALT 2459
Cdd:PRK08314  252 ---------APIYAGATVVLMP--RWDREAAARLIERYRVTHWTNIP---TMVVDFLASpglAERDLSSLRYIGGGGAAM 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2460 GEHL-QRIRQAFApASFFNAYGPTETVVmPLACLAPERLEEGAASVPIGSvVGARVayiLDAD-LALVPQGATGELYVGG 2537
Cdd:PRK08314  318 PEAVaERLKELTG-LDYVEGYGLTETMA-QTHSNPPDRPKLQCLGIPTFG-VDARV---IDPEtLEELPPGEVGEIVVHG 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2538 AGLARGYHERPALSAERFVpdpfAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREA 2617
Cdd:PRK08314  392 PQVFKGYWNRPEATAEAFI----EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467

                  ....
gi 15597620  2618 LVLA 2621
Cdd:PRK08314  468 CVIA 471
PRK07514 PRK07514
malonyl-CoA synthase; Validated
17-554 5.31e-33

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 136.93  E-value: 5.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    17 RRAVQEPERLALRflaedDGEGVVLSYRDLD-LRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP-- 93
Cdd:PRK07514   10 RAAFADRDAPFIE-----TPDGLRYTYGDLDaASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPln 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    94 -AY-PPEsarrhhqerLLSIIADAEPRLVLTTADLREPLLQMNAqlsAANAPQLLCVDQ------LDPAVAEAWDEPQVR 165
Cdd:PRK07514   85 tAYtLAE---------LDYFIGDAEPALVVCDPANFAWLSKIAA---AAGAPHVETLDAdgtgslLEAAAAAPDDFETVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 --PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLiggllqpiFSGVPCVLMS-- 241
Cdd:PRK07514  153 rgADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGL--------FVATNVALLAga 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   242 -----PRYFLERPVRWLEAisqygGTV-SGGPDFAYRLcserVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAA 315
Cdd:PRK07514  225 smiflPKFDPDAVLALMPR-----ATVmMGVPTFYTRL----LQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGH 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   316 S---RfdassffacYGLAEATLFVTGgqrgqgiPalaVDGEalarnRIAegeGSVlmccGRSQPEHAVLIVDAASGEVLG 392
Cdd:PRK07514  296 AileR---------YGMTETNMNTSN-------P---YDGE-----RRA---GTV----GFPLPGVSLRVTDPETGAELP 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   393 DDNVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIErTVES 471
Cdd:PRK07514  345 PGEIGMIEVKGPNVFKGYWRMPEKTAEEFRA-DG--FFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVE-GEID 420
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   472 EVPSarkgrVAAFAVT----VD-GEegiGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQeaPKVVALLNpgALPKTSSG 546
Cdd:PRK07514  421 ELPG-----VVESAVIgvphPDfGE---GVTAVVVPKPGAALDEAAILAALKGRLARFKQ--PKRVFFVD--ELPRNTMG 488

                  ....*...
gi 15597620   547 KLQRSACR 554
Cdd:PRK07514  489 KVQKNLLR 496
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
1113-1632 7.40e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 137.82  E-value: 7.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1113 AHLAEWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLL 1192
Cdd:PRK05605   17 QSYAPWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1193 VGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLL---TQAHLFERLPGAEGV-TPICLD-----------SLKL-- 1255
Cdd:PRK05605   97 VAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRRTTPLeTIVSVNmiaampllqrlALRLpi 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1256 -------DNWPSQAPGL----HLHG-----------------DNLAYVIYTSGSTGQPKGV----GNTHAALAERLQWMQ 1303
Cdd:PRK05605  177 palrkarAALTGPAPGTvpweTLVDaaiggdgsdvshprptpDDVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1304 ATYtlDGDDVLMQKAPV--SFDVSVWECFWPLVtGCRLVL-AAPgehrDPARLVELVRQFGVTTLHFVPPLLQLFID--- 1377
Cdd:PRK05605  257 GLG--DGPERVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaae 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1378 EPGVAACGsLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTETAINVThwqCRAEDGERSP--IGRPLGNVVCRVLD 1455
Cdd:PRK05605  330 ERGVDLSG-VRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVD 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1456 AEfNL---LPAGVAGELCIGGLGLARGYLGRPALSAERFVADpfsaagerLYRTGDRARWNADGVLEYLGRLDQQVKLRG 1532
Cdd:PRK05605  405 PE-DPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1533 FRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVgyyTGAVG-AEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPL 1611
Cdd:PRK05605  476 FNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV---VAAVVlEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPR 552
                         570       580
                  ....*....|....*....|.
gi 15597620  1612 GPSGKLDTRALPEPVWQQREH 1632
Cdd:PRK05605  553 DQLGKVRRREVREELLEKLGA 573
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1120-1615 7.84e-33

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 137.18  E-value: 7.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1120 SAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIV 1199
Cdd:PRK06164    2 PHDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1200 KAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH-----LFERL--------PGAEGVTPICLDSLKL-DNWP---SQA 1262
Cdd:PRK06164   82 RLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILaavppdalPPLRAIAVVDDAADATpAPAPgarVQL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1263 PGLHLHG------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECF 1330
Cdd:PRK06164  162 FALPDPAppaaageraadpDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1331 WPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPA--ELRNRVLQR 1408
Cdd:PRK06164  242 GALAGGAPLVCE---PVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPAlgELAALARAR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1409 lpAVALHNRYGPTETAINV------THWQCRAEDGERspIGRPLGNVvcRVLDAEFN-LLPAGVAGELCIGGLGLARGYL 1481
Cdd:PRK06164  319 --GVPLTGLYGSSEVQALValqpatDPVSVRIEGGGR--PASPEARV--RARDPQDGaLLPDGESGEIEIRAPSLMRGYL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1482 GRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGV 1561
Cdd:PRK06164  393 DNPDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620  1562 AGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSG 1615
Cdd:PRK06164  466 GKTVPVAFVIPTDGASPDEAG---LMAACREALAGFKVPARVQVVEAFPVTESA 516
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1130-1639 9.28e-33

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 136.71  E-value: 9.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK07470    9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNL--------------AYV 1275
Cdd:PRK07470   89 FRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLgarvanaavdhddpCWF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1276 IYTSGSTGQPKGVGNTHAALA----ERL-QWMQATytlDGDDVLMQKAPVSFDVSVWEcFWPLVTGCRLVLAaPGEHRDP 1350
Cdd:PRK07470  169 FFTSGTTGRPKAAVLTHGQMAfvitNHLaDLMPGT---TEQDASLVVAPLSHGAGIHQ-LCQVARGAATVLL-PSERFDP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1351 ARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC--GSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTETAINVT 1428
Cdd:PRK07470  244 AEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNIT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1429 ------HwqcRAEDGERSPIG---RPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaa 1499
Cdd:PRK07470  323 vlppalH---DAEDGPDARIGtcgFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF--- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1500 gerlyRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYYTGAVGAEA 1578
Cdd:PRK07470  397 -----RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEvAVLGVPDPVWGEVGVAVCVARDGAPV 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  1579 EAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALpepvwqqREHVEPRTEL 1639
Cdd:PRK07470  472 DEAE---LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV-------REELEERGLL 522
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
678-1096 1.35e-32

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 133.46  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  678 SAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDE---RGEFA---- 750
Cdd:cd19537    5 SPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSsppRVQRVdtld 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  751 -WQFVDLaalaeheraaaaaqrreaeaqqPFDLEKGPLLRVSLVRLdeqehQLWVTLHHIVADGWSLNLLLDEFSRLYAe 829
Cdd:cd19537   85 vWKEINR----------------------PFDLEREDPIRVFISPD-----TLLVVMSHIICDLTTLQLLLREVSAAYN- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  830 acGGQpadLAPLELHYAEFAAWQRQwldagEGARQLAYWRERLGDTAPVLELATDHPRTARQASpaarYSLRVDEALARA 909
Cdd:cd19537  137 --GKL---LPPVRREYLDSTAWSRP-----ASPEDLDFWSEYLSGLPLLNLPRRTSSKSYRGTS----RVFQLPGSLYRS 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  910 IREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIGVPSANRQRLETQGLVGFFINTLVLR-GTPRARQPFA-ALLGEAR 987
Cdd:cd19537  203 LLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFPSSSDASAaDFLRAVR 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  988 EATLGAQANQdLPFDQVLAACGQGGQ-----LFQVL--FnHQQRDLSALRRLPGllADELPWHSREAKFDLQLQSEEDAR 1060
Cdd:cd19537  283 RSSQAALAHA-IPWHQLLEHLGLPPDspnhpLFDVMvtF-HDDRGVSLALPIPG--VEPLYTWAEGAKFPLMFEFTALSD 358
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15597620 1061 GRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAED 1096
Cdd:cd19537  359 DSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
2181-2689 1.80e-32

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 136.04  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2181 EAGL--QDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILK 2258
Cdd:COG1021   18 EAGYwrGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2259 AGG------------------------AYVPLDpEYPLERLQYMIED-----SGVR--LLLSHAALFEALGELPAGVArw 2307
Cdd:COG1021   98 AGAipvfalpahrraeishfaeqseavAYIIPD-RHRGFDYRALARElqaevPSLRhvLVVGDAGEFTSLDALLAAPA-- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2308 clEEDGPALDAEDPApLAALSGpqhqayliytsGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED---CEL---Hfysi 2381
Cdd:COG1021  175 --DLSEPRPDPDDVA-FFQLSG-----------GTTGLPKLIPRTHDDYLYSVRASAEICGLDADTvylAALpaaH---- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2382 NFDAASERLLAPLLCGARVVLRAQGqwGAEEICELIRAEGVSILGFTPSygsQLAQWLESQGRQLP----VRMCITGGEA 2457
Cdd:COG1021  237 NFPLSSPGVLGVLYAGGTVVLAPDP--SPDTAFPLIERERVTVTALVPP---LALLWLDAAERSRYdlssLRVLQVGGAK 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2458 LTGEHLQRIRQAFaPASFFNAYG-------------PTETVV----MPLaCLAPERLeegaasvpigsvvgarvayILDA 2520
Cdd:COG1021  312 LSPELARRVRPAL-GCTLQQVFGmaeglvnytrlddPEEVILttqgRPI-SPDDEVR-------------------IVDE 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2521 DLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVkIR-GFRI 2599
Cdd:COG1021  371 DGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKI 442
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2600 ELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVASAVAEQDedaqaalREALKTHLKQQ-LPDYMVPAHLLLLASLP 2677
Cdd:COG1021  443 AAEEVENLLLAHPAVHDAAVVAMpDEYLGERSCAFVVPRGEPLT-------LAELRRFLRERgLAAFKLPDRLEFVDALP 515
                        570
                 ....*....|..
gi 15597620 2678 LTANGKLDRRAL 2689
Cdd:COG1021  516 LTAVGKIDKKAL 527
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
41-554 1.92e-32

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 133.62  E-value: 1.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   41 LSYRDLDLR-ARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYppesarrhHQerllsiiadaeprl 119
Cdd:cd05972    1 WSFRELKREsAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLT--------TL-------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  120 vLTTADLREpllqmnaQLSAANApQLLCVDQLDPAvaeawdepqvrpehiaFLQYTSGSTALPKGVQVSHGNLVANEVLI 199
Cdd:cd05972   59 -LGPKDIEY-------RLEAAGA-KAIVTDAEDPA----------------LIYFTSGTTGLPKGVLHTHSYPLGHIPTA 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  200 RRGFGIGADDVIvsWLPlyHDMGLIGGLLQPIFS----GVPCVLMSPRYFleRPVRWLEAISQYGGTVSGGPDFAYRlcs 275
Cdd:cd05972  114 AYWLGLRPDDIH--WNI--ADPGWAKGAWSSFFGpwllGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYR--- 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  276 eRVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVtGGQRGQGI-Palavdgea 354
Cdd:cd05972  185 -MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDG------YGQTETGLTV-GNFPDMPVkP-------- 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  355 larnriaegeGSVlmccGRSQPEHAVLIVDAAsGEVLGDDNVGEI-----WaagPSIAHGYWRNPEASAKAFveRDGrtW 429
Cdd:cd05972  249 ----------GSM----GRPTPGYDVAIIDDD-GRELPPGEEGDIaiklpP---PGLFLGYVGDPEKTEASI--RGD--Y 306
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  430 LRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-------RTVESEV---PSARKGR-VAAFAVTVDGEEGigia 497
Cdd:cd05972  307 YLTGDRAyRDEDGYFWFVGRADDIIKSSGYRIGPFEVEsallehpAVAEAAVvgsPDPVRGEvVKAFVVLTSGYEP---- 382
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  498 aeigrgvqKSVPAQELIDSIRQAVAeAYqEAPKVVALlnPGALPKTSSGKLQRSACR 554
Cdd:cd05972  383 --------SEELAEELQGHVKKVLA-PY-KYPREIEF--VEELPKTISGKIRRVELR 427
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
23-552 2.32e-32

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 134.03  E-value: 2.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRFlaeddgEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesar 101
Cdd:cd17649    1 PDAVALVF------GDQSLSYAELDARAnRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDP----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  102 RHHQERLLSIIADAEPRLVLTTadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEHIAFLQYTSGSTAL 181
Cdd:cd17649   70 EYPAERLRYMLEDSGAGLLLTH-----------------------------------------HPRQLAYVIYTSGSTGT 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  182 PKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDmGLIGGLLQPIFSGVpCVLMSPRYFLERPVRWLEAISQYGG 261
Cdd:cd17649  109 PKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGA-CVVLRPDELWASADELAEMVRELGV 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  262 TVSG-GPDFAYRLCSERVAESALQRLDLsgwRVAFSGSEPIRQDSLERFAEKfaasrfdASSFFACYGLAEATlfvtggq 340
Cdd:cd17649  187 TVLDlPPAYLQQLAEEADRTGDGRPPSL---RLYIFGGEALSPELLRRWLKA-------PVRLFNAYGPTEAT------- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  341 rgqgIPALAVDGEAlarnriAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLgDDNVGEIWAAGPSIAHGYWRNPEASAKA 420
Cdd:cd17649  250 ----VTPLVWKCEA------GAARAGASMPIGRPLGGRSAYILDADLNPVP-VGVTGELYIGGEGLARGYLGRPELTAER 318
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  421 FVER----DGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVeSEVPSARkgrvAAFAVTVDGEEGIG 495
Cdd:cd17649  319 FVPDpfgaPGSRLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAAL-LEHPGVR----EAAVVALDGAGGKQ 393
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  496 IAAEIGRGVQKSVPaqELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSA 552
Cdd:cd17649  394 LVAYVVLRAAAAQP--ELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKA 448
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
64-552 2.68e-32

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 133.34  E-value: 2.68e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyppesARRHHQERLLSIIADAEPRLVLTTADLREPLLQmnaqlsAANAP 143
Cdd:TIGR01923   24 GSRVALVGQNSIEMVLLLHACLLLGAEIAML-----NTRLTENERTNQLEDLDVQLLLTDSLLEEKDFQ------ADSLD 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    144 QLLCVDQLDPAVaeawdEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGL 223
Cdd:TIGR01923   93 RIEAAGRYETSL-----SASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    224 iGGLLQPIFSGVPCVLMSPRYFLerpvrwLEAISQYGGT-VSGGPDFAYRLCSERVAESALQRLDLSGwrvafsgsEPIR 302
Cdd:TIGR01923  168 -SILFRWLIEGATLRIVDKFNQL------LEMIANERVThISLVPTQLNRLLDEGGHNENLRKILLGG--------SAIP 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    303 QDSLERFAEKfaasRFDAssfFACYGLAE-ATLFVTggqrgqgipalavdgealARNRIAEGEGSVlmccGRSQPEHAVL 381
Cdd:TIGR01923  233 APLIEEAQQY----GLPI---YLSYGMTEtCSQVTT------------------ATPEMLHARPDV----GRPLAGREIK 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    382 IvdaasgEVLGDDNVGEIWAAGPSIAHGYWRNPEasAKAFVERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNL 460
Cdd:TIGR01923  284 I------KVDNKEGHGEIMVKGANLMKGYLYQGE--LTPAFEQQG--WFNTGDIGELdGEGFLYVLGRRDDLIISGGENI 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    461 YPQDIERTVESEVPSARKGRVAAfavtVDGEEGIGIAAEIgrgVQKSVPAQELIDSIRQAVAEAYQeAPKVVALLNpgAL 540
Cdd:TIGR01923  354 YPEEIETVLYQHPGIQEAVVVPK----PDAEWGQVPVAYI---VSESDISQAKLIAYLTEKLAKYK-VPIAFEKLD--EL 423
                          490
                   ....*....|..
gi 15597620    541 PKTSSGKLQRSA 552
Cdd:TIGR01923  424 PYNASGKILRNQ 435
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2773-3267 2.71e-32

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 139.61  E-value: 2.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2773 ARHSQASQAEQGPVQGDSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEW 2852
Cdd:COG1020    3 AAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2853 LAQHRPLREQELLWHVPVQSFDECAE------LFAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVL 2926
Cdd:COG1020   83 VQVIQPVVAAPLPVVVLLVDLEALAEaaaeaaAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2927 LEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGGQPV--EWPCDRPQGDNREALAESVS 3004
Cdd:COG1020  163 LAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPllELPTDRPRPAVQSYRGARVS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3005 LRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGRealfDDIDLTRSVGWFTSAYPLR--LT 3082
Cdd:COG1020  243 FRLPAELTAALRALA-RRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGR----PRPELEGLVGFFVNTLPLRvdLS 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3083 PAQSPGESIKAIKEQ-LRAVPHKGLGYGVLRYLADPAVRQAMAALPTAPITFNYLGQFDQSFADALFQPLDQPTGPIHDe 3161
Cdd:COG1020  318 GDPSFAELLARVRETlLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKF- 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3162 qaplpnELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQALIEHcledgaGGLTPSDFPLaqLSQAQLDALA 3241
Cdd:COG1020  397 ------DLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD------PDQPLGDLPL--LTAAERQQLL 462
                        490       500
                 ....*....|....*....|....*.
gi 15597620 3242 VPAGEIEDVYPltpmqEGLLLHTLLE 3267
Cdd:COG1020  463 AEWNATAAPYP-----ADATLHELFE 483
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1758-2155 2.96e-32

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 132.42  E-value: 2.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1758 RLSGPLDVARFEAALQALVQRHETLRTTF-PSVDGVPVQRVHGDGglHMDWQDFSALDrdsrqQHLQtlADSEahRPFDL 1836
Cdd:cd19545   29 ELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKES--PISWTESTSLD-----EYLE--EDRA--APMGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1837 eSGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYeaflddrESPLEPLPVQYLDYSvwqrEWLESGERQ 1916
Cdd:cd19545   98 -GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY-------QGEPVPQPPPFSRFV----KYLRQLDDE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1917 RQLDYWKAQLGN----EHPLLelpgdrPRPPVQSHQGDLYRfdlspelAERVRRFNAARGLTMFMTMTATLAALLYRYSG 1992
Cdd:cd19545  166 AAAEFWRSYLAGldpaVFPPL------PSSRYQPRPDATLE-------HSISLPSSASSGVTLATVLRAAWALVLSRYTG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1993 QQDLRIGAPVANRIRPES--EGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQtvidgQSHQDLPFDHL----VEALQPPR 2066
Cdd:cd19545  233 SDDVVFGVTLSGRNAPVPgiEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEHTglqnIRRLGPDA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2067 SAAynPLFQVMCNVQ--------RWEFQQTRQlagMTVEYIANDARAtkfdLNLEVTDLDQRLGCCLTYSRDLFDEPRIA 2138
Cdd:cd19545  308 RAA--CNFQTLLVVQpalpsstsESLELGIEE---ESEDLEDFSSYG----LTLECQLSGSGLRVRARYDSSVISEEQVE 378
                        410
                 ....*....|....*..
gi 15597620 2139 RMAGHWQNLLEALLGDP 2155
Cdd:cd19545  379 RLLDQFEHVLQQLASAP 395
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2822-3213 3.07e-32

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 133.10  E-value: 3.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2822 IDLGLLRKSLQRLVEQHDALRLAFRQvdgEWLAQ-------HRPLREQELLW-HVPVQSFDECAELFAKA--QRSLDLEQ 2891
Cdd:cd19543   36 LDPDRFRAAWQAVVDRHPILRTSFVW---EGLGEplqvvlkDRKLPWRELDLsHLSEAEQEAELEALAEEdrERGFDLAR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2892 GPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSaFRDWAGRLQAYAGSESLRee 2971
Cdd:cd19543  113 APLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVRP-YRDYIAWLQRQDKEAAEA-- 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2972 lgWWQARLGG--QPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVLCRWSGQPSTL 3049
Cdd:cd19543  190 --YWREYLAGfeEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVV 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3050 VQLEGHGREALFDDIDltRSVGWFTSAYPLR--LTPAQSPGESIKAI-KEQLRAVPHKGLGygvlryLADPavrQAMAAL 3126
Cdd:cd19543  267 FGTTVSGRPAELPGIE--TMVGLFINTLPVRvrLDPDQTVLELLKDLqAQQLELREHEYVP------LYEI---QAWSEG 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3127 PTAPI----TF-NYlgqfdqsfadalfqPLDQPTGPIHDEQAPLPNELSVDGQV-Y--------GGELVLRWTYSRERYD 3192
Cdd:cd19543  336 KQALFdhllVFeNY--------------PVDESLEEEQDEDGLRITDVSAEEQTnYpltvvaipGEELTIKLSYDAEVFD 401
                        410       420
                 ....*....|....*....|.
gi 15597620 3193 ARTVNELAQAYLAELQALIEH 3213
Cdd:cd19543  402 EATIERLLGHLRRVLEQVAAN 422
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
2188-2689 3.27e-32

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 135.01  E-value: 3.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2188 LHGLFAARVAASPQAPALTFAGQ--TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVP 2265
Cdd:PRK05852   18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2266 LDPEYPLERLQYMIEDSGVRLLLSHAalfEALGELPAGVARWCL------EEDGPALDAEDP------APLAALSGPQ-- 2331
Cdd:PRK05852   98 LDPALPIAEQRVRSQAAGARVVLIDA---DGPHDRAEPTTRWWPltvnvgGDSGPSGGTLSVhldaatEPTPATSTPEgl 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2332 --HQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCE---LHFYSINFDAASerLLAPLLCGARVVLRAQG 2406
Cdd:PRK05852  175 rpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATvavMPLYHGHGLIAA--LLATLASGGAVLLPARG 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2407 QWGAEEICELIRAEGVSILGFTPSYGSQLAQW--LESQGRQLP----VRMCitgGEALTGEHLQRIRQAFApASFFNAYG 2480
Cdd:PRK05852  253 RFSAHTFWDDIKAVGATWYTAVPTIHQILLERaaTEPSGRKPAalrfIRSC---SAPLTAETAQALQTEFA-APVVCAFG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2481 PTETV--VMPLACLAPERLEEGAASV-PIGSVVGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVP 2557
Cdd:PRK05852  329 MTEAThqVTTTQIEGIGQTENPVVSTgLVGRSTGAQIR-IVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2558 DPFaaeggrlyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSpsgkQLAGYVASA 2637
Cdd:PRK05852  408 GWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPD----QLYGEAVAA 475
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597620  2638 VAEQDEDAqAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK05852  476 VIVPRESA-PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1153-1593 4.09e-32

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 135.06  E-value: 4.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGvGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPS---ERLAYMLADSGVELL 1229
Cdd:cd05931   24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGrhaERLAAILADAGPRVV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1230 LTQA------HLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQ 1303
Cdd:cd05931  103 LTTAaalaavRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIR 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1304 ATYTLDGDDVLmqkapvsfdvsvweCFW---------------PLVTGCRLVLAAPGEH-RDPARLVELVRQFGVTTlHF 1367
Cdd:cd05931  183 RAYGLDPGDVV--------------VSWlplyhdmgligglltPLYSGGPSVLMSPAAFlRRPLRWLRLISRYRATI-SA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1368 VP----PLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQR-----LPAVALHNRYGPTETAINVTH------- 1429
Cdd:cd05931  248 APnfayDLCVRRVRDEDLEGldLSSWRVALNGAEPVRPATLRRFAEAfapfgFRPEAFRPSYGLAEATLFVSGgppgtgp 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1430 ----------WQCRAEDGERSPIGRPL---GNVVC----RVLDAEFN-LLPAGVAGELCIGGLGLARGYLGRPALSAERF 1491
Cdd:cd05931  328 vvlrvdrdalAGRAVAVAADDPAARELvscGRPLPdqevRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPEATAETF 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1492 VADpfSAAGERLY-RTGDRARWnADGVLEYLGRLDQQVKLRGFRIEPEEI-----QARLLAQPGVAQAVVVIREGVAGSQ 1565
Cdd:cd05931  408 GAL--AATDEGGWlRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIeataeEAHPALRPGCVAAFSVPDDGEERLV 484
                        490       500
                 ....*....|....*....|....*...
gi 15597620 1566 LVGYYTGAVGAEAEAEQNQRLRAALQAE 1593
Cdd:cd05931  485 VVAEVERGADPADLAAIAAAIRAAVARE 512
PRK09274 PRK09274
peptide synthase; Provisional
2193-2619 1.07e-31

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 133.87  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2193 AARvaASPQAPALTFAG----------QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGA 2262
Cdd:PRK09274   15 AAQ--ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2263 YVPLDPEYPLERLQYMIEDSG------------VRLLLSHAalFEALGELPAGVARWCLEedGPALD------AEDPAPL 2324
Cdd:PRK09274   93 PVLVDPGMGIKNLKQCLAEAQpdafigipkahlARRLFGWG--KPSVRRLVTVGGRLLWG--GTTLAtllrdgAAAPFPM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2325 AALsGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHfysiNFDAASerLLAPLLCGARVV--- 2401
Cdd:PRK09274  169 ADL-APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TFPLFA--LFGPALGMTSVIpdm 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2402 -LRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAP-ASFFNA 2478
Cdd:PRK09274  242 dPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPsLRRVISAGAPVPIAVIERFRAMLPPdAEILTP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2479 YGPTEtvVMPLACLAP-ERLEEGA------ASVPIGSVV-GARVAYI---------LDADLALvPQGATGELYVGGAGLA 2541
Cdd:PRK09274  322 YGATE--ALPISSIESrEILFATRaatdngAGICVGRPVdGVEVRIIaisdapipeWDDALRL-ATGEIGEIVVAGPMVT 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  2542 RGYHERPALSAERFVPDPfaaEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQV-REALV 2619
Cdd:PRK09274  399 RSYYNRPEATRLAKIPDG---QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRSALV 474
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3274-3554 1.16e-31

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 131.42  E-value: 1.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3274 YMQD--------RYRIDSPLDPERFAAAWQAVVARHEALRASFVWNA--GETMlQVIHKPGRTRIEFLDWSElpEDGHEE 3343
Cdd:cd19532   17 YLEDpttfnvtfSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPedGEPM-QGVLASSPLRLEHVQISD--EAEVEE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3344 RLQALHKREreagFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSalgesRPANLPTPPRYRD 3423
Cdd:cd19532   94 EFERLKNHV----YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN-----GQPLLPPPLQYLD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3424 YIAwLQRQDLEQSRrwWSESLRgF---ERPTLVP----------SDRPFLREHagesgGMIVGDRytRLDAADGARLREL 3490
Cdd:cd19532  165 FAA-RQRQDYESGA--LDEDLA-YwksEFSTLPEplpllpfakvKSRPPLTRY-----DTHTAER--RLDAALAARIKEA 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 3491 AQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPvgMPEMQRTVGLFINSIPLRVQMPA 3554
Cdd:cd19532  234 SRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRT--DEDFMETIGFFLNLLPLRFRRDP 295
PRK07787 PRK07787
acyl-CoA synthetase; Validated
2191-2661 1.37e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 132.04  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2191 LFAARVAASPQ-APALTFAGQTLSYAELDARSNRLArvlrsHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2269
Cdd:PRK07787    4 LNPAAVAAAADiADAVRIGGRVLSRSDLAGAATAVA-----ERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2270 YPLERLQYMIEDSGVRLLLshAALFEALGELPAGVARwcLEEDGPALDAEDPAPLAALsgpqhqayLIYTSGSTGKPKGV 2349
Cdd:PRK07787   79 SGVAERRHILADSGAQAWL--GPAPDDPAGLPHVPVR--LHARSWHRYPEPDPDAPAL--------IVYTSGTTGPPKGV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2350 AVSHGEIAMHCAAVIECFGMRAEDCELH----FYSINFDAAserLLAPLLCGARVVlrAQGQWGAEEICELIRAEGVSIL 2425
Cdd:PRK07787  147 VLSRRAIAADLDALAEAWQWTADDVLVHglplFHVHGLVLG---VLGPLRIGNRFV--HTGRPTPEAYAQALSEGGTLYF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2426 GfTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRqAFAPASFFNAYGPTETVvMPLACLAPERLEEGAASVP 2505
Cdd:PRK07787  222 G-VPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLA-ALTGHRPVERYGMTETL-ITLSTRADGERRPGWVGLP 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2506 IGsvvGARVAYILDADLALVPQGAT-GELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEY 2584
Cdd:PRK07787  299 LA---GVETRLVDEDGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHRI 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2585 VGR--IDhQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaVAEQDEDAqaalrEALKTHLKQQL 2661
Cdd:PRK07787  369 VGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVpDDDLGQRIVAYV---VGADDVAA-----DELIDFVAQQL 439
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
10-554 2.39e-31

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 132.97  E-value: 2.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFLAEddgeGVVLSYRDL----DLRARSIAAALQAHaqlGDRAVLLFPSGPDYVAAFFGCL 85
Cdd:PRK12583   19 TIGDAFDATVARFPDREALVVRHQ----ALRYTWRQLadavDRLARGLLALGVQP---GDRVGIWAPNCAEWLLTQFATA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAV---PAYppesaRRHHQERLLS-------IIADAeprlvLTTADLREPLLQM--------NAQLSAANAPQLLC 147
Cdd:PRK12583   92 RIGAILVninPAY-----RASELEYALGqsgvrwvICADA-----FKTSDYHAMLQELlpglaegqPGALACERLPELRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   148 VDQLDPAVAE---AWDEPQVRPEHIAF-----------------LQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGA 207
Cdd:PRK12583  162 VVSLAPAPPPgflAWHELQARGETVSRealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   208 DDVIVSWLPLYHDMGLIGGLLQPIFSGVpCVLMSPRYFleRPVRWLEAISQYGGTVSGG-----------PDFAyrlcse 276
Cdd:PRK12583  242 HDRLCVPVPLYHCFGMVLANLGCMTVGA-CLVYPNEAF--DPLATLQAVEEERCTALYGvptmfiaeldhPQRG------ 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   277 rvaesalqRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASsffacYGLAEATLFVTGGQRGQGIPalavdgeala 356
Cdd:PRK12583  313 --------NFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIA-----YGMTETSPVSLQTTAADDLE---------- 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   357 rNRIAegegSVlmccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAfVERDGrtWLRTGDLG 436
Cdd:PRK12583  370 -RRVE----TV----GRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAES-IDEDG--WMHTGDLA 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   437 FL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSArkgRVAAFAVTVD--GEEgigIAAEIGRGVQKSVPAQEL 513
Cdd:PRK12583  437 TMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVA---DVQVFGVPDEkyGEE---IVAWVRLHPGHAASEEEL 510
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 15597620   514 IDSIRQAVaeAYQEAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:PRK12583  511 REFCKARI--AHFKVPRYFRFVD--EFPMTVTGKVQKFRMR 547
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3706-4230 2.41e-31

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 131.68  E-value: 2.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3706 ARDYPLEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFK 3785
Cdd:cd05920    8 AAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3786 AGAGYLPLDPGHPTQRLTRIVELSR-TLVLVCTQACREQALALFDELgcvdrprllvwdeiqqgegAEHDPQVysgpqnl 3864
Cdd:cd05920   88 LGAVPVLALPSHRRSELSAFCAHAEaVAYIVPDRHAGFDHRALAREL-------------------AESIPEV------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3865 AYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDV--IAQTASQSFDISVWQFLAAPLFGARVAIVPNAvahDP 3942
Cdd:cd05920  142 ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---SP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3943 QGLLAHVGEQGITVLESVPSLIQ---GMLAEERQALDGLRWMLPTGEAMPPELARQwlkRYPRIG--LVNAYGPAEcsDD 4017
Cdd:cd05920  219 DAAFPLIEREGVTVTALVPALVSlwlDAAASRRADLSSLRLLQVGGARLSPALARR---VPPVLGctLQQVFGMAE--GL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4018 VAFFRVD-----LASTESTylPIgSPTDNNRLyllgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHP 4092
Cdd:cd05920  294 LNYTRLDdpdevIIHTQGR--PM-SPDDEIRV------VDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDG 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4093 FgapgerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAA-VAVQEGANGKYLVGYLVPGE 4171
Cdd:cd05920  365 F-------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAvVAMPDELLGERSCAFVVLRD 437
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4172 TPRSSADspaglmveqgawferIKQQLR-ADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05920  438 PPPSAAQ---------------LRRFLReRGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1106-1556 3.34e-31

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 132.71  E-value: 3.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1106 LVDAEQAAHLAEWGSApcEPARAWLP--------ELLERQLAQS-AERVALEWDGG----SLGYAELHARANRLAHYLRD 1172
Cdd:PRK04319   15 LKDYEETYATFSWEEV--EKEFSWLEtgkvniayEAIDRHADGGrKDKVALRYLDAsrkeKYTYKELKELSNKFANVLKE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1173 KGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAE--------- 1243
Cdd:PRK04319   93 LGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDlpslkhvll 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1244 -----GVTPICLDSLKL-DNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAerLQWMQATYTLD--GDDVLM 1315
Cdd:PRK04319  173 vgedvEEGPGTLDFNALmEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAML--QHYQTGKYVLDlhEDDVYW 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1316 QKA-P-----VSFDVsvwecFWPLVTGCRLVLAapGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDE-PGVAAC---G 1385
Cdd:PRK04319  251 CTAdPgwvtgTSYGI-----FAPWLNGATNVID--GGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAgDDLVKKydlS 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1386 SLRRLFSGGEALPAEL---RNRVLQrLPavaLHNRYGPTET-AINVTHWqcRAEDGERSPIGRPLGNVVCRVLDAEFNLL 1461
Cdd:PRK04319  324 SLRHILSVGEPLNPEVvrwGMKVFG-LP---IHDNWWMTETgGIMIANY--PAMDIKPGSMGKPLPGIEAAIVDDQGNEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1462 PAGVAGELCI--GGLGLARGYLGRPALSAERFVADpfsaagerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEE 1539
Cdd:PRK04319  398 PPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
                         490
                  ....*....|....*..
gi 15597620  1540 IQARLLAQPGVAQAVVV 1556
Cdd:PRK04319  470 VESKLMEHPAVAEAGVI 486
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
2213-2689 3.72e-31

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 131.60  E-value: 3.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2213 SYAELDARSNRLARVLRSHGVGPEVRVG-LALE--RSLEMvvgLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS 2289
Cdd:cd12119   27 TYAEVAERARRLANALRRLGVKPGDRVAtLAWNthRHLEL---YYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 HAALF----EALGELPAgVARWCLEEDGPALDAEDPAPLAA---LSGPQHQAY------------LIYTSGSTGKPKGVA 2350
Cdd:cd12119  104 DRDFLplleAIAPRLPT-VEHVVVMTDDAAMPEPAGVGVLAyeeLLAAESPEYdwpdfdentaaaICYTSGTTGNPKGVV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2351 VSHGEIAMHCAAVI--ECFGMRAEDCELHFYSInFDAASERL-LAPLLCGARVVL---RAQGqwgaEEICELIRAEGVSI 2424
Cdd:cd12119  183 YSHRSLVLHAMAALltDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLpgpYLDP----ASLAELIEREGVTF 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2425 LGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEALTGEHLQRIRQAFAPasFFNAYGPTETvvMPLACLAPERLEEGAAS 2503
Cdd:cd12119  258 AAGVPTVWQGLLDHLEANGRDLsSLRRVVIGGSAVPRSLIEAFEERGVR--VIHAWGMTET--SPLGTVARPPSEHSNLS 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2504 ------------VPIGSVvgarVAYILDADLALVPQ--GATGELYVGGAGLARGYHERPALSAERFvpdpfaaEGGRLyR 2569
Cdd:cd12119  334 edeqlalrakqgRPVPGV----ELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALT-------EDGWL-R 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2570 TGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGkqlaGYVASAVAEQDEDAQAAl 2649
Cdd:cd12119  402 TGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKW----GERPLAVVVLKEGATVT- 476
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15597620 2650 REALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd12119  477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1269-1622 4.22e-31

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 127.98  E-value: 4.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1269 GDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFDV--SVWECFWPLVTGCRLVLAAPGE 1346
Cdd:cd05944    1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLAGPAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1347 HRDPA---RLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTET 1423
Cdd:cd05944   80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDAT-GLPVVEGYGLTEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1424 AINVThwqCRAEDGERSP--IGRPL--GNVVCRVLDAEFNLL-PAGV--AGELCIGGLGLARGYL----GRPALSAERFV 1492
Cdd:cd05944  159 TCLVA---VNPPDGPKRPgsVGLRLpyARVRIKVLDGVGRLLrDCAPdeVGEICVAGPGVFGGYLytegNKNAFVADGWL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1493 adpfsaagerlyRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIR-EGVAGSQLVGYYT 1571
Cdd:cd05944  236 ------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQpDAHAGELPVAYVQ 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15597620 1572 GAVGAEAEAEQnqrLRAALQAELPEY-MVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05944  304 LKPGAVVEEEE---LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3728-4230 4.46e-31

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 130.10  E-value: 4.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3728 QRIAASCLEQRWSYAELNRRANRLGHALRAAG-VGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPtqrltrIV 3806
Cdd:cd05941    1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYP------LA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRTLvlvcTQAcreqalalfdelgcvdRPRLLVwdeiqqgegaehdpqvysgpqNLAYVIYTSGSTGLPKGVMVEQAG 3886
Cdd:cd05941   75 ELEYVI----TDS----------------EPSLVL---------------------DPALILYTSGTTGRPKGVVLTHAN 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3887 MLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNavaHDPQGLLAHVGEQGITVLESVPS--- 3962
Cdd:cd05941  114 LAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFaGASVEFLPK---FDPKEVAISRLMPSITVFMGVPTiyt 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3963 -LIQG-------MLAEERQALDGLRWMLPTGEAMPPELARQW--------LKRY--PRIGlVNAYGPAECSddvaffRVD 4024
Cdd:cd05941  191 rLLQYyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEWeaitghtlLERYgmTEIG-MALSNPLDGE------RRP 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4025 LAstestylpIGSPTDNNRLYLLgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTG 4104
Cdd:cd05941  264 GT--------VGMPLPGVQARIV---DEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTG 325
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4105 DLARRRADGVLEYVGRI-DHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVpgetPRSSADSPAg 4182
Cdd:cd05941  326 DLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAViGVPDPDWGERVVAVVV----LRAGAAALS- 400
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 4183 lmveqgawFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05941  401 --------LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK07529 PRK07529
AMP-binding domain protein; Validated
7-556 5.29e-31

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 132.77  E-value: 5.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     7 LPTTLVQALRRRAVQEPERLALRFL--AEDDGEGVVLSYRDLDLR-ARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFG 83
Cdd:PRK07529   23 LPASTYELLSRAAARHPDAPALSFLldADPLDRPETWTYAELLADvTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    84 CLYAGvIAVPAYPPESArrhhqERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEA----W 159
Cdd:PRK07529  103 GEAAG-IANPINPLLEP-----EQIAELLRAAGAKVLVTLGPFPGTDIWQKVAEVLAALPELRTVVEVDLARYLPgpkrL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   160 DEPQVRPE-HIAFLQY----------------------------TSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDV 210
Cdd:PRK07529  177 AVPLIRRKaHARILDFdaelarqpgdrlfsgrpigpddvaayfhTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDT 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   211 IVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPR-YFLERPVR--WlEAISQYGGTVSGGPDFAYRLCSERVAESAlqrlD 287
Cdd:PRK07529  257 VFCGLPLFHVNALLVTGLAPLARGAHVVLATPQgYRGPGVIAnfW-KIVERYRINFLSGVPTVYAALLQVPVDGH----D 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   288 LSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVT----GGQR-----GQGIPALAVdgealarn 358
Cdd:PRK07529  332 ISSLRYALCGAAPLPVEVFRRFEAATGVRIVEG------YGLTEATCVSSvnppDGERrigsvGLRLPYQRV-------- 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   359 RIAEGEGSvlmccGRsqpehavLIVDAASGEVlgddnvGEIWAAGPSIAHGYwRNPEASAKAFVERDgrtWLRTGDLGFL 438
Cdd:PRK07529  398 RVVILDDA-----GR-------YLRDCAVDEV------GVLCIAGPNVFSGY-LEAAHNKGLWLEDG---WLNTGDLGRI 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   439 -RDGELFVTGRLKDMLIVRGHNLYPQDIErtvesevpsarkgrvAAFAvtvdGEEGIGIAAEIGR-----G------VQ- 505
Cdd:PRK07529  456 dADGYFWLTGRAKDLIIRGGHNIDPAAIE---------------EALL----RHPAVALAAAVGRpdahaGelpvayVQl 516
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620   506 ---KSVPAQELIDSIRQAVAE--AyqeAPKVVALLNpgALPKTSSGKLQRSACRLR 556
Cdd:PRK07529  517 kpgASATEAELLAFARDHIAEraA---VPKHVRILD--ALPKTAVGKIFKPALRRD 567
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2821-3045 5.60e-31

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 129.40  E-value: 5.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2821 AIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWL-----AQHRPLREQELLWHVPVQSFDECAELFAK-AQRSLDLEQGPL 2894
Cdd:cd19531   35 PLDVAALERALNELVARHEALRTTFVEVDGEPVqvilpPLPLPLPVVDLSGLPEAEREAEAQRLAREeARRPFDLARGPL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2895 LRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSESLREELGW 2974
Cdd:cd19531  115 LRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAY 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2975 WQARLGG--QPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVLCRWSGQ 3045
Cdd:cd19531  195 WREQLAGapPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALA-RREGATLFMTLLAAFQVLLHRYSGQ 266
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1143-1622 6.00e-31

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 130.78  E-value: 6.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1143 ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:PRK06145   17 DRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1223 DSGVELLLTQAHlFERLPGAEgvTPICL-------DSLKLDNWPSQAPGLHLHG-DNLAYVIYTSGSTGQPKGVGNTHAA 1294
Cdd:PRK06145   97 DAGAKLLLVDEE-FDAIVALE--TPKIVidaaaqaDSRRLAQGGLEIPPQAAVApTDLVRLMYTSGTTDRPKGVMHSYGN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1295 LAerlqWMQATYT----LDGDDVLMQKAPVsfdVSVWECFWPLVTgcrlVLAAPGEHR-----DPARLVELVRQFGVTTL 1365
Cdd:PRK06145  174 LH----WKSIDHVialgLTASERLLVVGPL---YHVGAFDLPGIA----VLWVGGTLRihrefDPEAVLAAIERHRLTCA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1366 HFVPPLLQ--LFIDEPGVAACGSLRRLFSGGEALPaELRNRVLQRLPAVALH-NRYGPTETAINVTHWQCRAEDGERSPI 1442
Cdd:PRK06145  243 WMAPVMLSrvLTVPDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTETCSGDTLMEAGREIEKIGST 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1443 GRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlyRTGDRARWNADGVLEYLG 1522
Cdd:PRK06145  322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEGFLYLTD 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1523 RLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPT 1601
Cdd:PRK06145  394 RKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVVLNPGATLTLEA---LDRHCRQRLASFKVPR 470
                         490       500
                  ....*....|....*....|.
gi 15597620  1602 QLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK06145  471 QLKVRDELPRNPSGKVLKRVL 491
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
38-554 6.27e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 131.81  E-value: 6.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    38 GVVLSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR-HHQ-----ERLL 109
Cdd:PRK05677   47 GKTLTYGELYKLSGAFAAwlQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREmEHQfndsgAKAL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   110 SIIAD----AE---PR------LVLTTADLREPL--LQMNA-------QLSAANAPQLLCV-DQLDPAVAEAWDEPQVRP 166
Cdd:PRK05677  127 VCLANmahlAEkvlPKtgvkhvIVTEVADMLPPLkrLLINAvvkhvkkMVPAYHLPQAVKFnDALAKGAGQPVTEANPQA 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   167 EHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADD---VIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMS-P 242
Cdd:PRK05677  207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILISnP 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   243 R---YFLERPVRWleaisQYGGTVSGGPDFAyRLCSERvaesALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFD 319
Cdd:PRK05677  287 RdlpAMVKELGKW-----KFSGFVGLNTLFV-ALCNNE----AFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICE 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   320 AssffacYGLAEATLFVTGGQRGQ------GIPAlavdgealarnriaegegsvlmccgrsqPEHAVLIVDAASGEV-LG 392
Cdd:PRK05677  357 G------YGMTETSPVVSVNPSQAiqvgtiGIPV----------------------------PSTLCKVIDDDGNELpLG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   393 DdnVGEIWAAGPSIAHGYWRNPEASAKAFverDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIErtves 471
Cdd:PRK05677  403 E--VGELCVKGPQVMKGYWQRPEATDEIL---DSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELE----- 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   472 EVPSARKGRVAAFAVTV-DGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAeAYQeAPKVVALLNpgALPKTSSGKLQR 550
Cdd:PRK05677  473 DVLAALPGVLQCAAIGVpDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLT-GYK-VPKAVEFRD--ELPTTNVGKILR 548

                  ....
gi 15597620   551 SACR 554
Cdd:PRK05677  549 RELR 552
PRK09088 PRK09088
acyl-CoA synthetase; Validated
19-557 6.66e-31

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 130.31  E-value: 6.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    19 AVQEPERLALRFLAEddgeGVVLSYRDLD-LRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPP 97
Cdd:PRK09088    5 ARLQPQRLAAVDLAL----GRRWTYAELDaLVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    98 ESARRHHqerllSIIADAEPRLVLTTADLrepllqmnaqlsAANAPQLLCVDQLDPAV--AEAWDEPQVRPEHIAFLQYT 175
Cdd:PRK09088   81 LSASELD-----ALLQDAEPRLLLGDDAV------------AAGRTDVEDLAAFIASAdaLEPADTPSIPPERVSLILFT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   176 SGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGlLQPIFSGVPCVLMSPRYFLERPVRWLE- 254
Cdd:PRK09088  144 SGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITS-VRPVLAVGGSILVSNGFEPKRTLGRLGd 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   255 ---AISQYGGTvsggPDFAYRLCSE-RVAESALQRLDlsgwrVAFSGSEPIRQDSLERFaekfaasrFDASSFFAC-YGL 329
Cdd:PRK09088  223 palGITHYFCV----PQMAQAFRAQpGFDAAALRHLT-----ALFTGGAPHAAEDILGW--------LDDGIPMVDgFGM 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   330 AEA-TLFvtggqrgqGIPALAvdgealarNRIAEGEGSVlmccGRSQPEHAVLIVDAASGEVLGDDNvGEIWAAGPSIAH 408
Cdd:PRK09088  286 SEAgTVF--------GMSVDC--------DVIRAKAGAA----GIPTPTVQTRVVDDQGNDCPAGVP-GELLLRGPNLSP 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   409 GYWRNPEASAKAFverDGRTWLRTGDLGfLRDGELFVT--GRLKDMLIVRGHNLYPQDIErTVESEVPSARKGRVAAFAv 486
Cdd:PRK09088  345 GYWRRPQATARAF---TGDGWFRTGDIA-RRDADGFFWvvDRKKDMFISGGENVYPAEIE-AVLADHPGIRECAVVGMA- 418
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620   487 tvDGEEGigiaaEIGRGVqkSVPAQE---LIDSIRQAVAE--AYQEAPKVVALLNpgALPKTSSGKLQRSACRLRL 557
Cdd:PRK09088  419 --DAQWG-----EVGYLA--IVPADGaplDLERIRSHLSTrlAKYKVPKHLRLVD--ALPRTASGKLQKARLRDAL 483
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
675-1097 7.72e-31

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 128.19  E-value: 7.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  675 LPQSAAQQRLWLTWQIDPQSaaYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLE--RDGAALQRIDERGEFAWQ 752
Cdd:cd19542    2 YPCTPMQEGMLLSQLRSPGL--YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVEssAEGTFLQVVLKSLDPPIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  753 FVDLAALAEHERAAAAAQRReaeaqqpfDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAeacg 832
Cdd:cd19542   80 EVETDEDSLDALTRDLLDDP--------TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN---- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  833 GQPADLAPlelHYAEFAAWQRQwldaGEGARQLAYWRERLGDTAPVLE-LATDHPRTARQASPAARYSLRVDEalARAIR 911
Cdd:cd19542  148 GQLLPPAP---PFSDYISYLQS----QSQEESLQYWRKYLQGASPCAFpSLSPKRPAERSLSSTRRSLAKLEA--FCASL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  912 EAALdheASVFMwllAAFQALLHRHSGQGEIRIGVPSANRQ--RLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREA 989
Cdd:cd19542  219 GVTL---ASLFQ---AAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQ 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  990 TLGAQANQDLPFDQVLAACGQ--GGQLFQVLFNHQQRDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDaRGRLTLNF 1067
Cdd:cd19542  293 YLRSLPHQHLSLREIQRALGLwpSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPS-GDSLKVSL 371
                        410       420       430
                 ....*....|....*....|....*....|
gi 15597620 1068 DYAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19542  372 AYSTSVLSEEQAEELLEQFDDILEALLANP 401
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
1144-1622 1.00e-30

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 128.75  E-value: 1.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1144 RVALEWDGGSLGYAELHARANRLAHYLRDKGVG-PDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLA 1222
Cdd:cd05958    1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1223 DSGVELLLtqahlferlpgaegvtpiCLDSLKldnwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ-W 1301
Cdd:cd05958   81 KARITVAL------------------CAHALT-------------ASDDICILAFTSGTTGAPKATMHFHRDPLASADrY 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1302 MQATYTLDGDDVLMQKAPVSFDVSV-WECFWPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPG 1380
Cdd:cd05958  130 AVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL---EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPD 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1381 VAA--CGSLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTEtainVTHWQCRAEDGERSP--IGRPLGNVVCRVLDA 1456
Cdd:cd05958  207 AAGpdLSSLRKCVSAGEALPAALHRA-WKEATGIPIIDGIGSTE----MFHIFISARPGDARPgaTGKPVPGYEAKVVDD 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1457 EFNLLPAGVAGELCIGGLGLARgYLGRPalSAERFVADPFSAAGERLYRtgdrarwNADGVLEYLGRLDQQVKLRGFRIE 1536
Cdd:cd05958  282 EGNPVPDGTIGRLAVRGPTGCR-YLADK--RQRTYVQGGWNITGDTYSR-------DPDGYFRHQGRSDDMIVSGGYNIA 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1537 PEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYtgaVGAEAEAEQNQRLRAALQ----AELPEYMVPTQLMRLAQMPLG 1612
Cdd:cd05958  352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAF---VVLRPGVIPGPVLARELQdhakAHIAPYKYPRAIEFVTELPRT 428
                        490
                 ....*....|
gi 15597620 1613 PSGKLDTRAL 1622
Cdd:cd05958  429 ATGKLQRFAL 438
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
34-491 1.18e-30

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 129.76  E-value: 1.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   34 DDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGviAVPAYPPESArrhHQERLLSIIA 113
Cdd:cd05909    1 EDTLGTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTA---GLRELRACIK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  114 DAEPRLVLTTADLREpLLQMNAQLSAANAPQLLCVDQLDPAVAEA--------------WDEPQ-----VRPEHIAFLQY 174
Cdd:cd05909   76 LAGIKTVLTSKQFIE-KLKLHHLFDVEYDARIVYLEDLRAKISKAdkckaflagkfppkWLLRIfgvapVQPDDPAVILF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  175 TSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-SPRYFLERPvrwl 253
Cdd:cd05909  155 TSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpNPLDYKKIP---- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  254 EAISQYGGTVSGGPDFAYRLCSERVAESalqrlDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEAT 333
Cdd:cd05909  231 ELIYDKKATILLGTPTFLRGYARAAHPE-----DFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEG------YGTTECS 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  334 lfvtggqrgqgiPALAVDGEALARNriaegEGSVlmccGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRN 413
Cdd:cd05909  300 ------------PVISVNTPQSPNK-----EGTV----GRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNE 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  414 PEASAKAFverdGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRG------------HNLYPQDIERTVESeVPSARKG- 479
Cdd:cd05909  359 PELTSFAF----GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGemvsleaiedilSEILPEDNEVAVVS-VPDGRKGe 433
                        490
                 ....*....|..
gi 15597620  480 RVAAFAVTVDGE 491
Cdd:cd05909  434 KIVLLTTTTDTD 445
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
1156-1628 1.25e-30

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 132.46  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHL 1235
Cdd:PRK06060   33 HGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDAL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1236 FERLPGAEGVTPICLDSLKLDNWPSQAPglHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM-QATYTLDGDDVL 1314
Cdd:PRK06060  113 RDRFQPSRVAEAAELMSEAARVAPGGYE--PMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDTG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1315 MQKAPVSFDVSVWECFW-PLVTGCRLVLAAPGEHRDPARLveLVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSG 1393
Cdd:PRK06060  191 LCSARMYFAYGLGNSVWfPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSA 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1394 GEALPAELRNRVLQRLPAVALHNRYGPTEtaINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGG 1473
Cdd:PRK06060  269 GEALELGLAERLMEFFGGIPILDGIGSTE--VGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRG 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1474 LGLARGYLGRPalsaerfvaDPFSAAGERLyRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQA 1553
Cdd:PRK06060  347 PAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEA 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1554 VVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL-----PEPVW 1627
Cdd:PRK06060  417 AVVaVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqspTKPIW 496

                  .
gi 15597620  1628 Q 1628
Cdd:PRK06060  497 E 497
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1150-1628 1.27e-30

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 129.81  E-value: 1.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1150 DGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELL 1229
Cdd:PRK13391   21 TGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARAL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1230 LTQAHLFERLPGAEGVTPICLDSLKLDNwPSQAPGLHLHGDNLAYV--------------IYTSGSTGQPKGVgntHAAL 1295
Cdd:PRK13391  101 ITSAAKLDVARALLKQCPGVRHRLVLDG-DGELEGFVGYAEAVAGLpatpiadeslgtdmLYSSGTTGRPKGI---KRPL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1296 AER--------LQWMQATYTLDGDDVLMQKAPVSFDVsvwecfwPLvTGCRLVLAAPG-----EHRDPARLVELVRQFGV 1362
Cdd:PRK13391  177 PEQppdtplplTAFLQRLWGFRSDMVYLSPAPLYHSA-------PQ-RAVMLVIRLGGtvivmEHFDAEQYLALIEEYGV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1363 TTLHFVPPL----LQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTE----TAINVTHWQCRa 1434
Cdd:PRK13391  249 THTQLVPTMfsrmLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEglgfTACDSEEWLAH- 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1435 edgeRSPIGRPLGNVVcRVLDAEFNLLPAGVAGELCIGGlGLARGYLGRPALSAERFVADPfsaageRLYRTGDRARWNA 1514
Cdd:PRK13391  327 ----PGTVGRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG------TWSTVGDIGYVDE 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1515 DGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQNQRLRAAL 1590
Cdd:PRK13391  395 DGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVF---GVPnedlGEEVKAVVQPVDGVDPGPALAAELIAFC 471
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 15597620  1591 QAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQ 1628
Cdd:PRK13391  472 RQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
1132-1610 1.37e-30

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 131.46  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDG-----GSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYV 1206
Cdd:cd05968   65 QLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1207 PLDPDYPSERLAYMLADSGVELLLTqAHLFER-------LPGAEGVTPICLDSLKL----------------DNWPSQ-- 1261
Cdd:cd05968  145 PIFSGFGKEAAATRLQDAEAKALIT-ADGFTRrgrevnlKEEADKACAQCPTVEKVvvvrhlgndftpakgrDLSYDEek 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1262 -APGLHL---HGDNLAYVIYTSGSTGQPKGVGNTHAALA-ERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTG 1336
Cdd:cd05968  224 eTAGDGAertESEDPLMIIYTSGTTGKPKGTVHVHAGFPlKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILG 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1337 CRLVL--AAPGeHRDPARLVELVRQFGVTTLHFVPPLLQLFI---DEPgVAACG--SLRRLFSGGEALPAE-----LRNR 1404
Cdd:cd05968  304 ATMVLydGAPD-HPKADRLWRMVEDHEITHLGLSPTLIRALKprgDAP-VNAHDlsSLRVLGSTGEPWNPEpwnwlFETV 381
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1405 VLQRLPAValhNRYGPTETAinvthwqcraedgerspiGRPLGNVVCR-----------------VLDAEFNLLPAGVaG 1467
Cdd:cd05968  382 GKGRNPII---NYSGGTEIS------------------GGILGNVLIKpikpssfngpvpgmkadVLDESGKPARPEV-G 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1468 ELCIGG--LGLARGYLGRPalsaERFVADPFSAAgERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLL 1545
Cdd:cd05968  440 ELVLLApwPGMTRGFWRDE----DRYLETYWSRF-DNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLN 514
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 1546 AQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMP 1610
Cdd:cd05968  515 AHPAVLESAAIgVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLP 580
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
3739-4152 1.70e-30

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 127.84  E-value: 1.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPldpghptqrltrivelsrtlvlvCTQ 3818
Cdd:cd05972    1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVP-----------------------LTT 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3819 ACREQALALFDELGcvdRPRLLVWDEiqqgegaehdpqvysgpQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL 3898
Cdd:cd05972   58 LLGPKDIEYRLEAA---GAKAIVTDA-----------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3899 ELDENDVIAQTASQSFDISVWQFLAAP-LFGARVaIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAE--ERQAL 3975
Cdd:cd05972  118 GLRPDDIHWNIADPGWAKGAWSSFFGPwLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQdlSSYKF 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3976 DGLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPAECSDDVAFFRvdlastestYLPI-----GSPTDNNRLYLLgag 4050
Cdd:cd05972  197 SHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFP---------DMPVkpgsmGRPTPGYDVAII--- 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4051 aDDAFELVPLGAVGELCVAGTGVG--RGYVGDPLRTAQAFVphpfgapgERLYRTGDLARRRADGVLEYVGRIDHQVKIR 4128
Cdd:cd05972  264 -DDDGRELPPGEEGDIAIKLPPPGlfLGYVGDPEKTEASIR--------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSS 334
                        410       420
                 ....*....|....*....|....
gi 15597620 4129 GFRIELGEIEARLHERADVREAAV 4152
Cdd:cd05972  335 GYRIGPFEVESALLEHPAVAEAAV 358
PRK06164 PRK06164
acyl-CoA synthetase; Validated
2178-2666 2.13e-30

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 129.86  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2178 TAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAIL 2257
Cdd:PRK06164    2 PHDAAPRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2258 KAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAA-----LFEALGE-----LPAGVARWCLEEDGPAL----------- 2316
Cdd:PRK06164   82 RLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAvppdaLPPLRAIAVVDDAADATpapapgarvql 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2317 -DAEDPAPLAALSGPQHQ----AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLL 2391
Cdd:PRK06164  162 fALPDPAPPAAAGERAADpdagALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2392 APLLCGARVVLRAqgQWGAEEICELIRAEGVsilgfTPSYGSQ--LAQWLESQGRQLPV----RMCITGGEALTGEHLQR 2465
Cdd:PRK06164  242 GALAGGAPLVCEP--VFDAARTARALRRHRV-----THTFGNDemLRRILDTAGERADFpsarLFGFASFAPALGELAAL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2466 IRQAFAPASffNAYGPTEtvVMPLACLAPERLEEGAASVPIGSVV--GARVAYILDADLALVPQGATGELYVGGAGLARG 2543
Cdd:PRK06164  315 ARARGVPLT--GLYGSSE--VQALVALQPATDPVSVRIEGGGRPAspEARVRARDPQDGALLPDGESGEIEIRAPSLMRG 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2544 YHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALD 2623
Cdd:PRK06164  391 YLDNPDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT 463
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 15597620  2624 SpSGKQLAgyVASAVAEQDEDAQAAlreALKTHLKQQLPDYMV 2666
Cdd:PRK06164  464 R-DGKTVP--VAFVIPTDGASPDEA---GLMAACREALAGFKV 500
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
1154-1556 2.86e-30

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 127.30  E-value: 2.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPldpdypserlaymladsgVELLLTQA 1233
Cdd:cd05974    1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 HLFERLPGAEGVTPICLDSLkldnwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAALA----ERLQWMqatyTLD 1309
Cdd:cd05974   63 DLRDRVDRGGAVYAAVDENT--------------HADDPMLLYFTSGTTSKPKLVEHTHRSYPvghlSTMYWI----GLK 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1310 GDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRR 1389
Cdd:cd05974  125 PGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLRE 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1390 LFSGGEALPAELRNRVlQRLPAVALHNRYGPTETAINVTHwqCRAEDGERSPIGRPLGNVVCRVLDAEFNllpAGVAGEL 1469
Cdd:cd05974  205 VVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN--SPGQPVKAGSMGRPLPGYRVALLDPDGA---PATEGEV 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1470 CIG-----GLGLARGYLGRPALSAErfvadpfsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARL 1544
Cdd:cd05974  279 ALDlgdtrPVGLMKGYAGDPDKTAH--------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
                        410
                 ....*....|..
gi 15597620 1545 LAQPGVAQAVVV 1556
Cdd:cd05974  351 IEHPAVAEAAVV 362
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
2185-2666 2.93e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 129.73  E-value: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2185 QDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYV 2264
Cdd:PRK05605   31 DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2265 PLDPEYPLERLQYMIEDSGVRLLL---SHAALFEAL---------------GELPAgVARWCL------------EEDGP 2314
Cdd:PRK05605  111 EHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLrrttpletivsvnmiAAMPL-LQRLALrlpipalrkaraALTGP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2315 ALDAE------DPAPLAALSGPQHQ-------AYLIYTSGSTGKPKGVAVSHGEIAMHCA---AVIECFGMRAEDC---- 2374
Cdd:PRK05605  190 APGTVpwetlvDAAIGGDGSDVSHPrptpddvALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGLGDGPERVlaal 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2375 -ELHFYSINFDAAserlLAPLlCGARVVLRAQGQwgAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCI 2452
Cdd:PRK05605  270 pMFHAYGLTLCLT----LAVS-IGGELVLLPAPD--IDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSgVRNAF 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2453 TGG-----------EALTGEHLqrirqafapasfFNAYGPTETVvmPLAC---LAPERlEEGAASVPIGSVVgARVAYIL 2518
Cdd:PRK05605  343 SGAmalpvstvelwEKLTGGLL------------VEGYGLTETS--PIIVgnpMSDDR-RPGYVGVPFPDTE-VRIVDPE 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2519 DADLALvPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaeggrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFR 2598
Cdd:PRK05605  407 DPDETM-PDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFN 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2599 IELGEIEARLLEHPQVREALVLALDSPSGKQLAgyVASAVAEQDEDAQAalrEALKTHLKQQLPDYMV 2666
Cdd:PRK05605  478 VYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV--VAAVVLEPGAALDP---EGLRAYCREHLTRYKV 540
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1-449 3.01e-30

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 128.47  E-value: 3.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDafelpttLVQALRRRAVQEPERLALRFLaeddgeGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFpsG---PDY 77
Cdd:PRK04813    1 IMD-------IIETIEEFAQTQPDFPAYDYL------GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVF--GhmsPEM 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    78 VAAFFGCLYAG--VIAVPAYPPEsarrhhqERLLSIIADAEPRLVLTTADLrePLLQMNAQ-LSAANAPQLLCVDqlDPA 154
Cdd:PRK04813   66 LATFLGAVKAGhaYIPVDVSSPA-------ERIEMIIEVAKPSLIIATEEL--PLEILGIPvITLDELKDIFATG--NPY 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   155 VAEAWdepqVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHD---MGL-----IGG 226
Cdd:PRK04813  135 DFDHA----VKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDlsvMDLyptlaSGG 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   227 LLQPIfsgvpcvlmsPRYFLERPVRWLEAISQYGGTV-SGGPDFayrlcservAESALqrLDLSgwrvaFSGSEpirQDS 305
Cdd:PRK04813  211 TLVAL----------PKDMTANFKQLFETLPQLPINVwVSTPSF---------ADMCL--LDPS-----FNEEH---LPN 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   306 LERF-----------AEKFaASRFDASSFFACYGLAEATLFVTggqrgqgipALAVDGEALAR-NRIAegegsvlmcCGR 373
Cdd:PRK04813  262 LTHFlfcgeelphktAKKL-LERFPSATIYNTYGPTEATVAVT---------SIEITDEMLDQyKRLP---------IGY 322
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620   374 SQPEHAVLIVDaASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLRDGELFVTGRL 449
Cdd:PRK04813  323 AKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGDAGYLEDGLLFYQGRI 397
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
1153-1622 3.02e-30

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 126.69  E-value: 3.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELlltq 1232
Cdd:cd05912    1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 ahlferlpgaegvtpicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHaalaeRLQWMQATYT----- 1307
Cdd:cd05912   77 -------------------------------------DDIATIMYTSGTTGKPKGVQQTF-----GNHWWSAIGSalnlg 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1308 LDGDDVLMQKAPVsFDVS-VWECFWPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGS 1386
Cdd:cd05912  115 LTEDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNN 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1387 LRRLFSGGEALPAELRNRVLQR-LPavaLHNRYGPTETAINVThwQCRAEDGERSP--IGRPLGNVVCRVLDAEFNllPA 1463
Cdd:cd05912  191 LRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIV--TLSPEDALNKIgsAGKPLFPVELKIEDDGQP--PY 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1464 GVaGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlyRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQAR 1543
Cdd:cd05912  264 EV-GEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1544 LLAQPGVAQAVVV-IREGVAGSQLVGYytgaVGAEAEAEQNQrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05912  335 LLSHPAIKEAGVVgIPDDKWGQVPVAF----VVSERPISEEE-LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1145-1617 3.93e-30

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 129.02  E-value: 3.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1145 VALEWDGGS---LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML 1221
Cdd:PRK13295   44 TAVRLGTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFML 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1222 ADSGVELLLTQAH------------LFERLPGAE------GVTPICLDSLKLDNWPSQAP-------GLHLHGDNLAYVI 1276
Cdd:PRK13295  124 KHAESKVLVVPKTfrgfdhaamarrLRPELPALRhvvvvgGDGADSFEALLITPAWEQEPdapailaRLRPGPDDVTQLI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1277 YTSGSTGQPKGVGNTH-------AALAERLQwmqatytLDGDDVLMQKAPVSFDVS-VWECFWPLVTGCRLVLAapgEHR 1348
Cdd:PRK13295  204 YTSGTTGEPKGVMHTAntlmaniVPYAERLG-------LGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIW 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1349 DPARLVELVRQFGVT-TLHFVPPLLQLF--IDEPGVAAcGSLRRLFSGGEALPAELRNRVLQRLPAVALhNRYGPTETAI 1425
Cdd:PRK13295  274 DPARAAELIRTEGVTfTMASTPFLTDLTraVKESGRPV-SSLRTFLCAGAPIPGALVERARAALGAKIV-SAWGMTENGA 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1426 NVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAErfvadpfsaAGERLYR 1505
Cdd:PRK13295  352 VTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT---------DADGWFD 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1506 TGDRARWNADGVLEYLGRlDQQVKLRGFR-IEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYYTGAVGAEAEAEQN 1583
Cdd:PRK13295  423 TGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQvAIVAYPDERLGERACAFVVPRPGQSLDFEEM 501
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 15597620  1584 QR-LRAALQAElpEYMvPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK13295  502 VEfLKAQKVAK--QYI-PERLVVRDALPRTPSGKI 533
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
2204-2684 5.98e-30

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 128.85  E-value: 5.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2204 ALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSG 2283
Cdd:cd17634   77 DDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2284 VRLLLSHAALFEA--LGELPAGV----------------------------ARWC----LEEDGPAldAEDPAPLAalsg 2329
Cdd:cd17634  157 SRLLITADGGVRAgrSVPLKKNVddalnpnvtsvehvivlkrtgsdidwqeGRDLwwrdLIAKASP--EHQPEAMN---- 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2330 PQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAEDCELHFYSINFDAASERLL-APLLCGARVVL-RAQG 2406
Cdd:cd17634  231 AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGPGDIYWCTADVGWVTGHSYLLyGPLACGATTLLyEGVP 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2407 QW-GAEEICELIRAEGVSILGFTPSYGSQLA----QWLESQGRQlPVRMCITGGEALTGE----HLQRIRQAFAPAsfFN 2477
Cdd:cd17634  311 NWpTPARMWQVVDKHGVNILYTAPTAIRALMaagdDAIEGTDRS-SLRILGSVGEPINPEayewYWKKIGKEKCPV--VD 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2478 AYGPTET---VVMPLACLAPerLEEGAASVPigsVVGARVAyILDADLALVPQGATGELYVGGA--GLARGYHERPalsa 2552
Cdd:cd17634  388 TWWQTETggfMITPLPGAIE--LKAGSATRP---VFGVQPA-VVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH---- 457
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2553 ERFVPDPFAAEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP-SGKQLA 2631
Cdd:cd17634  458 ERFEQTYFSTFKG-MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAiKGQAPY 536
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2632 GYVASAVAEQDEDaqaALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKL 2684
Cdd:cd17634  537 AYVVLNHGVEPSP---ELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
703-1095 7.74e-30

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 125.83  E-value: 7.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  703 LRLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRI--DERGEFAWQFVDLAALAEHERAAAAAQRREAEaqqpF 780
Cdd:cd19534   28 LRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRLEVVDLSSLAQAAAIEALAAEAQSS----L 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  781 DLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLaPLELHYAEFAAWQRQWLDAGE 860
Cdd:cd19534  104 DLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPL-PSKTSFQTWAELLAEYAQSPA 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  861 GARQLAYWRERLGDTAPvlELATDHPRTARQASpaaRYSLRVDEALARAI-REA--ALDheASVFMWLLAAFQALLHRHS 937
Cdd:cd19534  183 LLEELAYWRELPAADYW--GLPKDPEQTYGDAR---TVSFTLDEEETEALlQEAnaAYR--TEINDLLLAALALAFQDWT 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  938 GQGEIRIGVPSANRQRLEtQGL-----VGFF--INTLVLrgTPRARQPFAALLGEAREAtLGAQANQDLPFDQVLAACGQ 1010
Cdd:cd19534  256 GRAPPAIFLEGHGREEID-PGLdlsrtVGWFtsMYPVVL--DLEASEDLGDTLKRVKEQ-LRRIPNKGIGYGILRYLTPE 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1011 GGQLF------QVLFN----HQQ------RDLSALRRLPGLLADELPwhsREAKFDLQLQSEEdarGRLTLNFDYAADLF 1074
Cdd:cd19534  332 GTKRLafhpqpEISFNylgqFDQgerddaLFVSAVGGGGSDIGPDTP---RFALLDINAVVEG---GQLVITVSYSRNMY 405
                        410       420
                 ....*....|....*....|.
gi 15597620 1075 DEASIRRFAAQYLELLRQVAE 1095
Cdd:cd19534  406 HEETIQQLADSYKEALEALIE 426
PRK07514 PRK07514
malonyl-CoA synthase; Validated
2189-2653 8.36e-30

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 127.30  E-value: 8.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2189 HGLFAARVA--ASPQAPAL-TFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVP 2265
Cdd:PRK07514    3 NNLFDALRAafADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2266 LDPEYPLERLQYMIEDSGVRLLLSHAALFEALGEL--PAGVAR-WCLEEDG----PALDAEDPAPLAALS-GPQHQAYLI 2337
Cdd:PRK07514   83 LNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIaaAAGAPHvETLDADGtgslLEAAAAAPDDFETVPrGADDLAAIL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2338 YTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELH----------FYSINfdaaserllAPLLCGARVVLRAqgQ 2407
Cdd:PRK07514  163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHalpifhthglFVATN---------VALLAGASMIFLP--K 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2408 WGAEEICELI-RAE---GVsilgftPSYGSQLaqwLESQG--RQL--PVRMCITGG-----------EALTGeH--LQRi 2466
Cdd:PRK07514  232 FDPDAVLALMpRATvmmGV------PTFYTRL---LQEPRltREAaaHMRLFISGSapllaethrefQERTG-HaiLER- 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2467 rqafapasffnaYGPTETVVMPLACLAPERLEegaasvpiGSV------VGARVAyilDADL-ALVPQGATGELYVGGAG 2539
Cdd:PRK07514  301 ------------YGMTETNMNTSNPYDGERRA--------GTVgfplpgVSLRVT---DPETgAELPPGEIGMIEVKGPN 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2540 LARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALV 2619
Cdd:PRK07514  358 VFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAV 430
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 15597620  2620 LALDSPS-GKQ-LAGYVASAVAEQDEDA-QAALREAL 2653
Cdd:PRK07514  431 IGVPHPDfGEGvTAVVVPKPGAALDEAAiLAALKGRL 467
PLN02246 PLN02246
4-coumarate--CoA ligase
1151-1563 9.22e-30

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 127.79  E-value: 9.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1151 GGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLL 1230
Cdd:PLN02246   48 GRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLII 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1231 TQAHLFERLPG---AEGVTPICLDSLK---------LDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAAL--- 1295
Cdd:PLN02246  128 TQSCYVDKLKGlaeDDGVTVVTIDDPPegclhfselTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLvts 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1296 -AERLQWMQATYTLDGDDVLMQKAPVsFDV----SVWECfwPLVTGCRLVLAAPGEhrdPARLVELVRQFGVTTLHFVPP 1370
Cdd:PLN02246  208 vAQQVDGENPNLYFHSDDVILCVLPM-FHIyslnSVLLC--GLRVGAAILIMPKFE---IGALLELIQRHKVTIAPFVPP 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1371 LLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVThwQCRAEDGERSPI-----G 1443
Cdd:PLN02246  282 IVLAIAKSPVVEKydLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLA--MCLAFAKEPFPVksgscG 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1444 RPLGNVVCRVLDAEFNL-LPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLG 1522
Cdd:PLN02246  360 TVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW-------LHTGDIGYIDDDDELFIVD 432
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 15597620  1523 RLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAG 1563
Cdd:PLN02246  433 RLKELIKYKGFQVAPAELEALLISHPSIADAAVVpMKDEVAG 474
PRK07529 PRK07529
AMP-binding domain protein; Validated
1132-1616 1.30e-29

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 128.53  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1132 ELLERQLAQSAERVAL-------EWDGG-SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGG 1203
Cdd:PRK07529   29 ELLSRAAARHPDAPALsflldadPLDRPeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1204 AyVPLDPDYPSERLAYMLADSGVELLLTQA----------------------HLFErLPGAEGVTPICLDSLKLDNWPSQ 1261
Cdd:PRK07529  109 A-NPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpelrTVVE-VDLARYLPGPKRLAVPLIRRKAH 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1262 A------------PGLHL------HGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFD 1323
Cdd:PRK07529  187 ArildfdaelarqPGDRLfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL-FH 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1324 V--SVWECFWPLVTGCRLVLAAPGEHRDP---ARLVELVRQFGVTTLHFVPP----LLQLFIDEPGVaacGSLRRLFSGG 1394
Cdd:PRK07529  266 VnaLLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTvyaaLLQVPVDGHDI---SSLRYALCGA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1395 EALPAELRNRVLQRLpAVALHNRYGPTETAINVThwqCRAEDGERSP--IGRPLGNVVCRV--LDAEFNLL---PAGVAG 1467
Cdd:PRK07529  343 APLPVEVFRRFEAAT-GVRIVEGYGLTEATCVSS---VNPPDGERRIgsVGLRLPYQRVRVviLDDAGRYLrdcAVDEVG 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1468 ELCIGGLGLARGYLgrpalsAERFVADPFsaAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQ 1547
Cdd:PRK07529  419 VLCIAGPNVFSGYL------EAAHNKGLW--LEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRH 490
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  1548 PGVAQAVVVIR-EGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPE-YMVPTQLMRLAQMPLGPSGK 1616
Cdd:PRK07529  491 PAVALAAAVGRpDAHAGELPVAYVQLKPGASATEAE---LLAFARDHIAErAAVPKHVRILDALPKTAVGK 558
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2194-2689 1.30e-29

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 126.51  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2194 ARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2272
Cdd:PRK06839   10 KRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2273 ERLQYMIEDSGVRLLLSHAALFEALGELP--AGVARwCLEEDGPAlDAEDPAPLAALSGPQHQAYLI-YTSGSTGKPKGV 2349
Cdd:PRK06839   90 NELIFQLKDSGTTVLFVEKTFQNMALSMQkvSYVQR-VISITSLK-EIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2350 AVSHGEI---AMHCAAVIEcfgMRAEDCEL------HFYSINFDAaserlLAPLLCGARVVLraQGQWGAEEICELIRAE 2420
Cdd:PRK06839  168 VLTQENMfwnALNNTFAID---LTMHDRSIvllplfHIGGIGLFA-----FPTLFAGGVIIV--PRKFEPTKALSMIEKH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2421 GVSILGFTPSYGSQLaqwLESQGRQLP----VRMCITGGEALTGEHLQRIRQAFAPasFFNAYGPTE---TVVMplacla 2493
Cdd:PRK06839  238 KVTVVMGVPTIHQAL---INCSKFETTnlqsVRWFYNGGAPCPEELMREFIDRGFL--FGQGFGMTEtspTVFM------ 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2494 peRLEEGAASVP--IGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAErfvpdpfAAEGGRLYrTG 2571
Cdd:PRK06839  307 --LSEEDARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE-------TIQDGWLC-TG 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2572 DLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAgyVASAVAEqdedAQAALRE 2651
Cdd:PRK06839  377 DLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP--IAFIVKK----SSSVLIE 450
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 15597620  2652 A-LKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK06839  451 KdVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1130-1631 1.67e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 127.46  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPI-------CLDSLKLDN---WP-------------SQAPGLH 1266
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIehvivtrIADFLPFPKnllYPfvqkkqsnlvvkvSESETIH 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1267 LHG-----------------DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQAtyTLDGDDVLMQKAPVsFDVS 1325
Cdd:PRK06710  186 LWNsvekevntgvevpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLYN--CKEGEEVVLGVLPF-FHVY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1326 VWECFWPL--VTGCRLVLAApgeHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAEL 1401
Cdd:PRK06710  263 GMTAVMNLsiMQGYKMVLIP---KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEydISSIRACISGSAPLPVEV 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1402 RNRvLQRLPAVALHNRYGPTETAiNVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEF-NLLPAGVAGELCIGGLGLARGY 1480
Cdd:PRK06710  340 QEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGY 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1481 LGRPALSAerfvadpfSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IRE 1559
Cdd:PRK06710  418 WNKPEETA--------AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgVPD 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  1560 GVAGSQLVGYYTGAVGAE-AEAEQNQRLRAALQAelpeYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQRE 1631
Cdd:PRK06710  490 PYRGETVKAFVVLKEGTEcSEEELNQFARKYLAA----YKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNE 558
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3739-4230 2.13e-29

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 125.89  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTlVLVCTQ 3818
Cdd:cd05926   15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS-KLVLTP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3819 AC----------REQALALfdELGcVDRPRLLVWDEIQQ-----GEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVE 3883
Cdd:cd05926   94 KGelgpasraasKLGLAIL--ELA-LDVGVLIRAPSAESlsnllADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3884 QAGMLNNQLSKVPYLELDEND----------VIAQTASqsfdisvwqfLAAPLF-GARVAIvpnavahdPQGLLAH---- 3948
Cdd:cd05926  171 HRNLAASATNITNTYKLTPDDrtlvvmplfhVHGLVAS----------LLSTLAaGGSVVL--------PPRFSAStfwp 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3949 -VGEQGITVLESVPSLIQGMLAEE----RQALDGLRWMLPTGEAMPPELARQwLKRYPRIGLVNAYGPAECSDDVAffrv 4023
Cdd:cd05926  233 dVRDYNATWYTAVPTIHQILLNRPepnpESPPPKLRFIRSCSASLPPAVLEA-LEATFGAPVLEAYGMTEAAHQMT---- 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4024 dlasteSTYLP-----IGS--PTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgap 4096
Cdd:cd05926  308 ------SNPLPpgprkPGSvgKPVGVEVRIL----DEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW--- 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4097 gerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRS 4175
Cdd:cd05926  375 ----FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfGVPDEKYGEEVAAAVVLREGASV 450
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620 4176 SAdspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05926  451 TE--------------EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
2202-2689 2.21e-29

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 124.90  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2202 APALTFAGQTLSYAELDARSNRLARVLRSHGVG-PEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIE 2280
Cdd:cd05958    1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2281 DSGVrlllSHAALFEALGElpagvarwcleedgpaldAEDPAPLAalsgpqhqayliYTSGSTGKPKGVAVSHGEIAmhc 2360
Cdd:cd05958   81 KARI----TVALCAHALTA------------------SDDICILA------------FTSGTTGAPKATMHFHRDPL--- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2361 aAVIECFG---MRAEDCELH------FYSINFDAAserLLAPLLCGARVVLRAQGQwgAEEICELIRAEGVSILGFTP-S 2430
Cdd:cd05958  124 -ASADRYAvnvLRLREDDRFvgspplAFTFGLGGV---LLFPFGVGASGVLLEEAT--PDLLLSAIARYKPTVLFTAPtA 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2431 YGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVVMPLAClAPERLEEGAAsvpiGSVV 2510
Cdd:cd05958  198 YRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATG-IPIIDGIGSTEMFHIFISA-RPGDARPGAT----GKPV 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2511 GARVAYILDADLALVPQGATGELYVGGAGLARGYHERpalSAERFVpdpfaaEGGRLYrTGDLVRLCDNGQVEYVGRIDH 2590
Cdd:cd05958  272 PGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADK---RQRTYV------QGGWNI-TGDTYSRDPDGYFRHQGRSDD 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2591 QVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGyvASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHL 2670
Cdd:cd05958  342 MIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVK--AFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAI 419
                        490
                 ....*....|....*....
gi 15597620 2671 LLLASLPLTANGKLDRRAL 2689
Cdd:cd05958  420 EFVTELPRTATGKLQRFAL 438
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3280-3552 2.83e-29

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 124.29  E-value: 2.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3280 RIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMLQVIHKPGrTRIEFLDWSELPEDghEERLQALHKREREAGFDL 3359
Cdd:cd20483   31 HIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPS-FHLIVIDLSEAADP--EAALDQLVRNLRRQELDI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3360 LEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESRP-ANLPTPP-RYRDYI----AWLQRQDL 3433
Cdd:cd20483  108 EEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDlATVPPPPvQYIDFTlwhnALLQSPLV 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3434 EQSRRWWSESLRGF-ERPTLVP---SDRPFLREHAgesggmiVGDRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALT 3509
Cdd:cd20483  188 QPLLDFWKEKLEGIpDASKLLPfakAERPPVKDYE-------RSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAF 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 15597620 3510 LRRFSGERDVLFGVTVAGRPvgMPEMQRTVGLFINSIPLRVQM 3552
Cdd:cd20483  261 LYRYTEDEDLTIGMVDGDRP--HPDFDDLVGFFVNMLPIRCRM 301
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
2192-2634 3.46e-29

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 125.31  E-value: 3.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2192 FAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2271
Cdd:cd05923    9 RAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2272 LERLQYMIEDS------------GVRLLLSHAALFEALGELPA-GVArwclEEDGPALdaEDPAPlaalsGPQHQAYLIY 2338
Cdd:cd05923   89 AAELAELIERGemtaaviavdaqVMDAIFQSGVRVLALSDLVGlGEP----ESAGPLI--EDPPR-----EPEQPAFVFY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2339 TSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCE-------LHfYSINFDAAserLLAPLLCGAR-VVLRAqgqWGA 2410
Cdd:cd05923  158 TSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNvvlglmpLY-HVIGFFAV---LVAALALDGTyVVVEE---FDP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2411 EEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEALTGEHLQRIRQAFaPASFFNAYGPTETvvmpL 2489
Cdd:cd05923  231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLERVNQHL-PGEKVNIYGTTEA----M 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2490 ACLAPERLEEGAASVPiGSVVGARVAYILDADLALVPQGATGELYVGGAGLA--RGYHERPALSAERFVPdpfaaeggRL 2567
Cdd:cd05923  306 NSLYMRDARTGTEMRP-GFFSEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD--------GW 376
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 2568 YRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYV 2634
Cdd:cd05923  377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaDERWGQSVTACV 444
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1132-1622 3.90e-29

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 125.31  E-value: 3.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEWDGGS--LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:cd05923    5 EMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALIN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1210 PDYPSERLAYMLADSgvellltQAHLFERLPGAEGVTPICLDSLKLDNWpSQAPGLHL---HGDNL----------AYVI 1276
Cdd:cd05923   85 PRLKAAELAELIERG-------EMTAAVIAVDAQVMDAIFQSGVRVLAL-SDLVGLGEpesAGPLIedpprepeqpAFVF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1277 YTSGSTGQPKGVGNTHAALAERLQWM--QATYTLDGDDVLMQKAPVSFDVSVWECF-WPLVTGCRLVLAapgEHRDPARL 1353
Cdd:cd05923  157 YTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVV---EEFDPADA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1354 VELVRQFGVTTLHFVPPLLQLFI--DEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALhNRYGPTEtAINVTHwq 1431
Cdd:cd05923  234 LKLIEQERVTSLFATPTHLDALAaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKV-NIYGTTE-AMNSLY-- 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1432 crAEDGERSPIGRPLGNV---VCRVLDAEFNLLPAGVAGELCIGGLGLA--RGYLGRPALSAERFVadpfsaagERLYRT 1506
Cdd:cd05923  310 --MRDARTGTEMRPGFFSevrIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ--------DGWYRT 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1507 GDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQ 1582
Cdd:cd05923  380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI---GVAderwGQSVTACVVPREGTLSADEL 456
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15597620 1583 NQRLRAalqAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05923  457 DQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK07788 PRK07788
acyl-CoA synthetase; Validated
2192-2693 4.50e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 125.81  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2192 FAARVAasPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2271
Cdd:PRK07788   57 HAARRA--PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2272 LERLQYMIEDSGVRLLLSHAALFEALGELPAGVARW-----CLEEDGPA----------LDAEDPAPLAALsgPQHQAYL 2336
Cdd:PRK07788  135 GPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLrawggNPDDDEPSgstdetlddlIAGSSTAPLPKP--PKPGGIV 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2337 IYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELH----FYSINFDAASerlLAPLLcGARVVLRAQgqWGAEE 2412
Cdd:PRK07788  213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLpapmFHATGWAHLT---LAMAL-GSTVVLRRR--FDPEA 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2413 ICELIRAEGVSILGFTPSYGSQLAQwLESQGRQLP----VRMCITGGEALTGEHLQRIRQAFAPaSFFNAYGPTETVVMP 2488
Cdd:PRK07788  287 TLEDIAKHKATALVVVPVMLSRILD-LGPEVLAKYdtssLKIIFVSGSALSPELATRALEAFGP-VLYNLYGSTEVAFAT 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2489 LAclAPERLEEGAASV-PIgsVVGARVAyILDADLALVPQGATGELYVGGAGLARGYherpalsaerfvpdpfaaEGGR- 2566
Cdd:PRK07788  365 IA--TPEDLAEAPGTVgRP--PKGVTVK-ILDENGNEVPRGVVGRIFVGNGFPFEGY------------------TDGRd 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2567 ------LYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLAGYVasaVA 2639
Cdd:PRK07788  422 kqiidgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEfGQRLRAFV---VK 498
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620  2640 EQDEDAQAalrEALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPD 2693
Cdd:PRK07788  499 APGAALDE---DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
1140-1556 5.86e-29

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 123.83  E-value: 5.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1140 QSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAY 1219
Cdd:PRK09029   15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1220 MLADSGVELLLTQAHLFerlpgaegvTPICLDSLKLdNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA-LAER 1298
Cdd:PRK09029   95 LLPSLTLDFALVLEGEN---------TFSALTSLHL-QLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhLASA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1299 ---LQWMQATytlDGDDVLmqkapVS---FDVS----VWEcfWpLVTGCRLVLaapgehRDPARLVELVRqfGVTTLHFV 1368
Cdd:PRK09029  165 egvLSLMPFT---AQDSWL-----LSlplFHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQALA--GCTHASLV 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1369 PPLLQLFIDEPGVAAcgSLRRLFSGGEALPAELRNRVLQRlpAVALHNRYGPTETAINVTHWQCRAEDGerspIGRPLGN 1448
Cdd:PRK09029  226 PTQLWRLLDNRSEPL--SLKAVLLGGAAIPVELTEQAEQQ--GIRCWCGYGLTEMASTVCAKRADGLAG----VGSPLPG 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1449 vvcRvldaEFNLlpagVAGELCIGGLGLARGYL--GR--PALSAERFVAdpfsaagerlyrTGDRARWNaDGVLEYLGRL 1524
Cdd:PRK09029  298 ---R----EVKL----VDGEIWLRGASLALGYWrqGQlvPLVNDEGWFA------------TRDRGEWQ-NGELTILGRL 353
                         410       420       430
                  ....*....|....*....|....*....|..
gi 15597620  1525 DQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:PRK09029  354 DNLFFSGGEGIQPEEIERVINQHPLVQQVFVV 385
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3736-4230 1.05e-28

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 122.97  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVGI-DQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPghptqrLTRIVELSRTLvl 3814
Cdd:cd05958    8 EREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP------LLRPKELAYIL-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3815 vctQACREqALALFDElgcvdrpRLLVWDEIqqgegaehdpqvysgpqnlAYVIYTSGSTGLPKGVMVEQAGMLNN-QLS 3893
Cdd:cd05958   80 ---DKARI-TVALCAH-------ALTASDDI-------------------CILAFTSGTTGAPKATMHFHRDPLASaDRY 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3894 KVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNAVahdPQGLLAHVGEQGITVLESVPSLIQGMLAEER 3972
Cdd:cd05958  130 AVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGvGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAMLAHPD 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3973 QA---LDGLRWMLPTGEAMPPELARQWlKRYPRIGLVNAYGPAEcsddvaFFRVDLASTESTYLP--IGSPTDNNRLYLL 4047
Cdd:cd05958  207 AAgpdLSSLRKCVSAGEALPAALHRAW-KEATGIPIIDGIGSTE------MFHIFISARPGDARPgaTGKPVPGYEAKVV 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4048 gagaDDAFELVPLGAVGELCVAGTgvgRGYVGDPLRTAQAFVPhpfgapGERLYrTGDLARRRADGVLEYVGRIDHQVKI 4127
Cdd:cd05958  280 ----DDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQ------GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVS 345
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4128 RGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLV--PGETPrssadSPAglMVEQgawferIKQQLRADLPD 4204
Cdd:cd05958  346 GGYNIAPPEVEDVLLQHPAVAECAVvGHPDESRGVVVKAFVVlrPGVIP-----GPV--LARE------LQDHAKAHIAP 412
                        490       500
                 ....*....|....*....|....*.
gi 15597620 4205 YMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05958  413 YKYPRAIEFVTELPRTATGKLQRFAL 438
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
2187-2689 1.30e-28

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 124.49  E-value: 1.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2187 TLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL 2266
Cdd:PRK06155   22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2267 DPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGV----ARWCLEEDG-------------PALDAedPAPLAALSg 2329
Cdd:PRK06155  102 NTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpAVWLLDAPAsvsvpagwstaplPPLDA--PAPAAAVQ- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2330 PQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL----RAQ 2405
Cdd:PRK06155  179 PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLeprfSAS 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2406 GQWGAeeicelIRAEG----------VSILgftpsygsqLAQWLESQGRQLPVRMCITGGEAltGEHLQRIRQAFAPAsF 2475
Cdd:PRK06155  259 GFWPA------VRRHGatvtyllgamVSIL---------LSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVD-L 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2476 FNAYGPTETVVmPLACLAPERlEEGAAsvpiGSVVGARVAYILDADLALVPQGATGELYVGGA---GLARGYHERPALSA 2552
Cdd:PRK06155  321 LDGYGSTETNF-VIAVTHGSQ-RPGSM----GRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTV 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2553 ErfvpdpfaAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSpsgkQLAG 2632
Cdd:PRK06155  395 E--------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPS----ELGE 462
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2633 -YVASAVAEqdEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK06155  463 dEVMAAVVL--RDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK06145 PRK06145
acyl-CoA synthetase; Validated
2192-2689 1.37e-28

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 123.46  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2192 FAARvaASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2271
Cdd:PRK06145   10 FHAR--RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2272 LERLQYMIEDSGVRLLLsHAALFEALGEL--PAGVARWCLEEDGPALDA-EDPAPLAALSGPQHQAYLIYTSGSTGKPKG 2348
Cdd:PRK06145   88 ADEVAYILGDAGAKLLL-VDEEFDAIVALetPKIVIDAAAQADSRRLAQgGLEIPPQAAVAPTDLVRLMYTSGTTDRPKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2349 VAVSHGEIAMHCAAVIECFGMRAEDCEL---HFYSIN-FDAASerlLAPLLCGArvVLRAQGQWGAEEICELIRAEGVSI 2424
Cdd:PRK06145  167 VMHSYGNLHWKSIDHVIALGLTASERLLvvgPLYHVGaFDLPG---IAVLWVGG--TLRIHREFDPEAVLAAIERHRLTC 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2425 LGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEAlTGEhlQRIR---QAFAPASFFNAYGPTETvvmplaCLAPERLEEG 2500
Cdd:PRK06145  242 AWMAPVMLSRVLTVPDRDRFDLdSLAWCIGGGEK-TPE--SRIRdftRVFTRARYIDAYGLTET------CSGDTLMEAG 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2501 AASVPIGSvVGARVAY----ILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlyRTGDLVRL 2576
Cdd:PRK06145  313 REIEKIGS-TGRALAHveirIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2577 CDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLagyvaSAVAEQDEDAQAALrEALKT 2655
Cdd:PRK06145  384 DEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERI-----TAVVVLNPGATLTL-EALDR 457
                         490       500       510
                  ....*....|....*....|....*....|....
gi 15597620  2656 HLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK06145  458 HCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
15-556 1.45e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 124.12  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    15 LRRRAVQEPERLALRFLaeddgeGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:PRK07786   23 LARHALMQPDAPALRFL------GNTTTWRELDDRVAALAGALSRRgVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    94 A----YPPESArrhhqerllSIIADAEPRLVLTTADLR---------EPLLQMNAQLSAANAPQLLCVDQL----DPAVA 156
Cdd:PRK07786   97 VnfrlTPPEIA---------FLVSDCGAHVVVTEAALApvatavrdiVPLLSTVVVAGGSSDDSVLGYEDLlaeaGPAHA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   157 EAwDEPQVRPehiAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIG-ADDVIVSWLPLYHDMGLiGGLLQPIFSGV 235
Cdd:PRK07786  168 PV-DIPNDSP---ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADiNSDVGFVGVPLFHIAGI-GSMLPGLLLGA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   236 PCVLMSPRYFleRPVRWLEAISQYGGT-VSGGPDFAYRLCSERVAESALQRLDLSGWrvafsGSEPIRQDSLERFAEKFa 314
Cdd:PRK07786  243 PTVIYPLGAF--DPGQLLDVLEAEKVTgIFLVPAQWQAVCAEQQARPRDLALRVLSW-----GAAPASDTLLRQMAATF- 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   315 asrfdassffacyglAEATLFVTGGQRGQGIPALAVDGEALARNRiaegeGSVlmccGRSQPEHAVLIVDAASGEVlGDD 394
Cdd:PRK07786  315 ---------------PEAQILAAFGQTEMSPVTCMLLGEDAIRKL-----GSV----GKVIPTVAARVVDENMNDV-PVG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   395 NVGEIWAAGPSIAHGYWRNPEASAKAFverDGrTWLRTGDLgfLR---DGELFVTGRLKDMLIVRGHNLYPQDIERTVES 471
Cdd:PRK07786  370 EVGEIVYRAPTLMSGYWNNPEATAEAF---AG-GWFHSGDL--VRqdeEGYVWVVDRKKDMIISGGENIYCAEVENVLAS 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   472 EvPSARKGRVAAFAVTVDGEEGIGIAAEigRGVQKSVPAQELIDSIRQAVAEaYQEaPKVVALLNpgALPKTSSGKLQRS 551
Cdd:PRK07786  444 H-PDIVEVAVIGRADEKWGEVPVAVAAV--RNDDAALTLEDLAEFLTDRLAR-YKH-PKALEIVD--ALPRNPAGKVLKT 516

                  ....*
gi 15597620   552 ACRLR 556
Cdd:PRK07786  517 ELRER 521
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
145-548 1.46e-28

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 126.96  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   145 LLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLI 224
Cdd:PRK08633  760 LLAARLLPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLT 839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   225 GGLLQPIFSGVPCVLM-SPryflerpvrwLEA------ISQYGGTV-SGGPDF--AYrLCSERVAesalqRLDLSGWRVA 294
Cdd:PRK08633  840 VTLWLPLLEGIKVVYHpDP----------TDAlgiaklVAKHRATIlLGTPTFlrLY-LRNKKLH-----PLMFASLRLV 903
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   295 FSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVTggqrgQGIP-ALAVDGEALARNRiaegEGSVlmccGR 373
Cdd:PRK08633  904 VAGAEKLKPEVADAFEEKFGIRILEG------YGATETSPVAS-----VNLPdVLAADFKRQTGSK----EGSV----GM 964
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   374 SQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFL-RDGELFVTGRLKDM 452
Cdd:PRK08633  965 PLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLdEDGFLTITDRYSRF 1044
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   453 LIVRG----HnlypqdieRTVESEVPSARKGRVAAFAVT-VDGEEgigiaaeigRGVQKSV---PAQELIDSIRQAVAEA 524
Cdd:PRK08633 1045 AKIGGemvpL--------GAVEEELAKALGGEEVVFAVTaVPDEK---------KGEKLVVlhtCGAEDVEELKRAIKES 1107
                         410       420       430
                  ....*....|....*....|....*....|
gi 15597620   525 yqEAPKvvaLLNPG------ALPKTSSGKL 548
Cdd:PRK08633 1108 --GLPN---LWKPSryfkveALPLLGSGKL 1132
PRK08315 PRK08315
AMP-binding domain protein; Validated
10-466 1.87e-28

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 124.15  E-value: 1.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFLAEddgeGVVLSYRDLD---------LRARSIAAalqahaqlGDRAVLLFPSGPDYVAA 80
Cdd:PRK08315   17 TIGQLLDRTAARYPDREALVYRDQ----GLRWTYREFNeevdalakgLLALGIEK--------GDRVGIWAPNVPEWVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGVIAV---PAYppesaRRHHQERLLS-------IIADA--EPRLVLTTADLREPLLQMNA-QLSAANAPQLLC 147
Cdd:PRK08315   85 QFATAKIGAILVtinPAY-----RLSELEYALNqsgckalIAADGfkDSDYVAMLYELAPELATCEPgQLQSARLPELRR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   148 V---DQLDPAVAEAWDE-----PQVRPEHIAFL------------QYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGA 207
Cdd:PRK08315  160 ViflGDEKHPGMLNFDEllalgRAVDDAELAARqatldpddpiniQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   208 DDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYfleRPVRWLEAISQYGGTVSGG-----------PDFAyrlcse 276
Cdd:PRK08315  240 EDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEGF---DPLATLAAVEEERCTALYGvptmfiaeldhPDFA------ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   277 rvaesalqRLDLSGWRVA-FSGSE-PIRqdslerfAEKFAASRFDASSFFACYGLAEAT--LFVTggqrgqgipalAVDg 352
Cdd:PRK08315  311 --------RFDLSSLRTGiMAGSPcPIE-------VMKRVIDKMHMSEVTIAYGMTETSpvSTQT-----------RTD- 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   353 EALARnRIAegegSVlmccGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAfVERDGrtWLRT 432
Cdd:PRK08315  364 DPLEK-RVT----TV----GRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADG--WMHT 431
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 15597620   433 GDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIE 466
Cdd:PRK08315  432 GDLAVMDeEGYVNIVGRIKDMIIRGGENIYPREIE 466
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
3861-4233 1.89e-28

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 122.83  E-value: 1.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3861 PQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTA----SQSFDISVWQFLaapLFGARVAIVPN 3936
Cdd:cd05909  146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALpffhSFGLTGCLWLPL---LSGIKVVFHPN 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3937 AVahDPQGLLAHVGEQGITVLESVPSLIQGML-AEERQALDGLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPAECS 4015
Cdd:cd05909  223 PL--DYKKIPELIYDKKATILLGTPTFLRGYArAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECS 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4016 DDVAFFRVDLASTESTylpIGSPTDNNRLYLLgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfga 4095
Cdd:cd05909  300 PVISVNTPQSPNKEGT---VGRPLPGMEVKIV---SVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF------- 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4096 pGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHE--RADVREAAVAVQEGANGKYLVGYLVPGETP 4173
Cdd:cd05909  367 -GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEilPEDNEVAVVSVPDGRKGEKIVLLTTTTDTD 445
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 4174 RSSadspaglmveqgawferIKQQLR-ADLPDYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:cd05909  446 PSS-----------------LNDILKnAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1129-1617 2.93e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 122.38  E-value: 2.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1129 WLpelleRQLAQ-SAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVP 1207
Cdd:PRK03640    7 WL-----KQRAFlTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1208 LDPDYPSERLAYMLADSGVELLLTQAHLFERLpgaEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKG 1287
Cdd:PRK03640   82 LNTRLSREELLWQLDDAEVKCLITDDDFEAKL---IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1288 VGNTHAAlaerlQWMQATYT-----LDGDDVLMQKAPVsFDVSVWEC-FWPLVTGCRLVLAapgEHRDPARLVELVRQFG 1361
Cdd:PRK03640  159 VIQTYGN-----HWWSAVGSalnlgLTEDDCWLAAVPI-FHISGLSIlMRSVIYGMRVVLV---EKFDAEKINKLLQTGG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1362 VTTLHFVPPLLQLFIDEPGVAAC-GSLR-RLFSGGEALPAELRNRVLQRLPAValhNRYGPTETAInvthwQCRAEDGER 1439
Cdd:PRK03640  230 VTIISVVSTMLQRLLERLGEGTYpSSFRcMLLGGGPAPKPLLEQCKEKGIPVY---QSYGMTETAS-----QIVTLSPED 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1440 S-----PIGRPLGNVVCRVLDaEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlyRTGDRARWNA 1514
Cdd:PRK03640  302 AltklgSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDE 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1515 DGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYytgaVGAEAEAEQNQrLRAAL 1590
Cdd:PRK03640  373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVV---GVPddkwGQVPVAF----VVKSGEVTEEE-LRHFC 444
                         490       500
                  ....*....|....*....|....*..
gi 15597620  1591 QAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK03640  445 EEKLAKYKVPKRFYFVEELPRNASGKL 471
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1277-1616 4.31e-28

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 118.92  E-value: 4.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1277 YTSGSTGQPKGVGNTH-------AALAERLQWMQatytldgDDVLMqkAPVSFdvsvWECFW-------PLVTGCRLVLA 1342
Cdd:cd05917    9 FTSGTTGSPKGATLTHhnivnngYFIGERLGLTE-------QDRLC--IPVPL----FHCFGsvlgvlaCLTHGATMVFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1343 APGehRDPARLVELVRQFGVTTLHFVPpllQLFIDE-----PGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNR 1417
Cdd:cd05917   76 SPS--FDPLAVLEAIEKEKCTALHGVP---TMFIAElehpdFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1418 YGPTETAINVThwQCRAEDGERSPI---GRPLGNVVCRVLDAEFN-LLPAGVAGELCIGGLGLARGYLGRPALSAErfva 1493
Cdd:cd05917  151 YGMTETSPVST--QTRTDDSIEKRVntvGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAE---- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1494 dpfSAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGY 1569
Cdd:cd05917  225 ---AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVV---GVPderyGEEVCAW 298
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 1570 YTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGK 1616
Cdd:cd05917  299 IRLKEGAELTEED---IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
1270-1622 4.80e-28

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 121.67  E-value: 4.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1270 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPV--SFDVSVweCFW-PLVTGCRLVLAA-Pg 1345
Cdd:cd05909  147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTG--CLWlPLLSGIKVVFHPnP- 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1346 ehRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTET-- 1423
Cdd:cd05909  224 --LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECsp 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1424 --AINVTHWQCRAEDgerspIGRPLGNVVCRVLDAE-FNLLPAGVAGELCIGGLGLARGYLGRPALSAErfvadpfsAAG 1500
Cdd:cd05909  301 viSVNTPQSPNKEGT-----VGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF--------AFG 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1501 ERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIE---PEEIQARLLAQPGVAqAVVVIREGVAGSQLVGYYTGAVGAE 1577
Cdd:cd05909  368 DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSleaIEDILSEILPEDNEV-AVVSVPDGRKGEKIVLLTTTTDTDP 446
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620 1578 AEaeqnqrLRAALQ-AELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05909  447 SS------LNDILKnAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
15-550 5.40e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 121.61  E-value: 5.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    15 LRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:PRK03640    8 LKQRAFLTPDRTAIEF------EEKKVTFMELHEAVVSVAGKlAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    94 AyppeSARRHHQERLLSIiADAEPRLVLTtADLREPLLQMNAQLSAANAPQLLCVDqldPAVAEAWDEPQVrpehiAFLQ 173
Cdd:PRK03640   82 L----NTRLSREELLWQL-DDAEVKCLIT-DDDFEAKLIPGISVKFAELMNGPKEE---AEIQEEFDLDEV-----ATIM 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   174 YTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDvivSWL---PLYHdmglIGGL---LQPIFSGVPCVLMsPRYFLE 247
Cdd:PRK03640  148 YTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDD---CWLaavPIFH----ISGLsilMRSVIYGMRVVLV-EKFDAE 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   248 RPVRWLeaISQYGGTVSggpdfayrlcserVAESALQRL--DL------SGWRVAFSGSEPIRQDSLERFAEKfaasrfd 319
Cdd:PRK03640  220 KINKLL--QTGGVTIIS-------------VVSTMLQRLleRLgegtypSSFRCMLLGGGPAPKPLLEQCKEK------- 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   320 ASSFFACYGLAEatlfvTGGQrgqgIPALAVDgeaLARNRIaegeGSVlmccgrSQPEHAVLIVDAASGEVLGDDNVGEI 399
Cdd:PRK03640  278 GIPVYQSYGMTE-----TASQ----IVTLSPE---DALTKL----GSA------GKPLFPCELKIEKDGVVVPPFEEGEI 335
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   400 WAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIErtvesEVPSARK 478
Cdd:PRK03640  336 VVKGPNVTKGYLNREDATRETF--QDG--WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIE-----EVLLSHP 406
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620   479 GrVAAFAVT--VDGEEGIGIAAEIGRGVqkSVPAQELIDSIRQAVAEaYQeAPKVVALLNpgALPKTSSGKLQR 550
Cdd:PRK03640  407 G-VAEAGVVgvPDDKWGQVPVAFVVKSG--EVTEEELRHFCEEKLAK-YK-VPKRFYFVE--ELPRNASGKLLR 473
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
1270-1624 5.69e-28

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 125.04  E-value: 5.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1270 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPV--SFDVSVwECFWPLVTGCRLVLaapgeH 1347
Cdd:PRK08633  782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPLLEGIKVVY-----H 855
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1348 RDP---ARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC--GSLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTE 1422
Cdd:PRK08633  856 PDPtdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLmfASLRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGATE 934
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1423 TA--INVTHWQCRAEDGERSP------IGRPLGNVVCRVLDAE-FNLLPAGVAGELCIGGLGLARGYLGRPALSAErFVA 1493
Cdd:PRK08633  935 TSpvASVNLPDVLAADFKRQTgskegsVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIK 1013
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1494 DpfsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRG-----FRIEpEEIQARLLAQPGVAqAVVVIREGVAGSQLVG 1568
Cdd:PRK08633 1014 D---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGemvplGAVE-EELAKALGGEEVVF-AVTAVPDEKKGEKLVV 1088
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  1569 YYTGAVGAEAEAEqnqrlRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK08633 1089 LHTCGAEDVEELK-----RAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
38-554 6.51e-28

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 122.29  E-value: 6.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    38 GVVLSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR-HHQ--------- 105
Cdd:PRK08751   48 GKTITYREADQLVEQFAAylLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRElKHQlidsgasvl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   106 -------ERLLSIIADAEPRLVLTT--ADLRE------------------PLLQMNAQLSAANAPQLLCVDQLDPAvaea 158
Cdd:PRK08751  128 vvidnfgTTVQQVIADTPVKQVITTglGDMLGfpkaalvnfvvkyvkklvPEYRINGAIRFREALALGRKHSMPTL---- 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   159 wdepQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVAN-----EVLIRRGFGIGADDVIVSWLPLYHDMGLIG-GLLQPIF 232
Cdd:PRK08751  204 ----QIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqahQWLAGTGKLEEGCEVVITALPLYHIFALTAnGLVFMKI 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   233 SGVPCVLMSPRyflERPvRWLEAISQYGGTVSGGPDfayRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEK 312
Cdd:PRK08751  280 GGCNHLISNPR---DMP-GFVKELKKTRFTAFTGVN---TLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQV 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   313 FAASRFDAssffacYGLAEATlfvtggqrgqgiPALAVDGEALArnriaEGEGSVlmccGRSQPEHAVLIVDAAsGEVLG 392
Cdd:PRK08751  353 TGLTLVEA------YGLTETS------------PAACINPLTLK-----EYNGSI----GLPIPSTDACIKDDA-GTVLA 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   393 DDNVGEIWAAGPSIAHGYWRNPEASAKAFverDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIErtves 471
Cdd:PRK08751  405 IGEIGELCIKGPQVMKGYWKRPEETAKVM---DADGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIE----- 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   472 EVPSARKGRVAAFAVTVDGEEgigiAAEIGRGV-QKSVPA--QELIDSIRQAVAEAYQEaPKVVALLNpgALPKTSSGKL 548
Cdd:PRK08751  477 DVIAMMPGVLEVAAVGVPDEK----SGEIVKVViVKKDPAltAEDVKAHARANLTGYKQ-PRIIEFRK--ELPKTNVGKI 549

                  ....*.
gi 15597620   549 QRSACR 554
Cdd:PRK08751  550 LRRELR 555
PRK09088 PRK09088
acyl-CoA synthetase; Validated
2192-2694 7.60e-28

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 121.07  E-value: 7.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2192 FAARvaASPQAPALT--FAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2269
Cdd:PRK09088    3 FHAR--LQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2270 YPLERLQYMIEDSGVRLLLSHAALfEALGELPAGVARWCLEedgpaLDAEDPAPLAALSgPQHQAYLIYTSGSTGKPKGV 2349
Cdd:PRK09088   81 LSASELDALLQDAEPRLLLGDDAV-AAGRTDVEDLAAFIAS-----ADALEPADTPSIP-PERVSLILFTSGTSGQPKGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2350 AVSHgeiamhcaaviecfgmRAEDCELHFYSI--NFDAASERLL-AP------LLCGARVVLRAQGQW----GAEEICEL 2416
Cdd:PRK09088  154 MLSE----------------RNLQQTAHNFGVlgRVDAHSSFLCdAPmfhiigLITSVRPVLAVGGSIlvsnGFEPKRTL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2417 IRAEGVSiLGFTPSYG-SQLAQWLESQGRQLPVRM-----CITGGEALTGEHLQRIRQAFAPasFFNAYGPTE--TVV-M 2487
Cdd:PRK09088  218 GRLGDPA-LGITHYFCvPQMAQAFRAQPGFDAAALrhltaLFTGGAPHAAEDILGWLDDGIP--MVDGFGMSEagTVFgM 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2488 PLAClAPERLEEGAASVPIGSVvGARVayiLDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrl 2567
Cdd:PRK09088  295 SVDC-DVIRAKAGAAGIPTPTV-QTRV---VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------- 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2568 YRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLaGYVASAVAeqdeDAQA 2647
Cdd:PRK09088  363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEV-GYLAIVPA----DGAP 437
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15597620  2648 ALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLD----RRALPAPDP 2694
Cdd:PRK09088  438 LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQkarlRDALAAGRK 488
PRK09274 PRK09274
peptide synthase; Provisional
1-492 8.73e-28

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 121.93  E-value: 8.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAFELPTTLVQALRRRavqePERLALRFLAEDDGEGVV----LSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGP 75
Cdd:PRK09274    2 MASMANIARHLPRAAQER----PDQLAVAVPGGRGADGKLaydeLSFAELDARSDAIAHGLNAAgIGRGMRAVLMVTPSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    76 DYVAAFFGCLYAGVIAVPAYPPESARRhhqerLLSIIADAEPRLVLTTadlrePLLQMNAQL---SAANAPQLLCVDQ-- 150
Cdd:PRK09274   78 EFFALTFALFKAGAVPVLVDPGMGIKN-----LKQCLAEAQPDAFIGI-----PKAHLARRLfgwGKPSVRRLVTVGGrl 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   151 ----------LDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLyhd 220
Cdd:PRK09274  148 lwggttlatlLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   221 MGLIGGLLqpifsGVPCVL--MSPRyfleRPV-----RWLEAISQYG-GTVSGGPdfAYrlcSERVAESALQR-LDLSGW 291
Cdd:PRK09274  225 FALFGPAL-----GMTSVIpdMDPT----RPAtvdpaKLFAAIERYGvTNLFGSP--AL---LERLGRYGEANgIKLPSL 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   292 RVAFSGSEPIRQDSLERFAEKFAasrfDASSFFACYGLAEAtlfvtggqrgqgIPALAVDGEAL---ARNRIAEGEGsvl 368
Cdd:PRK09274  291 RRVISAGAPVPIAVIERFRAMLP----PDAEILTPYGATEA------------LPISSIESREIlfaTRAATDNGAG--- 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   369 MCCGRSQPEHAVLIVD------AASGEV--LGDDNVGEIWAAGPSIAHGYWRNPEASAKAFV-ERDGRTWLRTGDLGFLR 439
Cdd:PRK09274  352 ICVGRPVDGVEVRIIAisdapiPEWDDAlrLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIpDGQGDVWHRMGDLGYLD 431
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620   440 D-GELFVTGRLKDMLIVRGHNLYPQDIERtVESEVPSARkgRVAAFAVTVDGEE 492
Cdd:PRK09274  432 AqGRLWFCGRKAHRVETAGGTLYTIPCER-IFNTHPGVK--RSALVGVGVPGAQ 482
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1136-1617 1.07e-27

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 121.39  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1136 RQLAQSAERVALEWD-GGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPS 1214
Cdd:PRK06087   31 QTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1215 ERLAYMLADSGVELLLT-----------QAH-LFERLPGAEGVtpICLDSLK-----------LDNWPSQAPGLHLHGDN 1271
Cdd:PRK06087  111 AELVWVLNKCQAKMFFAptlfkqtrpvdLILpLQNQLPQLQQI--VGVDKLApatsslslsqiIADYEPLTTAITTHGDE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1272 LAYVIYTSGSTGQPKGVGNTHAAL--AERlqWMQATYTLDGDDVLMQKAPVSFDVSVWE-CFWPLVTGCRLVLAapgEHR 1348
Cdd:PRK06087  189 LAAVLFTSGTEGLPKGVMLTHNNIlaSER--AYCARLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGARSVLL---DIF 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1349 DPARLVELVRQFGVTTLH----FVPPLLQLFIDEPgvAACGSLRRLFSGGEALPAELRNRVLQRlpAVALHNRYGPTETA 1424
Cdd:PRK06087  264 TPDACLALLEQQRCTCMLgatpFIYDLLNLLEKQP--ADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESS 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1425 --INVTHWQCRAEDGERSpiGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaager 1502
Cdd:PRK06087  340 phAVVNLDDPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW------ 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1503 lYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLvGYYTGAVGAEAEAEQ 1582
Cdd:PRK06087  412 -YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV---AMPDERL-GERSCAYVVLKAPHH 486
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 15597620  1583 NQRLRAAL----QAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK06087  487 SLTLEEVVaffsRKRVAKYKYPEHIVVIDKLPRTASGKI 525
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1-556 1.10e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 121.25  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAFELPTT----LVQALRRRavqePERLALRFlaeddgEGVVLSYRDL-DLRARSIAAALQAHAQLGDRAVLLFPSGP 75
Cdd:PRK06188    4 MADLLHSGATyghlLVSALKRY----PDRPALVL------GDTRLTYGQLaDRISRYIQAFEALGLGTGDAVALLSLNRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    76 DYVAAFFGCLYAGVIAVPAYPPESARRHhqerlLSIIADAEPR-LVLTTADLREPLLQMNAQlsAANAPQLLCVDQLDPA 154
Cdd:PRK06188   74 EVLMAIGAAQLAGLRRTALHPLGSLDDH-----AYVLEDAGIStLIVDPAPFVERALALLAR--VPSLKHVLTLGPVPDG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   155 V-----AEAWDEPQVRPEH----IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdmglIG 225
Cdd:PRK06188  147 VdllaaAAKFGPAPLVAAAlppdIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH----AG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   226 GLLQpifsgVPCVLMSPRYFLER---PVRWLEAISQYGGTVSG-GPDFAYRLcserVAESALQRLDLSGWRVAFSGSEPI 301
Cdd:PRK06188  223 GAFF-----LPTLLRGGTVIVLAkfdPAEVLRAIEEQRITATFlVPTMIYAL----LDHPDLRTRDLSSLETVYYGASPM 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   302 rqdSLERFAEkfAASRFdASSFFACYGLAEATLFVTggqrgqgipalavdgeALARNRIAEGEGSVLMCCGRSQPEHAVL 381
Cdd:PRK06188  294 ---SPVRLAE--AIERF-GPIFAQYYGQTEAPMVIT----------------YLRKRDHDPDDPKRLTSCGRPTPGLRVA 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   382 IVDAASGEVlGDDNVGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNL 460
Cdd:PRK06188  352 LLDEDGREV-AQGEVGEICVRGPLVMDGYWNRPEETAEAF--RDG--WLHTGDVAREdEDGFYYIVDRKKDMIVTGGFNV 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   461 YPQDIERTVeSEVPSarkgrVAAFAVtvdgeegIGIAAEI-GRGVQ--------KSVPAQELIDSIRQAVAEAYqeAPKV 531
Cdd:PRK06188  427 FPREVEDVL-AEHPA-----VAQVAV-------IGVPDEKwGEAVTavvvlrpgAAVDAAELQAHVKERKGSVH--APKQ 491
                         570       580
                  ....*....|....*....|....*
gi 15597620   532 VALLNpgALPKTSSGKLQRSACRLR 556
Cdd:PRK06188  492 VDFVD--SLPLTALGKPDKKALRAR 514
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1730-2055 1.33e-27

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 119.34  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVD-GVPVQRVHGDggLHMDWQ 1808
Cdd:cd19547    3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDD--LAPPWA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1809 --DFSALDRDSRQQHLQTLADSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLD 1886
Cdd:cd19547   81 llDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1887 DRESPLEPLPvQYLDYSVWQREWLESGERQRQldYWKAQLGN--EHPLLELPGDRprppvqSHQGDLYRFDLSPELAERV 1964
Cdd:cd19547  161 GREPQLSPCR-PYRDYVRWIRARTAQSEESER--FWREYLRDltPSPFSTAPADR------EGEFDTVVHEFPEQLTRLV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1965 RRFNAARGLTMFMTMTATLAALLYRYSGQQDLRIGAPVANRiRPESEG---LIGAFLNTQVLRCRLDGQMSVGELLEQVR 2041
Cdd:cd19547  232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR-PPELEGsehMVGIFINTIPLRIRLDPDQTVTGLLETIH 310
                        330
                 ....*....|....
gi 15597620 2042 QTVIDGQSHQDLPF 2055
Cdd:cd19547  311 RDLATTAAHGHVPL 324
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2212-2664 1.42e-27

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 119.21  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVP----LDPEYPLERLQymiedsgvrll 2287
Cdd:cd05974    1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVD----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2288 lshaalfealgelpAGVARWCLEEDGPAldAEDPAplaalsgpqhqaYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECF 2367
Cdd:cd05974   70 --------------RGGAVYAAVDENTH--ADDPM------------LLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWI 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2368 GMRAEDCELHFYSINF-DAASERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQwLESQGRQL 2446
Cdd:cd05974  122 GLKPGDVHWNISSPGWaKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFDV 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2447 PVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETVVmpLACLAP-ERLEEGAASVPIGsvvGARVAyILDADLALV 2525
Cdd:cd05974  201 KLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETTA--LVGNSPgQPVKAGSMGRPLP---GYRVA-LLDPDGAPA 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2526 PQGATGeLYVGG---AGLARGYHERPALSAErfvpdpfaAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELG 2602
Cdd:cd05974  274 TEGEVA-LDLGDtrpVGLMKGYAGDPDKTAH--------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPF 344
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620 2603 EIEARLLEHPQVREALVLAldSPSGKQLAGYVASAVAEQDEDAQAALREALKTHLKQQLPDY 2664
Cdd:cd05974  345 ELESVLIEHPAVAEAAVVP--SPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPY 404
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
1153-1629 1.42e-27

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 120.57  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ 1232
Cdd:PRK12406   11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1233 AHLFERLPGA--EGVTPICLDS---------------------LKLDNW-PSQAPGLHLHGDNLAYVIYTSGSTGQPKGV 1288
Cdd:PRK12406   91 ADLLHGLASAlpAGVTVLSVPTppeiaaayrispalltppagaIDWEGWlAQQEPYDGPPVPQPQSMIYTSGTTGHPKGV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1289 GNT-----HAALAERlqwMQAT-YTLD-GDDVLM-----QKAPVSFDVSVWEcfwplvTGCRLVLaapgEHR-DPARLVE 1355
Cdd:PRK12406  171 RRAaptpeQAAAAEQ---MRALiYGLKpGIRALLtgplyHSAPNAYGLRAGR------LGGVLVL----QPRfDPEELLQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1356 LVRQFGVTTLHFVPPLLQLFIDEP-GVAA---CGSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTETAINVThwq 1431
Cdd:PRK12406  238 LIERHRITHMHMVPTMFIRLLKLPeEVRAkydVSSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGAVTF--- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1432 CRAEDGERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLAR-GYLGRPAlsaERfvadpfsAAGER--LYRT 1506
Cdd:PRK12406  314 ATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPE---KR-------AEIDRggFITS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1507 GDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYYTGAVGAEAEAEQnqr 1585
Cdd:PRK12406  384 GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDcAVFGIPDAEFGEALMAVVEPQPGATLDEAD--- 460
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 15597620  1586 LRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQ 1629
Cdd:PRK12406  461 IRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWAN 504
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
2176-2686 1.43e-27

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 121.42  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2176 AGTAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTL--SYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGL 2253
Cdd:PRK12583    8 QGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2254 LAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS---------HAALFEALGELPAGVARWCLEEDGPAL------DA 2318
Cdd:PRK12583   88 FATARIGAILVNINPAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGQPGALACERLPELrgvvslAP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2319 EDP------------------APLAALSGPQHQAYLI---YTSGSTGKPKGVAVSHGEI---------AMH-------CA 2361
Cdd:PRK12583  168 APPpgflawhelqargetvsrEALAERQASLDRDDPIniqYTSGTTGFPKGATLSHHNIlnngyfvaeSLGltehdrlCV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2362 AV--IECFGMraedcelhfysinfdaaserLLAPLLC---GARVVLRAQG-------QWGAEEICeliraegVSILGFTP 2429
Cdd:PRK12583  248 PVplYHCFGM--------------------VLANLGCmtvGACLVYPNEAfdplatlQAVEEERC-------TALYGVPT 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2430 SYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPERLEEGAASVpiGSV 2509
Cdd:PRK12583  301 MFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVETV--GRT 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2510 VGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaegGRLYrTGDLVRLCDNGQVEYVGRID 2589
Cdd:PRK12583  379 QPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDED------GWMH-TGDLATMDEQGYVRIVGRSK 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2590 HQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasavaeQDEDAQAALREALKTHLKQQLPDYMVPA 2668
Cdd:PRK12583  452 DMIIRGGENIYPREIEEFLFTHPAVADVQVFGVpDEKYGEEIVAWV------RLHPGHAASEEELREFCKARIAHFKVPR 525
                         570
                  ....*....|....*...
gi 15597620  2669 HLLLLASLPLTANGKLDR 2686
Cdd:PRK12583  526 YFRFVDEFPMTVTGKVQK 543
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3723-4225 3.28e-27

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 119.65  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3723 VAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRL 3802
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3803 TRIVELSRTLVLVCTQACREQALALFDELGCVDRPRLLVWDEIQQGEG-----------AEHDPQVYSGPQNLAYVIYTS 3871
Cdd:PRK08316  101 AYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGwldfadwaeagSVAEPDVELADDDLAQILYTS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3872 GSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVI---------AQtasqsFDIsvwqFLaAPLF--GARVAIVPnavAH 3940
Cdd:PRK08316  181 GTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPlhalplyhcAQ-----LDV----FL-GPYLyvGATNVILD---AP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3941 DPQGLLAHVGEQGITVLESVPSLIQGML---AEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAEcsdd 4017
Cdd:PRK08316  248 DPELILRTIEAERITSFFAPPTVWISLLrhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTE---- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4018 vaffrvdLASTeSTYLpigSPTDNNRlYLLGAG----------ADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQA 4087
Cdd:PRK08316  324 -------IAPL-ATVL---GPEEHLR-RPGSAGrpvlnvetrvVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEA 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4088 FVPHPFgapgerlyRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGyl 4167
Cdd:PRK08316  392 FRGGWF--------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV-----------IG-- 450
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  4168 VPGET----------PRSSAD-SPAGLMveqgawferikQQLRADLPDYMVPLHWLVLDRMPLNANGKL 4225
Cdd:PRK08316  451 LPDPKwieavtavvvPKAGATvTEDELI-----------AHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
PRK06145 PRK06145
acyl-CoA synthetase; Validated
19-558 4.85e-27

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 118.84  E-value: 4.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    19 AVQEPERLALRFLAEDdgegvvLSYRDLDLRARSIAAALQAHA-QLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAY-- 95
Cdd:PRK06145   12 ARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGiGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINyr 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    96 --PPESARrhhqerllsIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLlCVDQLDPAVAEAWDEPQVRPEHIAFLQ 173
Cdd:PRK06145   86 laADEVAY---------ILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQA-DSRRLAQGGLEIPPQAAVAPTDLVRLM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   174 YTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYH----DMGLIGGLLQpifSGVPCVLmspRYFleRP 249
Cdd:PRK06145  156 YTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHvgafDLPGIAVLWV---GGTLRIH---REF--DP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   250 VRWLEAISQYGGTvsgGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRF-DAssffacYG 328
Cdd:PRK06145  228 EAVLAAIERHRLT---CAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYiDA------YG 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   329 LAEATLFVTGGQRGQGIPALAVDGEALArnriaegegsvlmccgrsqpeHAVLIVDAASGEVLGDDNVGEIWAAGPSIAH 408
Cdd:PRK06145  299 LTETCSGDTLMEAGREIEKIGSTGRALA---------------------HVEIRIADGAGRWLPPNMKGEICMRGPKVTK 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   409 GYWRNPEASAKAFVErdgrTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIERTVeSEVPSARKgrvAAFAVT 487
Cdd:PRK06145  358 GYWKDPEKTAEAFYG----DWFRSGDVGYLDEeGFLYLTDRKKDMIISGGENIASSEVERVI-YELPEVAE---AAVIGV 429
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620   488 VDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAyqEAPKVVALLNpgALPKTSSGKLQRSACRLRLE 558
Cdd:PRK06145  430 HDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASF--KVPRQLKVRD--ELPRNPSGKVLKRVLRDELN 496
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3869-4227 5.15e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 115.84  E-value: 5.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3869 YTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAqtasqsfdISVWQF---------LAAPLFGArvAIVPNAVA 3939
Cdd:cd05917    9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLC--------IPVPLFhcfgsvlgvLACLTHGA--TMVFPSPS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3940 HDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSD 4016
Cdd:cd05917   79 FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDkfdLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4017 DVAFFRVDlASTESTYLPIGSPTDNNRLYLLGAGADdafELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAfvphpfgAP 4096
Cdd:cd05917  159 VSTQTRTD-DSIEKRVNTVGRIMPHTEAKIVDPEGG---IVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA-------ID 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4097 GERLYRTGDLARRRADGVLEYVGRIDHQVkIRGFR-IELGEIEARLHERADVREAAVA-VQEGANGKYLVGYLVPGETPR 4174
Cdd:cd05917  228 GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVgVPDERYGEEVCAWIRLKEGAE 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 4175 SSAdspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDR 4227
Cdd:cd05917  307 LTE--------------EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3723-4157 5.45e-27

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 119.27  E-value: 5.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3723 VAAHPQRIA------ASCLEQRWSYAELNRRANRLGHALRAAG-VGidQPVALLAERGLDLLGMIVGSFKAGAGYLPL-- 3793
Cdd:cd05931    3 AAARPDRPAytflddEGGREETLTYAELDRRARAIAARLQAVGkPG--DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3794 -DPGHPTQRLTRIVELSRTLVLVCTQACREQALALFDELGCVDRPRLLVWDEIQqGEGAEHDPQVYSGPQNLAYVIYTSG 3872
Cdd:cd05931   81 pTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLP-DTSAADWPPPSPDPDDIAYLQYTSG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3873 STGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GAR-VAIVPNAVAHDPQGLLAHVG 3950
Cdd:cd05931  160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYsGGPsVLMSPAAFLRRPLRWLRLIS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3951 EQGITVlESVPS-----LIQGMLAEERQALD--GLRWMLPTGEAMPPELARQWLKRYPRIGL-----VNAYGPAECSDDV 4018
Cdd:cd05931  240 RYRATI-SAAPNfaydlCVRRVRDEDLEGLDlsSWRVALNGAEPVRPATLRRFAEAFAPFGFrpeafRPSYGLAEATLFV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4019 AF---------FRVDLASTESTYLPIGSPTDNNRlYLLGAGADDAFELV-----------PLGAVGELCVAGTGVGRGYV 4078
Cdd:cd05931  319 SGgppgtgpvvLRVDRDALAGRAVAVAADDPAAR-ELVSCGRPLPDQEVrivdpetgrelPDGEVGEIWVRGPSVASGYW 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4079 GDPLRTAQAFvpHPFGAPGERLY-RTGDLArRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADV----REAAVA 4153
Cdd:cd05931  398 GRPEATAETF--GALAATDEGGWlRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpgCVAAFS 474

                 ....
gi 15597620 4154 VQEG 4157
Cdd:cd05931  475 VPDD 478
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
692-1097 8.64e-27

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 116.64  E-value: 8.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  692 PQSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERDGA-ALQRIDERGEFAWQFVDLAALAEHERAAAAAQ 770
Cdd:cd19547   19 PDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAePLQYVRDDLAPPWALLDWSGEDPDRRAELLER 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  771 RREAEAQQPFDLEKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLElHYAEFAA 850
Cdd:cd19547   99 LLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQLSPCR-PYRDYVR 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  851 WQRQwlDAGEGARQLAYWRERLGDTAPvlelatdhprTARQASPAARYSL------RVDEALARAIREAALDHEASVFMW 924
Cdd:cd19547  178 WIRA--RTAQSEESERFWREYLRDLTP----------SPFSTAPADREGEfdtvvhEFPEQLTRLVNEAARGYGVTTNAI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  925 LLAAFQALLHRHSGQGEIRIGVPSANR-QRLE-TQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFD 1002
Cdd:cd19547  246 SQAAWSMLLALQTGARDVVHGLTIAGRpPELEgSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1003 QVLAACG----QGGQLFQ--VLFNHQQRDlsalrRLPGllaDELPWHSreakFDLQLQSEED--------ARGRLTLNFD 1068
Cdd:cd19547  326 QIKSWASgerlSGGRVFDnlVAFENYPED-----NLPG---DDLSIQI----IDLHAQEKTEypiglivlPLQKLAFHFN 393
                        410       420
                 ....*....|....*....|....*....
gi 15597620 1069 YAADLFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19547  394 YDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PRK09274 PRK09274
peptide synthase; Provisional
1120-1592 1.00e-26

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 118.46  E-value: 1.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1120 SAPCEPARaWLPELLERQLAQSAERVALEWDGG------SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLV 1193
Cdd:PRK09274    3 ASMANIAR-HLPRAAQERPDQLAVAVPGGRGADgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1194 GLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ--AHLFERL--PGAEGVTPIC------------LDSLKLDN 1257
Cdd:PRK09274   82 LTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIpkAHLARRLfgWGKPSVRRLVtvggrllwggttLATLLRDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1258 WPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVsFdvsvweCFWPLVTGC 1337
Cdd:PRK09274  162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL-F------ALFGPALGM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1338 RLVL-----AAPGEhRDPARLVELVRQFGVTTLhFVPPLLqlfIDEPGVAACG------SLRRLFSGGEALPAELRNRVL 1406
Cdd:PRK09274  235 TSVIpdmdpTRPAT-VDPAKLFAAIERYGVTNL-FGSPAL---LERLGRYGEAngiklpSLRRVISAGAPVPIAVIERFR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1407 QRLPAVA-LHNRYGPTE---------TAINVTHWQcRAEDGERSPIGRPLGNVVCRVLD---------AEFNLLPAGVAG 1467
Cdd:PRK09274  310 AMLPPDAeILTPYGATEalpissiesREILFATRA-ATDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIG 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1468 ELCIGGLGLARGYLGRPALSAERFVADPfsaAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQ 1547
Cdd:PRK09274  389 EIVVAGPMVTRSYYNRPEATRLAKIPDG---QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620  1548 PGVAQ-AVVVIreGVAGSQL----VGYYTGAVGAEAEAEqnQRLRAALQA 1592
Cdd:PRK09274  466 PGVKRsALVGV--GVPGAQRpvlcVELEPGVACSKSALY--QELRALAAA 511
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
167-550 1.08e-26

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 114.67  E-value: 1.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  167 EHIAFLQYTSGSTALPKGVQVSHGNLVAN-EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVpCVLMSPRYF 245
Cdd:cd17635    1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVpDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGL-CVTGGENTT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  246 LERpvrWLEAISQYGGTVSG-GPDFAYRLCSE---RVAESALQRLdlsgwrVAFSGSEPIRQDSleRFAEKFAASRFDAS 321
Cdd:cd17635   80 YKS---LFKILTTNAVTTTClVPTLLSKLVSElksANATVPSLRL------IGYGGSRAIAADV--RFIEATGLTNTAQV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  322 sffacYGLAEAT--LFVTGGQRGQGIPALavdgealarnriaegegsvlmccGRSQPEHAVLIVDAASGEVLGDDNvGEI 399
Cdd:cd17635  149 -----YGLSETGtaLCLPTDDDSIEINAV-----------------------GRPYPGVDVYLAATDGIAGPSASF-GTI 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  400 WAAGPSIAHGYWRNPEASAKAFVErdgrTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERtVESEVPSARK 478
Cdd:cd17635  200 WIKSPANMLGYWNNPERTAEVLID----GWVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVER-IAEGVSGVQE 274
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  479 GRVAAFAVTVDGEEgIGIAAEIGRGVQKSVpAQELIDSIRQAVAEAYQeaPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd17635  275 CACYEISDEEFGEL-VGLAVVASAELDENA-IRALKHTIRRELEPYAR--PSTIVIVT--DIPRTQSGKVKR 340
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
2205-2664 1.51e-26

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 116.77  E-value: 1.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2205 LTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGV 2284
Cdd:cd05914    1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2285 RLLlshaalfealgelpagvarWCLEEDGPALdaedpaplaalsgpqhqayLIYTSGSTGKPKGVAVSHGEIAMHCAAVI 2364
Cdd:cd05914   81 KAI-------------------FVSDEDDVAL-------------------INYTSGTTGNSKGVMLTYRNIVSNVDGVK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2365 ECFGMRAEDCEL------HFYSINFDaaserLLAPLLCGARVVL-------RAQGQWGAE-----EICELIRAEGVSILG 2426
Cdd:cd05914  123 EVVLLGKGDKILsilplhHIYPLTFT-----LLLPLLNGAHVVFldkipsaKIIALAFAQvtptlGVPVPLVIEKIFKMD 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2427 FTPSYGSQLAQW-------------------LESQGRQLpvRMCITGGEALTGEHLQRIRQAFAPasFFNAYGPTETVvm 2487
Cdd:cd05914  198 IIPKLTLKKFKFklakkinnrkirklafkkvHEAFGGNI--KEFVIGGAKINPDVEEFLRTIGFP--YTIGYGMTETA-- 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2488 PLACLA-PERLEEGAASVPIgSVVGARVAyildadlALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggr 2566
Cdd:cd05914  272 PIISYSpPNRIRLGSAGKVI-DGVEVRID-------SPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------ 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2567 lYRTGDLVRLCDNGQVEYVGRIDHQ-VKIRGFRIELGEIEARLLEHPQVREALVLALDSPSgkQLAGYV----ASAVAEQ 2641
Cdd:cd05914  338 -FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL--VALAYIdpdfLDVKALK 414
                        490       500
                 ....*....|....*....|...
gi 15597620 2642 DEDAQAALREALKTHLKQQLPDY 2664
Cdd:cd05914  415 QRNIIDAIKWEVRDKVNQKVPNY 437
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3252-3574 1.85e-26

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 115.66  E-value: 1.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3252 PLTPMQ--------EGLLL-----HTLLEpgtgiyymqdryrIDSP-LDPERFAAAWQAVVARHEALRASFVWNAgetML 3317
Cdd:cd19535    3 PLTDVQyaywigrqDDQELggvgcHAYLE-------------FDGEdLDPDRLERAWNKLIARHPMLRAVFLDDG---TQ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3318 QVIHKPGRTRIEFLDWSELPEDGHEERLQAL-----HKRereagFDLLEQPPFHLRLIRLGEARY--WFMMSNhhILIDA 3390
Cdd:cd19535   67 QILPEVPWYGITVHDLRGLSEEEAEAALEELrerlsHRV-----LDVERGPLFDIRLSLLPEGRTrlHLSIDL--LVADA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3391 WCRGLLMNDFFEIYSALGESRPanlPTPPRYRDYIAWLQRQ---DLEQSRRWWSESLrgferPTLVPS-DRPFLREHAge 3466
Cdd:cd19535  140 LSLQILLRELAALYEDPGEPLP---PLELSFRDYLLAEQALretAYERARAYWQERL-----PTLPPApQLPLAKDPE-- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3467 sggMIVGDRYTR----LDAADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGVTVAGRPVGMPEMQRTVGLF 3542
Cdd:cd19535  210 ---EIKEPRFTRrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDF 286
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 15597620 3543 INSIPLRVQMpaaGQRCTVREWLNRL---FERNLE 3574
Cdd:cd19535  287 TSLLLLEVDG---SEGQSFLERARRLqqqLWEDLD 318
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
1085-1622 1.94e-26

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 118.50  E-value: 1.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1085 QYLELLRQVAEDPQRCLGdialvdaEQAAHLAEW---------GSAPcePARAWLPE--------LLERQLAQSAERVAL 1147
Cdd:TIGR02188    6 QYKELYEESIEDPDKFWA-------KLARELLDWfkpftkvldWSFP--PFYKWFVGgelnvsynCVDRHLEARPDKVAI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1148 EWDGGSLG------YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML 1221
Cdd:TIGR02188   77 IWEGDEPGevrkitYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1222 ADSGVELLLTQAHLFER-----LPGA--EGVTpICLDSLK-----------LDNWpsqAPGLHLHGDNLA---------- 1273
Cdd:TIGR02188  157 NDAGAKLVITADEGLRGgkvipLKAIvdEALE-KCPVSVEhvlvvrrtgnpVVPW---VEGRDVWWHDLMakasaycepe 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1274 --------YVIYTSGSTGQPKGVGNT------HAALAerlqwMQATYTLDGDDVLMQKAPV------SFDVsvwecFWPL 1333
Cdd:TIGR02188  233 pmdsedplFILYTSGSTGKPKGVLHTtggyllYAAMT-----MKYVFDIKDGDIFWCTADVgwitghSYIV-----YGPL 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1334 VTGCRLVL--AAPgEHRDPARLVELVRQFGVTTLHFVPPLLQLFI----DEPGVAACGSLRRLFSGGEALPAElrnrvlq 1407
Cdd:TIGR02188  303 ANGATTVMfeGVP-TYPDPGRFWEIIEKHKVTIFYTAPTAIRALMrlgdEWVKKHDLSSLRLLGSVGEPINPE------- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1408 rlpavA---LHNRYGPTETAINVTHWQcrAEDGER--SPI-----------GRPLGNVVCRVLDAEFNLLP-AGVAGELC 1470
Cdd:TIGR02188  375 -----AwmwYYKVVGKERCPIVDTWWQ--TETGGImiTPLpgatptkpgsaTLPFFGIEPAVVDEEGNPVEgPGEGGYLV 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   1471 IGGL--GLARGYLGRPalsaERFVADPFSAAgERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQP 1548
Cdd:TIGR02188  448 IKQPwpGMLRTIYGDH----ERFVDTYFSPF-PGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHP 522
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620   1549 GVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:TIGR02188  523 AVAEAAVVgIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLL 597
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
174-550 2.17e-26

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 113.52  E-value: 2.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  174 YTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLiGGLLQPIFSGVPCVLMSpRYfleRPVRWL 253
Cdd:cd17637    7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVME-KF---DPAEAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  254 EAISQYGGTVSGgpDFAYRLcSERVAESALQRLDLSGWRVAFSGSEPirqDSLERFAEKFAAsrfdasSFFACYGLAEAT 333
Cdd:cd17637   82 ELIEEEKVTLMG--SFPPIL-SNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGA------TFWSLYGQTETS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  334 LFVTGGqrgqgipalavdgealarnRIAEGEGSVlmccGRSQPEHAVLIVDAASGEVlGDDNVGEIWAAGPSIAHGYWRN 413
Cdd:cd17637  150 GLVTLS-------------------PYRERPGSA----GRPGPLVRVRIVDDNDRPV-PAGETGEIVVRGPLVFQGYWNL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  414 PEASAKAFveRDGrtWLRTGDLG-FLRDGELFVTGRL--KDMLIVRGHNLYPQDIERTVEsEVPSARKgrVAAFAVTvDG 490
Cdd:cd17637  206 PELTAYTF--RNG--WHHTGDLGrFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVIL-EHPAIAE--VCVIGVP-DP 277
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  491 EEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEaYQEaPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd17637  278 KWGEGIKAVCVLKPGATLTADELIEFVGSRIAR-YKK-PRYVVFVE--ALPKTADGSIDR 333
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3739-4230 2.29e-26

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 116.16  E-value: 2.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCtq 3818
Cdd:cd05907    6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3819 acreqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL 3898
Cdd:cd05907   84 ----------------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3899 ELDENDVI------AQTASQSFDISVWQflaapLFGARVAIVPnavahDPQGLLAHVGEQGITVLESVPSL-------IQ 3965
Cdd:cd05907  124 PATEGDRHlsflplAHVFERRAGLYVPL-----LAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVwekvyaaIK 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3966 GMLAEE-------RQALDGLRWMLPTGEAMPPELARQWLKryprIGL--VNAYGPAECSDDVAFFRVDLASTEStylpIG 4036
Cdd:cd05907  194 VKAVPGlkrklfdLAVGGRLRFAASGGAPLPAELLHFFRA----LGIpvYEGYGLTETSAVVTLNPPGDNRIGT----VG 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4037 SPTDNNRLYLlgagADDafelvplgavGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRADGVLE 4116
Cdd:cd05907  266 KPLPGVEVRI----ADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLH 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4117 YVGRI-DHQVKIRGFRIELGEIEARLHERADVREAAVAvqeGANGKYLVGYLVP------------GETPRSSADSPAGL 4183
Cdd:cd05907  325 ITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALIVPdpealeawaeehGIAYTDVAELAANP 401
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 4184 MVEqgAWFERIKQQLRADLPDYMVPLHWLVLDRMP------LNANGKLDRKAL 4230
Cdd:cd05907  402 AVR--AEIEAAVEAANARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRPVI 452
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
2192-2666 2.31e-26

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 118.05  E-value: 2.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2192 FAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2271
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2272 LERLQYMIEDSGVRLLLSHAALFEALGELPAGVA---RWCLEEDGPALDAEDPAPLAALSGPQHQ--------------A 2334
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADLArppRLWVAGGDTLDDPEGYEDLAAAAAGAPTtnpasrsgvtakdtA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2335 YLIYTSGSTGKPKGVAVSHGEI--AMHCAAVIecFGMRAED---CELHFYSINfdAASERLLAPLLCGARVVLR----AQ 2405
Cdd:PRK08279  203 FYIYTSGTTGLPKAAVMSHMRWlkAMGGFGGL--LRLTPDDvlyCCLPLYHNT--GGTVAWSSVLAAGATLALRrkfsAS 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2406 GQWgaeeicELIRAEGVSILGftpsYGSQLAQWL-----ESQGRQLPVRMCItgGEALTGEHLQRIRQAFA--------- 2471
Cdd:PRK08279  279 RFW------DDVRRYRATAFQ----YIGELCRYLlnqppKPTDRDHRLRLMI--GNGLRPDIWDEFQQRFGiprilefya 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2472 ----PASFFNAYGPTETV-VMPLACLAPERLeegaasvpigsvvgarVAYILDADLAL---------VPQGATGELY--V 2535
Cdd:PRK08279  347 asegNVGFINVFNFDGTVgRVPLWLAHPYAI----------------VKYDVDTGEPVrdadgrcikVKPGEVGLLIgrI 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2536 GGAGLARGYhERPALSAERFVPDPFaAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVR 2615
Cdd:PRK08279  411 TDRGPFDGY-TDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVE 488
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  2616 EALVLALDSP--SGKqlAGYVASAVAEQDEDAQAALREalktHLKQQLPDYMV 2666
Cdd:PRK08279  489 EAVVYGVEVPgtDGR--AGMAAIVLADGAEFDLAALAA----HLYERLPAYAV 535
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3718-4226 2.37e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 117.29  E-value: 2.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3798 PTQRLTRIVELSRTLVLVCTQACREQALALFDELgcvDRPRLLV----------------WDEIQQGEGAEHDPQVYSgP 3861
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYEREFAPRVAEVLPRL---PKLRTLVvvedgsgndllpgavdYEDALAAGSPERDFGERS-P 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3862 QNLaYVIYTSGSTGLPKGVMVEQAGMLNNQLS-----KVPYLElDENDVIAQTASQSFDI-----------SVWQFLAAP 3925
Cdd:PRK07798  164 DDL-YLLYTGGTTGMPKGVMWRQEDIFRVLLGgrdfaTGEPIE-DEEELAKRAAAGPGMRrfpapplmhgaGQWAAFAAL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3926 LFGARVAIVPNaVAHDPQGLLAHVGEQGITVLESV------PsLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKR 3999
Cdd:PRK07798  242 FSGQTVVLLPD-VRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGPYDLSSLFAIASGGALFSPSVKEALLEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4000 YPRIGLVNAYGpaecsddvaffrvdlaSTE-----STYLPIGSPTDNNRLYLLGAG---ADDAFELVPLGAVGELCVAGT 4071
Cdd:PRK07798  320 LPNVVLTDSIG----------------SSEtgfggSGTVAKGAVHTGGPRFTIGPRtvvLDEDGNPVEPGSGEIGWIARR 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4072 G-VGRGYVGDPLRTAQAFvphpFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREA 4150
Cdd:PRK07798  384 GhIPLGYYKDPEKTAETF----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADA 459
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  4151 AVavqegangkylVGylVPGEtpRSSADSPAGLMVEQGAWF--ERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLD 4226
Cdd:PRK07798  460 LV-----------VG--VPDE--RWGQEVVAVVQLREGARPdlAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
10-466 2.49e-26

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 117.17  E-value: 2.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   10 TLVQALRRRAVQEPERLALRflaedDGEGVvLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAG 88
Cdd:COG1021   26 TLGDLLRRRAERHPDRIAVV-----DGERR-LSYAELDRRADRLAAGLLALgLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   89 VIAVPAYPpesARRHHQerLLSIIADAEPRLVLTTA-----DLREpllqMNAQLsAANAPQL---LCVDQLDPAVA---- 156
Cdd:COG1021  100 AIPVFALP---AHRRAE--ISHFAEQSEAVAYIIPDrhrgfDYRA----LAREL-QAEVPSLrhvLVVGDAGEFTSldal 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  157 ----EAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIG-GLLQPI 231
Cdd:COG1021  170 laapADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  232 FSGvPCVLMSPRyflERPVRWLEAISQYGGTVSG-GPdFAYRLCserVAESALQRLDLSGWRVAFSGSepirqdslERFA 310
Cdd:COG1021  250 YAG-GTVVLAPD---PSPDTAFPLIERERVTVTAlVP-PLALLW---LDAAERSRYDLSSLRVLQVGG--------AKLS 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  311 EKfAASRFDASsfFAC-----YGLAEATLFVTggqrgqgipalavdgealarnRIAEGEGSVLMCCGRSQPEH-AVLIVD 384
Cdd:COG1021  314 PE-LARRVRPA--LGCtlqqvFGMAEGLVNYT---------------------RLDDPEEVILTTQGRPISPDdEVRIVD 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  385 AAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDL-GFLRDGELFVTGRLKDMlIVR-GHNLYP 462
Cdd:COG1021  370 ED-GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTP-DG--FYRTGDLvRRTPDGYLVVEGRAKDQ-INRgGEKIAA 444

                 ....
gi 15597620  463 QDIE 466
Cdd:COG1021  445 EEVE 448
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3738-4225 2.55e-26

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 115.56  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3738 RWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCT 3817
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3818 QACREqalalfdelgcvdrprllvwdeiqqgegaeHDPQvySGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPY 3897
Cdd:cd05903   81 ERFRQ------------------------------FDPA--AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAER 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3898 LELDENDVIAQTASQSFDI-SVWQFLAAPLFGARVAIVPnavAHDPQGLLAHVGEQGITVLESVPSLIQGML-AEERQA- 3974
Cdd:cd05903  129 LGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLTDLLnAVEEAGe 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3975 -LDGLRWMLPTGEAMPPELARQWLKRYPRIgLVNAYGPAECSDDVAffRVDLASTESTYLPIGSPTDNNRLYLLgagaDD 4053
Cdd:cd05903  206 pLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECPGAVT--SITPAPEDRRLYTDGRPLPGVEIKVV----DD 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4054 AFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgapGERLYRTGDLARRRADGVLEYVGRiDHQVKIR-GFRI 4132
Cdd:cd05903  279 TGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA--------PEGWFRTGDLARLDEDGYLRITGR-SKDIIIRgGENI 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4133 ELGEIEARLHERADVREAA-VAVQEGANGKYLVGYLVPgetprssaDSPAGLMVEQ-GAWFERIKqqlradLPDYMVPLH 4210
Cdd:cd05903  350 PVLEVEDLLLGHPGVIEAAvVALPDERLGERACAVVVT--------KSGALLTFDElVAYLDRQG------VAKQYWPER 415
                        490
                 ....*....|....*
gi 15597620 4211 WLVLDRMPLNANGKL 4225
Cdd:cd05903  416 LVHVDDLPRTPSGKV 430
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3704-4230 3.50e-26

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 116.78  E-value: 3.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3704 RSARDYPL-EQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVG 3782
Cdd:PRK06155   11 RAVDPLPPsERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3783 SFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALfdELGCVDRPRLLVWDeiqqGEGAEHDPQVYS--- 3859
Cdd:PRK06155   91 CAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAA--DPGDLPLPAVWLLD----APASVSVPAGWStap 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3860 -------------GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPL 3926
Cdd:PRK06155  165 lppldapapaaavQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3927 FGARVAIVPNAVAhdpQGLLAHVGEQGITV---LESVPSLIQGMLAEERQALDGLRWMLptGEAMPPELARQWLKRYPrI 4003
Cdd:PRK06155  245 AGATYVLEPRFSA---SGFWPAVRRHGATVtylLGAMVSILLSQPARESDRAHRVRVAL--GPGVPAALHAAFRERFG-V 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4004 GLVNAYGpaecsddvaffrvdlaSTEsTYLPIGSPTDNNRLYLLGAGAdDAFEL---------VPLGAVGELCVAGT--- 4071
Cdd:PRK06155  319 DLLDGYG----------------STE-TNFVIAVTHGSQRPGSMGRLA-PGFEArvvdehdqeLPDGEPGELLLRADepf 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4072 GVGRGYVGDPLRTAQAFvphpfgapGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAA 4151
Cdd:PRK06155  381 AFATGYFGMPEKTVEAW--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAA 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4152 VavqegangkylvgYLVPGETprSSADSPAGLMVEQG--AWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKA 4229
Cdd:PRK06155  453 V-------------FPVPSEL--GEDEVMAAVVLRDGtaLEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFV 517

                  .
gi 15597620  4230 L 4230
Cdd:PRK06155  518 L 518
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3717-4234 3.59e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 116.95  E-value: 3.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3717 RLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG 3796
Cdd:PRK07788   53 GLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3797 HPTQRLTRIVElsrtlvlvctqacREQALALF--DE----LGCV--DRPRLLVWdeiqqGEGAEHDPQVYSGPQNLA--- 3865
Cdd:PRK07788  133 FSGPQLAEVAA-------------REGVKALVydDEftdlLSALppDLGRLRAW-----GGNPDDDEPSGSTDETLDdli 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3866 ----------------YVIYTSGSTGLPKGVM-------VEQAGMlnnqLSKVPyleLDENDVIAQTAS--QSFDISVWQ 3920
Cdd:PRK07788  195 agsstaplpkppkpggIVILTSGTTGTPKGAPrpepsplAPLAGL----LSRVP---FRAGETTLLPAPmfHATGWAHLT 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3921 fLAAPLfGARVaivpnaVAH---DPQGLLAHVGEQGITVLESVPSLIQGMLAEERQALDG-----LRWMLPTGEAMPPEL 3992
Cdd:PRK07788  268 -LAMAL-GSTV------VLRrrfDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKydtssLKIIFVSGSALSPEL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3993 ARQWLKRYPRIgLVNAYGPAECSDDVAFFRVDLASTESTylpIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTG 4072
Cdd:PRK07788  340 ATRALEAFGPV-LYNLYGSTEVAFATIATPEDLAEAPGT---VGRPPKGVTVKIL----DENGNEVPRGVVGRIFVGNGF 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4073 VGRGYVGDplrtaqafvPHPFGAPGerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:PRK07788  412 PFEGYTDG---------RDKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAV 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4153 -AVQEGANGKYLVGYLVPGETPRSSADSpaglmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:PRK07788  481 iGVDDEEFGQRLRAFVVKAPGAALDEDA--------------IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546

                  ...
gi 15597620  4232 ALD 4234
Cdd:PRK07788  547 EMD 549
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
1085-1622 4.08e-26

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 117.28  E-value: 4.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1085 QYLELLRQVAEDPQRCLGDIA--LVDAEQAAHLAEWGSAPcePARAWLPE--------LLERQLAQSAERVALEWDGG-- 1152
Cdd:cd05966    2 QYKELYKQSIEDPEEFWGEIAkeLDWFKPWDKVLDWSKGP--PFIKWFEGgklnisynCLDRHLKERGDKVAIIWEGDep 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 ----SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLA---------IVKAGgayvpldpdYPSERLAY 1219
Cdd:cd05966   80 dqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAG---------FSAESLAD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1220 MLADSGVELLLT----------------------QAHL------FERLPGAEGVTP---ICLDSLKLDNwPSQAPGLHLH 1268
Cdd:cd05966  151 RINDAQCKLVITadggyrggkviplkeivdealeKCPSvekvlvVKRTGGEVPMTEgrdLWWHDLMAKQ-SPECEPEWMD 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1269 GDNLAYVIYTSGSTGQPKGVGNTHAALaerLQWMQAT--YTLD--GDDVLMQKAPV------SFDVsvwecFWPLVTGCR 1338
Cdd:cd05966  230 SEDPLFILYTSGSTGKPKGVVHTTGGY---LLYAATTfkYVFDyhPDDIYWCTADIgwitghSYIV-----YGPLANGAT 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1339 LVL--AAPgEHRDPARLVELVRQFGVTTLHFVPPLLQLFI---DEPgVAAC--GSLRRLFSGGEALPAElrnrvlqrlpa 1411
Cdd:cd05966  302 TVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMkfgDEW-VKKHdlSSLRVLGSVGEPINPE----------- 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1412 vA---LHNRYGPTETAINVTHWQcrAEDGER--SPI-----------GRPLGNVVCRVLDAEFNLLPAGVAGELCIGGL- 1474
Cdd:cd05966  369 -AwmwYYEVIGKERCPIVDTWWQ--TETGGImiTPLpgatplkpgsaTRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPw 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1475 -GLARGYLGRPalsaERFVADPFSA-AGerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ 1552
Cdd:cd05966  446 pGMARTIYGDH----ERYEDTYFSKfPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAE 519
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 1553 AVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05966  520 AAVVgRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1138-1624 5.28e-26

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 116.14  E-value: 5.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1138 LAQSAERVALEwdggslgYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERL 1217
Cdd:PRK05852   35 LVVTADRIAIS-------YRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1218 AYMLADSGVELLLTQAH-LFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLH---------------GDNLAYVIYTSGS 1281
Cdd:PRK05852  108 RVRSQAAGARVVLIDADgPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDaateptpatstpeglRPDDAMIMFTGGT 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1282 TGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVS-VWECFWPLVTGCRLVLAAPGEHR-----DPARLVE 1355
Cdd:PRK05852  188 TGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARGRFSahtfwDDIKAVG 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1356 LVRQFGVTTLHFVppLLQLFIDEPGVAACGSLRRLFSGGEALPAELRnRVLQRLPAVALHNRYGPTETAINVT----HWQ 1431
Cdd:PRK05852  268 ATWYTAVPTIHQI--LLERAATEPSGRKPAALRFIRSCSAPLTAETA-QALQTEFAAPVVCAFGMTEATHQVTttqiEGI 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1432 CRAEDGERS--PIGRPLGnVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVadpfsaagERLYRTGDR 1509
Cdd:PRK05852  345 GQTENPVVStgLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT--------DGWLRTGDL 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1510 ARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREgvagSQLVGYYTGA--VGAEAEAEQNQRLR 1587
Cdd:PRK05852  416 GSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP----DQLYGEAVAAviVPRESAPPTAEELV 491
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 15597620  1588 AALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK05852  492 QFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
160-550 5.34e-26

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 113.98  E-value: 5.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  160 DEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdmglIGGL---LQPIFSGVP 236
Cdd:cd05912   70 KDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH----ISGLsilMRSVIYGMT 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  237 CVLMspRYFLERPVrwLEAI-SQYGGTVSggpdfayrlcserVAESALQRL---DLSGW----RVAFSGSEPIRQDSLER 308
Cdd:cd05912  146 VYLV--DKFDAEQV--LHLInSGKVTIIS-------------VVPTMLQRLleiLGEGYpnnlRCILLGGGPAPKPLLEQ 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  309 FAEKfaasrfdASSFFACYGLAEatlfvTGGQrgqgIPALAVDgeaLARNRIaegeGSVlmccGRSQPEHAVLIVDAASG 388
Cdd:cd05912  209 CKEK-------GIPVYQSYGMTE-----TCSQ----IVTLSPE---DALNKI----GSA----GKPLFPVELKIEDDGQP 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  389 EvlgdDNVGEIWAAGPSIAHGYWRNPEASAKAFVErdgrTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIER 467
Cdd:cd05912  262 P----YEVGEILLKGPNVTKGYLNRPDATEESFEN----GWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEE 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  468 TVESEVPSARKGRVAAfavtVDGEEG-IGIAAEIGrgvQKSVPAQELIDSIRQAVAEaYQeAPKVVALLNpgALPKTSSG 546
Cdd:cd05912  334 VLLSHPAIKEAGVVGI----PDDKWGqVPVAFVVS---ERPISEEELIAYCSEKLAK-YK-VPKKIYFVD--ELPRTASG 402

                 ....
gi 15597620  547 KLQR 550
Cdd:cd05912  403 KLLR 406
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1128-1729 5.41e-26

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 118.27  E-value: 5.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1128 AWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVP 1207
Cdd:COG3319    1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1208 LDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKG 1287
Cdd:COG3319   81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1288 VGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVELVRQFGVTTLHF 1367
Cdd:COG3319  161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1368 VPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPIGRPLG 1447
Cdd:COG3319  241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1448 NVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGE----RLYRTGDRARWNADGVLEYLGR 1523
Cdd:COG3319  321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAgargRLRRGGDRGRRLGGGLLLGLGR 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1524 LDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYtgaVGAEAEAEQNQRLRAALQAELPEYMVPTQL 1603
Cdd:COG3319  401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAA---VVAAAALAAAALLLLLLLLLLPPPLPPALL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1604 MRLAQMPLGPSGKLDTRALPEPVWQQREH-VEPRTELQRRIAAIWSEVLGLPRVGLRDDFFELGGHSLLATRIVSRTRQA 1682
Cdd:COG3319  478 LLLLLLLLLLLAALLLAAAAPAAAAAAAAaPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLAL 557
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 1683 CDVELPLRALFEASELEAFCEQVRAAQAAGRTDSHGAIRRIDREQPV 1729
Cdd:COG3319  558 LLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPL 604
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
1156-1556 5.84e-26

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 115.15  E-value: 5.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLtqahl 1235
Cdd:cd17640    8 YKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV----- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 ferlpgaegvtpicldslkLDNwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLM 1315
Cdd:cd17640   83 -------------------VEN----------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1316 QKAPV--SFDVSVwECFWpLVTGC-------------------RLVLAAPgehrdpaRLVELVRQFGVTTLHFVPP---- 1370
Cdd:cd17640  134 SILPIwhSYERSA-EYFI-FACGCsqaytsirtlkddlkrvkpHYIVSVP-------RLWESLYSGIQKQVSKSSPikqf 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 LLQLFIdepgvaACGSLRRLFSGGEALPAELrNRVLQRLpAVALHNRYGPTETAINVThwqCRAEDGE-RSPIGRPLGNV 1449
Cdd:cd17640  205 LFLFFL------SGGIFKFGISGGGALPPHV-DTFFEAI-GIEVLNGYGLTETSPVVS---ARRLKCNvRGSVGRPLPGT 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1450 VCRVLDAEFN-LLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRL-DQQ 1527
Cdd:cd17640  274 EIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAkDTI 346
                        410       420
                 ....*....|....*....|....*....
gi 15597620 1528 VKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:cd17640  347 VLSNGENVEPQPIEEALMRSPFIEQIMVV 375
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
709-1097 9.01e-26

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 113.74  E-value: 9.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  709 LDEAALRASFQRLVERHEALRTRFLErDGaaLQRI-DERGEFAWQFVDLAALAEHERAAAAAQRREAEAQQPFDLEKGPL 787
Cdd:cd19535   37 LDPDRLERAWNKLIARHPMLRAVFLD-DG--TQQIlPEVPWYGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  788 LRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAeacgGQPADLAPLELHYAEFAAWQRQwLDAGEGARQLAY 867
Cdd:cd19535  114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYE----DPGEPLPPLELSFRDYLLAEQA-LRETAYERARAY 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  868 WRERLGD--TAPVLELATDhPRTARQASpAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRIG 945
Cdd:cd19535  189 WQERLPTlpPAPQLPLAKD-PEEIKEPR-FTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLN 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  946 VPSANRQRLETQ--GLVGFFINTLVLRGTPRARQPFAALlgeareatlgAQANQDlpfdqvlaacgqggQLFQVLfNH-- 1021
Cdd:cd19535  267 LTLFNRLPLHPDvnDVVGDFTSLLLLEVDGSEGQSFLER----------ARRLQQ--------------QLWEDL-DHss 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1022 -----QQRDLSALRR-----LP---------GLLADELPWHSREAKF----------DLQLqSEEDarGRLTLNFDYAAD 1072
Cdd:cd19535  322 ysgvvVVRRLLRRRGgqpvlAPvvftsnlglPLLDEEVREVLGELVYmisqtpqvwlDHQV-YEED--GGLLLNWDAVDE 398
                        410       420
                 ....*....|....*....|....*
gi 15597620 1073 LFDEASIRRFAAQYLELLRQVAEDP 1097
Cdd:cd19535  399 LFPEGMLDDMFDAYVRLLERLADDD 423
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3723-4232 9.42e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 115.08  E-value: 9.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3723 VAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP-GHPTQR 3801
Cdd:PRK06188   22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPlGSLDDH 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3802 LTRIVELSRTLVLVCTQACREQALALFDELgcvdrPRLLVW----------DEIQQGEGAEHDPQV-YSGPQNLAYVIYT 3870
Cdd:PRK06188  102 AYVLEDAGISTLIVDPAPFVERALALLARV-----PSLKHVltlgpvpdgvDLLAAAAKFGPAPLVaAALPPDIAGLAYT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3871 SGSTGLPKGVMV---EQAGMLNNQLSKvpyLELDEN-DVIAQT----ASQSFdisvwqFLAAPLFGARVAIVPnavAHDP 3942
Cdd:PRK06188  177 GGTTGKPKGVMGthrSIATMAQIQLAE---WEWPADpRFLMCTplshAGGAF------FLPTLLRGGTVIVLA---KFDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3943 QGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYPRIgLVNAYGPAECSDDVA 4019
Cdd:PRK06188  245 AEVLRAIEEQRITATFLVPTMIYALLDHPDLRtrdLSSLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEAPMVIT 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4020 FFRVD--LASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgaPG 4097
Cdd:PRK06188  324 YLRKRdhDPDDPKRLTSCGRPTPGLRVALL----DEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4098 ERLyRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVreAAVAVqegangkylVGylVP----GET- 4172
Cdd:PRK06188  393 GWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV--AQVAV---------IG--VPdekwGEAv 458
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  4173 -----PRSSADSPAglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK06188  459 tavvvLRPGAAVDA----------AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2792-3211 1.05e-25

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 113.31  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2792 LTPIQHWFFDLPLARREH--WNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDG----EWLAQHRPLREQEL- 2864
Cdd:cd19536    4 LSSLQEGMLFHSLLNPGGsvYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvQVVHRQAQVPVTELd 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2865 LWHVPVQ--SFDECAELfaKAQRSLDLEQGPLLRAVLVDGPAGEQRLL-LAIHHLVVDGVSWRVLLEDLQQVYRQFAEGA 2941
Cdd:cd19536   84 LTPLEEQldPLRAYKEE--TKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2942 EPALPaKTSAFRDWAGRLQAYAGSEslrEELGWWQARLGG---QPVEWPCDRPQGDNRE--ALAESVSLrldPQRTRQLl 3016
Cdd:cd19536  162 PLSLP-PAQPYRDFVAHERASIQQA---ASERYWREYLAGatlATLPALSEAVGGGPEQdsELLVSVPL---PVRSRSL- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3017 qqapaAYRTQVN--DLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDltRSVGWFTSAYPLRLT-PAQSPGESIKA 3093
Cdd:cd19536  234 -----AKRSGIPlsTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTlSEETVEDLLKR 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3094 IKEQLR-AVPHkglgygvlRYLADPAVRQAMAALPTAPITFNYLGQFDQSFADALFQPLDQPTGPIHDEQAP-LPNELSV 3171
Cdd:cd19536  307 AQEQELeSLSH--------EQVPLADIQRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEFKSnYDVNLSV 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 15597620 3172 DGQvyGGELVLRWTYSRERYDARTVNELAQAYLAELQALI 3211
Cdd:cd19536  379 LPK--QDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELA 416
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
65-554 1.19e-25

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 114.93  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   65 DRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRhhqerLLSIIADAEPRLVLTTADLREPLLQMNAQL------- 137
Cdd:cd17642   70 DRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERE-----LDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiiktii 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  138 ---SAANAPQLLCVD----QLDPAVAEAWD---EPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRR---GFG 204
Cdd:cd17642  145 ildSKEDYKGYQCLYtfitQNLPPGFNEYDfkpPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQ 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  205 IGADDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLMsPRyFLERpvRWLEAISQYG--GTVSGGPDFAYrlcserVAESA 282
Cdd:cd17642  225 IIPDTAILTVIPFHHGFGMF-TTLGYLICGFRVVLM-YK-FEEE--LFLRSLQDYKvqSALLVPTLFAF------FAKST 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  283 L-QRLDLSGWRVAFSGSEPIRQDSLERFAEkfaasRFDASSFFACYGLAEATLFVTGGQRGQGIPalavdgealarnria 361
Cdd:cd17642  294 LvDKYDLSNLHEIASGGAPLSKEVGEAVAK-----RFKLPGIRQGYGLTETTSAILITPEGDDKP--------------- 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  362 egeGSvlmcCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASaKAFVERDGrtWLRTGDLGFL-RD 440
Cdd:cd17642  354 ---GA----VGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEAT-KALIDKDG--WLHSGDIAYYdED 423
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  441 GELFVTGRLKDMLIVRGHNLYPQDIErTVESEVPSARKGRVAAFAVTVDGE-EGIGIAAEIGrgvqKSVPAQELIDSIRQ 519
Cdd:cd17642  424 GHFFIVDRLKSLIKYKGYQVPPAELE-SILLQHPKIFDAGVAGIPDEDAGElPAAVVVLEAG----KTMTEKEVMDYVAS 498
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620  520 AVAEAYQEAPKVVALlnpGALPKTSSGKLQRSACR 554
Cdd:cd17642  499 QVSTAKRLRGGVKFV---DEVPKGLTGKIDRRKIR 530
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
41-554 1.22e-25

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 114.55  E-value: 1.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     41 LSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQerllsIIADAEPRL 119
Cdd:TIGR02262   31 LSYGELEAQVRRLAAALRRLgVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAY-----MLEDSRARV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    120 VLTTADL---------REPLLQMNAQLSAANAPQLLCVDQLdPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHG 190
Cdd:TIGR02262  106 VFVSGALlpvikaalgKSPHLEHRVVVGRPEAGEVQLAELL-ATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHS 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    191 NLVAN-EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRyflERPVRWLEAISQYGGTV-SGGPD 268
Cdd:TIGR02262  185 NPYWTaELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGER---PTPDAVFDRLRRHQPTIfYGVPT 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    269 -FAYRLCSERVAESALQRLdlsgwRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEAT-LFVTGgqrgqgip 346
Cdd:TIGR02262  262 lYAAMLADPNLPSEDQVRL-----RLCTSAGEALPAEVGQRWQARFGVDIVDG------IGSTEMLhIFLSN-------- 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    347 alavdgealARNRIAEGEGsvlmccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVERdg 426
Cdd:TIGR02262  323 ---------LPGDVRYGTS------GKPVPGYRLRLVGDG-GQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE-- 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    427 rtWLRTGDlGFLRDGELFVT--GRLKDMLIVRGHNLYPQDIERTVesevpSARKGRVAAFAVTVDGEEG-IGIAAEIGRG 503
Cdd:TIGR02262  385 --WTRSGD-KYVRNDDGSYTyaGRTDDMLKVSGIYVSPFEIESAL-----IQHPAVLEAAVVGVADEDGlIKPKAFVVLR 456
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 15597620    504 VQKSVPAQELIDSIRQAVAE-AYQEAPKVVAllnpgALPKTSSGKLQRSACR 554
Cdd:TIGR02262  457 PGQTALETELKEHVKDRLAPyKYPRWIVFVD-----DLPKTATGKIQRFKLR 503
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
64-552 1.39e-25

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 114.49  E-value: 1.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSIIADAEPRLVLTTADLREPLlqmnaQLSAANAP 143
Cdd:TIGR03098   50 GERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKA-----EQVAHILADCNVRLLVTSSERLDLL-----HPALPGCH 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    144 QLLCV--------DQLDPAVAE--AWDE----------PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGF 203
Cdd:TIGR03098  120 DLRTLiivgdpahASEGHPGEEpaSWPKllalgdadppHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYL 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    204 GIGADDVIVSWLPLYHDMGLiGGLLQPIFSGVPCVLMSprYFLERPVrwLEAISQYGGT-VSGGPDFAYRLCSERVAESA 282
Cdd:TIGR03098  200 ENRPDDRLLAVLPLSFDYGF-NQLTTAFYVGATVVLHD--YLLPRDV--LKALEKHGITgLAAVPPLWAQLAQLDWPESA 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    283 ---LQRLDLSGWRVAFSGSEPIRqdslerfaekfaaSRFDASSFFACYGLAEATlfvtggqRGQGIPALAVDGEAlarnr 359
Cdd:TIGR03098  275 apsLRYLTNSGGAMPRATLSRLR-------------SFLPNARLFLMYGLTEAF-------RSTYLPPEEVDRRP----- 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    360 iaegeGSVlmccGRSQPEHAVLIVDAASGEVLGDDnVGEIWAAGPSIAHGYWRNPEASAKAFVERDGR--------TWLR 431
Cdd:TIGR03098  330 -----DSI----GKAIPNAEVLVLREDGSECAPGE-EGELVHRGALVAMGYWNDPEKTAERFRPLPPFpgelhlpeLAVW 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    432 TGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIErtvESEVPSARKGRVAAFAVTvDGEEGIGIAAEIGRGVQKSVPA 510
Cdd:TIGR03098  400 SGDTVRRdEEGFLYFVGRRDEMIKTSGYRVSPTEVE---EVAYATGLVAEAVAFGVP-DPTLGQAIVLVVTPPGGEELDR 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 15597620    511 QELIDSIRQAVAeAYQeAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:TIGR03098  476 AALLAECRARLP-NYM-VPALIHVRQ--ALPRNANGKIDRKA 513
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2793-3213 1.59e-25

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 112.40  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2793 TPIQHWFFDLplarrehwnqalllqpRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGE-WLAQhRPLREqellWHVPVQ 2871
Cdd:cd19542   21 LYFNHFVFDL----------------DSSVDVERLRNAWRQLVQRHDILRTVFVESSAEgTFLQ-VVLKS----LDPPIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2872 SFDECAELFAKAQRSLD----LEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQfaegaepALPA 2947
Cdd:cd19542   80 EVETDEDSLDALTRDLLddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2948 KTSAFRDWAgrlqAYAGSESLREELGWWQARLGG-QPVEWPCDRPQGDNREALAESvslrldpQRTRQLLQQAPAAYRTQ 3026
Cdd:cd19542  153 PAPPFSDYI----SYLQSQSQEESLQYWRKYLQGaSPCAFPSLSPKRPAERSLSST-------RRSLAKLEAFCASLGVT 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3027 VNDLLLTALARVLCRWSGQP----STLVqlegHGREALFDDIDLTrsVGWFTSAYPLR--LTPAQSPGESIKAIKEQ-LR 3099
Cdd:cd19542  222 LASLFQAAWALVLARYTGSRdvvfGYVV----SGRDLPVPGIDDI--VGPCINTLPVRvkLDPDWTVLDLLRQLQQQyLR 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3100 AVPHKGLGygvlryLADpavRQAMAALPTAPITFNYLGQFDQSFADALFQPLDQPTGPIHDEQAPLPNELSVDGQVYGGE 3179
Cdd:cd19542  296 SLPHQHLS------LRE---IQRALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDS 366
                        410       420       430
                 ....*....|....*....|....*....|....
gi 15597620 3180 LVLRWTYSRERYDARTVNELAQAYLAELQALIEH 3213
Cdd:cd19542  367 LKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3718-4242 1.78e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 114.87  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQ--RWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:PRK12583   23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3796 GHPTQRLTRIVELSRTLVLVCTQACR-------------EQALALFDELGCVDRPRL--------------LVWDEIQ-Q 3847
Cdd:PRK12583  103 AYRASELEYALGQSGVRWVICADAFKtsdyhamlqellpGLAEGQPGALACERLPELrgvvslapapppgfLAWHELQaR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3848 GEG------AEHDPQVYSG-PQNLAYviyTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDEND--VIAQTASQSFDIsV 3918
Cdd:PRK12583  183 GETvsrealAERQASLDRDdPINIQY---TSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDrlCVPVPLYHCFGM-V 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3919 WQFLAAPLFGArvAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQ 3995
Cdd:PRK12583  259 LANLGCMTVGA--CLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGnfdLSSLRTGIMAGAPCPIEVMRR 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3996 WLKRYPRIGLVNAYGPAECSDdvaffrVDLASTESTYLPIGSPT-DNNRLYLLGAGADDAFELVPLGAVGELCVAGTGVG 4074
Cdd:PRK12583  337 VMDEMHMAEVQIAYGMTETSP------VSLQTTAADDLERRVETvGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4075 RGYVGDPLRTAQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-A 4153
Cdd:PRK12583  411 KGYWNNPEATAESI-------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVfG 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4154 VQEGANGKYLVGY--LVPGetprssadspaglmveQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALP 4231
Cdd:PRK12583  484 VPDEKYGEEIVAWvrLHPG----------------HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
                         570
                  ....*....|.
gi 15597620  4232 ALDIGQMQNQA 4242
Cdd:PRK12583  548 EISIEELALPV 558
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
38-554 1.79e-25

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 114.92  E-value: 1.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    38 GVVLSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR-HHQ--------- 105
Cdd:PRK12492   47 GVTLSYAELERHSAAFAAylQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREmRHQfkdsgaral 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   106 -------ERLLSIIADAEPRLVLTT--ADLREPLL---------QMNAQLSAANAPQLLCVDQ-LDPAVAEAWDEPQVRP 166
Cdd:PRK12492  127 vylnmfgKLVQEVLPDTGIEYLIEAkmGDLLPAAKgwlvntvvdKVKKMVPAYHLPQAVPFKQaLRQGRGLSLKPVPVGL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   167 EHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFG-IGAD---------DVIVSWLPLYHDMGLIGGLLQPIFSGVP 236
Cdd:PRK12492  207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqLGPDgqplmkegqEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   237 CVLMS-PR---YFLERPVRW----LEAISQYGGTVSGGPDFayrlcservaesalQRLDLSGWRVAFSGSEPIRQDSLER 308
Cdd:PRK12492  287 NVLITnPRdipGFIKELGKWrfsaLLGLNTLFVALMDHPGF--------------KDLDFSALKLTNSGGTALVKATAER 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   309 FAEkfaasrFDASSFFACYGLAEATLFVTGGQRGQgipalavdgeaLARnriaegegsvLMCCGRSQPEHAVLIVDAASG 388
Cdd:PRK12492  353 WEQ------LTGCTIVEGYGLTETSPVASTNPYGE-----------LAR----------LGTVGIPVPGTALKVIDDDGN 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   389 EV-LGDDnvGEIWAAGPSIAHGYWRNPEASAKAFverDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIE 466
Cdd:PRK12492  406 ELpLGER--GELCIKGPQVMKGYWQQPEATAEAL---DAEGWFKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   467 RTVESEvpsarkGRVAAFAVtvdgeegIGIAAE-IGRGVQKSVPAQELIDSIRQAVA------EAYQeAPKVVALLNpgA 539
Cdd:PRK12492  481 DVVMAH------PKVANCAA-------IGVPDErSGEAVKLFVVARDPGLSVEELKAyckenfTGYK-VPKHIVLRD--S 544
                         570
                  ....*....|....*
gi 15597620   540 LPKTSSGKLQRSACR 554
Cdd:PRK12492  545 LPMTPVGKILRRELR 559
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
1154-1560 1.87e-25

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 113.31  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQa 1233
Cdd:cd05914    8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaegvtpicldslklDNwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDV 1313
Cdd:cd05914   87 ----------------------DE------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDK 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKAPVSfdvSVWECFWPLVTGcrLVLAAPGEHRD--PARLVELVRQFGVTTLHFVPPLLQLF---------------- 1375
Cdd:cd05914  133 ILSILPLH---HIYPLTFTLLLP--LLNGAHVVFLDkiPSAKIIALAFAQVTPTLGVPVPLVIEkifkmdiipkltlkkf 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1376 ---------------------IDEPGvaacGSLRRLFSGGEALPAELRnRVLQRL--PAVAlhnRYGPTETA--INVTHW 1430
Cdd:cd05914  208 kfklakkinnrkirklafkkvHEAFG----GNIKEFVIGGAKINPDVE-EFLRTIgfPYTI---GYGMTETApiISYSPP 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1431 QCRAEDGerspIGRPLGNVVCRVLDAEfnllPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRA 1510
Cdd:cd05914  280 NRIRLGS----AGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW-------FHTGDLG 344
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597620 1511 RWNADGVLEYLGRLDQQVKL-RGFRIEPEEIQARLLAQPGVAQAVVVIREG 1560
Cdd:cd05914  345 KIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEK 395
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
15-552 2.07e-25

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 113.80  E-value: 2.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    15 LRRRAVQEPERLALRflaeddGEGVVLSYRDLDLRARSIAAALQAH--AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAV 92
Cdd:PRK06839    8 IEKRAYLHPDRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElnVKKGERIAILSQNSLEYIVLLFAIAKVECIAV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    93 PAyppesARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEP-QVRPEHIAf 171
Cdd:PRK06839   82 PL-----NIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKnESASFIIC- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   172 lqYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdmglIGGL----LQPIFSGvpCVLMSPRYFle 247
Cdd:PRK06839  156 --YTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFH----IGGIglfaFPTLFAG--GVIIVPRKF-- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   248 RPVRWLEAISQYGGTVSGGPDFAYrlcsERVAESAL-QRLDLSGWRVAFSGSEPIRQDSLERFAEKfaasrfdASSFFAC 326
Cdd:PRK06839  226 EPTKALSMIEKHKVTVVMGVPTIH----QALINCSKfETTNLQSVRWFYNGGAPCPEELMREFIDR-------GFLFGQG 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   327 YGLAEA--TLFVtggqrgqgipalavdgeaLARNRIAEGEGSVlmccGRSQPEHAVLIVDAASGEVlGDDNVGEIWAAGP 404
Cdd:PRK06839  295 FGMTETspTVFM------------------LSEEDARRKVGSI----GKPVLFCDYELIDENKNKV-EVGEVGELLIRGP 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   405 SIAHGYWRNPEASAKAFveRDGrtWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVEsEVPSARKgrVAA 483
Cdd:PRK06839  352 NVMKEYWNRPDATEETI--QDG--WLCTGDLArVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVIN-KLSDVYE--VAV 424
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620   484 FAVTvDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEayQEAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:PRK06839  425 VGRQ-HVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAK--YKIPKEIVFLK--ELPKNATGKIQKAQ 488
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3738-4230 2.24e-25

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 113.88  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3738 RWSYAELNRRANRLGHALRAAGVGIDQPVALLA---ERGLDLLGMIVGsfkAGAGYLPLDPGHPTQRLT--------RIV 3806
Cdd:cd12119   25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPG---MGAVLHTINPRLFPEQIAyiinhaedRVV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3807 ELSRTLV-LVctQACREQA-------LALFDELGCVDRPRLLV--WDEIQQGEGAEHDPQVysgPQNLAYVI-YTSGSTG 3875
Cdd:cd12119  102 FVDRDFLpLL--EAIAPRLptvehvvVMTDDAAMPEPAGVGVLayEELLAAESPEYDWPDF---DENTAAAIcYTSGTTG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3876 LPKGVM------VEQAGMLNNQLSkvpyLELDENDVIaQTASQSFDISVWQF-LAAPLFGARvaIVPNAVAHDPQGLLAH 3948
Cdd:cd12119  177 NPKGVVyshrslVLHAMAALLTDG----LGLSESDVV-LPVVPMFHVNAWGLpYAAAMVGAK--LVLPGPYLDPASLAEL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3949 VGEQGITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIglVNAYGPAECSddvaffrvdl 4025
Cdd:cd12119  250 IEREGVTFAAGVPTVWQGLLDHleaNGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRV--IHAWGMTETS---------- 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4026 astestylPIGSPtdnNRL--YLLGAGADDAFEL-------VPL-----------------GAVGELCVAGTGVGRGYVG 4079
Cdd:cd12119  318 --------PLGTV---ARPpsEHSNLSEDEQLALrakqgrpVPGvelrivdddgrelpwdgKAVGELQVRGPWVTKSYYK 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4080 DPLRTAQAFVPHPFgapgerlyRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegan 4159
Cdd:cd12119  387 NDEESEALTEDGWL--------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAV------- 451
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 4160 gkylVGylVP----GETPRssadspAGLMVEQGAW--FERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd12119  452 ----IG--VPhpkwGERPL------AVVVLKEGATvtAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
64-554 2.75e-25

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 112.53  E-value: 2.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP--PESARRHHqerllsiIADAEPRLVLTtadlrepllqmnaqlsaan 141
Cdd:cd05971   31 GDRVGVFLSQGPECAIAHIAILRSGAIAVPLFAlfGPEALEYR-------LSNSGASALVT------------------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  142 apqllcvdqldpavaEAWDEPqvrpehiAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLyhDM 221
Cdd:cd05971   85 ---------------DGSDDP-------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPA--DW 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  222 GLIGGLLQPIFS----GVPCVLMSPRYFleRPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLsgwRVAFSG 297
Cdd:cd05971  141 AWIGGLLDVLLPslyfGVPVLAHRMTKF--DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKL---RAIATG 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  298 SEPIRQDSLERFAEKFAAsrfDASSFfacYGLAEATLFVTggqrgqgipalavDGEALARNRiaegEGSVlmccGRSQPE 377
Cdd:cd05971  216 GESLGEELLGWAREQFGV---EVNEF---YGQTECNLVIG-------------NCSALFPIK----PGSM----GKPIPG 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  378 HAVLIVDAAsGEVLGDDNVGEIWAAGP-SIAH-GYWRNPEASAKAFVErdgrTWLRTGDLGFL-RDGELFVTGRLKDMLI 454
Cdd:cd05971  269 HRVAIVDDN-GTPLPPGEVGEIAVELPdPVAFlGYWNNPSATEKKMAG----DWLLTGDLGRKdSDGYFWYVGRDDDVIT 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  455 VRGHNLYPQDIERTVESE----------VPSARKGR-VAAFAVTVDGEEGI-GIAAEIgrgvqksvpaQELIdsirqAVA 522
Cdd:cd05971  344 SSGYRIGPAEIEECLLKHpavlmaavvgIPDPIRGEiVKAFVVLNPGETPSdALAREI----------QELV-----KTR 408
                        490       500       510
                 ....*....|....*....|....*....|..
gi 15597620  523 EAYQEAPKVVAllNPGALPKTSSGKLQRSACR 554
Cdd:cd05971  409 LAAHEYPREIE--FVNELPRTATGKIRRRELR 438
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
2-556 2.87e-25

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 113.83  E-value: 2.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     2 MDAFELP--TTLVQALRRRAvqePERLALRFLAEDdgegVVLSYRDL-----DLRARsiaaALQAHAQLGDRAVLLFPSG 74
Cdd:PRK05852   10 MASDFGPriADLVEVAATRL---PEAPALVVTADR----IAISYRDLarlvdDLAGQ----LTRSGLLPGDRVALRMGSN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    75 PDYVAAFFGCLYAGVIAVPAYP--PESARRHHQERL--LSIIADAE-------------PRLVLTTADLREPLLQMNAQL 137
Cdd:PRK05852   79 AEFVVALLAASRADLVVVPLDPalPIAEQRVRSQAAgaRVVLIDADgphdraepttrwwPLTVNVGGDSGPSGGTLSVHL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   138 SAANAPQllcvdqldPAVAEawdePQ-VRPEHiAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLP 216
Cdd:PRK05852  159 DAATEPT--------PATST----PEgLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   217 LYHDMGLIGGLLQPIFSGvPCVLMSPRYFLERPVRWlEAISQYGGTVSGGPDFAYRLCSERVAESALQRlDLSGWRVAFS 296
Cdd:PRK05852  226 LYHGHGLIAALLATLASG-GAVLLPARGRFSAHTFW-DDIKAVGATWYTAVPTIHQILLERAATEPSGR-KPAALRFIRS 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   297 GSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVTggqrgqgipALAVDGEALARNRiAEGEGSVlmccGRSQP 376
Cdd:PRK05852  303 CSAPLTAETAQALQTEFAAPVVCA------FGMTEATHQVT---------TTQIEGIGQTENP-VVSTGLV----GRSTG 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   377 ehAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVerDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIV 455
Cdd:PRK05852  363 --AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT--DG--WLRTGDLGSLsAAGDLSIRGRIKELINR 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   456 RGHNLYPQDIERTVESEvPSARKgrVAAFAVTvDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAeAYqEAPkvVALL 535
Cdd:PRK05852  437 GGEKISPERVEGVLASH-PNVME--AAVFGVP-DQLYGEAVAAVIVPRESAPPTAEELVQFCRERLA-AF-EIP--ASFQ 508
                         570       580
                  ....*....|....*....|.
gi 15597620   536 NPGALPKTSSGKLQRSACRLR 556
Cdd:PRK05852  509 EASGLPHTAKGSLDRRAVAEQ 529
PRK09088 PRK09088
acyl-CoA synthetase; Validated
3722-4230 3.49e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 112.98  E-value: 3.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3722 QVAAHPQRIAAS--CLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPT 3799
Cdd:PRK09088    4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3800 QRLTRIVELSrtlvlvctqacrEQALALFDELGCVDRPRLLVWDE-IQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPK 3878
Cdd:PRK09088   84 SELDALLQDA------------EPRLLLGDDAVAAGRTDVEDLAAfIASADALEPADTPSIPPERVSLILFTSGTSGQPK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3879 GVMV-----EQAGMLNNQLSKVpyleldendviaqTASQSFdisvwqFLAAPLF---GARVAIVPnAVAH---------- 3940
Cdd:PRK09088  152 GVMLsernlQQTAHNFGVLGRV-------------DAHSSF------LCDAPMFhiiGLITSVRP-VLAVggsilvsngf 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3941 DPQGLLAHVGEQ--GITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPPELARQWLKRypRIGLVNAYGPAEcS 4015
Cdd:PRK09088  212 EPKRTLGRLGDPalGITHYFCVPQMAQAFRAQpgfDAAALRHLTALFTGGAPHAAEDILGWLDD--GIPMVDGFGMSE-A 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4016 DDVAFFRVDLASTESTYLPIGSPTDNNRLYLLGAGADDafelVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfga 4095
Cdd:PRK09088  289 GTVFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGND----CPAGVPGELLLRGPNLSPGYWRRPQATARAFT------ 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4096 pGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKylVGYLVPgeTPR 4174
Cdd:PRK09088  359 -GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVvGMADAQWGE--VGYLAI--VPA 433
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4175 SSADSPAglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK09088  434 DGAPLDL----------ERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
10-554 4.60e-25

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 113.31  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAG 88
Cdd:PRK06155   22 TLPAMLARQAERYPDRPLLVF------GGTRWTYAEAARAAaAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    89 VIAVPAyppESARRHHQerLLSIIADAEPRLVLTTADLREPLLQMNAQL------------SAANAPQLLCVDQLdPAVA 156
Cdd:PRK06155   96 AIAVPI---NTALRGPQ--LEHILRNSGARLLVVEAALLAALEAADPGDlplpavwlldapASVSVPAGWSTAPL-PPLD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   157 EAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLiGGLLQPIFSGVP 236
Cdd:PRK06155  170 APAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGAT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   237 CVLmSPRYfleRPVRWLEAISQYGGTVSG--GPDFAYRLCSERVAESALQRLdlsgwRVAFSGSEPIRqdSLERFAEKFA 314
Cdd:PRK06155  249 YVL-EPRF---SASGFWPAVRRHGATVTYllGAMVSILLSQPARESDRAHRV-----RVALGPGVPAA--LHAAFRERFG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   315 ASRFDAssffacYGLAEaTLFVTGGQRGQGIPalavdgealarnriaegeGSVlmccGRSQPEHAVLIVDaASGEVLGDD 394
Cdd:PRK06155  318 VDLLDG------YGSTE-TNFVIAVTHGSQRP------------------GSM----GRLAPGFEARVVD-EHDQELPDG 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   395 NVGEIW--AAGP-SIAHGYWRNPEASAKAFveRDgrTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVE 470
Cdd:PRK06155  368 EPGELLlrADEPfAFATGYFGMPEKTVEAW--RN--LWFHTGDRVVRDaDGWFRFVDRIKDAIRRRGENISSFEVEQVLL 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   471 SEvPSArkGRVAAFAVTVD-GEEGIGIAAEIGRGVqksvpAQELIDSIRQAVAE-AYQEAPKVVALLNpgALPKTSSGKL 548
Cdd:PRK06155  444 SH-PAV--AAAAVFPVPSElGEDEVMAAVVLRDGT-----ALEPVALVRHCEPRlAYFAVPRYVEFVA--ALPKTENGKV 513

                  ....*.
gi 15597620   549 QRSACR 554
Cdd:PRK06155  514 QKFVLR 519
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
1271-1618 5.01e-25

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 109.03  E-value: 5.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1271 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAApgeHRDP 1350
Cdd:cd17633    1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFNP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1351 ARLVELVRQFGVTTLHFVPPLLQLFI--DEPgvaaCGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETaiNVT 1428
Cdd:cd17633   78 KSWIRKINQYNATVIYLVPTMLQALArtLEP----ESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL--SFI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1429 HWQCRAEDGERSPIGRPLGNVVCRVLDAEfnllpAGVAGELCIGGLGLARGYLGRPALSAERFvadpfsaagerlYRTGD 1508
Cdd:cd17633  152 TYNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------MSVGD 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1509 RARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGavgaeaEAEQNQRLR 1587
Cdd:cd17633  215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgIPDARFGEIAVALYSG------DKLTYKQLK 288
                        330       340       350
                 ....*....|....*....|....*....|.
gi 15597620 1588 AALQAELPEYMVPTQLMRLAQMPLGPSGKLD 1618
Cdd:cd17633  289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3251-3672 5.65e-25

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 111.25  E-value: 5.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3251 YPLTPMQEGL-LLHTLLePGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVWNAGeTMLQVIHKPGRTRIE 3329
Cdd:cd20484    2 SPLSEGQKGLwMLQKMS-PEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDG-VPFQKIEPSKPLSFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3330 FLDWSELPEdghEERLQALHKREREAgFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGE 3409
Cdd:cd20484   80 EEDISSLKE---SEIIAYLREKAKEP-FVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3410 SR-PANLPTPPRYRDYIAWLQR----QDLEQSRRWWSESLRGfERPTL-VPSDRPflrehaGESGGMIVGDRYT-RLDAA 3482
Cdd:cd20484  156 GKqPTLASSPASYYDFVAWEQDmlagAEGEEHRAYWKQQLSG-TLPILeLPADRP------RSSAPSFEGQTYTrRLPSE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3483 DGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLfgvtvagrpVGMPEMQR-------TVGLFINSIPLRVQmpAA 3555
Cdd:cd20484  229 LSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDII---------VGMPTMGRpeerfdsLIGYFINMLPIRSR--IL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3556 GQRcTVREwlnrlFERNLELR-----EHEHLPLVAIQESSELPK---GQPLFDSLFVFENapvevsVLdraQSLNASSDS 3627
Cdd:cd20484  298 GEE-TFSD-----FIRKLQLTvldglDHAAYPFPAMVRDLNIPRsqaNSPVFQVAFFYQN------FL---QSTSLQQFL 362
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3628 GRTHTNFPLTVVCY---------------PGDDLGLHLSYDQRYFEAPTVERLLGEFKRL 3672
Cdd:cd20484  363 AEYQDVLSIEFVEGihqegeyelvlevyeQEDRFTLNIKYNPDLFDASTIERMMEHYVKL 422
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
2189-2691 6.36e-25

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 113.74  E-value: 6.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2189 HGLFAARVAASPQAPALTFAGQ-----TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAY 2263
Cdd:cd05968   64 EQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2264 VPLDPEYPLERLQYMIEDSGVRLLLShAALFEALGEL--PAGVARWCLEED------------------------GPALD 2317
Cdd:cd05968  144 VPIFSGFGKEAAATRLQDAEAKALIT-ADGFTRRGREvnLKEEADKACAQCptvekvvvvrhlgndftpakgrdlSYDEE 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2318 AEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAEDCELHFYSINFDAASERLLAPLLC 2396
Cdd:cd05968  223 KETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYfQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2397 GARVVLR--AQGQWGAEEICELIRAEGVSILGFTPSYGSQLA----QWLESQGRqLPVRMCITGGEALTGEhlqrirqaf 2470
Cdd:cd05968  303 GATMVLYdgAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKprgdAPVNAHDL-SSLRVLGSTGEPWNPE--------- 372
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2471 aPASFF------------NAYGPTETVVMPLACLAPERLEEGAASvpiGSVVGARvAYILDADLALVPqGATGELYVGGA 2538
Cdd:cd05968  373 -PWNWLfetvgkgrnpiiNYSGGTEISGGILGNVLIKPIKPSSFN---GPVPGMK-ADVLDESGKPAR-PEVGELVLLAP 446
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2539 --GLARGYHERPalsaERFVpDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVRE 2616
Cdd:cd05968  447 wpGMTRGFWRDE----DRYL-ETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2617 ALVLALDSP-SGKQLagyVASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPA 2691
Cdd:cd05968  522 SAAIGVPHPvKGEAI---VCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
64-556 7.67e-25

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 111.05  E-value: 7.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPPESARrhhqERLlsiiADAEPRLVLTTADLREpllqmnaqlsaa 140
Cdd:cd05969   25 GDRVFVLSPRSPELYFSMLGIGKIGAVICPlfsAFGPEAIR----DRL----ENSEAKVLITTEELYE------------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  141 napqllcvdqldpavaeawdepQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVI-----VSWL 215
Cdd:cd05969   85 ----------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYwctadPGWV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  216 plyhdMGLIGGLLQPIFSGVPCVLMSPRYfleRPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESAlQRLDLSGWRVAF 295
Cdd:cd05969  143 -----TGTVYGIWAPWLNGVTNVVYEGRF---DAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELA-RKYDLSSLRFIH 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  296 SGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEatlfvTGGQRGQGIPALAVDgealarnriaegEGSVlmccGRSQ 375
Cdd:cd05969  214 SVGEPLNPEAIRWGMEVFGVPIHDT------WWQTE-----TGSIMIANYPCMPIK------------PGSM----GKPL 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  376 PEHAVLIVDaASGEVLGDDNVGE--IWAAGPSIAHGYWRNPEASAKAFVerDGrtWLRTGDLGFL-RDGELFVTGRLKDM 452
Cdd:cd05969  267 PGVKAAVVD-ENGNELPPGTKGIlaLKPGWPSMFRGIWNDEERYKNSFI--DG--WYLTGDLAYRdEDGYFWFVGRADDI 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  453 LIVRGHNLYPQDIERTV-------ESEV---PSARKG-RVAAFAVTvdgEEGIGIAAEIGRgvqksvpaqELIDSIRQAV 521
Cdd:cd05969  342 IKTSGHRVGPFEVESALmehpavaEAGVigkPDPLRGeIIKAFISL---KEGFEPSDELKE---------EIINFVRQKL 409
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620  522 AEAYqeAPKVVALLNpgALPKTSSGKLQRSACRLR 556
Cdd:cd05969  410 GAHV--APREIEFVD--NLPKTRSGKIMRRVLKAK 440
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1763-2057 7.97e-25

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 110.66  E-value: 7.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1763 LDVARFEAALQALVQRHETLRTTFPSvDGVpvQRVHGDGGL-HMDWQDFSALDRDSRQQHLQTLADSEAHRPFDLESGPL 1841
Cdd:cd19535   37 LDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVPWyGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1842 LRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEafldDRESPLEPLPVQYLDYsVWQREWLESGERQRQLDY 1921
Cdd:cd19535  114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYE----DPGEPLPPLELSFRDY-LLAEQALRETAYERARAY 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1922 WKAQlgnehpLLELPGdRPRPPVQSHQGDL-------YRFDLSPELAERVRRFNAARGLTMFMTMTATLAALLYRYSGQQ 1994
Cdd:cd19535  189 WQER------LPTLPP-APQLPLAKDPEEIkeprftrREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQP 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620 1995 DLRIGAPVANR--IRPESEGLIGAFLNTQVLRCRLDGQMSVGELLEQVRQTVidgqsHQDLpfDH 2057
Cdd:cd19535  262 RFLLNLTLFNRlpLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQL-----WEDL--DH 319
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
2211-2689 9.94e-25

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 110.51  E-value: 9.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2211 TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVrlllsh 2290
Cdd:cd05912    1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2291 aalfealgelpagvarwcleedgpALDAedpaplaalsgpqhQAYLIYTSGSTGKPKGVAVSHGeiaMHCAAVIEC---F 2367
Cdd:cd05912   75 ------------------------KLDD--------------IATIMYTSGTTGKPKGVQQTFG---NHWWSAIGSalnL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2368 GMRAEDCEL------HF--YSInfdaaserLLAPLLCGARVVLraQGQWGAEEICELIRAEGVSILGFTPsygSQLAQWL 2439
Cdd:cd05912  114 GLTEDDNWLcalplfHIsgLSI--------LMRSVIYGMTVYL--VDKFDAEQVLHLINSGKVTIISVVP---TMLQRLL 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2440 ESQGRQLP--VRMCITGGEALTGEHLQRIRQAFAPasFFNAYGPTETVVMPLAcLAPERLEEgaasvPIGSVVGArvayI 2517
Cdd:cd05912  181 EILGEGYPnnLRCILLGGGPAPKPLLEQCKEKGIP--VYQSYGMTETCSQIVT-LSPEDALN-----KIGSAGKP----L 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2518 LDADL----ALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlyRTGDLVRLCDNGQVEYVGRIDHQVK 2593
Cdd:cd05912  249 FPVELkiedDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLII 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2594 IRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAgyVASAVAEQDEDAqaalrEALKTHLKQQLPDYMVPAHLLLL 2673
Cdd:cd05912  321 SGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVP--VAFVVSERPISE-----EELIAYCSEKLAKYKVPKKIYFV 393
                        490
                 ....*....|....*.
gi 15597620 2674 ASLPLTANGKLDRRAL 2689
Cdd:cd05912  394 DELPRTASGKLLRHEL 409
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1130-1556 1.32e-24

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 112.04  E-value: 1.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD 1209
Cdd:PRK07059   25 LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1210 PDYPSERLAYMLADSGVE---LLLTQAHLFERLPGAEGVTPICL----DSLKLDNW--------------PSQAPG---- 1264
Cdd:PRK07059  105 PLYTPRELEHQLKDSGAEaivVLENFATTVQQVLAKTAVKHVVVasmgDLLGFKGHivnfvvrrvkkmvpAWSLPGhvrf 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1265 --------------LHLHGDNLAYVIYTSGSTGQPKGVGNTHA-ALAERLQ---WMQATYTLDGDDvlmqkapvsfDVSV 1326
Cdd:PRK07059  185 ndalaegarqtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLQmeaWLQPAFEKKPRP----------DQLN 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1327 WECFWPL-----VTGCRLVLAAPGEH-------RDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRLFS 1392
Cdd:PRK07059  255 FVCALPLyhifaLTVCGLLGMRTGGRnilipnpRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1393 GGEALPAELRNRVLQrLPAVALHNRYGPTETAINVThwqC-RAEDGERS-PIGRPLGNVVCRVLDAEFNLLPAGVAGELC 1470
Cdd:PRK07059  335 GGMAVQRPVAERWLE-MTGCPITEGYGLSETSPVAT---CnPVDATEFSgTIGLPLPSTEVSIRDDDGNDLPLGEPGEIC 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1471 IGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGV 1550
Cdd:PRK07059  411 IRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGV 483

                  ....*.
gi 15597620  1551 AQAVVV 1556
Cdd:PRK07059  484 LEVAAV 489
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
3726-4230 1.43e-24

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 111.61  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3726 HPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH----PTQR 3801
Cdd:cd05906   27 GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPtydePNAR 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3802 LTRIVELSRTL--VLVCTQACREQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPQvySGPQNLAYVIYTSGSTGLPKG 3879
Cdd:cd05906  107 LRKLRHIWQLLgsPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQ--SRPDDLALLMLTSGSTGFPKA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3880 VMVEQAGMLNNQLSKVPYLELDENDVI-------------------AQTASQSFDISVWQFLAAPL--------FGARVA 3932
Cdd:cd05906  185 VPLTHRNILARSAGKIQHNGLTPQDVFlnwvpldhvgglvelhlraVYLGCQQVHVPTEEILADPLrwldlidrYRVTIT 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3933 IVPNAvahdpqgLLAHVGEQgitvLESVPSliqgmlaeERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGL-----VN 4007
Cdd:cd05906  265 WAPNF-------AFALLNDL----LEEIED--------GTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLppdaiRP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4008 AYGPAECSDDVAFFRVDLA---STESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRT 4084
Cdd:cd05906  326 AFGMTETCSGVIYSRSFPTydhSQALEFVSLGRPIPGVSMRIV----DDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEAN 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4085 AQAFVPHPFgapgerlYRTGDLARRRaDGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE---AAVAVQ-EGANG 4160
Cdd:cd05906  402 AEAFTEDGW-------FRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAFAVRdPGAET 473
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 4161 KYLVGYLVPGETPrssADSPAGLMveqgawfERIKQQLRADL---PDYMVPLHwlvLDRMPLNANGKLDRKAL 4230
Cdd:cd05906  474 EELAIFFVPEYDL---QDALSETL-------RAIRSVVSREVgvsPAYLIPLP---KEEIPKTSLGKIQRSKL 533
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
169-550 1.59e-24

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 107.97  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  169 IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSG---VPCVLMSPRYF 245
Cdd:cd17638    2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGatvVPVAVFDVDAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  246 LERPVRwlEAISqyggTVSGGPDFAYRLcserVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAasrFDAssFFA 325
Cdd:cd17638   82 LEAIER--ERIT----VLPGPPTLFQSL----LDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELG---FET--VLT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  326 CYGLAEAtlfvtggqrgqGIPALAvdgealarnRIAEGEGSVLMCCGRSQPEHAVLIVDAasgevlgddnvGEIWAAGPS 405
Cdd:cd17638  147 AYGLTEA-----------GVATMC---------RPGDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYN 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  406 IAHGYWRNPEASAKAFverDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIERTVeSEVPSARKgrVAAF 484
Cdd:cd17638  196 VMQGYLDDPEATAEAI---DADGWLHTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGAL-AEHPGVAQ--VAVI 269
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  485 AVTVDGEEGIGIAAEIGRGVQkSVPAQELIDSIRQAVAEAyqEAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd17638  270 GVPDERMGEVGKAFVVARPGV-TLTEEDVIAWCRERLANY--KVPRFVRFLD--ELPRNASGKVMK 330
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1728-1959 1.76e-24

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 110.03  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1728 PVPLSYSQQrmWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSVDGVPVQRVHGDGGlhmDW 1807
Cdd:cd19534    1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVE---EL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSALDRDSRQQHLQTLA-DSEAHRPFDLESGPLLRVCMVKMAEREHYLVVTLHHIVTEGWAMDIFARELGALYEAFLD 1886
Cdd:cd19534   76 FRLEVVDLSSLAQAAAIEAlAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620 1887 DRESPLEPLPvQYLDYSVWQREWLESGERQRQLDYWKAQLGneHPLLELPGDRPRppvqsHQGDL--YRFDLSPE 1959
Cdd:cd19534  156 GEPIPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPA--ADYWGLPKDPEQ-----TYGDArtVSFTLDEE 222
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
166-555 1.83e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 108.34  E-value: 1.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  166 PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYF 245
Cdd:cd05944    1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  246 lerpvRWLEAISQYGGTVSggpdfAYRLCSERVAESALQRL-------DLSGWRVAFSGSEPIRQDSLERFAEKFAASRF 318
Cdd:cd05944   81 -----RNPGLFDNFWKLVE-----RYRITSLSTVPTVYAALlqvpvnaDISSLRFAMSGAAPLPVELRARFEDATGLPVV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  319 DAssffacYGLAEATLFVT----GGQRGQGIPALAVDgEALARNRIAEGEGSVLMCCGrsqpehavlivdaasgevlgDD 394
Cdd:cd05944  151 EG------YGLTEATCLVAvnppDGPKRPGSVGLRLP-YARVRIKVLDGVGRLLRDCA--------------------PD 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  395 NVGEIWAAGPSIAHGYwRNPEASAKAFVErDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEV 473
Cdd:cd05944  204 EVGEICVAGPGVFGGY-LYTEGNKNAFVA-DG--WLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHP 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  474 PSARKGRVA---AFAvtvdGEEGIGIaAEIGRGVqkSVPAQELIDSIRQAVAEAyQEAPKVVALLNPgaLPKTSSGKLQR 550
Cdd:cd05944  280 AVAFAGAVGqpdAHA----GELPVAY-VQLKPGA--VVEEEELLAWARDHVPER-AAVPKHIEVLEE--LPVTAVGKVFK 349

                 ....*
gi 15597620  551 SACRL 555
Cdd:cd05944  350 PALRA 354
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
1132-1625 3.07e-24

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 111.07  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDP 1210
Cdd:PRK12492   28 EVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1211 DYPSERLAYMLADSGVELL---------------------LTQAHLFERLPGAEG-VTPICLDSLKldnwpSQAPGLHL- 1267
Cdd:PRK12492  108 LYTAREMRHQFKDSGARALvylnmfgklvqevlpdtgieyLIEAKMGDLLPAAKGwLVNTVVDKVK-----KMVPAYHLp 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1268 ------------HG----------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDD----------VLM 1315
Cdd:PRK12492  183 qavpfkqalrqgRGlslkpvpvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMI 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1316 QKAPV----SFDVSvweCFWPLVTGCRLVLAApgEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC--GSLRR 1389
Cdd:PRK12492  263 APLPLyhiyAFTAN---CMCMMVSGNHNVLIT--NPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLdfSALKL 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1390 LFSGGEALPAELRNRvLQRLPAVALHNRYGPTETAINVthwqCRAEDGERSPIGR---PLGNVVCRVLDAEFNLLPAGVA 1466
Cdd:PRK12492  338 TNSGGTALVKATAER-WEQLTGCTIVEGYGLTETSPVA----STNPYGELARLGTvgiPVPGTALKVIDDDGNELPLGER 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1467 GELCIGGLGLARGYLGRPALSAERFVAdpfsaagERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLA 1546
Cdd:PRK12492  413 GELCIKGPQVMKGYWQQPEATAEALDA-------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1547 QPGVAQAVVV----IREGVAGSQLVGYYTGAVGAEaeaeqnqRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK12492  486 HPKVANCAAIgvpdERSGEAVKLFVVARDPGLSVE-------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558

                  ...
gi 15597620  1623 PEP 1625
Cdd:PRK12492  559 RDI 561
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1132-1555 3.73e-24

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 110.28  E-value: 3.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1132 ELLERQLAQSAERVALEW--DGGS---LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYV 1206
Cdd:cd05970   21 DVVDAMAKEYPDKLALVWcdDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1207 PLDPDYPSERLAYMLADSGVELLLTQAH--LFERLPGAEGVTPI------CLDSLkLDNW---------------PSQAP 1263
Cdd:cd05970  101 PATHQLTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSkpklvwVGDPV-PEGWidfrkliknaspdfeRPTAN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1264 GlHLHGDNLAYVIYTSGSTGQPKGVGNTH----AALAERLQWmqatYTLDGDDVLMQKAPVSFDVSVWECF---WplVTG 1336
Cdd:cd05970  180 S-YPCGEDILLVYFSSGTTGMPKMVEHDFtyplGHIVTAKYW----QNVREGGLHLTVADTGWGKAVWGKIygqW--IAG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1337 CRlVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEP-GVAACGSLRRLFSGGEALPAELRNRVLQrLPAVALH 1415
Cdd:cd05970  253 AA-VFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDlSRYDLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLM 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1416 NRYGPTETAINVTHWQCRaedgERSP--IGRPLGNVVCRVLDAEFNLLPAGVAGELCIG-----GLGLARGYLGRPALSA 1488
Cdd:cd05970  331 EGFGQTETTLTIATFPWM----EPKPgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTA 406
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 1489 ERFvadpfsaaGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVV 1555
Cdd:cd05970  407 EVW--------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
PRK07638 PRK07638
acyl-CoA synthetase; Validated
1140-1622 4.07e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 109.87  E-value: 4.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1140 QSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDvRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAY 1219
Cdd:PRK07638   13 LQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1220 MLADSGVELLLTQAHLFERLPGAEGvtPIcldsLKLDNW--------PSQAPGLHLHGDNLaYVIYTSGSTGQPKGVGNT 1291
Cdd:PRK07638   92 RLAISNADMIVTERYKLNDLPDEEG--RV----IEIDEWkrmiekylPTYAPIENVQNAPF-YMGFTSGSTGKPKAFLRA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1292 HAALAERLQWMQATYTLDGDD-VLMQKAPVSfDVSVWECFWPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPP 1370
Cdd:PRK07638  165 QQSWLHSFDCNVHDFHMKREDsVLIAGTLVH-SLFLYGAISTLYVGQTVHLM---RKFIPNQVLDKLETENISVMYTVPT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1371 LLQLFIDEPGVAAcgSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAInVTHWQcrAEDGERSP--IGRPLGN 1448
Cdd:PRK07638  241 MLESLYKENRVIE--NKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALV--DEESERRPnsVGRPFHN 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1449 VVCRVLDAefnllpagvAGELCigglglARGYLGRPalsaerFVADPFSAAG----ERLYRTGDRARW---------NAD 1515
Cdd:PRK07638  316 VQVRICNE---------AGEEV------QKGEIGTV------YVKSPQFFMGyiigGVLARELNADGWmtvrdvgyeDEE 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1516 GVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGavgaeaeAEQNQRLRAALQ 1591
Cdd:PRK07638  375 GFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI---GVPdsywGEKPVAIIKG-------SATKQQLKSFCL 444
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  1592 AELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK07638  445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1156-1624 4.12e-24

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 110.31  E-value: 4.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHL 1235
Cdd:cd17642   47 YAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKG 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 FERLPGAEGVTPI-----------------CLDSLKLDNWPsqaPGLHLHG---------DNLAYVIYTSGSTGQPKGVG 1289
Cdd:cd17642  127 LQKVLNVQKKLKIiktiiildskedykgyqCLYTFITQNLP---PGFNEYDfkppsfdrdEQVALIMNSSGSTGLPKGVQ 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1290 NTHAALAERL-QWMQATY--TLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRdpaRLVELVRQFGVTTLH 1366
Cdd:cd17642  204 LTHKNIVARFsHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEE---LFLRSLQDYKVQSAL 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1367 FVPPLLQLFIDEPGVAA--CGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTET--AINVThwqcraEDGERSP- 1441
Cdd:cd17642  281 LVPTLFAFFAKSTLVDKydLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETtsAILIT------PEGDDKPg 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1442 -IGRPLGNVVCRVLDAEF-NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLE 1519
Cdd:cd17642  355 aVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFF 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1520 YLGRLDQQVKLRGFRIEPEEIQARLLAQP-----GVA-----------QAVVVIREGVAGSQ--LVGYYTGAVGAEaeae 1581
Cdd:cd17642  428 IVDRLKSLIKYKGYQVPPAELESILLQHPkifdaGVAgipdedagelpAAVVVLEAGKTMTEkeVMDYVASQVSTA---- 503
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 15597620 1582 qnQRLRAALQAelpeymvptqlmrLAQMPLGPSGKLDTRALPE 1624
Cdd:cd17642  504 --KRLRGGVKF-------------VDEVPKGLTGKIDRRKIRE 531
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
3719-4230 5.62e-24

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 109.52  E-value: 5.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3719 FEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHP 3798
Cdd:cd05923    9 RAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3799 TQRLTRIVELSRTLVLVCTQAcREQALALFDELGCVDRPRLLVWDEIQQGEG-AEHDPQvySGPQNLAYVIYTSGSTGLP 3877
Cdd:cd05923   89 AAELAELIERGEMTAAVIAVD-AQVMDAIFQSGVRVLALSDLVGLGEPESAGpLIEDPP--REPEQPAFVFYTSGTTGLP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3878 KGV-------------MVEQAGML----NNQLSKVPYLELdendviaqtasqsfdISVWQFLAAPLFGARVAIVPNAvaH 3940
Cdd:cd05923  166 KGAvipqraaesrvlfMSTQAGLRhgrhNVVLGLMPLYHV---------------IGFFAVLVAALALDGTYVVVEE--F 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3941 DPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQwLKRYPRIGLVNAYGPAECSDd 4017
Cdd:cd05923  229 DPADALKLIEQERVTSLFATPTHLDALAAAAEFAglkLSSLRHVTFAGATMPDAVLER-VNQHLPGEKVNIYGTTEAMN- 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4018 vafFRVDLASTESTylpIGSPTDNNRLYLLGAGADDAfELVPLGAVGELCVAGTG--VGRGYVGDPLRTAQAFVphpfga 4095
Cdd:cd05923  307 ---SLYMRDARTGT---EMRPGFFSEVRIVRIGGSPD-EALANGEEGELIVAAAAdaAFTGYLNQPEATAKKLQ------ 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4096 pgERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPR 4174
Cdd:cd05923  374 --DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVViGVADERWGQSVTACVVPREGTL 451
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 4175 SSadspaglmveqgawfERIKQQLRA-DLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05923  452 SA---------------DELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
1142-1622 6.58e-24

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 110.48  E-value: 6.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1142 AERVALEWDGGSLG------YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSE 1215
Cdd:cd05967   65 GDQIALIYDSPVTGtertytYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1216 RLAYMLADSGVELLLTQAHlferlpGAEGVTPICL-----DSLKLDNWPS---------------QAPGLHLHGDNL--- 1272
Cdd:cd05967  145 ELASRIDDAKPKLIVTASC------GIEPGKVVPYkplldKALELSGHKPhhvlvlnrpqvpadlTKPGRDLDWSELlak 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1273 --------------AYVIYTSGSTGQPKGVGNTHAALAERLQW-MQATYTLDGDDVLMQKAPVSFDVS-VWECFWPLVTG 1336
Cdd:cd05967  219 aepvdcvpvaatdpLYILYTSGTTGKPKGVVRDNGGHAVALNWsMRNIYGIKPGDVWWAASDVGWVVGhSYIVYGPLLHG 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1337 CRLVL--AAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACG------SLRRLFSGGEALPAELRNRVLQR 1408
Cdd:cd05967  299 ATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIkkydlsSLRTLFLAGERLDPPTLEWAENT 378
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1409 LPaVALHNRYGPTETAINVThwqCRAEDGERSPI-----GRPLGNVVCRVLDAEFNLLPAGVAGELCIGgLGLARGYLGR 1483
Cdd:cd05967  379 LG-VPVIDHWWQTETGWPIT---ANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLT 453
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1484 PALSAERFVADPFSAAgERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVA 1562
Cdd:cd05967  454 LWKNDERFKKLYLSKF-PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEcAVVGVRDELK 532
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 1563 GSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLA----QMPLGPSGKLDTRAL 1622
Cdd:cd05967  533 GQVPLGLVVLKEGVKITAEE---LEKELVALVREQIGPVAAFRLVifvkRLPKTRSGKILRRTL 593
PRK07470 PRK07470
acyl-CoA synthetase; Validated
2200-2664 7.23e-24

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 109.36  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2200 PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMI 2279
Cdd:PRK07470   21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2280 EDSGVRLLLSHAAlFEALGELPAGVA---RWCLEEDGPALDAEDPAPLAALSGPQHQ---------AYLIYTSGSTGKPK 2347
Cdd:PRK07470  101 EASGARAMICHAD-FPEHAAAVRAASpdlTHVVAIGGARAGLDYEALVARHLGARVAnaavdhddpCWFFFTSGTTGRPK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2348 GVAVSHGEIAM----HCAAVIEcfGMRAEDCELhfysinfdaaserLLAPL--------LC----GARVVLRAQGQWGAE 2411
Cdd:PRK07470  180 AAVLTHGQMAFvitnHLADLMP--GTTEQDASL-------------VVAPLshgagihqLCqvarGAATVLLPSERFDPA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2412 EICELIRAEGVSILGFTPSYGSQLAQWLESQGR-QLPVRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETV----V 2486
Cdd:PRK07470  245 EVWALVERHRVTNLFTVPTILKMLVEHPAVDRYdHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTgnitV 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2487 MPLACLAPerleEGAASVPIGSV----VGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaa 2562
Cdd:PRK07470  324 LPPALHDA----EDGPDARIGTCgferTGMEVQ-IQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2563 eggrlyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPsgkqLAGYVASAVAEQD 2642
Cdd:PRK07470  397 ------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP----VWGEVGVAVCVAR 466
                         490       500
                  ....*....|....*....|..
gi 15597620  2643 EDAQAAlREALKTHLKQQLPDY 2664
Cdd:PRK07470  467 DGAPVD-EAELLAWLDGKVARY 487
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
2195-2689 7.86e-24

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 108.90  E-value: 7.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2195 RVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLER 2274
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2275 LQYMIEDSGVRLLLSHAALFEALGELpaGVARWcleEDGPALDAEDPAPLAALSGPQhQAYLIYTSGSTGKPKGVAVSHG 2354
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKLIPG--ISVKF---AELMNGPKEEAEIQEEFDLDE-VATIMYTSGTTGKPKGVIQTYG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2355 EIAMHCAAVIECFGMRAEDCEL------HF--YSInfdaaserLLAPLLCGARVVLraQGQWGAEEICELIRAEGVSILG 2426
Cdd:PRK03640  165 NHWWSAVGSALNLGLTEDDCWLaavpifHIsgLSI--------LMRSVIYGMRVVL--VEKFDAEKINKLLQTGGVTIIS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2427 FTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPAsfFNAYGPTETVVMpLACLAPERLEEgaasvPI 2506
Cdd:PRK03640  235 VVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPV--YQSYGMTETASQ-IVTLSPEDALT-----KL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2507 GSV------VGARVAyildADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfaaEGGRLYrTGDLVRLCDNG 2580
Cdd:PRK03640  307 GSAgkplfpCELKIE----KDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-------QDGWFK-TGDIGYLDEEG 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2581 QVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAgyVASAVAEQDEDAqaalrEALKTHLKQQ 2660
Cdd:PRK03640  375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVP--VAFVVKSGEVTE-----EELRHFCEEK 447
                         490       500
                  ....*....|....*....|....*....
gi 15597620  2661 LPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK03640  448 LAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK07470 PRK07470
acyl-CoA synthetase; Validated
11-563 8.05e-24

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 109.36  E-value: 8.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    11 LVQALRRRAVQEPERLALrflaeDDGEGVVlSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGV 89
Cdd:PRK07470    9 LAHFLRQAARRFPDRIAL-----VWGDRSW-TWREIDARVDALAAALAARgVRKGDRILVHSRNCNQMFESMFAAFRLGA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    90 IAVPA----YPPESARRHHQerllsiiadAEPRLVLTTADLREpllqmNAQLSAANAPQLLCV---------DQLDPAVA 156
Cdd:PRK07470   83 VWVPTnfrqTPDEVAYLAEA---------SGARAMICHADFPE-----HAAAVRAASPDLTHVvaiggaragLDYEALVA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   157 EAWDEP----QVRPEHIAFLQYTSGSTALPKGVQVSHGNL---VANEV--LIRrgfGIGADDVIVSWLPLYHDMGlIGGL 227
Cdd:PRK07470  149 RHLGARvanaAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMafvITNHLadLMP---GTTEQDASLVVAPLSHGAG-IHQL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   228 LQpIFSGVPCVLMSPRYFlERPVRWlEAISQYG----GTVsggPDFAYRLcserVAESALQRLDLSGWR-VAFSGSEPIR 302
Cdd:PRK07470  225 CQ-VARGAATVLLPSERF-DPAEVW-ALVERHRvtnlFTV---PTILKML----VEHPAVDRYDHSSLRyVIYAGAPMYR 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   303 QDslerfaEKFAASRFdASSFFACYGLAEATLFVTGgqrgqgIPALAVDGEalarnriaEGEGSVLMCCGRSQPEHAVLI 382
Cdd:PRK07470  295 AD------QKRALAKL-GKVLVQYFGLGEVTGNITV------LPPALHDAE--------DGPDARIGTCGFERTGMEVQI 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   383 VDAAsGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLY 461
Cdd:PRK07470  354 QDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF--RDG--WFRTGDLGHLdARGFLYITGRASDMYISGGSNVY 428
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   462 PQDIERTVeSEVPSARKGRVAAFAVTVDGEegIGIAAEIGRGVQkSVPAQELIDSIRQAVAEaYQeAPKVVALLNpgALP 541
Cdd:PRK07470  429 PREIEEKL-LTHPAVSEVAVLGVPDPVWGE--VGVAVCVARDGA-PVDEAELLAWLDGKVAR-YK-LPKRFFFWD--ALP 500
                         570       580
                  ....*....|....*....|...
gi 15597620   542 KTSSGKLQRSACRLRLED-GSLD 563
Cdd:PRK07470  501 KSGYGKITKKMVREELEErGLLD 523
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
10-550 8.21e-24

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 108.75  E-value: 8.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   10 TLVQALRRRAVQEPERLALrflaEDDGEGVVLSYRDLDLR-ARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAG 88
Cdd:cd05923    2 TVFEMLRRAASRAPDACAI----ADPARGLRLTYSELRARiEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   89 VIAVPAYPpesarRHHQERLLSIIADAEPRLVLTTADlREPllqmnAQLSAANAPQLLCVDQLD----PAVA-EAWDEPQ 163
Cdd:cd05923   78 AVPALINP-----RLKAAELAELIERGEMTAAVIAVD-AQV-----MDAIFQSGVRVLALSDLVglgePESAgPLIEDPP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  164 VRPEHIAFLQYTSGSTALPKGVQVSHgNLVANEVLI---RRGFGIGADDVIVSWLPLYHDMGLIGGLLQP-IFSGVPCVl 239
Cdd:cd05923  147 REPEQPAFVFYTSGTTGLPKGAVIPQ-RAAESRVLFmstQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAAlALDGTYVV- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  240 msPRYFleRPVRWLEAISQYGGT-VSGGPDFAYRLcserVAESALQRLDLSGWR-VAFSGSEpIRQDSLERFaekfaaSR 317
Cdd:cd05923  225 --VEEF--DPADALKLIEQERVTsLFATPTHLDAL----AAAAEFAGLKLSSLRhVTFAGAT-MPDAVLERV------NQ 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  318 FDASSFFACYGLAEATLFVtggqrgqgipalaVDGEALARNRIAEGEGSvlmccgrsqpEHAVLIVDAASGEVLGDDNVG 397
Cdd:cd05923  290 HLPGEKVNIYGTTEAMNSL-------------YMRDARTGTEMRPGFFS----------EVRIVRIGGSPDEALANGEEG 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  398 EIWAAGPSIA--HGYWRNPEASAKAFVERdgrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERtVESEVP 474
Cdd:cd05923  347 ELIVAAAADAafTGYLNQPEATAKKLQDG----WYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIER-VLSRHP 421
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  475 SARKGRVAAFAvtvDGEEGIGIAAEIGRgvQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd05923  422 GVTEVVVIGVA---DERWGQSVTACVVP--REGTLSADELDQFCRASELADFKRPRRYFFLD--ELPKNAMNKVLR 490
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2165-2689 8.70e-24

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 109.45  E-value: 8.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2165 FAAEERKQLLLAGTAGEAGLQDtlhgLFAARVAASPQAPALT-FAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLAL 2243
Cdd:PRK06087    6 FNEQRRAAYRQQGYWGDASLAD----YWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2244 ERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLL------------------------LSHAALFEALGE 2299
Cdd:PRK06087   82 PGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFfaptlfkqtrpvdlilplqnqlpqLQQIVGVDKLAP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2300 LPAGVARWCLEEDGPALDAEDPAPLAALsgpqhqAYLIYTSGSTGKPKGVAVSHGEIamhcaavieCFGMRAEDCELHFY 2379
Cdd:PRK06087  162 ATSSLSLSQIIADYEPLTTAITTHGDEL------AAVLFTSGTEGLPKGVMLTHNNI---------LASERAYCARLNLT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2380 S--INFDAAS--------ERLLAPLLCGARVVLraQGQWGAEEICELIRAEGVS-ILGFTPsYGSQLAQWLESQGRQLP- 2447
Cdd:PRK06087  227 WqdVFMMPAPlghatgflHGVTAPFLIGARSVL--LDIFTPDACLALLEQQRCTcMLGATP-FIYDLLNLLEKQPADLSa 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2448 VRMCITGGEALTGEHLQRIRQAfaPASFFNAYGPTE----TVVMPLACLAPERLEEGAAsvpigsVVGARVAyILDADLA 2523
Cdd:PRK06087  304 LRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTEssphAVVNLDDPLSRFMHTDGYA------AAGVEIK-VVDEARK 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2524 LVPQGATGELYVGGAGLARGYHERPALSAErfVPDpfaAEGgrLYRTGDLVRLCDNGQVEYVGRiDHQVKIRGFR-IELG 2602
Cdd:PRK06087  375 TLPPGCEGEEASRGPNVFMGYLDEPELTAR--ALD---EEG--WYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSR 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2603 EIEARLLEHPQVREALVLAL-DSPSGKQLAGYVASAVAEQD---EDAQAALREalKTHLKQQLPDYMVPAHLLLLaslpl 2678
Cdd:PRK06087  447 EVEDILLQHPKIHDACVVAMpDERLGERSCAYVVLKAPHHSltlEEVVAFFSR--KRVAKYKYPEHIVVIDKLPR----- 519
                         570
                  ....*....|.
gi 15597620  2679 TANGKLDRRAL 2689
Cdd:PRK06087  520 TASGKIQKFLL 530
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
13-548 9.34e-24

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 109.59  E-value: 9.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   13 QALRRRAVQEPERLALRFLAEDDGEGVVLSYRDL-DLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
Cdd:cd17634   57 NALDRHLRENGDRTAIIYEGDDTSQSRTISYRELhREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   92 VPAY----PPESARRhhqerllsiIADAEPRLVLTTADLREP-----LLQMNAQLSAANAP---QLLCVD------QLDP 153
Cdd:cd17634  137 SVIFggfaPEAVAGR---------IIDSSSRLLITADGGVRAgrsvpLKKNVDDALNPNVTsveHVIVLKrtgsdiDWQE 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  154 AVAEAWDE------PQVRPEHIA-----FLQYTSGSTALPKGV-QVSHGNLVANEVLIRRGFGIGADDVI-----VSWLp 216
Cdd:cd17634  208 GRDLWWRDliakasPEHQPEAMNaedplFILYTSGTTGKPKGVlHTTGGYLVYAATTMKYVFDYGPGDIYwctadVGWV- 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  217 LYHDMGLIGGLL----QPIFSGVPcvlMSPryfleRPVRWLEAISQYGGTVSGGPDFAYRLCSeRVAESALQRLDLSGWR 292
Cdd:cd17634  287 TGHSYLLYGPLAcgatTLLYEGVP---NWP-----TPARMWQVVDKHGVNILYTAPTAIRALM-AAGDDAIEGTDRSSLR 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  293 VAFSGSEPIRQDSLERFAEKFAASRFDASSFfacYGLAEATLFVTGGQRGQ-----GIPALAVDGEALArnrIAEGEGsv 367
Cdd:cd17634  358 ILGSVGEPINPEAYEWYWKKIGKEKCPVVDT---WWQTETGGFMITPLPGAielkaGSATRPVFGVQPA---VVDNEG-- 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  368 lmccgrsQPEHAvlivdAASGEVLgddnVGEIWaagPSIAHGYWRNPEASAKAFVERDGRTWLrTGDLGFL-RDGELFVT 446
Cdd:cd17634  430 -------HPQPG-----GTEGNLV----ITDPW---PGQTRTLFGDHERFEQTYFSTFKGMYF-SGDGARRdEDGYYWIT 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  447 GRLKDMLIVRGHNLYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGEEgigiaaeigrgvqksvPAQELID 515
Cdd:cd17634  490 GRSDDVINVAGHRLGTAEIESVLVAHpkvaeaavvgIPHAIKGqAPYAYVVLNHGVE----------------PSPELYA 553
                        570       580       590
                 ....*....|....*....|....*....|...
gi 15597620  516 SIRQAVAEAYQEAPKVVALLNPGALPKTSSGKL 548
Cdd:cd17634  554 ELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
1137-1617 1.09e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 109.10  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1137 QLAQSA----ERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:PRK07786   22 QLARHAlmqpDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1213 PSERLAYMLADSGVELLLTQAHLFERLPGAEGVTP----------------ICLDSLKLDNWPSQAPgLHLHGDNLAYVI 1276
Cdd:PRK07786  102 TPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPllstvvvaggssddsvLGYEDLLAEAGPAHAP-VDIPNDSPALIM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1277 YTSGSTGQPKGVGNTHAALAErlQWMQATYT--LD-GDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHrDPARL 1353
Cdd:PRK07786  181 YTSGTTGRPKGAVLTHANLTG--QAMTCLRTngADiNSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1354 VELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLRRLFSGGEAlPAE--LRNRVLQRLPAVALHNRYGPTETAiNVThwq 1431
Cdd:PRK07786  258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAA-PASdtLLRQMAATFPEAQILAAFGQTEMS-PVT--- 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1432 CRAeDGE-----RSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFvadpfsAAGerLYRT 1506
Cdd:PRK07786  333 CML-LGEdairkLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG--WFHS 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1507 GDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQlVGYYTGAVGAEAEAEQNQRL 1586
Cdd:PRK07786  404 GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGE-VPVAVAAVRNDDAALTLEDL 482
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  1587 RAALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK07786  483 AEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
3739-4235 1.10e-23

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 107.59  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPL----DPGHPTQRLtrivELSRTLVL 3814
Cdd:cd05969    1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDRL----ENSEAKVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3815 VCTQACREQalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSK 3894
Cdd:cd05969   77 ITTEELYER-----------------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTG 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3895 VPYLELDENDVIAQTASQSFDISVWQFLAAPLFGArVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAE---- 3970
Cdd:cd05969  122 KYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNG-VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdel 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3971 -ERQALDGLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPAECSDDVaffrvdLASTESTYLPIGS---PtdnnrlyL 4046
Cdd:cd05969  201 aRKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSIM------IANYPCMPIKPGSmgkP-------L 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4047 LGAGA---DDAFELVPLGAVGELCV-AG-TGVGRGYVGDPLRTAQAFVphpfgapgERLYRTGDLARRRADGVLEYVGRI 4121
Cdd:cd05969  267 PGVKAavvDENGNELPPGTKGILALkPGwPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRA 338
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4122 DHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLV--PGETPRSSadspagLMVEqgawferIKQQL 4198
Cdd:cd05969  339 DDIIKTSGHRVGPFEVESALMEHPAVAEAGViGKPDPLRGEIIKAFISlkEGFEPSDE------LKEE-------IINFV 405
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15597620 4199 RADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDI 4235
Cdd:cd05969  406 RQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3703-4237 1.22e-23

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 109.07  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3703 NRSARDYPLEQGYVR------LFEAQVAAHPQRIAAS-CLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLD 3775
Cdd:PRK06087    7 NEQRRAAYRQQGYWGdasladYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3776 LLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQ------------ACREQA-----LALFDELGcVDRPR 3838
Cdd:PRK06087   87 FTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvdlilPLQNQLpqlqqIVGVDKLA-PATSS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3839 LLVWDEIQQGEGAEHDPQVYSgpQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISV 3918
Cdd:PRK06087  166 LSLSQIIADYEPLTTAITTHG--DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3919 WQFLAAP-LFGARVAIVPNavaHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELAR 3994
Cdd:PRK06087  244 LHGVTAPfLIGARSVLLDI---FTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQpadLSALRFFLCGGTTIPKKVAR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3995 QWLKRypRIGLVNAYGpaecsddvaffrvdlaSTES---TYLPIGSPTDNNRLYLLGAGA-------DDAFELVPLGAVG 4064
Cdd:PRK06087  321 ECQQR--GIKLLSVYG----------------STESsphAVVNLDDPLSRFMHTDGYAAAgveikvvDEARKTLPPGCEG 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4065 ELCVAGTGVGRGYVGDPLRTAQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGRiDHQVKIRGFR-IELGEIEARLHE 4143
Cdd:PRK06087  383 EEASRGPNVFMGYLDEPELTARAL-------DEEGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQ 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4144 RADVREAAV-AVQEGANGKYLVGYLVPGETPRSsadspagLMVEQ-GAWFERIKqqlradLPDYMVPLHWLVLDRMPLNA 4221
Cdd:PRK06087  455 HPKIHDACVvAMPDERLGERSCAYVVLKAPHHS-------LTLEEvVAFFSRKR------VAKYKYPEHIVVIDKLPRTA 521
                         570
                  ....*....|....*.
gi 15597620  4222 NGKLdRKALPALDIGQ 4237
Cdd:PRK06087  522 SGKI-QKFLLRKDIMR 536
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
2208-2689 1.23e-23

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 108.91  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2208 AGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL-------DPEYPLERLQYMIE 2280
Cdd:cd05906   36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHIWQ 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2281 DSGVRLLLSHAALFEALGEL--PAGVARWCLEEDGPALDAEDPAPLAAlSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAM 2358
Cdd:cd05906  116 LLGSPVVLTDAELVAEFAGLetLSGLPGIRVLSIEELLDTAADHDLPQ-SRPDDLALLMLTSGSTGFPKAVPLTHRNILA 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2359 HCAAVIECFGMRAEDCELHFysINFD---AASERLLAPLLCGARVV-------LRAQGQWgaeeiCELIRAEGVSIlGFT 2428
Cdd:cd05906  195 RSAGKIQHNGLTPQDVFLNW--VPLDhvgGLVELHLRAVYLGCQQVhvpteeiLADPLRW-----LDLIDRYRVTI-TWA 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2429 PSYG-SQLAQWLESQGRQ----LPVRMCITGGEAL---TGEHLQRIRQAF-APASFFN-AYGPTETVVMPLACLAPERLE 2498
Cdd:cd05906  267 PNFAfALLNDLLEEIEDGtwdlSSLRYLVNAGEAVvakTIRRLLRLLEPYgLPPDAIRpAFGMTETCSGVIYSRSFPTYD 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2499 EGAAS--VPIGSVV-GARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVR 2575
Cdd:cd05906  347 HSQALefVSLGRPIpGVSMR-IVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDLGF 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2576 LcDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL---DSPSGKQLAGYVASAVAEQDeDAQAALREA 2652
Cdd:cd05906  419 L-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFavrDPGAETEELAIFFVPEYDLQ-DALSETLRA 496
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15597620 2653 LKTHLKQQL---PDYMVpahLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05906  497 IRSVVSREVgvsPAYLI---PLPKEEIPKTSLGKIQRSKL 533
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3727-4230 1.41e-23

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 108.05  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:PRK06145   16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3807 ELSRTLVLVCTQ-----ACREQALALFDELGCVDRPRLlvwdeiQQGeGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVM 3881
Cdd:PRK06145   96 GDAGAKLLLVDEefdaiVALETPKIVIDAAAQADSRRL------AQG-GLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3882 VEQAGMLNNQLSKVPYLELDENDVIAQTAS----QSFDISVWQFLAAplfGARVAIVPNavaHDPQGLLAHVGEQGITVL 3957
Cdd:PRK06145  169 HSYGNLHWKSIDHVIALGLTASERLLVVGPlyhvGAFDLPGIAVLWV---GGTLRIHRE---FDPEAVLAAIERHRLTCA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3958 ESVPSLIQGMLA---EERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAE-CSDDVaffrvdLASTESTYL 4033
Cdd:PRK06145  243 WMAPVMLSRVLTvpdRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTEtCSGDT------LMEAGREIE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4034 PIGSpTDNNRLYLLGAGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlyRTGDLARRRADG 4113
Cdd:PRK06145  317 KIGS-TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4114 VLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLV--PGETPRssadspaglmveqgaw 4190
Cdd:PRK06145  388 FLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAViGVHDDRWGERITAVVVlnPGATLT---------------- 451
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 15597620  4191 FERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK06145  452 LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2810-3210 1.73e-23

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 106.69  E-value: 1.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2810 WNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFDECAE------LFAKA 2883
Cdd:cd19539   24 YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPDSDRErrleelLRERE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2884 QRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYA 2963
Cdd:cd19539  104 SRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPELRQQYKEYAAWQREAL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2964 GSESLREELGWWQARLGG-QPVEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAyRTQVNDLLLTALARVLCRW 3042
Cdd:cd19539  184 AAPRAAELLDFWRRRLRGaEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRA-RSSLFMVLLAAYCVLLRRY 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3043 SGQPSTLVQLEGHGRealfDDIDLTRSVGWFTSAYPLR--LTPAQSPGESIKAI-KEQLRAVPHKGLGYGvlRYLADPAV 3119
Cdd:cd19539  263 TGQTDIVVGTPVAGR----NHPRFESTVGFFVNLLPLRvdVSDCATFRDLIARVrKALVDAQRHQELPFQ--QLVAELPV 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3120 RQAMAALPTAPITFNYlgqfdQSFADALFQ-PLDQPTGPIHDEQAPLPNELSVDGQVYGGELVLRWTYSRERYDARTVNE 3198
Cdd:cd19539  337 DRDAGRHPLVQIVFQV-----TNAPAGELElAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQG 411
                        410
                 ....*....|..
gi 15597620 3199 LAQAYLAELQAL 3210
Cdd:cd19539  412 FLADYLQVLRQL 423
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3737-4230 1.89e-23

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 107.13  E-value: 1.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLdpghptqrltrivelsrtlvlvc 3816
Cdd:cd05971    5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL----------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3817 tqacreqaLALFDELGCVDR-----PRLLVWDeiqqgegaehdpqvysGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNq 3891
Cdd:cd05971   62 --------FALFGPEALEYRlsnsgASALVTD----------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGH- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3892 lskVPYLELDEN------DVIAQTASQS-----FDIsvwqFLAAPLFGARVaivpnaVAH-----DPQGLLAHVGEQGIT 3955
Cdd:cd05971  117 ---LPGVQFPFNlfprdgDLYWTPADWAwigglLDV----LLPSLYFGVPV------LAHrmtkfDPKAALDLMSRYGVT 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3956 VLESVPSLIQGMLAEERQALD---GLRWMLPTGEAMPPELArQWLKRYPRIGLVNAYGPAEC----SDDVAFFRVDLASt 4028
Cdd:cd05971  184 TAFLPPTALKMMRQQGEQLKHaqvKLRAIATGGESLGEELL-GWAREQFGVEVNEFYGQTECnlviGNCSALFPIKPGS- 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4029 estylpIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCV--AGTGVGRGYVGDPLRTAQAFVphpfgapGERLyRTGDL 4106
Cdd:cd05971  262 ------MGKPIPGHRVAIV----DDNGTPLPPGEVGEIAVelPDPVAFLGYWNNPSATEKKMA-------GDWL-LTGDL 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4107 ARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAA-VAVQEGANGKYLVGYLV--PGETPRSsadspagl 4183
Cdd:cd05971  324 GRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAvVGIPDPIRGEIVKAFVVlnPGETPSD-------- 395
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 4184 mveqgAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05971  396 -----ALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1154-1592 2.11e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 107.16  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLtqa 1233
Cdd:cd05910    3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaeGVTpicldslkldnwpsqapglhlHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDV 1313
Cdd:cd05910   80 ----------GIP---------------------KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKAPvsfdvsVWECFWPLVtGCRLVLAAPGEHR----DPARLVELVRQFGVTTLHFVPPLLQLfidepgVAACG---- 1385
Cdd:cd05910  129 DLATFP------LFALFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLER------VARYCaqhg 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1386 ----SLRRLFSGGEALPAELRNRVLQRLPAVA-LHNRYGPTEtAINVTHWQCRAEDGERSP---------IGRPLGNVVC 1451
Cdd:cd05910  196 itlpSLRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATE-ALPVSSIGSRELLATTTAatsggagtcVGRPIPGVRV 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1452 RVLDA---------EFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPfsaAGERLYRTGDRARWNADGVLEYLG 1522
Cdd:cd05910  275 RIIEIddepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCG 351
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 1523 RLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIreGVAGSQL-VGYYTGAVGAEAEAEQ-NQRLRAALQA 1592
Cdd:cd05910  352 RKAHRVITTGGTLYTEPVERVFNTHPGVRRsALVGV--GKPGCQLpVLCVEPLPGTITPRARlEQELRALAKD 422
PRK07787 PRK07787
acyl-CoA synthetase; Validated
9-552 2.37e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 107.00  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPErlALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHaqlgDR-AVLLFPSgPDYVAAFFGCLYA 87
Cdd:PRK07787    2 ASLNPAAVAAAADIAD--AVRI------GGRVLSRSDLAGAATAVAERVAGA----RRvAVLATPT-LATVLAVVGALIA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    88 GVIAVPAyPPESA---RRHhqerllsIIADAEPRLVLTTADlrepllqmnaqlsaaNAPQLLCVDQLDPAVAEAWDEPQV 164
Cdd:PRK07787   69 GVPVVPV-PPDSGvaeRRH-------ILADSGAQAWLGPAP---------------DDPAGLPHVPVRLHARSWHRYPEP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   165 RPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCV-LMSPr 243
Cdd:PRK07787  126 DPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhTGRP- 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   244 yfleRPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESAlqrldLSGWRVAFSGSEPIRQDSLERFAE---KFAASRfda 320
Cdd:PRK07787  205 ----TPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-----LRGARLLVSGSAALPVPVFDRLAAltgHRPVER--- 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   321 ssffacYGLAEaTLFVTG----GQRGQGIPALAVDGealARNRIAEGEGSVLMCCGRSqpehavlivdaasgevlgddnV 396
Cdd:PRK07787  273 ------YGMTE-TLITLStradGERRPGWVGLPLAG---VETRLVDEDGGPVPHDGET---------------------V 321
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   397 GEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFLR-DGELFVTGRLK-DMLIVRGHNLYPQDIErTVESEVP 474
Cdd:PRK07787  322 GELQVRGPTLFDGYLNRPDATAAAFTA-DG--WFRTGDVAVVDpDGMHRIVGREStDLIKSGGYRIGAGEIE-TALLGHP 397
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   475 SARKG------------RVAAFAVTVDGeegigiaaeigrgvqksVPAQELIDSIrqAVAEAYQEAPKVVALLNpgALPK 542
Cdd:PRK07787  398 GVREAavvgvpdddlgqRIVAYVVGADD-----------------VAADELIDFV--AQQLSVHKRPREVRFVD--ALPR 456
                         570
                  ....*....|
gi 15597620   543 TSSGKLQRSA 552
Cdd:PRK07787  457 NAMGKVLKKQ 466
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
13-552 2.66e-23

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 106.24  E-value: 2.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   13 QALRRRAVQEPERLALrflaedDGEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
Cdd:cd17653    1 DAFERIAAAHPDAVAV------ESLGGSLTYGELDAASNALANRlLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   92 VP---AYPpeSARRHHqerllsIIADAEPRLVLTTAdlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEH 168
Cdd:cd17653   75 VPldaKLP--SARIQA------ILRTSGATLLLTTD----------------------------------------SPDD 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  169 IAFLQYTSGSTALPKGVQVSHGNLVAnevlirrgfgigaddvIVSWLPlyHDMGL-----IGGLLQPIFSgvPCVLMspr 243
Cdd:cd17653  107 LAYIIFTSGSTGIPKGVMVPHRGVLN----------------YVSQPP--ARLDVgpgsrVAQVLSIAFD--ACIGE--- 163
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  244 YFlerpvrwleAISQYGGT-VSGGP--DFAY--RLCSERVAE-SALQRLDLSGW---RVAFSGSEPIRQDSLERFAEkfa 314
Cdd:cd17653  164 IF---------STLCNGGTlVLADPsdPFAHvaRTVDALMSTpSILSTLSPQDFpnlKTIFLGGEAVPPSLLDRWSP--- 231
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  315 aSRfdasSFFACYGLAEATLFVTggqrgqgipalavDGEALARNRIAegegsvlmcCGRSQPEHAVLIVDAASGEVLgDD 394
Cdd:cd17653  232 -GR----RLYNAYGPTECTISST-------------MTELLPGQPVT---------IGKPIPNSTCYILDADLQPVP-EG 283
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  395 NVGEIWAAGPSIAHGYWRNPEASAKAFVE---RDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVE 470
Cdd:cd17653  284 VVGEICISGVQVARGYLGNPALTASKFVPdpfWPGSRMYRTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVL 363
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  471 SEVPSARkgRVAAFAVTvdgeegigiaaeiGRGVQKSVPAQELIDSIRQAVAE---AYQEAPKVVALlnpGALPKTSSGK 547
Cdd:cd17653  364 QSQPEVT--QAAAIVVN-------------GRLVAFVTPETVDVDGLRSELAKhlpSYAVPDRIIAL---DSFPLTANGK 425

                 ....*
gi 15597620  548 LQRSA 552
Cdd:cd17653  426 VDRKA 430
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
15-559 2.89e-23

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 106.86  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   15 LRRRAVQEPERLALrflAEDDGEgvvLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAV- 92
Cdd:cd05918    5 IEERARSQPDAPAV---CAWDGS---LTYAELDRLSSRLAHHLRSLGVGPGVFVpLCFEKSKWAVVAMLAVLKAGGAFVp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   93 --PAYPPEsarrhhqeRLLSIIADAEPRLVLTTadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEHIA 170
Cdd:cd05918   79 ldPSHPLQ--------RLQEILQDTGAKVVLTS-----------------------------------------SPSDAA 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  171 FLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADD-------------VIVSWLPLYHdmgliGGllqpifsgvpC 237
Cdd:cd05918  110 YVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrvlqfasytfdvsILEIFTTLAA-----GG----------C 174
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  238 VLMSPRYflERPVRWLEAISQYGGTVSG-GPDFAyRLcservaesaLQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAAs 316
Cdd:cd05918  175 LCIPSEE--DRLNDLAGFINRLRVTWAFlTPSVA-RL---------LDPEDVPSLRTLVLGGEALTQSDVDTWADRVRL- 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  317 rfdassfFACYGLAEATLFVTGGQrgqgipalaVDGEALARNrIAEGEGSVLmccgrsqpehavLIVDAASGEVL---Gd 393
Cdd:cd05918  242 -------INAYGPAECTIAATVSP---------VVPSTDPRN-IGRPLGATC------------WVVDPDNHDRLvpiG- 291
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  394 dNVGEIWAAGPSIAHGYWRNPEASAKAFVE----------RDGRTWLRTGDLG-FLRDGEL-FVtGRlKDMLI-VRGHNL 460
Cdd:cd05918  292 -AVGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqegsGRGRRLYRTGDLVrYNPDGSLeYV-GR-KDTQVkIRGQRV 368
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  461 YPQDIERTVESEVPSAR--------------KGRVAAFaVTVDGEEGIGiAAEIGRGVQKSVPAQELIDSIRQAVAE--- 523
Cdd:cd05918  369 ELGEIEHHLRQSLPGAKevvvevvkpkdgssSPQLVAF-VVLDGSSSGS-GDGDSLFLEPSDEFRALVAELRSKLRQrlp 446
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 15597620  524 AYQeAPKVVALLNpgALPKTSSGKLQRSACRLRLED 559
Cdd:cd05918  447 SYM-VPSVFLPLS--HLPLTASGKIDRRALRELAES 479
PLN02246 PLN02246
4-coumarate--CoA ligase
2188-2621 3.11e-23

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 107.76  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2188 LHGLFAARVAASPQAPALTFA--GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVP 2265
Cdd:PLN02246   25 LHDYCFERLSEFSDRPCLIDGatGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2266 LDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVARWCLEEDGPA---------LDAEDPAPLAALSGPQHQAYL 2336
Cdd:PLN02246  105 ANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPegclhfselTQADENELPEVEISPDDVVAL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2337 IYTSGSTGKPKGVAVSHGEIAMHCAAVIEC----FGMRAED---CEL---HFYSINfdaasERLLAPLLCGARVVLRAQG 2406
Cdd:PLN02246  185 PYSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFHSDDvilCVLpmfHIYSLN-----SVLLCGLRVGAAILIMPKF 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2407 QWGAeeICELIRAEGVSILGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEALtGEHLQR-IRQAFAPASFFNAYGPTET 2484
Cdd:PLN02246  260 EIGA--LLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLsSIRMVLSGAAPL-GKELEDaFRAKLPNAVLGQGYGMTEA 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2485 VVMPLACLA----PERLEEGAAsvpiGSVVGARVAYILDADLAL-VPQGATGELYVGGAGLARGYHERPALSAERFVPDp 2559
Cdd:PLN02246  337 GPVLAMCLAfakePFPVKSGSC----GTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKD- 411
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  2560 faaegGRLYrTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLA 2621
Cdd:PLN02246  412 -----GWLH-TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVP 467
PLN02574 PLN02574
4-coumarate--CoA ligase-like
34-550 3.38e-23

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 107.62  E-value: 3.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    34 DDGEGVVLSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQErllsi 111
Cdd:PLN02574   60 DSSTGFSISYSELQPLVKSMAAglYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKR----- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   112 IADAEPRLVLTTADLREPLLQMNaqLSAANAPQLLCVDQLDPAVAEAWD----------EPQVRPEHIAFLQYTSGSTAL 181
Cdd:PLN02574  135 VVDCSVGLAFTSPENVEKLSPLG--VPVIGVPENYDFDSKRIEFPKFYElikedfdfvpKPVIKQDDVAAIMYSSGTTGA 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   182 PKGVQVSHGNLVAN-EVLIRRGFGI----GADDVIVSWLPLYHDMGL---IGGLLQpifSGVPCVLMspRYFLERPVrwL 253
Cdd:PLN02574  213 SKGVVLTHRNLIAMvELFVRFEASQyeypGSDNVYLAALPMFHIYGLslfVVGLLS---LGSTIVVM--RRFDASDM--V 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   254 EAISQYGgtVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFaaSRFDassFFACYGLAEAT 333
Cdd:PLN02574  286 KVIDRFK--VTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL--PHVD---FIQGYGMTEST 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   334 LFvtgGQRGqgipalaVDGEALARnriaegEGSVlmccGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRN 413
Cdd:PLN02574  359 AV---GTRG-------FNTEKLSK------YSSV----GLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   414 PEASAKAFVErDGrtWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEvPSARKgrvAAFAVTVDGEE 492
Cdd:PLN02574  419 PKATQSTIDK-DG--WLRTGDIAyFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISH-PEIID---AAVTAVPDKEC 491
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   493 G-IGIAAEIGRgvQKSVPAQE-LIDSIRQAVAeAYQEAPKVVaLLNPgaLPKTSSGKLQR 550
Cdd:PLN02574  492 GeIPVAFVVRR--QGSTLSQEaVINYVAKQVA-PYKKVRKVV-FVQS--IPKSPAGKILR 545
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
32-554 5.93e-23

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 106.56  E-value: 5.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   32 AEDDGEGVVLSYRDLDLRARSIAAALQAH-AQLGDR-AVLLFPSGpDYVAAFFGCLYAGVIAVPAYPpesarRHHQERLL 109
Cdd:cd12119   17 RTHEGEVHRYTYAEVAERARRLANALRRLgVKPGDRvATLAWNTH-RHLELYYAVPGMGAVLHTINP-----RLFPEQIA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  110 SIIADAEPRLVLTTADLrEPLLQ----------------MNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQ 173
Cdd:cd12119   91 YIINHAEDRVVFVDRDF-LPLLEaiaprlptvehvvvmtDDAAMPEPAGVGVLAYEELLAAESPEYDWPDFDENTAAAIC 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  174 YTSGSTALPKGVQVSHGNLV--ANEVLIRRGFGIGADDVIVSWLPLYHDMGLigGLlqPI---FSGVPCVLMSPRYfleR 248
Cdd:cd12119  170 YTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPMFHVNAW--GL--PYaaaMVGAKLVLPGPYL---D 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  249 PVRWLEAISQYGGTVSGG-PDFAYRLCSERvaeSALQRLDLSGWRVAFSGSEPIRqdSL-ERFAEKFaasrfdaSSFFAC 326
Cdd:cd12119  243 PASLAELIEREGVTFAAGvPTVWQGLLDHL---EANGRDLSSLRRVVIGGSAVPR--SLiEAFEERG-------VRVIHA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  327 YGLAEATLFVTGGQRGQGIPALAVDGEAlarnriaegegSVLMCCGRSQPEHAVLIVDAASGEVLGDDN-VGEIWAAGPS 405
Cdd:cd12119  311 WGMTETSPLGTVARPPSEHSNLSEDEQL-----------ALRAKQGRPVPGVELRIVDDDGRELPWDGKaVGELQVRGPW 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  406 IAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------VP 474
Cdd:cd12119  380 VTKSYYKNDEESEALT--EDG--WLRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHpavaeaavigVP 455
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  475 SARKG-RVAAFAVTVDGEEgigiaaeigrgvqksVPAQELIDSIRQAVAEAYqeAPKVVALLNpgALPKTSSGKLQRSAC 553
Cdd:cd12119  456 HPKWGeRPLAVVVLKEGAT---------------VTAEELLEFLADKVAKWW--LPDDVVFVD--EIPKTSTGKIDKKAL 516

                 .
gi 15597620  554 R 554
Cdd:cd12119  517 R 517
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
38-554 1.35e-22

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 104.48  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   38 GVVLSYRDLDLRARSIA--AALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQerllsIIADA 115
Cdd:cd05958    8 EREWTYRDLLALANRIAnvLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAY-----ILDKA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  116 EPRLVLttadlrepllqmnaqlsaanapqllCVDQLDPAvaeawdepqvrpEHIAFLQYTSGSTALPKGVQVSHGNLVAN 195
Cdd:cd05958   83 RITVAL-------------------------CAHALTAS------------DDICILAFTSGTTGAPKATMHFHRDPLAS 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  196 -EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRyfleRPVRWLEAISQYGGTVSGGPDFAYRLC 274
Cdd:cd05958  126 aDRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA----TPDLLLSAIARYKPTVLFTAPTAYRAM 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  275 SERVAESAlqrLDLSGWRVAFSGSEPIRQDSLERFAEKFaasrfdassffacyglaeatlfvtggqrgqGIPalAVDG-- 352
Cdd:cd05958  202 LAHPDAAG---PDLSSLRKCVSAGEALPAALHRAWKEAT------------------------------GIP--IIDGig 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  353 --EALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSiahGYWRNPEASAKAFVERDgrtWL 430
Cdd:cd05958  247 stEMFHIFISARPGDARPGATGKPVPGYEAKVVDDE-GNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGG---WN 319
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  431 RTGDLgFLR--DGELFVTGRLKDMLIVRGHNLYPQDIERTVESEvPSarkgrVAAFAV--TVDGEEGIGIAAEI--GRGV 504
Cdd:cd05958  320 ITGDT-YSRdpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQH-PA-----VAECAVvgHPDESRGVVVKAFVvlRPGV 392
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597620  505 QKS-VPAQELIDSIRQAVAeAYQEaPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05958  393 IPGpVLARELQDHAKAHIA-PYKY-PRAIEFVT--ELPRTATGKLQRFALR 439
PRK13382 PRK13382
bile acid CoA ligase;
2135-2692 1.46e-22

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 105.61  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2135 PRIARMAGHWQNLLEALLGDPQRRIAELPLFAAEERKQLLLAGtageaglqdtlhgLFAARVAASPQAPALTFAGQTLSY 2214
Cdd:PRK13382    5 DRLRDTLGLIATLRRAGLIAPMRPDRYLRIVAAMRREGMGPTS-------------GFAIAAQRCPDRPGLIDELGTLTW 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2215 AELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSH---- 2290
Cdd:PRK13382   72 RELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDeefs 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2291 AALFEALGELPAG--VARWCLEEDGPALDA--EDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIEC 2366
Cdd:PRK13382  152 ATVDRALADCPQAtrIVAWTDEDHDLTVEVliAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAILDR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2367 FGMRAEDCEL----HFYSINFdaaSERLLAPLLCGARVVLRaqgQWGAEEICELI---RAEGVSILgftPSYGSQLAQWL 2439
Cdd:PRK13382  232 TPWRAEEPTVivapMFHAWGF---SQLVLAASLACTIVTRR---RFDPEATLDLIdrhRATGLAVV---PVMFDRIMDLP 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2440 ES-----QGRQLpvRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVVMPLAclAPERLEegAASVPIGSVVGARV 2514
Cdd:PRK13382  303 AEvrnrySGRSL--RFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIATA--TPADLR--AAPDTAGRPAEGTE 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2515 AYILDADLALVPQGATGELYVGGAGLARGYHErpalSAERFVPDPFAAeggrlyrTGDLVRLCDNGQVEYVGRIDHQVKI 2594
Cdd:PRK13382  376 IRILDQDFREVPTGEVGTIFVRNDTQFDGYTS----GSTKDFHDGFMA-------SGDVGYLDENGRLFVVGRDDEMIVS 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2595 RGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLAGYVASavaeqdEDAQAALREALKTHLKQQLPDYMVPAHLLLL 2673
Cdd:PRK13382  445 GGENVYPIEVEKTLATHPDVAEAAVIGVDDEQyGQRLAAFVVL------KPGASATPETLKQHVRDNLANYKVPRDIVVL 518
                         570
                  ....*....|....*....
gi 15597620  2674 ASLPLTANGKLDRRALPAP 2692
Cdd:PRK13382  519 DELPRGATGKILRRELQAR 537
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
162-554 1.48e-22

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 105.49  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   162 PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVAN----EVLIRRGFGIGADD---VIVSWLPLYHDMGL-IGGLLQPIFS 233
Cdd:PRK07059  199 VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANvlqmEAWLQPAFEKKPRPdqlNFVCALPLYHIFALtVCGLLGMRTG 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   234 GVPCVLMSPR-------YFLERPVRWLEAISQYGGTVSGGPDFayrlcservaesalQRLDLSGWRVAFSGSEPIRQDSL 306
Cdd:PRK07059  279 GRNILIPNPRdipgfikELKKYQVHIFPAVNTLYNALLNNPDF--------------DKLDFSKLIVANGGGMAVQRPVA 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   307 ERFAEKFAASRFDAssffacYGLAEATLFVTGgqrgqgipalavdgealarNRIAEGE--GSVlmccGRSQPEHAVLIVD 384
Cdd:PRK07059  345 ERWLEMTGCPITEG------YGLSETSPVATC-------------------NPVDATEfsGTI----GLPLPSTEVSIRD 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   385 AASGEV-LGDdnVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYP 462
Cdd:PRK07059  396 DDGNDLpLGE--PGEICIRGPQVMAGYWNRPDETAKVMTA-DG--FFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYP 470
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   463 QDIErtvesEVPSARKGRVAAFAVTV-DGEEGIGIAAEIgrgVQK--SVPAQELIDSIRQAVAeAYQEaPKVVALLNpgA 539
Cdd:PRK07059  471 NEIE-----EVVASHPGVLEVAAVGVpDEHSGEAVKLFV---VKKdpALTEEDVKAFCKERLT-NYKR-PKFVEFRT--E 538
                         410
                  ....*....|....*
gi 15597620   540 LPKTSSGKLQRSACR 554
Cdd:PRK07059  539 LPKTNVGKILRRELR 553
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3704-4169 1.55e-22

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 105.95  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3704 RSARDYPLEQGYVRLFEAQVAAHPQRIAASCLE----QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGM 3779
Cdd:COG1022    2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3780 IVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVC-TQACREQALAL------------FDELGCVDRPRLLVWDEI- 3845
Cdd:COG1022   82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVrdelpslrhivvLDPRGLRDDPRLLSLDELl 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3846 QQGEGAEHDPQVYS-----GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVI----------AQTa 3910
Cdd:COG1022  162 ALGREVADPAELEArraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTlsflplahvfERT- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3911 sqsfdISVWQFLAaplfGARVAIVPnavahDPQGLLAHVGEQGITVLESVPSL-------IQGMLAEE--------RQAL 3975
Cdd:COG1022  241 -----VSYYALAA----GATVAFAE-----SPDTLAEDLREVKPTFMLAVPRVwekvyagIQAKAEEAgglkrklfRWAL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3976 D-GLRWM--LPTGEAMPPELARQW----------LKRypRIG--LVNAY-GPAECSDDVA-FFR---VDLA----STEST 4031
Cdd:COG1022  307 AvGRRYAraRLAGKSPSLLLRLKHaladklvfskLRE--ALGgrLRFAVsGGAALGPELArFFRalgIPVLegygLTETS 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4032 ylPIGS--PTDNNRLYLLG---AGADdafelVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPhpfgapgERLYRTGDL 4106
Cdd:COG1022  385 --PVITvnRPGDNRIGTVGpplPGVE-----VKIAEDGEILVRGPNVMKGYYKNPEATAEAFDA-------DGWLHTGDI 450
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 4107 ARRRADGVLEYVGRIDHQVKIR-GFRIELGEIEARLHERADVREAAVAvqeGANGKYLVGYLVP 4169
Cdd:COG1022  451 GELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV---GDGRPFLAALIVP 511
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
165-473 1.95e-22

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 104.36  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  165 RPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHD-------MGLIGGLLQpIFSGVPC 237
Cdd:cd17640   86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSyersaeyFIFACGCSQ-AYTSIRT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  238 VL-----MSPRYFLERPVRWlEAIsqYGG---TVSGGPDFayrlcSERVAESALqrldlSG--WRVAFSGSepirqDSLE 307
Cdd:cd17640  165 LKddlkrVKPHYIVSVPRLW-ESL--YSGiqkQVSKSSPI-----KQFLFLFFL-----SGgiFKFGISGG-----GALP 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  308 RFAEKFaasrFDASS--FFACYGLAEatlfvTGGqrgqgipalavdgeALARNRIaegEGSVLMCCGRSQPEHAVLIVDA 385
Cdd:cd17640  227 PHVDTF----FEAIGieVLNGYGLTE-----TSP--------------VVSARRL---KCNVRGSVGRPLPGTEIKIVDP 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  386 ASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAfVERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVR-GHNLYPQ 463
Cdd:cd17640  281 EGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDG--WFNTGDLGWLtCGGELVLTGRAKDTIVLSnGENVEPQ 357
                        330
                 ....*....|.
gi 15597620  464 DIERT-VESEV 473
Cdd:cd17640  358 PIEEAlMRSPF 368
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3739-4225 2.00e-22

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 105.35  E-value: 2.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAG------VGIDQP------VALLA-ERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTR- 3804
Cdd:cd17634   85 ISYRELHREVCRFAGTLLDLGvkkgdrVAIYMPmipeaaVAMLAcARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAd 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3805 -IVELSRTLVL--VCTQACREQALALFDELgCVDRP---------RLLVWDEIQQGEGAEHDPqVYSGPQNLAYVIYTSG 3872
Cdd:cd17634  165 gGVRAGRSVPLkkNVDDALNPNVTSVEHVI-VLKRTgsdidwqegRDLWWRDLIAKASPEHQP-EAMNAEDPLFILYTSG 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3873 STGLPKGVMVEQAGMLNNQLSKVPYL-ELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNAVAH-DPQGLLAHV 3949
Cdd:cd17634  243 TTGKPKGVLHTTGGYLVYAATTMKYVfDYGPGDIYWCTADVGWVTGHSYLLYGPLAcGATTLLYEGVPNWpTPARMWQVV 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3950 GEQGITVLESVPSLIQGMLAE-----ERQALDGLRWMLPTGEAMPPElARQWLKRY---PRIGLVNAYGPAECSDDVAFF 4021
Cdd:cd17634  323 DKHGVNILYTAPTAIRALMAAgddaiEGTDRSSLRILGSVGEPINPE-AYEWYWKKigkEKCPVVDTWWQTETGGFMITP 401
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4022 RVDLAStestyLPIGSPTdNNRLYLLGAGADDAFELVPLGAVGELCVAGT--GVGRGYVGDPLRTAQAFVphpfgAPGER 4099
Cdd:cd17634  402 LPGAIE-----LKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYF-----STFKG 470
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4100 LYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAA-VAVQEGANGKYLVGYLV--PGETPrss 4176
Cdd:cd17634  471 MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAvVGIPHAIKGQAPYAYVVlnHGVEP--- 547
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 15597620 4177 adsPAGLMVEQGAWferikqqLRADLPDYMVPLHWLVLDRMPLNANGKL 4225
Cdd:cd17634  548 ---SPELYAELRNW-------VRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3-491 2.08e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 105.21  E-value: 2.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     3 DAFELPTTLVQALRRRAVQEPERLALRflaeddGEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAF 81
Cdd:PRK06164    4 DAAPRADTLASLLDAHARARPDAVALI------DEDRPLSRAELRALVDRLAAWLAAQgVRRGDRVAVWLPNCIEWVVLF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    82 FGC--LYAGVIAVPAyppesarRHHQERLLSIIADAEPRLVLTTADLRE----PLLQMNAQLSAANAPQLLCVD------ 149
Cdd:PRK06164   78 LACarLGATVIAVNT-------RYRSHEVAHILGRGRARWLVVWPGFKGidfaAILAAVPPDALPPLRAIAVVDdaadat 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   150 -------------QLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLP 216
Cdd:PRK06164  151 papapgarvqlfaLPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   217 LYHDMGLiGGLLQPIFSGVPcVLMSPRYFLERPVRwleAISQYGGTVSGGPDFAYRlcseRVAESALQRLDLSGWRV--- 293
Cdd:PRK06164  231 FCGVFGF-STLLGALAGGAP-LVCEPVFDAARTAR---ALRRHRVTHTFGNDEMLR----RILDTAGERADFPSARLfgf 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   294 -AFSGsepirqdsleRFAEKFAASRFDASSFFACYGLAEATLFVTGGQRgqgipALAVDGEALARNRIAEGEGSVLmccg 372
Cdd:PRK06164  302 aSFAP----------ALGELAALARARGVPLTGLYGSSEVQALVALQPA-----TDPVSVRIEGGGRPASPEARVR---- 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   373 rsqpehavlIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVeRDGrtWLRTGDLGFLRDGELFV-TGRLKD 451
Cdd:PRK06164  363 ---------ARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALT-DDG--YFRTGDLGYTRGDGQFVyQTRMGD 430
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620   452 MLIVRGHNLYPQDIERTVESE--------VPSARKG--RVAAFAVTVDGE 491
Cdd:PRK06164  431 SLRLGGFLVNPAEIEHALEALpgvaaaqvVGATRDGktVPVAFVIPTDGA 480
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
2195-2661 2.12e-22

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 105.36  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2195 RVAASPQA--PALTFAG----QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPL-- 2266
Cdd:PRK04319   51 RHADGGRKdkVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfe 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2267 --DPEYPLERLqymiEDSGVRLLLSHAALFEAL--GELPAgvARWCL------EEDGPALD-------AEDPAPLAALSg 2329
Cdd:PRK04319  131 afMEEAVRDRL----EDSEAKVLITTPALLERKpaDDLPS--LKHVLlvgedvEEGPGTLDfnalmeqASDEFDIEWTD- 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2330 PQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAviecfGMRAEDceLHFYSINFDAA--------SERLLAPLLCGARVV 2401
Cdd:PRK04319  204 REDGAILHYTSGSTGKPKGVLHVHNAMLQHYQT-----GKYVLD--LHEDDVYWCTAdpgwvtgtSYGIFAPWLNGATNV 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2402 LRAqGQWGAEEICELIRAEGVSILGFTP-------SYGSQLAQwlesQGRQLPVRMCITGGEALTGEHLQRIRQAFApAS 2474
Cdd:PRK04319  277 IDG-GRFSPERWYRILEDYKVTVWYTAPtairmlmGAGDDLVK----KYDLSSLRHILSVGEPLNPEVVRWGMKVFG-LP 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2475 FFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGArvayILDADLALVPQGATGELYV--GGAGLARGYHERPALSA 2552
Cdd:PRK04319  351 IHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAA----IVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYE 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2553 ERFVPDpfaaeggrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPsgkqLAG 2632
Cdd:PRK04319  427 SYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDP----VRG 494
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 15597620  2633 YVASA-VA-----EQDEdaqaALREALKTHLKQQL 2661
Cdd:PRK04319  495 EIIKAfVAlrpgyEPSE----ELKEEIRGFVKKGL 525
PRK08315 PRK08315
AMP-binding domain protein; Validated
1130-1616 2.22e-22

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 105.28  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVAL-EWDGG-SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVP 1207
Cdd:PRK08315   18 IGQLLDRTAARYPDREALvYRDQGlRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1208 LDPDYPSERLAYMLADSGVELLLTQAH---------LFERLPGAEGVTPICLDSLKL-----------------DNWPS- 1260
Cdd:PRK08315   98 INPAYRLSELEYALNQSGCKALIAADGfkdsdyvamLYELAPELATCEPGQLQSARLpelrrviflgdekhpgmLNFDEl 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1261 QAPGLHLHGDNLAY---------VI---YTSGSTGQPKGVGNTH-------AALAERLQwmqatYTlDGDDVLMqkaPVS 1321
Cdd:PRK08315  178 LALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHrnilnngYFIGEAMK-----LT-EEDRLCI---PVP 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1322 FdvsvWECFwplvtGCRL-VLAA---------PGEHRDPARLVELVRQFGVTTLHFVPpllQLFI---DEPGVAA--CGS 1386
Cdd:PRK08315  249 L----YHCF-----GMVLgNLACvthgatmvyPGEGFDPLATLAAVEEERCTALYGVP---TMFIaelDHPDFARfdLSS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1387 LRRLFSGGEALPAELRNRVLQRlpavaLHNR-----YGPTETAiNVTHwQCRAEDG-ER--SPIGRPLGNVVCRVLDAEF 1458
Cdd:PRK08315  317 LRTGIMAGSPCPIEVMKRVIDK-----MHMSevtiaYGMTETS-PVST-QTRTDDPlEKrvTTVGRALPHLEVKIVDPET 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1459 N-LLPAGVAGELCIGGLGLARGYLGRPALSAErfVADPfsaagERLYRTGDRARWNADGVLEYLGRLDQQVkLRGFR-IE 1536
Cdd:PRK08315  390 GeTVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA-----DGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGEnIY 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1537 PEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLG 1612
Cdd:PRK08315  462 PREIEEFLYTHPKIQDVQVV---GVPdekyGEEVCAWIILRPGATLTEED---VRDFCRGKIAHYKIPRYIRFVDEFPMT 535

                  ....
gi 15597620  1613 PSGK 1616
Cdd:PRK08315  536 VTGK 539
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
23-562 3.30e-22

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 104.36  E-value: 3.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    23 PERLALRFLAEDDGEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesAR 101
Cdd:PRK13295   38 PDKTAVTAVRLGTGAPRRFTYRELAALVdRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMP---IF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   102 RHHQERLLsiIADAEPRLVLTTADLRE-PLLQMNAQLSAAnAPQL---LCVD----------------QLDPAVAEAWDE 161
Cdd:PRK13295  115 RERELSFM--LKHAESKVLVVPKTFRGfDHAAMARRLRPE-LPALrhvVVVGgdgadsfeallitpawEQEPDAPAILAR 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   162 PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMS 241
Cdd:PRK13295  192 LRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   242 pryfLERPVRWLEAISQYGGTVS-GGPDFAYRLCsERVAESAlqrLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDA 320
Cdd:PRK13295  272 ----IWDPARAAELIRTEGVTFTmASTPFLTDLT-RAVKESG---RPVSSLRTFLCAGAPIPGALVERARAALGAKIVSA 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   321 ssffacYGLAEATLfVTGGQRGQgipalavdgealARNRIAEGEGSVLmccgrsqPEHAVLIVDAAsGEVLGDDNVGEIW 400
Cdd:PRK13295  344 ------WGMTENGA-VTLTKLDD------------PDERASTTDGCPL-------PGVEVRVVDAD-GAPLPAGQIGRLQ 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   401 AAGPSIAHGYWRNPEASAKAFverDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHN---------LYPQ-DIERTV 469
Cdd:PRK13295  397 VRGCSNFGGYLKRPQLNGTDA---DG--WFDTGDLARIdADGYIRISGRSKDVIIRGGENipvveiealLYRHpAIAQVA 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   470 ESEVPSARKG-RVAAFAVTVDGeEGIGIAAeigrgvqksvpAQELIDSirQAVAEAYQEAPKVVAllnpGALPKTSSGKL 548
Cdd:PRK13295  472 IVAYPDERLGeRACAFVVPRPG-QSLDFEE-----------MVEFLKA--QKVAKQYIPERLVVR----DALPRTPSGKI 533
                         570
                  ....*....|....
gi 15597620   549 QRSACRLRLEDGSL 562
Cdd:PRK13295  534 QKFRLREMLRGEDA 547
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3737-4152 3.65e-22

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 103.85  E-value: 3.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTlVLVC 3816
Cdd:cd05904   31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGA-KLAF 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3817 TQACREQALALFD-ELGCVDRPRLLVW--DEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLS 3893
Cdd:cd05904  110 TTAELAEKLASLAlPVVLLDSAEFDSLsfSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQ 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3894 KVPY--LELDENDVIaqtasqsfdisvwqFLAAPLF---------------GARVAIVPNAvahDPQGLLAHVGEQGITV 3956
Cdd:cd05904  190 FVAGegSNSDSEDVF--------------LCVLPMFhiyglssfalgllrlGATVVVMPRF---DLEELLAAIERYKVTH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIQGML---AEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSddvaffrvdlASTESTYL 4033
Cdd:cd05904  253 LPVVPPIVLALVkspIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST----------GVVAMCFA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4034 PIGSPTDNNRLYLLGAGAD------DAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPhpfgapgERLYRTGDLA 4107
Cdd:cd05904  323 PEKDRAKYGSVGRLVPNVEakivdpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK-------EGWLHTGDLC 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 15597620 4108 RRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:cd05904  396 YIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
3696-4152 4.86e-22

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 103.73  E-value: 4.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3696 DFLLDGCNRSARDYPLEQGYVRLFEAQVaahpqriaasclEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLD 3775
Cdd:cd05970   17 NFAYDVVDAMAKEYPDKLALVWCDDAGE------------ERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3776 LLGMIVGSFKAGAGYLPldpghPTQRLT------RIVELS-RTLVLVCTQACREQALALFDELGCVDRpRLLVWDEIQQG 3848
Cdd:cd05970   85 FWYSLLALHKLGAIAIP-----ATHQLTakdivyRIESADiKMIVAIAEDNIPEEIEKAAPECPSKPK-LVWVGDPVPEG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3849 -----EGAEHDPQVYSGPQNLAY--------VIYTSGSTGLPKgvMVEQAGM--LNNQLSKVPYLELDENDVIAQTASQS 3913
Cdd:cd05970  159 widfrKLIKNASPDFERPTANSYpcgedillVYFSSGTTGMPK--MVEHDFTypLGHIVTAKYWQNVREGGLHLTVADTG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3914 FDISVW-QFLAAPLFGARVaIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAE--ERQALDGLRWMLPTGEAMPP 3990
Cdd:cd05970  237 WGKAVWgKIYGQWIAGAAV-FVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREdlSRYDLSSLRYCTTAGEALNP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3991 ELARQWlKRYPRIGLVNAYGPAECSDDVAFFrvdlASTESTYLPIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCV-- 4068
Cdd:cd05970  316 EVFNTF-KEKTGIKLMEGFGQTETTLTIATF----PWMEPKPGSMGKPAPGYEIDLI----DREGRSCEAGEEGEIVIrt 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4069 -AGTGVG--RGYVGDPLRTAQAFvphpfgapGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERA 4145
Cdd:cd05970  387 sKGKPVGlfGGYYKDAEKTAEVW--------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP 458

                 ....*..
gi 15597620 4146 DVREAAV 4152
Cdd:cd05970  459 AVLECAV 465
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
169-557 6.03e-22

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 100.10  E-value: 6.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  169 IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdmglIGGL---LQPIFSGVPCVLMSPRYF 245
Cdd:cd17630    2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH----VGGLailVRSLLAGAELVLLERNQA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  246 LerpvrwLEAISQYGGT-VSGGPDFAYRLCSERVAESALQRLdlsgwRVAFSGSEPIRQDSLERFAEKFAASrfdassfF 324
Cdd:cd17630   78 L------AEDLAPPGVThVSLVPTQLQRLLDSGQGPAALKSL-----RAVLLGGAPIPPELLERAADRGIPL-------Y 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  325 ACYGLAEatlfvTGGQrgqgIPALAVDGEALARnriaegegsvlmcCGRSQPEHAVLIVDAasgevlgddnvGEIWAAGP 404
Cdd:cd17630  140 TTYGMTE-----TASQ----VATKRPDGFGRGG-------------VGVLLPGRELRIVED-----------GEIWVGGA 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  405 SIAHGYWRNPEASakafvERDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVEsevpsARKGRVAA 483
Cdd:cd17630  187 SLAMGYLRGQLVP-----EFNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALA-----AHPAVRDA 256
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  484 FAVTVDGEE-GIGIAAEI-GRGvqkSVPAQELIDSIRQAVAEAyqEAPKVVALLNpgALPKTSSGKLQRSACRLRL 557
Cdd:cd17630  257 FVVGVPDEElGQRPVAVIvGRG---PADPAELRAWLKDKLARF--KLPKRIYPVP--ELPRTGGGKVDRRALRAWL 325
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
67-474 6.35e-22

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 103.98  E-value: 6.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   67 AVLLFPSgPDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSIIADAEPR-LVLTTADLREPLLQMNAQLsaanaPQL 145
Cdd:cd05933   37 GILGFNS-PEWFIAAVGAIFAGGIAVGIYTTNSP-----EACQYVAETSEANiLVVENQKQLQKILQIQDKL-----PHL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  146 LCVDQLDPAVAEA------WDEPQ-----------------VRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRG 202
Cdd:cd05933  106 KAIIQYKEPLKEKepnlysWDEFMelgrsipdeqldaiissQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQH 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  203 FGIGADDV----IVSWLPLYH------DMGL---IGGLL---QP-----------------IFSGVPCVL---------- 239
Cdd:cd05933  186 MDLRPATVgqesVVSYLPLSHiaaqilDIWLpikVGGQVyfaQPdalkgtlvktlrevrptAFMGVPRVWekiqekmkav 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  240 -MSPRYFLERPVRW-----LEAISQYGGTVSGGPDFaYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKF 313
Cdd:cd05933  266 gAKSGTLKRKIASWakgvgLETNLKLMGGESPSPLF-YRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLN 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  314 AAsrfdassFFACYGLAEATlfvtggqrgqgipalavdGEALARNRIAEGEGSvlmcCGRSQPEHAVLIVDAasgevlGD 393
Cdd:cd05933  345 IP-------IMELYGMSETS------------------GPHTISNPQAYRLLS----CGKALPGCKTKIHNP------DA 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  394 DNVGEIWAAGPSIAHGYWRNPEASAKAfVERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVR-GHNLYPQDIERTVES 471
Cdd:cd05933  390 DGIGEICFWGRHVFMGYLNMEDKTEEA-IDEDG--WLHSGDLGKLdEDGFLYITGRIKELIITAgGENVPPVPIEDAVKK 466

                 ...
gi 15597620  472 EVP 474
Cdd:cd05933  467 ELP 469
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2487-2781 7.36e-22

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 99.44  E-value: 7.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2487 MPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFAAEGGR 2566
Cdd:COG3433    1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2567 LYRTGDLVRLCDNGQVeyvGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAEQDEDAQ 2646
Cdd:COG3433   81 QADDLRLLLRRGLGPG---GGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2647 AALRealkTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPALNRQAYEAPRS-----VLEQQLAGVWREVLN 2721
Cdd:COG3433  158 AAAA----LAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaletaLTEEELRADVAELLG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620 2722 V--ERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQSLAAVARHSQASQA 2781
Cdd:COG3433  234 VdpEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1151-1622 9.89e-22

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 102.07  E-value: 9.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1151 GGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVK---AGGAYVPLDPDYPSERLAYMLADSGVE 1227
Cdd:cd05929   15 RRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKcgaCPAYKSSRAPRAEACAIIEIKAAALVC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1228 LLLT--QAH----LFERLPGAEGVTPIcldslkldnwPSQAPGlhlhgdnlAYVIYTSGSTGQPKGV---------GNTH 1292
Cdd:cd05929   95 GLFTggGALdgleDYEAAEGGSPETPI----------EDEAAG--------WKMLYSGGTTGRPKGIkrglpggppDNDT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1293 AALAERLQWMQAtytldgDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPP-- 1370
Cdd:cd05929  157 LMAAALGFGPGA------DSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAQFVPTmf 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1371 --LLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTE----TAINVTHWQcraedGERSPIGR 1444
Cdd:cd05929  228 vrLLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEgqglTIINGEEWL-----THPGSVGR 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1445 PLGNVVCrVLDAEFNLLPAGVAGELCIGGlGLARGYLGRPALSAERFVADPFSAagerlyrTGDRARWNADGVLEYLGRL 1524
Cdd:cd05929  302 AVLGKVH-ILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST-------LGDVGYLDEDGYLYLTDRR 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1525 DQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVP 1600
Cdd:cd05929  373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVV---GVPdeelGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCP 449
                        490       500
                 ....*....|....*....|..
gi 15597620 1601 TQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:cd05929  450 RSIEFVAELPRDDTGKLYRRLL 471
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
2213-2686 1.05e-21

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 102.96  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2213 SYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAA 2292
Cdd:cd05970   49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2293 ------LFEALGELPAGVAR----------WCLEEDGPALDAED-PAPLAALSGPQHQAYLIY-TSGSTGKPKGVAVSH- 2353
Cdd:cd05970  129 dnipeeIEKAAPECPSKPKLvwvgdpvpegWIDFRKLIKNASPDfERPTANSYPCGEDILLVYfSSGTTGMPKMVEHDFt 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2354 ---GEIamhcaaVIECFGMRAEDCELHfYSIN----FDAASERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILG 2426
Cdd:cd05970  209 yplGHI------VTAKYWQNVREGGLH-LTVAdtgwGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFC 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2427 FTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRqAFAPASFFNAYGPTETVV----MPLACLAPERLEEGAA 2502
Cdd:cd05970  282 APPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEGFGQTETTLtiatFPWMEPKPGSMGKPAP 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2503 SVPIGsvvgarvayILDADLALVPQGATGELYVGGA-----GLARGYHERPALSAERFvpdpfaAEGgrLYRTGDLVRLC 2577
Cdd:cd05970  361 GYEID---------LIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW------HDG--YYHTGDAAWMD 423
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2578 DNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGyvASAVAEQDEDAQAALREALKTHL 2657
Cdd:cd05970  424 EDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVK--ATIVLAKGYEPSEELKKELQDHV 501
                        490       500
                 ....*....|....*....|....*....
gi 15597620 2658 KQQLPDYMVPAHLLLLASLPLTANGKLDR 2686
Cdd:cd05970  502 KKVTAPYKYPRIVEFVDELPKTISGKIRR 530
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
17-552 1.08e-21

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 101.63  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   17 RRAVQEPERLALRflAEDDGegvvLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP-- 93
Cdd:cd12115    7 AQAARTPDAIALV--CGDES----LTYAELNRRANRLAARLRAAgVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPld 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 -AYPPEsarrhhqeRLLSIIADAEPRLVLTTadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvrPEHIAFL 172
Cdd:cd12115   81 pAYPPE--------RLRFILEDAQARLVLTD------------------------------------------PDDLAYV 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  173 QYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPRYFLERPVRW 252
Cdd:cd12115  111 IYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLS-VFELFGPLATGGKVVLADNVLALPDLPAA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  253 LEA--ISqyggTVsggPDFAYRLCSERVAESALQRLDLSGwrvafsgsEPIRQDSLERFAEKFAASRFdassfFACYGLA 330
Cdd:cd12115  190 AEVtlIN----TV---PSAAAELLRHDALPASVRVVNLAG--------EPLPRDLVQRLYARLQVERV-----VNLYGPS 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  331 EATLFVTGGQRGQGipalavdgealarnriAEGEGSVlmccGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGPSIAHGY 410
Cdd:cd12115  250 EDTTYSTVAPVPPG----------------ASGEVSI----GRPLANTQAYVLDRA-LQPVPLGVPGELYIGGAGVARGY 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  411 WRNPEASAKAFV---ERDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERTVESeVPSARKgrvAAFAV 486
Cdd:cd12115  309 LGRPGLTAERFLpdpFGPGARLYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRS-IPGVRE---AVVVA 384
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  487 TVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEaYQEAPKVVALlnpGALPKTSSGKLQRSA 552
Cdd:cd12115  385 IGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPA-YMVPSRFVRL---DALPLTPNGKIDRSA 446
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3740-4152 1.30e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 101.11  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLP----LDPGHPTQRLTRivelsrtlvlv 3815
Cdd:cd05974    2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVDR----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3816 ctqacREQALALFDELGCVDRPRLLVwdeiqqgegaehdpqvysgpqnlayviYTSGSTGLPKGVMVEQAGMLNNQLSKV 3895
Cdd:cd05974   71 -----GGAVYAAVDENTHADDPMLLY---------------------------FTSGTTSKPKLVEHTHRSYPVGHLSTM 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3896 PYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQAL 3975
Cdd:cd05974  119 YWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASF 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3976 D-GLRWMLPTGEAMPPELARQwLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTEStylpIGSPTDNNRLYLL---GAGA 4051
Cdd:cd05974  199 DvKLREVVGAGEPLNPEVIEQ-VRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGS----MGRPLPGYRVALLdpdGAPA 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4052 DDAFELVPLGAVGELcvagtGVGRGYVGDPLRTAqafvphpfGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFR 4131
Cdd:cd05974  274 TEGEVALDLGDTRPV-----GLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYR 340
                        410       420
                 ....*....|....*....|.
gi 15597620 4132 IELGEIEARLHERADVREAAV 4152
Cdd:cd05974  341 ISPFELESVLIEHPAVAEAAV 361
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
1275-1617 1.75e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 99.26  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1275 VIYTSGSTGQPKGVG-NTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAapGEHRDPARL 1353
Cdd:cd17635    6 VIFTSGTTGEPKAVLlANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG--GENTTYKSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1354 VELVRQFGVTTLHFVPPLLQLFIDE--PGVAACGSLRRLFSGGEaLPAELRNRVLQRLPAVALHNRYGPTETAiNVTHWQ 1431
Cdd:cd17635   84 FKILTTNAVTTTCLVPTLLSKLVSElkSANATVPSLRLIGYGGS-RAIAADVRFIEATGLTNTAQVYGLSETG-TALCLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1432 CRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVadpfsaaGERLYrTGDRAR 1511
Cdd:cd17635  162 TDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWVN-TGDLGE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1512 WNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVvirEGVAGSQLVGYYTGAVGAEAEAEQN--QRLRAA 1589
Cdd:cd17635  234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAC---YEISDEEFGELVGLAVVASAELDENaiRALKHT 310
                        330       340
                 ....*....|....*....|....*...
gi 15597620 1590 LQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:cd17635  311 IRRELEPYARPSTIVIVTDIPRTQSGKV 338
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
3252-3593 1.94e-21

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 101.02  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3252 PLTPMQEGLLLHTLLEPGTGIYYMQDRYRIDSPLDPERFAAAWQAVVARHEALRASFVwNAGETMLQVIHKPGRTRIEFL 3331
Cdd:cd19546    6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFP-GDGGDVHQRILDADAARPELP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3332 dwselPEDGHEERLQALHKREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDAWCRGLLMNDFFEIYSALGESR 3411
Cdd:cd19546   85 -----VVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3412 -PANLPTPPRYRDYIAWLQR----QDLEQSRRW-----WSESLRGFERPTLVPSDRPFLREHAGESGGMIVgdrytRLDA 3481
Cdd:cd19546  160 aPERAPLPLQFADYALWEREllagEDDRDSLIGdqiayWRDALAGAPDELELPTDRPRPVLPSRRAGAVPL-----RLDA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3482 ADGARLRELAQRYQLTVNTFAQAAWALTLRRFSGERDVLFGvTVAGRPVGMPEMQRTVGLFINSIPLRVQMPAAGqrcTV 3561
Cdd:cd19546  235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDP---TF 310
                        330       340       350
                 ....*....|....*....|....*....|..
gi 15597620 3562 REWLNRLFERNLELREHEHLPLVAIQESSELP 3593
Cdd:cd19546  311 RELLGRVREAVREARRHQDVPFERLAELLALP 342
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1151-1556 2.45e-21

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 101.84  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1151 GGSLGYAELHARANRLAHYLRDKG--VGPDVrVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVEL 1228
Cdd:PLN02574   64 GFSISYSELQPLVKSMAAGLYHVMgvRQGDV-VLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1229 LLTQAHLFERLPgAEGVTPICL-DSLKLDNWPSQAPGLH--------------LHGDNLAYVIYTSGSTGQPKGVGNTHA 1293
Cdd:PLN02574  143 AFTSPENVEKLS-PLGVPVIGVpENYDFDSKRIEFPKFYelikedfdfvpkpvIKQDDVAAIMYSSGTTGASKGVVLTHR 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1294 ---ALAERLQWMQAT-YTLDG-DDVLMQKAPVsFDVSVWECFWP--LVTGCRLVLAapgEHRDPARLVELVRQFGVTTLH 1366
Cdd:PLN02574  222 nliAMVELFVRFEASqYEYPGsDNVYLAALPM-FHIYGLSLFVVglLSLGSTIVVM---RRFDASDMVKVIDRFKVTHFP 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1367 FVPPLLQLFID--EPGVAAC-GSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSPIG 1443
Cdd:PLN02574  298 VVPPILMALTKkaKGVCGEVlKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVG 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1444 RPLGNVVCRVLDAEF-NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLG 1522
Cdd:PLN02574  378 LLAPNMQAKVVDWSTgCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------LRTGDIAYFDEDGYLYIVD 450
                         410       420       430
                  ....*....|....*....|....*....|....
gi 15597620  1523 RLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:PLN02574  451 RLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVT 484
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
35-548 2.87e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 101.13  E-value: 2.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    35 DGEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPA----YPPESArrhhqerll 109
Cdd:PRK08276    6 APSGEVVTYGELEARSnRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPInwhlTAAEIA--------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   110 SIIADAEPRLVLTTADLREPLLQMNAQLSAAnAPQLLCVD-------QLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALP 182
Cdd:PRK08276   77 YIVDDSGAKVLIVSAALADTAAELAAELPAG-VPLLLVVAgpvpgfrSYEEALAAQPDTPIADETAGADMLYSSGTTGRP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   183 KGVQVS------HGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGlLQPIFSGVPCVLMspryflER--PVRWLE 254
Cdd:PRK08276  156 KGIKRPlpgldpDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFG-MSALALGGTVVVM------EKfdAEEALA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   255 AISQYGGTVSGG-PDFAYRLCseRVAESALQRLDLSGWRVAFSGSEP----IRQDSLERFA----EKFAASrfdassffa 325
Cdd:PRK08276  229 LIERYRVTHSQLvPTMFVRML--KLPEEVRARYDVSSLRVAIHAAAPcpveVKRAMIDWWGpiihEYYASS--------- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   326 cyglaeatlfvtggqRGQGIpALAVDGEALARnriaegEGSVlmccGRsqPEHAVLIVDAASGEVLGDDNVGEIWAAGPS 405
Cdd:PRK08276  298 ---------------EGGGV-TVITSEDWLAH------PGSV----GK--AVLGEVRILDEDGNELPPGEIGTVYFEMDG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   406 IAHGYWRNPEASAKAfveRDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVesevpsARKGRVAAF 484
Cdd:PRK08276  350 YPFEYHNDPEKTAAA---RNPHGWVTVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLL------VTHPKVADV 420
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620   485 AVtvdgeegIGIA-AEIGRGVQKSV-----------PAQELIDSIRQAVAeAYQeAPKVVALLNpgALPKTSSGKL 548
Cdd:PRK08276  421 AV-------FGVPdEEMGERVKAVVqpadgadagdaLAAELIAWLRGRLA-HYK-CPRSIDFED--ELPRTPTGKL 485
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
1130-1622 4.28e-21

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 100.99  E-value: 4.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPL 1208
Cdd:PRK05677   26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1209 DPDYPSERLAYMLADSGVELLL---TQAHLFERLPGAEGVTPICL--------------------------------DSL 1253
Cdd:PRK05677  106 NPLYTAREMEHQFNDSGAKALVclaNMAHLAEKVLPKTGVKHVIVtevadmlpplkrllinavvkhvkkmvpayhlpQAV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1254 KLDNWPSQAPG-----LHLHGDNLAYVIYTSGSTGQPKGVGNTHAAL-AERLQW--MQATYTLDGDDVLMQKAPV----S 1321
Cdd:PRK05677  186 KFNDALAKGAGqpvteANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCraLMGSNLNEGCEILIAPLPLyhiyA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1322 FDVsvwECFWPLVTGCRLVLAApgehrDPARLVELVRQFGVTTLHFVPPLLQLFidepgVAACGS----------LRRLF 1391
Cdd:PRK05677  266 FTF---HCMAMMLIGNHNILIS-----NPRDLPAMVKELGKWKFSGFVGLNTLF-----VALCNNeafrkldfsaLKLTL 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1392 SGGEALPAELRNRvLQRLPAVALHNRYGPTETAINVThwQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCI 1471
Cdd:PRK05677  333 SGGMALQLATAER-WKEVTGCAICEGYGMTETSPVVS--VNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1472 GGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVA 1551
Cdd:PRK05677  410 KGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVL 482
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  1552 Q-AVVVIREGVAGSQLVGYYTGAVGAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK05677  483 QcAAIGVPDEKSGEAIKVFVVVKPGETLTKEQ---VMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
23-552 4.42e-21

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 99.63  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVP---AYPPE 98
Cdd:cd17652    1 PDAPAVVF------GDETLTYAELNARANRLARLLAARGVGPERLVaLALPRSAELVVAILAVLKAGAAYLPldpAYPAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   99 sarrhhqeRLLSIIADAEPRLVLTTadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvrPEHIAFLQYTSGS 178
Cdd:cd17652   75 --------RIAYMLADARPALLLTT------------------------------------------PDNLAYVIYTSGS 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  179 TALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHD-------MGLIGGllqpifsgvPCVLMSPRYflerpvr 251
Cdd:cd17652  105 TGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDasvwellMALLAG---------ATLVLAPAE------- 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  252 wleaisqyggTVSGGPDFAYRLCSERV--------AESALQRLDLSGWRVAFSGSEPIRQDslerFAEKFAASRfdasSF 323
Cdd:cd17652  169 ----------ELLPGEPLADLLREHRIthvtlppaALAALPPDDLPDLRTLVVAGEACPAE----LVDRWAPGR----RM 230
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  324 FACYGLAEATLFVT--GGQRGQGIPALavdgealarnriaegegsvlmccGRSQPEHAVLIVDAASgEVLGDDNVGEIWA 401
Cdd:cd17652  231 INAYGPTETTVCATmaGPLPGGGVPPI-----------------------GRPVPGTRVYVLDARL-RPVPPGVPGELYI 286
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  402 AGPSIAHGYWRNPEASAKAFV-----ERDGRTWlRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIErTVESEVPS 475
Cdd:cd17652  287 AGAGLARGYLNRPGLTAERFVadpfgAPGSRMY-RTGDLARWRaDGQLEFLGRADDQVKIRGFRIELGEVE-AALTEHPG 364
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  476 arkGRVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELidsiRQAVAEAYQE--APKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd17652  365 ---VAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAEL----RAHLAERLPGymVPAAFVVLD--ALPLTPNGKLDRRA 434
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
2209-2656 5.07e-21

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 100.10  E-value: 5.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2209 GQTLSYAELDARSNRLARVLRShGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL 2288
Cdd:cd05909    5 GTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2289 SHAALFEALGELPAGV----ARWCLEED---------------GPALDAEDPAPLAALSG--PQHQAYLIYTSGSTGKPK 2347
Cdd:cd05909   84 TSKQFIEKLKLHHLFDveydARIVYLEDlrakiskadkckaflAGKFPPKWLLRIFGVAPvqPDDPAVILFTSGSEGLPK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2348 GVAVSHGEIAMHCAAVIECFGMRAEDCELH----FYSINFDAAserLLAPLLCGARVVLrAQGQWGAEEICELIRAEGVS 2423
Cdd:cd05909  164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVVF-HPNPLDYKKIPELIYDKKAT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2424 ILGFTPSYGSQLAQ-WLESQGRQLpvRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVvmplACLAPERLEEGAA 2502
Cdd:cd05909  240 ILLGTPTFLRGYARaAHPEDFSSL--RLVVAGAEKLKDTLRQEFQEKFGIR-ILEGYGTTECS----PVISVNTPQSPNK 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2503 SVPIGSVVGARVAYILD-ADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfaaeGGRLYRTGDLVRLCDNGQ 2581
Cdd:cd05909  313 EGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIDGEGF 384
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 2582 VEYVGRIDHQVKIRGFRIELGEIEARLLEH--PQVREALVLALDSPSGKQLAGYVASAVAEQDEdaqaaLREALKTH 2656
Cdd:cd05909  385 LTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSS-----LNDILKNA 456
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2810-3213 6.23e-21

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 99.31  E-value: 6.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2810 WNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEwlaqhrPLREQEL-----LWHVPVQSFDEC---AELFA 2881
Cdd:cd20484   24 YNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV------PFQKIEPskplsFQEEDISSLKESeiiAYLRE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2882 KAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQA 2961
Cdd:cd20484   98 KAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAWEQD 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2962 YAGSESLREELGWWQARLGGQ-PV-EWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVL 3039
Cdd:cd20484  178 MLAGAEGEEHRAYWKQQLSGTlPIlELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA-RSQSINLSTVFLGIFKLLL 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3040 CRWSGQPSTLVQLEGHGR-EALFDDIdltrsVGWFTSAYPLR--LTPAQSPGESIKaiKEQLRAVphKGLGYGVLRYlad 3116
Cdd:cd20484  257 HRYTGQEDIIVGMPTMGRpEERFDSL-----IGYFINMLPIRsrILGEETFSDFIR--KLQLTVL--DGLDHAAYPF--- 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3117 PAVRQAMAALPT---APItfnylgqFDQSFadaLFQPLDQPTGpIHDEQAPLPNELS---VDG-----------QVYGGE 3179
Cdd:cd20484  325 PAMVRDLNIPRSqanSPV-------FQVAF---FYQNFLQSTS-LQQFLAEYQDVLSiefVEGihqegeyelvlEVYEQE 393
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15597620 3180 --LVLRWTYSRERYDARTVNELAQAYLAELQALIEH 3213
Cdd:cd20484  394 drFTLNIKYNPDLFDASTIERMMEHYVKLAEELIAN 429
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3739-4230 6.25e-21

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 98.96  E-value: 6.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDpghptQRLTRiVELSRTLvlvctq 3818
Cdd:cd05912    2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN-----TRLTP-NELAFQL------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3819 acrEQALALFDELgcvdrprllvwdeiqqgegaehdpqvysgpqnlAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL 3898
Cdd:cd05912   70 ---KDSDVKLDDI---------------------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3899 ELDENDviaqtasqsfdisvwQFLAA-PLF--------------GARVAIVPnavAHDPQGLLAHVGEQGITVLESVPSL 3963
Cdd:cd05912  114 GLTEDD---------------NWLCAlPLFhisglsilmrsviyGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTM 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3964 IQGMLAEERQAL-DGLRWMLPTGEAMPPELARQWLKRypRIGLVNAYGPAE-CSDDVAFfrvdlaSTESTYLPIGS---P 4038
Cdd:cd05912  176 LQRLLEILGEGYpNNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTEtCSQIVTL------SPEDALNKIGSagkP 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4039 tdnnrlyLLGAGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlyRTGDLARRRADGVLEYV 4118
Cdd:cd05912  248 -------LFPVELKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVL 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4119 GRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGAN-GKYLVGYLVpGETPRSSadspaglmveqgawfERIKQQ 4197
Cdd:cd05912  313 DRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVV-SERPISE---------------EELIAY 376
                        490       500       510
                 ....*....|....*....|....*....|...
gi 15597620 4198 LRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05912  377 CSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK07867 PRK07867
acyl-CoA synthetase; Validated
2186-2648 6.52e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 100.14  E-value: 6.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2186 DTLHGLFAARvaASPQAPALTFAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYV 2264
Cdd:PRK07867    5 PTVAELLLPL--AEDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2265 PLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVArwCLEEDGPALDAE-----DPAPLAALSGPQHQAYLIYT 2339
Cdd:PRK07867   83 GLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVR--VINVDSPAWADElaahrDAEPPFRVADPDDLFMLIFT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2340 SGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED-CELH---FYSinfDAASERLLAPLLCGARVVLRAqgQWGAEEICE 2415
Cdd:PRK07867  161 SGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDvCYVSmplFHS---NAVMAGWAVALAAGASIALRR--KFSASGFLP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2416 LIRAEGVSILGFTpsyGSQLAQWL----ESQGRQLPVRMcITGGEALTGEhLQRIRQAFApASFFNAYGPTETVVM---- 2487
Cdd:PRK07867  236 DVRRYGATYANYV---GKPLSYVLatpeRPDDADNPLRI-VYGNEGAPGD-IARFARRFG-CVVVDGFGSTEGGVAitrt 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2488 ---PLACLAPerLEEGAASVPIGSvvGARVA-YILDADLALVPQGATGELY-VGGAGLARGYHERPALSAERfvpdpfaA 2562
Cdd:PRK07867  310 pdtPPGALGP--LPPGVAIVDPDT--GTECPpAEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAER-------M 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2563 EGGRlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQ-LAGYVASAVAE 2640
Cdd:PRK07867  379 RGGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVpDPVVGDQvMAALVLAPGAK 457

                  ....*...
gi 15597620  2641 QDEDAQAA 2648
Cdd:PRK07867  458 FDPDAFAE 465
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1270-1622 6.97e-21

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 97.81  E-value: 6.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1270 DNLAYVIYTSGSTGQPKGVGNTHAAL-------AERL----QWMQA--TYTLDGDDVLMQKA-----PVSFDVSvwECFw 1331
Cdd:PRK07824   35 DDVALVVATSGTTGTPKGAMLTAAALtasadatHDRLggpgQWLLAlpAHHIAGLQVLVRSViagsePVELDVS--AGF- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1332 plvtgcrlvlaapgehrDPARLVELVRQFG----VTTLhfVPPLLQLFIDEP-GVAACGSLRRLFSGGEALPAELRNRVL 1406
Cdd:PRK07824  112 -----------------DPTALPRAVAELGggrrYTSL--VPMQLAKALDDPaATAALAELDAVLVGGGPAPAPVLDAAA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1407 Q-RLPAValhNRYGPTETAinvthwqcraedGERSPIGRPLGNVVCRVLDaefnllpagvaGELCIGGLGLARGYLGRPa 1485
Cdd:PRK07824  173 AaGINVV---RTYGMSETS------------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1486 lsaerfVADPFSAAGerLYRTGDRARWNaDGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA--- 1562
Cdd:PRK07824  226 ------DPDPFAEPG--WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF---GLPddr 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  1563 -GSQLVGYYtgaVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK07824  294 lGQRVVAAV---VGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
2334-2689 7.73e-21

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 97.02  E-value: 7.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2334 AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED---CELHFYSInfdAASERLLAPLLCGARVVLRaqgqwga 2410
Cdd:cd17630    3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDswlLSLPLYHV---GGLAILVRSLLAGAELVLL------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2411 eeicELIRAEGVSILGFTPSYGS----QLAQWLESQG---RQLPVRMCITGGEALTGEHLQRIRQAFAPAsfFNAYGPTE 2483
Cdd:cd17630   73 ----ERNQALAEDLAPPGVTHVSlvptQLQRLLDSGQgpaALKSLRAVLLGGAPIPPELLERAADRGIPL--YTTYGMTE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2484 TVVMPLAClaperleegAASVPIGSVVGARVAYIldaDLALVPQGatgELYVGGAGLARGYHERPalsaerfVPDPFAAE 2563
Cdd:cd17630  147 TASQVATK---------RPDGFGRGGVGVLLPGR---ELRIVEDG---EIWVGGASLAMGYLRGQ-------LVPEFNED 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2564 GgrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQL-AGYVASAVAEQ 2641
Cdd:cd17630  205 G--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQRPvAVIVGRGPADP 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 2642 DEdaqaalreaLKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd17630  283 AE---------LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1132-1556 7.97e-21

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 100.34  E-value: 7.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1132 ELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRD-----KGVgpdvRVAICAERSPQLLVGLLAIVKAGGAYV 1206
Cdd:PRK08751   29 EVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGelqlkKGD----RVALMMPNCLQYPIATFGVLRAGLTVV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1207 PLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPI-------------------------------------- 1248
Cdd:PRK08751  105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVkqvittglgdmlgfpkaalvnfvvkyvkklvpeyring 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1249 ---CLDSLKLDNwPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ----WMQATYTL-DGDDVLMQKAPV 1320
Cdd:PRK08751  185 airFREALALGR-KHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLeEGCEVVITALPL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1321 S--FDVSVWECFWPLVTGCRLVLAAPgehRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC--GSLRRLFSGGEA 1396
Cdd:PRK08751  264 YhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIdfSSLKMTLGGGMA 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1397 LPAELRNRvLQRLPAVALHNRYGPTETAINVTHWQCRAEDGERSpIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGL 1476
Cdd:PRK08751  341 VQRSVAER-WKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGS-IGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1477 ARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:PRK08751  419 MKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1133-1623 8.60e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 99.69  E-value: 8.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1133 LLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:PRK13383   40 LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1213 PSERLAYMLADSGVELLLTQAHLFERLPGAEG----VTPICLDSLKLDNWPSQAPGLHLhgdnlayVIYTSGSTGQPKGV 1288
Cdd:PRK13383  120 RSDALAAALRAHHISTVVADNEFAERIAGADDavavIDPATAGAEESGGRPAVAAPGRI-------VLLTSGTTGKPKGV 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1289 GnthaalaerlqwmqatytldgddvlmQKAPVSFDVSVWECFWP---LVTGCRLVLAAPGEHRDPARLVELVRQFGVTTL 1365
Cdd:PRK13383  193 P--------------------------RAPQLRSAVGVWVTILDrtrLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1366 ---HF-------------------VPPLLQLFIDEPGVAACGS----LRRLFSGGEALPAELRNRVLQRLPAVaLHNRYG 1419
Cdd:PRK13383  247 thrHFdaeaalaqaslhradaftaVPVVLARILELPPRVRARNplpqLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYG 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1420 PTETAINVTHWQCRAEDGERSpIGRPLGNVVCRVLDAefNLLPAG--VAGELCIGGlglargylgrpALSAERFVADPFS 1497
Cdd:PRK13383  326 STEVGIGALATPADLRDAPET-VGKPVAGCPVRILDR--NNRPVGprVTGRIFVGG-----------ELAGTRYTDGGGK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1498 AAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYYTGAVGA 1576
Cdd:PRK13383  392 AVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADnAVIGVPDERFGHRLAAFVVLHPGS 471
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 15597620  1577 EAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALP 1623
Cdd:PRK13383  472 GVDAAQ---LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
2202-2689 1.02e-20

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 99.21  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2202 APALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIED 2281
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2282 SGVRLLLSHAALF----EALGELPAGVARwCLEEDGP---------ALDAEDPAPLAALSGPQHqayLIYTSGSTGKPKG 2348
Cdd:PRK08276   82 SGAKVLIVSAALAdtaaELAAELPAGVPL-LLVVAGPvpgfrsyeeALAAQPDTPIADETAGAD---MLYSSGTTGRPKG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2349 V--AVSHGEIAMHCAA--VIECFGMRAEDCELHFY-SINFDAASERL-LAPLLCGARVVLRAqgQWGAEEICELIRAEGV 2422
Cdd:PRK08276  158 IkrPLPGLDPDEAPGMmlALLGFGMYGGPDSVYLSpAPLYHTAPLRFgMSALALGGTVVVME--KFDAEEALALIERYRV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2423 SILGFTPSygsqlaqwlesqgrqLPVRMCitggeALTGE--------HLQRIRQAFAP------ASFFNAYGP------- 2481
Cdd:PRK08276  236 THSQLVPT---------------MFVRML-----KLPEEvrarydvsSLRVAIHAAAPcpvevkRAMIDWWGPiiheyya 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2482 -TE----TVVMPlaclaperleEGAASVPiGSV---VGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAE 2553
Cdd:PRK08276  296 sSEgggvTVITS----------EDWLAHP-GSVgkaVLGEVR-ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2554 RFVPDPFAAEG--------GRLYrtgdlvrLCDngqveyvgRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DS 2624
Cdd:PRK08276  364 ARNPHGWVTVGdvgyldedGYLY-------LTD--------RKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpDE 428
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  2625 PSGKQLAGYVASAvaeQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK08276  429 EMGERVKAVVQPA---DGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
1156-1564 1.04e-20

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 99.37  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQA-- 1233
Cdd:PRK08008   40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAqf 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1234 ----------------HLF---ERLPGAEGVtpICLDSLKldnwpSQAPG-----LHLHGDNLAYVIYTSGSTGQPKGVG 1289
Cdd:PRK08008  120 ypmyrqiqqedatplrHICltrVALPADDGV--SSFTQLK-----AQQPAtlcyaPPLSTDDTAEILFTSGTTSRPKGVV 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1290 NTHAAL---AERLQWMQAtytLDGDDVLMQKAPvSFDVSvWEC---FWPLVTGCRLVLAapgEHRDPARLVELVRQFGVT 1363
Cdd:PRK08008  193 ITHYNLrfaGYYSAWQCA---LRDDDVYLTVMP-AFHID-CQCtaaMAAFSAGATFVLL---EKYSARAFWGQVCKYRAT 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1364 TLHFVPPLLQLFIDEPGVAA----CgsLRRLF-----SGGEALPAELRNrvlqrlpAVALHNRYGPTETAINVThwQCRA 1434
Cdd:PRK08008  265 ITECIPMMIRTLMVQPPSANdrqhC--LREVMfylnlSDQEKDAFEERF-------GVRLLTSYGMTETIVGII--GDRP 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1435 EDGERSP-IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGL---GLARGYLGRPALSAERFVADPFsaagerLYrTGDRA 1510
Cdd:PRK08008  334 GDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVLEADGW------LH-TGDTG 406
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620  1511 RWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGS 1564
Cdd:PRK08008  407 YVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV---GIKDS 457
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
2188-2689 1.18e-20

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 99.72  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2188 LHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2267
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2268 PEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAG-------VARWC------------------------LEEDGP-- 2314
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSAtkiehviVTRIAdflpfpknllypfvqkkqsnlvvkVSESETih 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2315 ---ALDAEDPAPLAALSGPQHQ-AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCE-----LHFYSINFDA 2385
Cdd:PRK06710  186 lwnSVEKEVNTGVEVPCDPENDlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEvvlgvLPFFHVYGMT 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2386 ASERLlaPLLCGARVVLRAQgqWGAEEICELIRAEGVSILGFTPS-YGSQLAQWLESQGRQLPVRMCITGGEALTGEhLQ 2464
Cdd:PRK06710  266 AVMNL--SIMQGYKMVLIPK--FDMKMVFEAIKKHKVTLFPGAPTiYIALLNSPLLKEYDISSIRACISGSAPLPVE-VQ 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2465 RIRQAFAPASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVvGARVAYILDADLalVPQGATGELYVGGAGLARGY 2544
Cdd:PRK06710  341 EKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDT-EAMIMSLETGEA--LPPGEIGEIVVKGPQIMKGY 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2545 HERPALSAErfvpdpfAAEGGRLYrTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDS 2624
Cdd:PRK06710  418 WNKPEETAA-------VLQDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPD 489
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  2625 P-SGKQLAGYVasaVAEQDEDAQaalREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK06710  490 PyRGETVKAFV---VLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
2209-2666 1.30e-20

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 98.58  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2209 GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL 2288
Cdd:cd05940    1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2289 SHAALfealgelpagvarwcleedgpaldaedpaplaalsgpqhqayLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFG 2368
Cdd:cd05940   81 VDAAL------------------------------------------YIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGG 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2369 MRAED----CeLHFYSINfdAASERLLAPLLCGARVVLRAQgqWGAEEICELIRAEGVSILGftpsYGSQLAQWLESQ-- 2442
Cdd:cd05940  119 ALPSDvlytC-LPLYHST--ALIVGWSACLASGATLVIRKK--FSASNFWDDIRKYQATIFQ----YIGELCRYLLNQpp 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2443 ---GRQLPVRMCItgGEALTGEHLQRIRQAFAPASFFNAYGPTETVV-------MPLAClaperleeGAASVPIGSVVGA 2512
Cdd:cd05940  190 kptERKHKVRMIF--GNGLRPDIWEEFKERFGVPRIAEFYAATEGNSgfinffgKPGAI--------GRNPSLLRKVAPL 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2513 R-VAYILDADLAL---------VPQGATGEL--YVGGAGLARGYHErPALSAERFVPDPFAaEGGRLYRTGDLVRLCDNG 2580
Cdd:cd05940  260 AlVKYDLESGEPIrdaegrcikVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFK-KGDAWFNTGDLMRLDGEG 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2581 QVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAV-AEQDEDAQaalreALKTHLKQ 2659
Cdd:cd05940  338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLqPNEEFDLS-----ALAAHLEK 412

                 ....*..
gi 15597620 2660 QLPDYMV 2666
Cdd:cd05940  413 NLPGYAR 419
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
152-451 1.49e-20

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 98.83  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  152 DPAVAEAWDEPQVR-------PEHIAFLQYTSGSTALPKGVQVSHGNLVA--NEVLIRRGFGIGADDVIVSWLPLYHDMG 222
Cdd:cd17639   66 EDALIHSLNETECSaiftdgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAgiAGLGDRVPELLGPDDRYLAYLPLAHIFE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  223 LI--------GGL-----------------------LQP-IFSGVPCVL----------MSPRYFLERPVRWLeAISQYG 260
Cdd:cd17639  146 LAaenvclyrGGTigygsprtltdkskrgckgdlteFKPtLMVGVPAIWdtirkgvlakLNPMGGLKRTLFWT-AYQSKL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  261 GTVSGGPDFAYrlCSERVAesALQRLDLSG-WRVAFSGSEPIRQDSlERFaekfaasrfdASSFFAC----YGLAEAtlf 335
Cdd:cd17639  225 KALKEGPGTPL--LDELVF--KKVRAALGGrLRYMLSGGAPLSADT-QEF----------LNIVLCPviqgYGLTET--- 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  336 VTGGqrgqgipALAVDGEaLARNRIaegeGSVLMCCgrsqpehAVLIVDAASGEVLGD--DNVGEIWAAGPSIAHGYWRN 413
Cdd:cd17639  287 CAGG-------TVQDPGD-LETGRV----GPPLPCC-------EIKLVDWEEGGYSTDkpPPRGEILIRGPNVFKGYYKN 347
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 15597620  414 PEASAKAFverDGRTWLRTGDLG-FLRDGELFVTGRLKD 451
Cdd:cd17639  348 PEKTKEAF---DGDGWFHTGDIGeFHPDGTLKIIDRKKD 383
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
41-527 1.52e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 98.30  E-value: 1.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   41 LSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVpAYPPESARRHhqerLLSIIADAEPRl 119
Cdd:cd05910    3 LSFRELDERSDRIAQGLTAYgIRRGMRAVLMVPPGPDFFALTFALFKAGAVPV-LIDPGMGRKN----LKQCLQEAEPD- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  120 vlttADLREPLLqmnaqlsaanapqllcvdqldpavaeawDEPqvrpehiAFLQYTSGSTALPKGVQVSHGNLVANEVLI 199
Cdd:cd05910   77 ----AFIGIPKA----------------------------DEP-------AAILFTSGSTGTPKGVVYRHGTFAAQIDAL 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  200 RRGFGIGADDVIVSWLPLYhdmGLIGGLLqpifsGVPCVL--MSPRyfleRPVR-----WLEAISQYGGTVSggpdFAYR 272
Cdd:cd05910  118 RQLYGIRPGEVDLATFPLF---ALFGPAL-----GLTSVIpdMDPT----RPARadpqkLVGAIRQYGVSIV----FGSP 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  273 LCSERVAESALQR-LDLSGWRVAFSGSEPIRQDSLERFaekfaaSRF--DASSFFACYGLAEAtlfvtggqrgqgIPALA 349
Cdd:cd05910  182 ALLERVARYCAQHgITLPSLRRVLSAGAPVPIALAARL------RKMlsDEAEILTPYGATEA------------LPVSS 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  350 VDGEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDN--------VGEIWAAGPSIAHGYWRNPEASAKAF 421
Cdd:cd05910  244 IGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEIDDEPIAEWDDtlelprgeIGEITVTGPTVTPTYVNRPVATALAK 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  422 V-ERDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARKGRVaafavtvdgeeGIGIAae 499
Cdd:cd05910  324 IdDNSEGFWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV-----------GVGKP-- 390
                        490       500
                 ....*....|....*....|....*...
gi 15597620  500 igrGVQKSVPAQELIDSIRQAVAEAYQE 527
Cdd:cd05910  391 ---GCQLPVLCVEPLPGTITPRARLEQE 415
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2174-2695 2.16e-20

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 99.72  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2174 LLAGTAGEAGLQDTlhglfaarvaaspqaPALtFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGL 2253
Cdd:PRK06060    9 LLAEQASEAGWYDR---------------PAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2254 LAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGelPAGVArwcleeDGPALDAE----DPAPLAALSG 2329
Cdd:PRK06060   73 LACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQ--PSRVA------EAAELMSEaarvAPGGYEPMGG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2330 PQHqAYLIYTSGSTGKPKGVAVSHGEI-----AMHCAAViecfGMRAEDCELHFYSINFD-AASERLLAPLLCGARVVLR 2403
Cdd:PRK06060  145 DAL-AYATYTSGTTGPPKAAIHRHADPltfvdAMCRKAL----RLTPEDTGLCSARMYFAyGLGNSVWFPLATGGSAVIN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2404 AQgQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQlPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTE 2483
Cdd:PRK06060  220 SA-PVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFR-SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTE 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2484 tVVMPLACLAPERLEEGAasvpIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPalsaerfvpDPFAAE 2563
Cdd:PRK06060  298 -VGQTFVSNRVDEWRLGT----LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVAN 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2564 GGRLyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQ-LAGYVASAVAEQ- 2641
Cdd:PRK06060  364 EGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGAStLQAFLVATSGATi 442
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620  2642 DEDAQAALREALKThlkqQLPDYMVPAHLLLLASLPLTANGKLDRRALPAPDPA 2695
Cdd:PRK06060  443 DGSVMRDLHRGLLN----RLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPT 492
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2791-3213 2.19e-20

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 97.17  E-value: 2.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2791 ALTPIQHWFFdlpLARRE---------HWNQALLLQPrqaIDLGLLRKSLQRLVEQHDALRLAFRQvDGEwlaQHRPlrE 2861
Cdd:cd19535    3 PLTDVQYAYW---IGRQDdqelggvgcHAYLEFDGED---LDPDRLERAWNKLIARHPMLRAVFLD-DGT---QQIL--P 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2862 QELLWHVPVQSFDECAELFAKAQ----------RSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQ 2931
Cdd:cd19535   71 EVPWYGITVHDLRGLSEEEAEAAleelrerlshRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2932 QVYRQfAEGAEPALPAktsAFRDWAGRLQAYAGSEsLREELGWWQARLGGQPvewpcDRPQ---GDNREALAESV----S 3004
Cdd:cd19535  151 ALYED-PGEPLPPLEL---SFRDYLLAEQALRETA-YERARAYWQERLPTLP-----PAPQlplAKDPEEIKEPRftrrE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3005 LRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDltRSVGWFTSAYPL--RLT 3082
Cdd:cd19535  221 HRLSAEQWQRLKERA-RQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSLLLLevDGS 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3083 PAQSPGESIKAIKEQL-RAVPHKGLgYG--VLRYLAdpavRQAMAALPTAPITFNY-LGQfdQSFADALFQPLDQPTGPI 3158
Cdd:cd19535  298 EGQSFLERARRLQQQLwEDLDHSSY-SGvvVVRRLL----RRRGGQPVLAPVVFTSnLGL--PLLDEEVREVLGELVYMI 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3159 hdEQAP---LpnelsvDGQVY--GGELVLRWTYSRERYDARTVNELAQAYLAELQALIEH 3213
Cdd:cd19535  371 --SQTPqvwL------DHQVYeeDGGLLLNWDAVDELFPEGMLDDMFDAYVRLLERLADD 422
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1122-1511 2.20e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 99.35  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1122 PCEPARAWLPELLERQLAQSAERVAL--------EWDGgsLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLV 1193
Cdd:PRK12582   43 PLGPYPRSIPHLLAKWAAEAPDRPWLaqrepghgQWRK--VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHAL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1194 GLLAIVKAGGAYVPLDPDYPS-----ERLAYM---------LADSGVellltqahLFER---LPGAEGVTPICLD----- 1251
Cdd:PRK12582  121 MTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLfdlvkprvvFAQSGA--------PFARalaALDLLDVTVVHVTgpgeg 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1252 --SLKLDNWPSQAPGLH-------LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDvlmqKAPVSF 1322
Cdd:PRK12582  193 iaSIAFADLAATPPTAAvaaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDP----PPPVSL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1323 DVSVWE-------CFWP-LVTGCRLVLAA----PGEHrdpARLVELVRQFGVTTLHFVPPLLQLFID--EPGVAACGS-- 1386
Cdd:PRK12582  269 DWMPWNhtmggnaNFNGlLWGGGTLYIDDgkplPGMF---EETIRNLREISPTVYGNVPAGYAMLAEamEKDDALRRSff 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1387 --LRRLFSGGEALPAELRNRvLQRLpAVA-------LHNRYGPTETA--INVTHWqcraeDGER-SPIGRPLGNVvcrvl 1454
Cdd:PRK12582  346 knLRLMAYGGATLSDDLYER-MQAL-AVRttghripFYTGYGATETAptTTGTHW-----DTERvGLIGLPLPGV----- 413
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  1455 daEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRAR 1511
Cdd:PRK12582  414 --ELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAAR 461
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
2195-2689 2.49e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 98.22  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2195 RVAASPQAPALTFA--GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2272
Cdd:PRK13391    6 HAQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2273 ERLQYMIEDSGVRLLL-SHAAL---FEALGELPAGVARWCLEEDG---------PALDAEDPAPLA--ALSGPqhqayLI 2337
Cdd:PRK13391   86 AEAAYIVDDSGARALItSAAKLdvaRALLKQCPGVRHRLVLDGDGelegfvgyaEAVAGLPATPIAdeSLGTD-----ML 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2338 YTSGSTGKPKGV--AVSHGEIAMhcAAVIECFGMRAedcelhfysINFDAASERLL-APLLCGA-----RVVLRAQG--- 2406
Cdd:PRK13391  161 YSSGTTGRPKGIkrPLPEQPPDT--PLPLTAFLQRL---------WGFRSDMVYLSpAPLYHSApqravMLVIRLGGtvi 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2407 ---QWGAEEICELIRAEGVSilgftpsyGSQLAQWLESQGRQLPvrmcitggEALTGEH----LQRIRQAFAPAS----- 2474
Cdd:PRK13391  230 vmeHFDAEQYLALIEEYGVT--------HTQLVPTMFSRMLKLP--------EEVRDKYdlssLEVAIHAAAPCPpqvke 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2475 ---------FFNAYGPTETVVMPlACLAPERLEEGaasvpiGSVVGARVA--YILDADLALVPQGATGELYVGGaGLARG 2543
Cdd:PRK13391  294 qmidwwgpiIHEYYAATEGLGFT-ACDSEEWLAHP------GTVGRAMFGdlHILDDDGAELPPGEPGTIWFEG-GRPFE 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2544 YHERPALSAERFVPDPfaaeggRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL- 2622
Cdd:PRK13391  366 YLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVp 439
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  2623 DSPSGKQLAGYV--ASAVaeqdeDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK13391  440 NEDLGEEVKAVVqpVDGV-----DPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
1137-1617 2.56e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 98.16  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1137 QLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSER 1216
Cdd:PRK13390    8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1217 LAYMLADSGVELLLTQAHLFERLPGAEGVTPICLD-SLKLDNWPSQAPGLHLHGDNL------AYVIYTSGSTGQPKGV- 1288
Cdd:PRK13390   88 ADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSfGGEIDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKGIq 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1289 -----------GNTHAALAerlqwmQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGEHRDPARLVElv 1357
Cdd:PRK13390  168 pdlpgrdvdapGDPIVAIA------RAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATLGHVE-- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1358 rQFGVTTLHFVPP----LLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTE----TAINVTH 1429
Cdd:PRK13390  240 -RYRITVTQMVPTmfvrLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEahgmTFIDSPD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1430 WQCRAEDGERSPIGrplgnvVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAE-RFVADPFSAAgerlyrTGD 1508
Cdd:PRK13390  318 WLAHPGSVGRSVLG------DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWTT------VGD 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1509 RARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYYTGAVGAEAEAEQNQRLR 1587
Cdd:PRK13390  386 LGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDvAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELI 465
                         490       500       510
                  ....*....|....*....|....*....|
gi 15597620  1588 AALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:PRK13390  466 DYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
PRK07867 PRK07867
acyl-CoA synthetase; Validated
8-486 2.95e-20

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 98.21  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     8 PTTLVQALRRRAvqEPERLALRFlaeddgEGVVLSYRDLdLRARSIAAALQAHAQLGDR----AVLLFPSgPDYVAAFFG 83
Cdd:PRK07867    4 APTVAELLLPLA--EDDDRGLYF------EDSFTSWREH-IRGSAARAAALRARLDPTRpphvGVLLDNT-PEFSLLLGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    84 CLYAGVIAVPAYPpesARRhhQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQ 163
Cdd:PRK07867   74 AALSGIVPVGLNP---TRR--GAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   164 VRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLmsPR 243
Cdd:PRK07867  149 ADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIAL--RR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   244 YFleRPVRWLEAISQYGGTVSG--GPDFAYRLCSERVAESALQRLdlsgwRVAFsGSEPIRQDsLERFAEKFAASRFDAs 321
Cdd:PRK07867  227 KF--SASGFLPDVRRYGATYANyvGKPLSYVLATPERPDDADNPL-----RIVY-GNEGAPGD-IARFARRFGCVVVDG- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   322 sffacYGLAEATLFVTG------GQRGQGIPALAV-DGEALARnriaegegsvlmcCGRSqpehavliVDAASGEVLGDD 394
Cdd:PRK07867  297 -----FGSTEGGVAITRtpdtppGALGPLPPGVAIvDPDTGTE-------------CPPA--------EDADGRLLNADE 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   395 NVGEIW-AAGPSIAHGYWRNPEASAKAFveRDGRTWlrTGDLGFlRD--GELFVTGRLKDMLIVRGHNLYPQDIERTVeS 471
Cdd:PRK07867  351 AIGELVnTAGPGGFEGYYNDPEADAERM--RGGVYW--SGDLAY-RDadGYAYFAGRLGDWMRVDGENLGTAPIERIL-L 424
                         490
                  ....*....|....*
gi 15597620   472 EVPSArkGRVAAFAV 486
Cdd:PRK07867  425 RYPDA--TEVAVYAV 437
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
2212-2692 3.05e-20

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 97.85  E-value: 3.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHA 2291
Cdd:PRK12406   12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2292 ALFEAL-GELPAGV------------ARWCLEEDGPALDA---------EDPAPLAALSGPQHQAyLIYTSGSTGKPKGV 2349
Cdd:PRK12406   92 DLLHGLaSALPAGVtvlsvptppeiaAAYRISPALLTPPAgaidwegwlAQQEPYDGPPVPQPQS-MIYTSGTTGHPKGV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2350 ---------AVSHGEIAMHCAAVIEcfGMRA-EDCELHFYSIN-FDAASERLlapllcGARVVLraQGQWGAEEICELIR 2418
Cdd:PRK12406  171 rraaptpeqAAAAEQMRALIYGLKP--GIRAlLTGPLYHSAPNaYGLRAGRL------GGVLVL--QPRFDPEELLQLIE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2419 AEGVSILGFTPSYGSQLAQWLESQGRQLPV---RMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVVMPLAClape 2495
Cdd:PRK12406  241 RHRITHMHMVPTMFIRLLKLPEEVRAKYDVsslRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGAVTFAT---- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2496 rlEEGAASVP--IGSVV-GARVAYIlDADLALVPQGATGELYVGGAGLAR-GYHERPALSAErfvpdpfaAEGGRLYRTG 2571
Cdd:PRK12406  316 --SEDALSHPgtVGKAApGAELRFV-DEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--------IDRGGFITSG 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2572 DLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAgyvasAVAEQDEDAQAALr 2650
Cdd:PRK12406  385 DVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIpDAEFGEALM-----AVVEPQPGATLDE- 458
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 15597620  2651 EALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPAP 2692
Cdd:PRK12406  459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
10-553 3.13e-20

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 97.78  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   10 TLVQALRRRAVQEPERLALRflaedDGEGVvLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAG 88
Cdd:cd05920   16 PLGDLLARSAARHPDRIAVV-----DGDRR-LTYRELDRRADRLAAGLRGLgIRPGDRVVVQLPNVAEFVVLFFALLRLG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   89 VIAVPAYPpesARRHHQerLLSIIADAEPRLVLTTADLREpllqmnaqlsaanapqllcVDQLDPAVAEAWDEPQVrpeh 168
Cdd:cd05920   90 AVPVLALP---SHRRSE--LSAFCAHAEAVAYIVPDRHAG-------------------FDHRALARELAESIPEV---- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  169 iAFLQYTSGSTALPKGVQVSHGNLVANevlIRRGF---GIGADDVIVSWLPLYHDM-----GLIGGLLqpiFSGvpCVLM 240
Cdd:cd05920  142 -ALFLLSGGTTGTPKLIPRTHNDYAYN---VRASAevcGLDQDTVYLAVLPAAHNFplacpGVLGTLL---AGG--RVVL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  241 SPRyflERPVRWLEAISQYGGTVSGgpdfayrlcseRVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASrfdA 320
Cdd:cd05920  213 APD---PSPDAAFPLIEREGVTVTA-----------LVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARR---V 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  321 SSFFAC-----YGLAEATLFVTggqrgqgipalavdgealarnRIAEGEGSVLMCCGRS-QPEHAVLIVDAASGEVlGDD 394
Cdd:cd05920  276 PPVLGCtlqqvFGMAEGLLNYT---------------------RLDDPDEVIIHTQGRPmSPDDEIRVVDEEGNPV-PPG 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  395 NVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFL-RDGELFVTGRLKDmLIVR-GHNLYPQDIERTVeSE 472
Cdd:cd05920  334 EEGELLTRGPYTIRGYYRAPEHNARAFTP-DG--FYRTGDLVRRtPDGYLVVEGRIKD-QINRgGEKIAAEEVENLL-LR 408
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  473 VPSARKGRVAAFAVTVDGEEgiGIAAEIGRGVQksVPAQELIDSIRQAVAEAYQeAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd05920  409 HPAVHDAAVVAMPDELLGER--SCAFVVLRDPP--PSAAQLRRFLRERGLAAYK-LPDRIEFVD--SLPLTAVGKIDKKA 481

                 .
gi 15597620  553 C 553
Cdd:cd05920  482 L 482
PRK13382 PRK13382
bile acid CoA ligase;
1144-1625 3.41e-20

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 97.91  E-value: 3.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1144 RVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLAD 1223
Cdd:PRK13382   59 RPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1224 SGVELLLTQAHLFERLPGAEGVTPiclDSLKLDNWPSqAPGLHLH---------------GDNLAYVIYTSGSTGQPKGV 1288
Cdd:PRK13382  139 EGVDTVIYDEEFSATVDRALADCP---QATRIVAWTD-EDHDLTVevliaahagqrpeptGRKGRVILLTSGTTGTPKGA 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1289 GNTHAALAERLQWMQATYTLDGDDVLMQKAPVsfdVSVWEcFWPLVTGcrLVLAAPGEHR---DPARLVELVRQFGVTTL 1365
Cdd:PRK13382  215 RRSGPGGIGTLKAILDRTPWRAEEPTVIVAPM---FHAWG-FSQLVLA--ASLACTIVTRrrfDPEATLDLIDRHRATGL 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1366 HFVPPLLQLFIDEP----GVAACGSLRRLFSGGEALPAELRNRVLQRLPAVaLHNRYGPTETAINVThwqCRAEDGERSP 1441
Cdd:PRK13382  289 AVVPVMFDRIMDLPaevrNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIAT---ATPADLRAAP 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1442 --IGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYL-GRPALSAERFVAdpfsaagerlyrTGDRARWNADGVL 1518
Cdd:PRK13382  365 dtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTsGSTKDFHDGFMA------------SGDVGYLDENGRL 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1519 EYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVA----GSQLVGYYTGAVGAEAEAEQnqrLRAALQAEL 1594
Cdd:PRK13382  433 FVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVI---GVDdeqyGQRLAAFVVLKPGASATPET---LKQHVRDNL 506
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  1595 PEYMVPTQLMRLAQMPLGPSGKLDTRALPEP 1625
Cdd:PRK13382  507 ANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK09192 PRK09192
fatty acyl-AMP ligase;
2212-2660 3.63e-20

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 98.15  E-value: 3.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL-------ERLQYMIEDSGV 2284
Cdd:PRK09192   50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFggresyiAQLRGMLASAQP 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2285 RLLLSHAALFEALGELpAGVARWCLEEDGPALDAEdPAPLAALSGPQHQ--AYLIYTSGSTGKPKGVAVSHGEIaMHCAA 2362
Cdd:PRK09192  130 AAIITPDELLPWVNEA-THGNPLLHVLSHAWFKAL-PEADVALPRPTPDdiAYLQYSSGSTRFPRGVIITHRAL-MANLR 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2363 VIECFGMRAEDCE-----LHFYS----INFdaaserLLAPLLCGARVVLRAQG-------QWgaeeiCELI-RAEGVsiL 2425
Cdd:PRK09192  207 AISHDGLKVRPGDrcvswLPFYHdmglVGF------LLTPVATQLSVDYLPTRdfarrplQW-----LDLIsRNRGT--I 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2426 GFTPSYGSQLAQwLESQGRQLPV------RMCITGGEALTGEHLQRIRQAFAPASF----FNA-YGPTETV----VMPLA 2490
Cdd:PRK09192  274 SYSPPFGYELCA-RRVNSKDLAEldlscwRVAGIGADMIRPDVLHQFAEAFAPAGFddkaFMPsYGLAEATlavsFSPLG 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2491 C------LAPERLEEGAASVPI-------------GSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPAlS 2551
Cdd:PRK09192  353 SgivveeVDRDRLEYQGKAVAPgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE-S 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2552 AERFVPDpfaaegGRLyRTGDLVRLCDnGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVR--EALVLALDSPSGKQ 2629
Cdd:PRK09192  432 QDVLAAD------GWL-DTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEK 503
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  2630 LAGYVASAVAeqDEDAQAALREALKTHLKQQ 2660
Cdd:PRK09192  504 IVLLVQCRIS--DEERRGQLIHALAALVRSE 532
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1-450 3.75e-20

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 99.65  E-value: 3.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     1 MMDAFELPTTLVQALrrraVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAA 80
Cdd:PRK06814  623 MFETSDYDRTLFEAL----IEAAKIHGFKKLAVEDPVNGPLTYRKLLTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVT 698
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    81 FFGCLYAGviAVPAYPPESArrhHQERLLSIIADAEPRLVLTTADLREP--LLQMNAQLSAANA--------PQLLCVDQ 150
Cdd:PRK06814  699 FFALQSAG--RVPAMINFSA---GIANILSACKAAQVKTVLTSRAFIEKarLGPLIEALEFGIRiiyledvrAQIGLADK 773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   151 LDPAVAeaWDEPQV-----RPEHIAFLQYTSGSTALPKGVQVSHGNLVAN--EVLIRRGFgiGADDVIVSWLPLYHDMGL 223
Cdd:PRK06814  774 IKGLLA--GRFPLVyfcnrDPDDPAVILFTSGSEGTPKGVVLSHRNLLANraQVAARIDF--SPEDKVFNALPVFHSFGL 849
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   224 IGGLLQPIFSGVPCVLM-SPRYFLERPvrwlEAISQYGGTVSGGPDF---AYrlcsERVAESalqrLDLSGWRVAFSGSE 299
Cdd:PRK06814  850 TGGLVLPLLSGVKVFLYpSPLHYRIIP----ELIYDTNATILFGTDTflnGY----ARYAHP----YDFRSLRYVFAGAE 917
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   300 PIRQDSLERFAEKFAASRFDAssffacYGLAEATlfvtggqrgqgiPALAVDGEalARNRIaegeGSVlmccGRSQPEha 379
Cdd:PRK06814  918 KVKEETRQTWMEKFGIRILEG------YGVTETA------------PVIALNTP--MHNKA----GTV----GRLLPG-- 967
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   380 vliVDAASGEVLGDDNVGEIWAAGPSIAHGYWRnpeASAKAFVERDGRTWLRTGDLGFLrDGELFVT--GRLK 450
Cdd:PRK06814  968 ---IEYRLEPVPGIDEGGRLFVRGPNVMLGYLR---AENPGVLEPPADGWYDTGDIVTI-DEEGFITikGRAK 1033
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
40-449 3.92e-20

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 97.96  E-value: 3.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    40 VLSYRDLdlRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRhhqerLLSIIADAEPRL 119
Cdd:PRK06334   45 KLSYNQV--RKAVIALATKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLRE-----VTACANLVGVTH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   120 VLTTADLREPLLQMNAQlsAANAP-QLLCVDQLDPAVAeAWDEPQV--------------------RPEHIAFLQYTSGS 178
Cdd:PRK06334  118 VLTSKQLMQHLAQTHGE--DAEYPfSLIYMEEVRKELS-FWEKCRIgiymsipfewlmrwfgvsdkDPEDVAVILFTSGT 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   179 TALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMS-PRYflerPVRWLEAIS 257
Cdd:PRK06334  195 EKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYnPLY----PKKIVEMID 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   258 QYGGTVSGGPD--FAYRLCSERVAESALQRLdlsgwRVAFSGSEPIRqDSLERFAEKFaasrFDASSFFACYGLAEATlf 335
Cdd:PRK06334  271 EAKVTFLGSTPvfFDYILKTAKKQESCLPSL-----RFVVIGGDAFK-DSLYQEALKT----FPHIQLRQGYGTTECS-- 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   336 vtggqrgqgiPALAVDGEALARNRiaegegsvlMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPE 415
Cdd:PRK06334  339 ----------PVITINTVNSPKHE---------SCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDF 399
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 15597620   416 asAKAFVERDGRTWLRTGDLGFL-RDGELFVTGRL 449
Cdd:PRK06334  400 --GQGFVELGGETWYVTGDLGYVdRHGELFLKGRL 432
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3719-4230 4.13e-20

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 97.82  E-value: 4.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3719 FEAQVAAHPQRIAA------SCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLP 3792
Cdd:PRK13295   30 LDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3793 LDPGHPTQRLTRIVELSRTLVLVCTQACR-----EQALALFDEL------------GCVDRPRLLVwdeIQQGEGAEHDP 3855
Cdd:PRK13295  110 LMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaAMARRLRPELpalrhvvvvggdGADSFEALLI---TPAWEQEPDAP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3856 QVYS----GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIaqtasqsfdisvwqFLAAPL----- 3926
Cdd:PRK13295  187 AILArlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVI--------------LMASPMahqtg 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3927 --FGARVAIVPNAVA-----HDPQGLLAHVGEQGIT-VLESVPSL--IQGMLAEERQALDGLRWMLPTGEAMPPELARQw 3996
Cdd:PRK13295  253 fmYGLMMPVMLGATAvlqdiWDPARAAELIRTEGVTfTMASTPFLtdLTRAVKESGRPVSSLRTFLCAGAPIPGALVER- 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3997 lkryPRIGL----VNAYGPAECS-------DDVAffrvDLASTEStylpiGSPTDNNRLYLL-GAGADdafelVPLGAVG 4064
Cdd:PRK13295  332 ----ARAALgakiVSAWGMTENGavtltklDDPD----ERASTTD-----GCPLPGVEVRVVdADGAP-----LPAGQIG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4065 ELCVAGTGVGRGYVGDPLRTAQAFvphpfgapgERLYRTGDLARRRADGVLEYVGRiDHQVKIRGFR-IELGEIEARLHE 4143
Cdd:PRK13295  394 RLQVRGCSNFGGYLKRPQLNGTDA---------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYR 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4144 RADVREAA-VAVQEGANGKYLVGYLVPgeTPRSSADSPAglMVEqgawFERIKQQLRADLPDYMVplhwlVLDRMPLNAN 4222
Cdd:PRK13295  464 HPAIAQVAiVAYPDERLGERACAFVVP--RPGQSLDFEE--MVE----FLKAQKVAKQYIPERLV-----VRDALPRTPS 530

                  ....*...
gi 15597620  4223 GKLDRKAL 4230
Cdd:PRK13295  531 GKIQKFRL 538
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
3727-4233 5.36e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 96.96  E-value: 5.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDpghptQRLTRiV 3806
Cdd:PRK03640   16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN-----TRLSR-E 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3807 ELSRTL-----VLVCTqacrEQALAlfDELGCVDRPRllvWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVM 3881
Cdd:PRK03640   90 ELLWQLddaevKCLIT----DDDFE--AKLIPGISVK---FAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3882 VEQAGMLNNQLSKVPYLELDENDviaqtasqsfdisVWqfLAA-PLF--------------GARVAIVPNAVAHDPQGLL 3946
Cdd:PRK03640  161 QTYGNHWWSAVGSALNLGLTEDD-------------CW--LAAvPIFhisglsilmrsviyGMRVVLVEKFDAEKINKLL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3947 AHvgeQGITVLESVPSLIQGMLAE--ERQALDGLRWMLPTGEAMPP---ELARQWlkrypRIGLVNAYGPAE-CSDDVAf 4020
Cdd:PRK03640  226 QT---GGVTIISVVSTMLQRLLERlgEGTYPSSFRCMLLGGGPAPKpllEQCKEK-----GIPVYQSYGMTEtASQIVT- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4021 frvdLASTESTyLPIGSptdnnrlyllgAG----------ADDAFELVPlGAVGELCVAGTGVGRGYVGDPLRTAQAFVP 4090
Cdd:PRK03640  297 ----LSPEDAL-TKLGS-----------AGkplfpcelkiEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQD 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4091 HPFgapgerlyRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVA-VQEGANGKYLVGYLVP 4169
Cdd:PRK03640  360 GWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgVPDDKWGQVPVAFVVK 431
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  4170 GETPRSsadspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:PRK03640  432 SGEVTE----------------EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
64-550 5.85e-20

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 97.36  E-value: 5.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPEsarrhHQERLLSIIADAEPRLVLTTA-------DLREPLLQMNAQ 136
Cdd:PLN02330   80 GQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTA-----LESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPVIVLGEE 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   137 L--SAANAPQLLcvDQLDPAvAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANevLIRRGFGIGADDV---- 210
Cdd:PLN02330  155 KieGAVNWKELL--EAADRA-GDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVAN--LCSSLFSVGPEMIgqvv 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   211 IVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSpRYFLERPVRWLeaISQYGGTVSGGPDFAYRLCSERVAES-ALQRLDLs 289
Cdd:PLN02330  230 TLGLIPFFHIYGITGICCATLRNKGKVVVMS-RFELRTFLNAL--ITQEVSFAPIVPPIILNLVKNPIVEEfDLSKLKL- 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   290 gwRVAFSGSEPIRQDSLERFAEKFAASRFDASsffacYGLAE-ATLFVTGG--QRGQGIPalavdgealARNRIaegeGS 366
Cdd:PLN02330  306 --QAIMTAAAPLAPELLTAFEAKFPGVQVQEA-----YGLTEhSCITLTHGdpEKGHGIA---------KKNSV----GF 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   367 VLmccgrsqPEHAVLIVDAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAfVERDGrtWLRTGDLGFL-RDGELFV 445
Cdd:PLN02330  366 IL-------PNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRT-IDEDG--WLHTGDIGYIdDDGDIFI 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   446 TGRLKDMLIVRGHNLYPQDIERTVESEvPSARKGRVaafaVTVDGEEGIGIAAEIgrgVQKSVPAQELIDSIRQAVAEAY 525
Cdd:PLN02330  436 VDRIKELIKYKGFQVAPAELEAILLTH-PSVEDAAV----VPLPDEEAGEIPAAC---VVINPKAKESEEDILNFVAANV 507
                         490       500
                  ....*....|....*....|....*
gi 15597620   526 QEAPKVVALLNPGALPKTSSGKLQR 550
Cdd:PLN02330  508 AHYKKVRVVQFVDSIPKSLSGKIMR 532
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3718-4230 7.08e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 96.88  E-value: 7.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQRW--SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:PRK05852   21 LVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3796 GHP-TQRLTRIVELSRTLVLVCTQACREQALA------LFDELGCVDRPRLLVWdEIQQGEGAEHDPqVYSGPQNL---- 3864
Cdd:PRK05852  101 ALPiAEQRVRSQAAGARVVLIDADGPHDRAEPttrwwpLTVNVGGDSGPSGGTL-SVHLDAATEPTP-ATSTPEGLrpdd 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3865 AYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQG 3944
Cdd:PRK05852  179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHT 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3945 LLAHVGEQGITVLESVPSLIQGMLAEERQALDG-----LRWMLPTGEAMPPELArQWLKRYPRIGLVNAYGPAECSDDVA 4019
Cdd:PRK05852  259 FWDDIKAVGATWYTAVPTIHQILLERAATEPSGrkpaaLRFIRSCSAPLTAETA-QALQTEFAAPVVCAFGMTEATHQVT 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4020 FFRVDLASTESTylpigsPTDNNRLYLLGAGAD------DAFELVPlGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpf 4093
Cdd:PRK05852  338 TTQIEGIGQTEN------PVVSTGLVGRSTGAQirivgsDGLPLPA-GAVGEVWLRGTTVVRGYLGDPTITAANFT---- 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4094 gapgERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGET 4172
Cdd:PRK05852  407 ----DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEAVAAVIVPRES 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  4173 PRSSADSpaglmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK05852  483 APPTAEE--------------LVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3722-4230 1.13e-19

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 96.26  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3722 QVAA-HPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQ 3800
Cdd:PRK07470   15 QAARrFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3801 RLTRIVELSRTLVLVC-------TQACREQALALFDELGCVDRPRLLVWDEI-QQGEGAEHDPQVYSGPQNLAYvIYTSG 3872
Cdd:PRK07470   95 EVAYLAEASGARAMIChadfpehAAAVRAASPDLTHVVAIGGARAGLDYEALvARHLGARVANAAVDHDDPCWF-FFTSG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3873 STGLPKGVMVEQAGM---LNNQLSkvpyleldenDVIAQTASQSFDISVwqflaAPL-FGARV-----------AIVPNA 3937
Cdd:PRK07470  174 TTGRPKAAVLTHGQMafvITNHLA----------DLMPGTTEQDASLVV-----APLsHGAGIhqlcqvargaaTVLLPS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3938 VAHDPQGLLAHVGEQGITVLESVPSLIQgMLAE----ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIgLVNAYGPAE 4013
Cdd:PRK07470  239 ERFDPAEVWALVERHRVTNLFTVPTILK-MLVEhpavDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4014 CSDDVAFFRVDLASTEstylpigsPTDNNRLYLLG--------AGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTA 4085
Cdd:PRK07470  317 VTGNITVLPPALHDAE--------DGPDARIGTCGfertgmevQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4086 QAFVPHPFgapgerlyRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLV 4164
Cdd:PRK07470  389 KAFRDGWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlGVPDPVWGEVGV 460
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4165 GYLVPGETPRSSADspaglmvEQGAWferikqqLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK07470  461 AVCVARDGAPVDEA-------ELLAW-------LDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
3861-4233 1.16e-19

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 98.07  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3861 PQNLAYVIYTSGSTGLPKGVMVEQAGMLNN--QLSKVpyLELDENDVIAQTAS--QSFDISVWQFLaaPLF-GARVAIVP 3935
Cdd:PRK08633  781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNieQISDV--FNLRNDDVILSSLPffHSFGLTVTLWL--PLLeGIKVVYHP 856
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3936 NAVahDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYpRIGLVNAYGPA 4012
Cdd:PRK08633  857 DPT--DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHplmFASLRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGAT 933
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4013 ECSDDVAffrVDLASTES--TYLPIGSPTDNNRLYLLGAGAD----DAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQ 4086
Cdd:PRK08633  934 ETSPVAS---VNLPDVLAadFKRQTGSKEGSVGMPLPGVAVRivdpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE 1010
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4087 AFVPhpfgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHER---ADVREAAVAVQEGANGKYL 4163
Cdd:PRK08633 1011 VIKD----IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlggEEVVFAVTAVPDEKKGEKL 1086
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  4164 VGYLVPGETPrssadspaglmveqgawFERIKQQLRA-DLPDYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:PRK08633 1087 VVLHTCGAED-----------------VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3708-4228 1.38e-19

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 96.22  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3708 DYPlEQGYVRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALL---------AERGLDLLG 3778
Cdd:PRK05605   28 DYG-DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVlpncpqhivAFYAVLRLG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3779 MIV-------------GSFK-AGAGY-LPLDPGHPT-QRLTRIVELsRTLVLV-CTQAC-REQALAL----------FDE 3830
Cdd:PRK05605  107 AVVvehnplytaheleHPFEdHGARVaIVWDKVAPTvERLRRTTPL-ETIVSVnMIAAMpLLQRLALrlpipalrkaRAA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3831 L-----GCVDRPRLLVWDEIQQGEGAEHdPQVysGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQL---SKVPYLElDE 3902
Cdd:PRK05605  186 LtgpapGTVPWETLVDAAIGGDGSDVSH-PRP--TPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGLG-DG 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3903 NDViaqtasqsfdisvwqFLAA-PLF---------------GARVAIVPnavAHDPQGLLAHVGEQGITVLESVPSLIQG 3966
Cdd:PRK05605  262 PER---------------VLAAlPMFhaygltlcltlavsiGGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEK 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3967 ML--AEERQ-ALDGLRWMLPTGEAMPPELARQWLKRyprIG--LVNAYGPAECSDDVAFFRVDlASTESTYLPIGSPTDN 4041
Cdd:PRK05605  324 IAeaAEERGvDLSGVRNAFSGAMALPVSTVELWEKL---TGglLVEGYGLTETSPIIVGNPMS-DDRRPGYVGVPFPDTE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4042 NRLyllgAGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHpfgapgerLYRTGDLARRRADGVLEYVGRI 4121
Cdd:PRK05605  400 VRI----VDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRI 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4122 DHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVPGEtpRSSADSPAGLMVEQGAWF--ERIKQQLR 4199
Cdd:PRK05605  468 KELIITGGFNVYPAEVEEVLREHPGVEDAAV-----------VG--LPRE--DGSEEVVAAVVLEPGAALdpEGLRAYCR 532
                         570       580
                  ....*....|....*....|....*....
gi 15597620  4200 ADLPDYMVPLHWLVLDRMPLNANGKLDRK 4228
Cdd:PRK05605  533 EHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
1271-1617 1.50e-19

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 93.33  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1271 NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPV--SFDVSVwECFWPLVTGCRLVlaaPGEHR 1348
Cdd:cd17638    1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAVF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1349 DPARLVELVRQFGVTTLHFVPPLLQLFIDEPGV--AACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTEtAIN 1426
Cdd:cd17638   77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRkkFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTE-AGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1427 VThwQCRAEDGER---SPIGRPLGNVVCRVLDAefnllpagvaGELCIGGLGLARGYLGRPALSAERFVADPFsaagerl 1503
Cdd:cd17638  156 AT--MCRPGDDAEtvaTTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW------- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1504 YRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQL--VGyYTGAVGAEAEAE 1581
Cdd:cd17638  217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVI---GVPDERMgeVG-KAFVVARPGVTL 292
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 15597620 1582 QNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKL 1617
Cdd:cd17638  293 TEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
64-554 1.58e-19

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 96.64  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyPPESARRHH--QERllsiiaDAEPRLVLTTADLREPLlqmnAQLSAAN 141
Cdd:PRK06060   55 GDRVLLCLPDSPDLVQLLLACLARGVMAFLA-NPELHRDDHalAAR------NTEPALVVTSDALRDRF----QPSRVAE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   142 APQLLCvdqlDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVA-NEVLIRRGFGIGADDVIVSWLPLYHD 220
Cdd:PRK06060  124 AAELMS----EAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTfVDAMCRKALRLTPEDTGLCSARMYFA 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   221 MGLIGGLLQPIFSGVPCVLMSpryflerpvrwLEAISQYGGTVS---------GGPDFAYRLCSERVAESalqrldLSGW 291
Cdd:PRK06060  200 YGLGNSVWFPLATGGSAVINS-----------APVTPEAAAILSarfgpsvlyGVPNFFARVIDSCSPDS------FRSL 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   292 RVAFSGSEPIRQDSLERFAEKFAasrfdassffacyglaeatlfvtggqrgqGIPAL-----AVDGEALARNRIAEGEGS 366
Cdd:PRK06060  263 RCVVSAGEALELGLAERLMEFFG-----------------------------GIPILdgigsTEVGQTFVSNRVDEWRLG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   367 VLmccGRSQPEHAVLIVdAASGEVLGDDNVGEIWAAGPSIAHGYWRNPEasakAFVERDGrtWLRTGDLGFLrDGELFVT 446
Cdd:PRK06060  314 TL---GRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD----SPVANEG--WLDTRDRVCI-DSDGWVT 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   447 --GRLKDMLIVRGHNLYPQDIERTV-------ESEVPSARKGRVA----AFAVTVDGEegiGIAAEIGRGVQKSVPAQel 513
Cdd:PRK06060  383 yrCRADDTEVIGGVNVDPREVERLIiedeavaEAAVVAVRESTGAstlqAFLVATSGA---TIDGSVMRDLHRGLLNR-- 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 15597620   514 idsirqavAEAYQeAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:PRK06060  458 --------LSAFK-VPHRFAVVD--RLPRTPNGKLVRGALR 487
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
2336-2619 1.86e-19

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 93.10  E-value: 1.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2336 LIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCEL------HFYSINFdaaserLLAPLLCGARVVLraQGQWG 2409
Cdd:cd17637    5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLnmlplfHIAGLNL------ALATFHAGGANVV--MEKFD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2410 AEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEalTGEHLQRIrQAFAPASFFNAYGPTETvvMPL 2489
Cdd:cd17637   77 PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLD--APETIQRF-EETTGATFWSLYGQTET--SGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2490 ACLAPERLEEGAASVPIgsvVGARVAyILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFvpdpfaaEGGrLYR 2569
Cdd:cd17637  152 VTLSPYRERPGSAGRPG---PLVRVR-IVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-------RNG-WHH 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15597620 2570 TGDLVRLCDNGQVEYVGRIDHQ--VKIRGFRIELGEIEARLLEHPQVREALV 2619
Cdd:cd17637  220 TGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCV 271
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
2197-2689 2.74e-19

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 94.75  E-value: 2.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2197 AASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQ 2276
Cdd:cd05929    3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEAC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2277 YMIEdsgvrlllsHAALFEALGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQhqaYLIYTSGSTGKPKGVAVSHGEI 2356
Cdd:cd05929   83 AIIE---------IKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGW---KMLYSGGTTGRPKGIKRGLPGG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2357 AMHCAAVIEC---FGMRAEDCELH----FYSINFDAAserLLAPLLCGARVVLRaqgQWGAEEICELIRAEGVSILGFTP 2429
Cdd:cd05929  151 PPDNDTLMAAalgFGPGADSVYLSpaplYHAAPFRWS---MTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVP 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2430 SYGSQLAQWLESQGRQLPV----RMCITGgeALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLaCLAPERLEEGAAsvp 2505
Cdd:cd05929  225 TMFVRLLKLPEAVRNAYDLsslkRVIHAA--APCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTI-INGEEWLTHPGS--- 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2506 IGSVVGARVaYILDADLALVPQGATGELYVGGAGlARGYHERPALSAERFVPDPFAAeggrlyrTGDLVRLCDNGQVEYV 2585
Cdd:cd05929  299 VGRAVLGKV-HILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST-------LGDVGYLDEDGYLYLT 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2586 GRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSgkqlAGYVASAVAE--QDEDAQAALREALKTHLKQQLPD 2663
Cdd:cd05929  370 DRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEE----LGQRVHAVVQpaPGADAGTALAEELIAFLRDRLSR 445
                        490       500
                 ....*....|....*....|....*.
gi 15597620 2664 YMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05929  446 YKCPRSIEFVAELPRDDTGKLYRRLL 471
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
149-484 2.77e-19

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 95.57  E-value: 2.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  149 DQLDPAVAEAwdepqvRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLL 228
Cdd:cd17641  146 GLYEREVAAG------KGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVG 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  229 QPIFSG--VPCV-----LMS------PRYFLERPVRWLEAISQYGGTVSGGPDFAYRLcSERVAESALQRLDlsgwrVAF 295
Cdd:cd17641  220 QALVCGfiVNFPeepetMMEdlreigPTFVLLPPRVWEGIAADVRARMMDATPFKRFM-FELGMKLGLRALD-----RGK 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  296 SGSEPIRQDSLER-FAEK--FAASRfdassffACYGLAEATLFVTGGQ----------RGQGIPALAVDGealarnriae 362
Cdd:cd17641  294 RGRPVSLWLRLASwLADAllFRPLR-------DRLGFSRLRSAATGGAalgpdtfrffHAIGVPLKQLYG---------- 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  363 gegsvlmccgrsQPEHAVLIVDAASGEVLGD-------------DNVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtW 429
Cdd:cd17641  357 ------------QTELAGAYTVHRDGDVDPDtvgvpfpgtevriDEVGEILVRSPGVFVGYYKNPEATAEDFDE-DG--W 421
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  430 LRTGDLGFLR-DGELFVTGRLKD-MLIVRGHNLYPQDIERTV-------ESEVPSARKGRVAAF 484
Cdd:cd17641  422 LHTGDAGYFKeNGHLVVIDRAKDvGTTSDGTRFSPQFIENKLkfspyiaEAVVLGAGRPYLTAF 485
PRK05857 PRK05857
fatty acid--CoA ligase;
6-552 3.51e-19

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 95.08  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     6 ELPTTLVQALRRRAVQEPERLALRflaEDDGEGvVLSYRDL---------DLRARSIaaalqahaQLGDRAVLLFPSGPD 76
Cdd:PRK05857   11 QLPSTVLDRVFEQARQQPEAIALR---RCDGTS-ALRYRELvaevgglaaDLRAQSV--------SRGSRVLVISDNGPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    77 YVAAFFGCLYAGVIAVPA---YPPESARRHHQ-ERLLSIIADAEPRlvLTTADLREPLLQMNAQLSAANAPQLLCVDQLD 152
Cdd:PRK05857   79 TYLSVLACAKLGAIAVMAdgnLPIAAIERFCQiTDPAAALVAPGSK--MASSAVPEALHSIPVIAVDIAAVTRESEHSLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   153 PAVAEAwdEPQVRPEHIAFLQYTSGSTALPKGVqvshgnLVANEVL-----IRRGFGIG-----ADDVIVSWLPLYHdmg 222
Cdd:PRK05857  157 AASLAG--NADQGSEDPLAMIFTSGTTGEPKAV------LLANRTFfavpdILQKEGLNwvtwvVGETTYSPLPATH--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   223 lIGGL---LQPIFSGVPCVLMSPRYFLERPVRWLEAISqyggTVSGGPDFAYRLCSE-RVAESALQRLDLsgwrVAFSGS 298
Cdd:PRK05857  226 -IGGLwwiLTCLMHGGLCVTGGENTTSLLEILTTNAVA----TTCLVPTLLSKLVSElKSANATVPSLRL----VGYGGS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   299 EPIRQDSleRFAEkfaASRFDASSFfacYGLAEAtlfvtggqrgqGIPALAVDGEALARNRIAEGegsvlmCCGRSQPEH 378
Cdd:PRK05857  297 RAIAADV--RFIE---ATGVRTAQV---YGLSET-----------GCTALCLPTDDGSIVKIEAG------AVGRPYPGV 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   379 AVLIVDAASGEVLGDD-----NVGEIWAAGPSIAHGYWRNPEASAKAFVErdgrTWLRTGDLGFLR-DGELFVTGRLKDM 452
Cdd:PRK05857  352 DVYLAATDGIGPTAPGagpsaSFGTLWIKSPANMLGYWNNPERTAEVLID----GWVNTGDLLERReDGFFYIKGRSSEM 427
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   453 LIVRGHNLYPQDIERTVESeVPSARKGrvAAFAVTvDGEEGigiaAEIGRGVqksVPAQELIDS----IRQAVAEAYQEA 528
Cdd:PRK05857  428 IICGGVNIAPDEVDRIAEG-VSGVREA--ACYEIP-DEEFG----ALVGLAV---VASAELDESaaraLKHTIAARFRRE 496
                         570       580
                  ....*....|....*....|....*...
gi 15597620   529 PKVVA----LLNPGALPKTSSGKLQRSA 552
Cdd:PRK05857  497 SEPMArpstIVIVTDIPRTQSGKVMRAS 524
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
2196-2664 3.75e-19

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 95.32  E-value: 3.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2196 VAASPQAPALTFAG------QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAG-------GA 2262
Cdd:cd05966   63 LKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavhsvvfAG 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2263 YVPldpeyplERLQYMIEDSGVRLLLSHAALF-------------EALGELP------------------AGVARWCLEE 2311
Cdd:cd05966  143 FSA-------ESLADRINDAQCKLVITADGGYrggkviplkeivdEALEKCPsvekvlvvkrtggevpmtEGRDLWWHDL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2312 DGPALDAEDPAPLAAlsgpQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAEDcelhfysINFDAA---- 2386
Cdd:cd05966  216 MAKQSPECEPEWMDS----EDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKyVFDYHPDD-------IYWCTAdigw 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2387 ----SERLLAPLLCGARVVLR-------AQGQWgaeeiCELIRAEGVSILgftpsYGSQLAqwlesqgrqlpVRMCITGG 2455
Cdd:cd05966  285 itghSYIVYGPLANGATTVMFegtptypDPGRY-----WDIVEKHKVTIF-----YTAPTA-----------IRALMKFG 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2456 EALTGEH-LQRIR------QAFAPAS---FFNAYG----P-------TET---VVMPLACLAPerLEEGAASVPIGSVVG 2511
Cdd:cd05966  344 DEWVKKHdLSSLRvlgsvgEPINPEAwmwYYEVIGkercPivdtwwqTETggiMITPLPGATP--LKPGSATRPFFGIEP 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2512 ArvayILDADLALVPQGATGELYVGGA--GLARGYHERPalsaERFVPDPFAAEGGrLYRTGDLVRLCDNGQVEYVGRID 2589
Cdd:cd05966  422 A----ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKFPG-YYFTGDGARRDEDGYYWITGRVD 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2590 HQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP-SGKQLAGYVasaVAEQDEDAQAALREALKTHLKQQL-----PD 2663
Cdd:cd05966  493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGEAIYAFV---TLKDGEEPSDELRKELRKHVRKEIgpiatPD 569

                 .
gi 15597620 2664 Y 2664
Cdd:cd05966  570 K 570
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
2203-2689 4.18e-19

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 94.89  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2203 PALTFAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIED 2281
Cdd:PRK12492   41 PAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKD 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2282 SGVRLL-------------LSHAA---LFEA-LGELPAGVARWCLEEDGPALDAEDPA---PLA-----AL---SGPQHQ 2333
Cdd:PRK12492  121 SGARALvylnmfgklvqevLPDTGieyLIEAkMGDLLPAAKGWLVNTVVDKVKKMVPAyhlPQAvpfkqALrqgRGLSLK 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2334 ---------AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFysinfDAASERLLAPL---------- 2394
Cdd:PRK12492  201 pvpvglddiAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLM-----KEGQEVMIAPLplyhiyafta 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2395 --LC----GARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYgsqLAQWLESQGRQL---PVRMCITGGEALTGEHLQR 2465
Cdd:PRK12492  276 ncMCmmvsGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLF---VALMDHPGFKDLdfsALKLTNSGGTALVKATAER 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2466 IRQaFAPASFFNAYGPTETvvMPLACLAP--ERLEEGAASVPigsVVGARVAYILDADLALvPQGATGELYVGGAGLARG 2543
Cdd:PRK12492  353 WEQ-LTGCTIVEGYGLTET--SPVASTNPygELARLGTVGIP---VPGTALKVIDDDGNEL-PLGERGELCIKGPQVMKG 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2544 YHERPALSAErfvpdPFAAEGgrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL- 2622
Cdd:PRK12492  426 YWQQPEATAE-----ALDAEG--WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVp 498
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  2623 DSPSGKQLAGYVASavaeqdEDAQAALREaLKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK12492  499 DERSGEAVKLFVVA------RDPGLSVEE-LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
165-550 6.44e-19

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 90.93  E-value: 6.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  165 RPEHIAFlqyTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGgLLQPIFSGVPCVLMspRY 244
Cdd:cd17633    1 NPFYIGF---TSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQ--RK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  245 FleRPVRWLEAISQYGGTVSGG-PDFAYRLCSERVAESALQRLdlsgwrvaFSGSEPIRQDSLERFAEKFA-ASRFDass 322
Cdd:cd17633   75 F--NPKSWIRKINQYNATVIYLvPTMLQALARTLEPESKIKSI--------FSSGQKLFESTKKKLKNIFPkANLIE--- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  323 fFacYGLAEATlFVTGGQRGQGIPALAVdgealarnriaegegsvlmccGRSQPEHAVLIVDAASGEVlgddnvGEIWAA 402
Cdd:cd17633  142 -F--YGTSELS-FITYNFNQESRPPNSV---------------------GRPFPNVEIEIRNADGGEI------GKIFVK 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  403 GPSIAHGYWRNPEASAkafverDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVES---------- 471
Cdd:cd17633  191 SEMVFSGYVRGGFSNP------DG--WMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAipgieeaivv 262
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  472 EVPSARKGRVAAFAVTVDGeegigiaaeigrgvqksVPAQELIDSIRQAVAEayQEAPKVVALLNpgALPKTSSGKLQR 550
Cdd:cd17633  263 GIPDARFGEIAVALYSGDK-----------------LTYKQLKRFLKQKLSR--YEIPKKIIFVD--SLPYTSSGKIAR 320
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3740-4230 7.34e-19

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 92.93  E-value: 7.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVctqa 3819
Cdd:cd05935    3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3820 creqalalfdelgcvdrprllvwdeiqqgegaehdpqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLE 3899
Cdd:cd05935   79 -------------------------------------VGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3900 LDENDVIAQTA----SQSFDISVwqfLAAPLFGARVAIVPNavaHDPQGLLAHVGEQGITVLESVPSLIQGMLAE---ER 3972
Cdd:cd05935  122 LTPSDVILACLplfhVTGFVGSL---NTAVYVGGTYVLMAR---WDRETALELIEKYKVTFWTNIPTMLVDLLATpefKT 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3973 QALDGLRWMLPTGEAMPPELARQWLKRYPrIGLVNAYGPAEcsddvaffrvdlASTESTYLPIGSPtdnnRLYLLGAGAD 4052
Cdd:cd05935  196 RDLSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTE------------TMSQTHTNPPLRP----KLQCLGIP*F 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4053 DAFELV---------PLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPhpfgAPGERLYRTGDLARRRADGVLEYVGRIDH 4123
Cdd:cd05935  259 GVDARVidietgrelPPNEVGEIVVRGPQIFKGYWNRPEETEESFIE----IKGRRFFRTGDLGYMDEEGYFFFVDRVKR 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4124 QVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSADSpaglmveqgawfERIKQQLRADL 4202
Cdd:cd05935  335 MINVSGFKVWPAEVEAKLYKHPAI*EVCViSVPDERVGEEVKAFIVLRPEYRGKVTE------------EDIIEWAREQM 402
                        490       500
                 ....*....|....*....|....*...
gi 15597620 4203 PDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05935  403 AAYKYPREVEFVDELPRSASGKILWRLL 430
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1133-1616 7.82e-19

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 93.52  E-value: 7.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1133 LLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDY 1212
Cdd:cd12118    9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1213 PSERLAYMLADSGVELLLT-QAHLFERL-----PGAEGVTPicldslkLDNWPSQApglhlhgdnlayVIYTSGSTGQPK 1286
Cdd:cd12118   89 DAEEIAFILRHSEAKVLFVdREFEYEDLlaegdPDFEWIPP-------ADEWDPIA------------LNYTSGTTGRPK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1287 GVGNTH-----AALAERLQWmqatyTLDGDDVLMQKAPVsFDVSVWeCF-WPlvtgcrlVLAAPGEH---R--DPARLVE 1355
Cdd:cd12118  150 GVVYHHrgaylNALANILEW-----EMKQHPVYLWTLPM-FHCNGW-CFpWT-------VAAVGGTNvclRkvDAKAIYD 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1356 LVRQFGVTtlHF--VPPLLQLFIDEPGVAACGSLRRL--FSGGEALPAelrnRVLQRLPAVALH--NRYGPTETA--INV 1427
Cdd:cd12118  216 LIEKHKVT--HFcgAPTVLNMLANAPPSDARPLPHRVhvMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYgpATV 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1428 THWQ-------------CRAEDGERSPIGRPLgnvvcRVLDAEFNL-LPA-GV-AGELCIGGLGLARGYLGRPALSAERF 1491
Cdd:cd12118  290 CAWKpewdelpteerarLKARQGVRYVGLEEV-----DVLDPETMKpVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1492 vadpfsAAGerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIR-EGVAGSQLVGYY 1570
Cdd:cd12118  365 ------RGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEKWGEVPCAFV 436
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620 1571 TGAVGAEAEAEQnqrLRAALQAELPEYMVPTQlMRLAQMPLGPSGK 1616
Cdd:cd12118  437 ELKEGAKVTEEE---IIAFCREHLAGFMVPKT-VVFGELPKTSTGK 478
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2822-3100 1.03e-18

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 92.13  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2822 IDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLW-HVPVQSFDECAELFAK-AQRSLDLEQGPLLRAVL 2899
Cdd:cd19532   36 LDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLeHVQISDEAEVEEEFERlKNHVYDLESGETMRIVL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2900 VDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQfaegaePALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARL 2979
Cdd:cd19532  116 LSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG------QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEF 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2980 GGQPvewpcdRP-------QGDNREALAE----SVSLRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVLCRWSGQpst 3048
Cdd:cd19532  190 STLP------EPlpllpfaKVKSRPPLTRydthTAERRLDAALAARIKEAS-RKLRVTPFHFYLAALQVLLARLLDV--- 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 3049 lvqleghgrealfDDI------------DLTRSVGWFTSAYPLRL--TPAQSPGESIKAIKEQLRA 3100
Cdd:cd19532  260 -------------DDIcigiadanrtdeDFMETIGFFLNLLPLRFrrDPSQTFADVLKETRDKAYA 312
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
28-467 1.03e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 93.55  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    28 LRFLAEDDGEGvvLSYRDLD------LRARSIAAALQAHAQLGDR----AVLLfPSGPDYVAAFFGCLYAGVIAVPAYPp 97
Cdd:PRK13388    9 LRDRAGDDTIA--VRYGDRTwtwrevLAEAAARAAALIALADPDRplhvGVLL-GNTPEMLFWLAAAALGGYVLVGLNT- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    98 esARRhhQERLLSIIADAEPRLVLTTADLRePLLQmNAQLSAAnapQLLCVDqlDPAVAEAWDEPQ-------VRPEHIA 170
Cdd:PRK13388   85 --TRR--GAALAADIRRADCQLLVTDAEHR-PLLD-GLDLPGV---RVLDVD--TPAYAELVAAAGaltphreVDAMDPF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   171 FLQYTSGSTALPKGVQVSHGNL-VANEVLIRRgFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLmsPRYFleRP 249
Cdd:PRK13388  154 MLIFTSGTTGAPKAVRCSHGRLaFAGRALTER-FGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVAL--PAKF--SA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   250 VRWLEAISQYGGTVSG--GPDFAYRLCSERVAESALQRLdlsgwRVAFsGSEPIRQDsLERFAEKFAASRFDAssffacY 327
Cdd:PRK13388  229 SGFLDDVRRYGATYFNyvGKPLAYILATPERPDDADNPL-----RVAF-GNEASPRD-IAEFSRRFGCQVEDG------Y 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   328 GLAEATLFVT------GGQRGQGIPALA-VDGEALArnriaegegsvlmccgrsqpEHAVLIVDAAsGEVL-GDDNVGEI 399
Cdd:PRK13388  296 GSSEGAVIVVrepgtpPGSIGRGAPGVAiYNPETLT--------------------ECAVARFDAH-GALLnADEAIGEL 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   400 W-AAGPSIAHGYWRNPEASAKAFveRDGRTWlrTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIER 467
Cdd:PRK13388  355 VnTAGAGFFEGYYNNPEATAERM--RHGMYW--SGDLAYRdADGWIYFAGRTADWMRVDGENLSAAPIER 420
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
9-550 1.11e-18

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 93.27  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALRflaedDGEGVVLSYRDLDLRARSIAA-ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYA 87
Cdd:PRK06087   23 ASLADYWQQTARAMPDKIAVV-----DNHGASYTYSALDHAASRLANwLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    88 GVIAVPAYPpesarRHHQERLLSIIADAEPRLVL--TTADLREPLLQMnaqLSAAN-APQL---LCVDQLDPAVAEAW-- 159
Cdd:PRK06087   98 GAVSVPLLP-----SWREAELVWVLNKCQAKMFFapTLFKQTRPVDLI---LPLQNqLPQLqqiVGVDKLAPATSSLSls 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   160 ----------DEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQ 229
Cdd:PRK06087  170 qiiadyepltTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   230 PIFSGVPCVLMSpRYfleRPVRWLEAISQYGGT-VSGGPDFAYR-LCSERVAESalqrlDLSGWRVAFSGSEPIRQDSLE 307
Cdd:PRK06087  250 PFLIGARSVLLD-IF---TPDACLALLEQQRCTcMLGATPFIYDlLNLLEKQPA-----DLSALRFFLCGGTTIPKKVAR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   308 RFAEKfaasrfdASSFFACYGLAEAtlfvtggqrgqgIPALAVD-GEALARNriaeGEGSvlmccGRSQPEHAVLIVDAA 386
Cdd:PRK06087  321 ECQQR-------GIKLLSVYGSTES------------SPHAVVNlDDPLSRF----MHTD-----GYAAAGVEIKVVDEA 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   387 SGEVLGdDNVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDI 465
Cdd:PRK06087  373 RKTLPP-GCEGEEASRGPNVFMGYLDEPELTARALDE-EG--WYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREV 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   466 E-------RTVESEV---PSARKG-RVAAFAVTVDGEEGIGIAAEIGRGVQKSVPAQ------ELIDsirqavaeayqea 528
Cdd:PRK06087  449 EdillqhpKIHDACVvamPDERLGeRSCAYVVLKAPHHSLTLEEVVAFFSRKRVAKYkypehiVVID------------- 515
                         570       580
                  ....*....|....*....|..
gi 15597620   529 pkvvallnpgALPKTSSGKLQR 550
Cdd:PRK06087  516 ----------KLPRTASGKIQK 527
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
2336-2686 1.43e-18

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 90.40  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2336 LIYTSGSTGKPKGVAVSHGE-IAMHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLC-GARVVLRAQGQWgaEEI 2413
Cdd:cd17635    6 VIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENTTY--KSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2414 CELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVmplACLa 2493
Cdd:cd17635   84 FKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGT---ALC- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2494 perLEEGAASVPIGSV----VGARVaYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVpdpfaaeGGRLYr 2569
Cdd:cd17635  160 ---LPTDDDSIEINAVgrpyPGVDV-YLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWVN- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2570 TGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAEQDEDAQAAL 2649
Cdd:cd17635  228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRAL 307
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 15597620 2650 REAlkthLKQQLPDYMVPAHLLLLASLPLTANGKLDR 2686
Cdd:cd17635  308 KHT----IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
2157-2689 1.64e-18

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 94.22  E-value: 1.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2157 RRIAELPLFAAEERKQLLlagtageaglqDTLHGLFAARVAASPQAPALTFA-GQTLSYAELDARSNRLARVLRsHGVGP 2235
Cdd:PRK08633  597 QAVFELSFDSWKSRKEAL-----------PPLAEAWIDTAKRNWSRLAVADStGGELSYGKALTGALALARLLK-RELKD 664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2236 EVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALG------ELPAGVARWCL 2309
Cdd:PRK08633  665 EENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKnkgfdlELPENVKVIYL 744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2310 EEDGPALDAEDP---------APLAALS-------GPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED 2373
Cdd:PRK08633  745 EDLKAKISKVDKltallaarlLPARLLKrlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD 824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2374 CELH----FYSINFDAAserLLAPLLCGARVVLRAQGQwGAEEICELIRAEGVSILGFTPSYgsqLAQWLESQgRQLP-- 2447
Cdd:PRK08633  825 VILSslpfFHSFGLTVT---LWLPLLEGIKVVYHPDPT-DALGIAKLVAKHRATILLGTPTF---LRLYLRNK-KLHPlm 896
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2448 ---VRMCITGGEALTgehlQRIRQAFApASF----FNAYGPTETVvmPLACL-APERLEEG--------AASV--PI-GS 2508
Cdd:PRK08633  897 fasLRLVVAGAEKLK----PEVADAFE-EKFgiriLEGYGATETS--PVASVnLPDVLAADfkrqtgskEGSVgmPLpGV 969
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2509 VVgarvaYILDAD-LALVPQGATGELYVGGAGLARGYHERPALSAErFVPDpfaAEGGRLYRTGDLVRLCDNGQVEYVGR 2587
Cdd:PRK08633  970 AV-----RIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD---IDGIGWYVTGDKGHLDEDGFLTITDR 1040
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2588 IDHQVKIRGFRIELGEIE---ARLLEHPQVREALVLALDSPSGKQLAgyvasAVAEQDEDAQAALREALKthlKQQLPDY 2664
Cdd:PRK08633 1041 YSRFAKIGGEMVPLGAVEeelAKALGGEEVVFAVTAVPDEKKGEKLV-----VLHTCGAEDVEELKRAIK---ESGLPNL 1112
                         570       580
                  ....*....|....*....|....*
gi 15597620  2665 MVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK08633 1113 WKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK07529 PRK07529
AMP-binding domain protein; Validated
3705-4242 2.01e-18

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 93.10  E-value: 2.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3705 SARDYPlEQGYVRLFEAqVAAHPQRIAASCLEQ--------RWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDL 3776
Cdd:PRK07529   19 AARDLP-ASTYELLSRA-AARHPDAPALSFLLDadpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPET 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3777 LGMIVGSFKAG--AGYLP-LDPGHptqrLTRIVELSRTLVLVC------------TQACREQALALFDELgCVDRPRLL- 3840
Cdd:PRK07529   97 HFALWGGEAAGiaNPINPlLEPEQ----IAELLRAAGAKVLVTlgpfpgtdiwqkVAEVLAALPELRTVV-EVDLARYLp 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3841 ---VW-----------------DEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLEL 3900
Cdd:PRK07529  172 gpkRLavplirrkaharildfdAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3901 DENDVIaqtasqsfdisvwqFLAAPLF---------------GARVAIVPNAVAHDPqGLLAH----VGEQGITVLESVP 3961
Cdd:PRK07529  252 GPGDTV--------------FCGLPLFhvnallvtglaplarGAHVVLATPQGYRGP-GVIANfwkiVERYRINFLSGVP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3962 SLIQGMLAEERQALD--GLRWMLPTGEAMPPELARQWLKRyPRIGLVNAYGPAECSDDVAffrVDLASTESTylpIGS-- 4037
Cdd:PRK07529  317 TVYAALLQVPVDGHDisSLRYALCGAAPLPVEVFRRFEAA-TGVRIVEGYGLTEATCVSS---VNPPDGERR---IGSvg 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4038 ---PTDNNRLYLLGAGADDAFELVPlGAVGELCVAGTGVGRGYVgDPLRTAQAFVphpfgapGERLYRTGDLARRRADGV 4114
Cdd:PRK07529  390 lrlPYQRVRVVILDDAGRYLRDCAV-DEVGVLCIAGPNVFSGYL-EAAHNKGLWL-------EDGWLNTGDLGRIDADGY 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4115 LEYVGRidhqVK---IR-GFRIELGEIEARLHERADVREAAVAVQEGAN-GKYLVGY--LVPGetprsSADSPAGLMveq 4187
Cdd:PRK07529  461 FWLTGR----AKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHaGELPVAYvqLKPG-----ASATEAELL--- 528
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4188 gAWferikqqLRADLPD-YMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQNQA 4242
Cdd:PRK07529  529 -AF-------ARDHIAErAAVPKHVRILDALPKTAVGKIFKPALRRDAIRRVLRAA 576
PRK05850 PRK05850
acyl-CoA synthetase; Validated
2187-2596 2.08e-18

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 92.70  E-value: 2.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2187 TLHGLFAARVAASPQAPALTF-------AG--QTLSYAELDARSNRLARVLRSHGVGPEVRVGLAlERSLEMVVGLLAIL 2257
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFidyeqdpAGvaETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2258 KAGGAYVPLDPEYP---LERLQYMIEDSGVRLLLSHAALFEALGE----LPAGVARWCLEEDGPALDAEDPAPLAALSGP 2330
Cdd:PRK05850   81 QAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVVDDVTEyvapQPGQSAPPVIEVDLLDLDSPRGSDARPRDLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2331 QhQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFgMRAEDCE----------LHFYSinfDAAserLL----APLLC 2396
Cdd:PRK05850  161 S-TAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY-FGDTGGVpppdttvvswLPFYH---DMG---LVlgvcAPILG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2397 GARVVL-------RAQGQWgaeeicelIRAEGVSILGFT--PSYGSQLAQWLESQ----GRQL-PVRMCITGGEALTGEH 2462
Cdd:PRK05850  233 GCPAVLtspvaflQRPARW--------MQLLASNPHAFSaaPNFAFELAVRKTSDddmaGLDLgGVLGIISGSERVHPAT 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2463 LQRIRQAFAPasfFN--------AYGPTETVVM----------PLACLAPERLEEGAAsVPIGSVVGAR-VAY------- 2516
Cdd:PRK05850  305 LKRFADRFAP---FNlretairpSYGLAEATVYvatrepgqppESVRFDYEKLSAGHA-KRCETGGGTPlVSYgsprspt 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2517 --ILDADLAL-VPQGATGELYVGGAGLARGYHERPALSAERF-----VPDPFAAEGGRLyRTGDLVRLCDnGQVEYVGRI 2588
Cdd:PRK05850  381 vrIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSPGTPEGPWL-RTGDLGFISE-GELFIVGRI 458

                  ....*...
gi 15597620  2589 DHQVKIRG 2596
Cdd:PRK05850  459 KDLLIVDG 466
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
1166-1566 2.26e-18

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 92.55  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1166 LAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLD-----------------------------------P 1210
Cdd:PLN02860   45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsfeeaksamllvrpvmlvtdetcsswyeelqnD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1211 DYPSERLaYMLADSGVELLLTQAHLFERlpgAEGVTPICLDSLKLDnwPSQAPglhlhgDNLAYVIYTSGSTGQPKGVGN 1290
Cdd:PLN02860  125 RLPSLMW-QVFLESPSSSVFIFLNSFLT---TEMLKQRALGTTELD--YAWAP------DDAVLICFTSGTTGRPKGVTI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1291 THAALAERLQWMQATYTLDGDDVLMQKAPVsfdvsvweCFWPLVTGCRLVLAAPGEHR-----DPARLVELVRQFGVTTL 1365
Cdd:PLN02860  193 SHSALIVQSLAKIAIVGYGEDDVYLHTAPL--------CHIGGLSSALAMLMVGACHVllpkfDAKAALQAIKQHNVTSM 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1366 HFVPPLLQLFID---EPGVAACG-SLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHwqCRAEDGERSP 1441
Cdd:PLN02860  265 ITVPAMMADLISltrKSMTWKVFpSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTF--MTLHDPTLES 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1442 IGRPLGNVVcrvldaEFNLLPAGVAGELCIG------------------GLGLARG------YLGRPALSAERFVADPFS 1497
Cdd:PLN02860  343 PKQTLQTVN------QTKSSSVHQPQGVCVGkpaphvelkigldessrvGRILTRGphvmlgYWGQNSETASVLSNDGWL 416
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  1498 AagerlyrTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQL 1566
Cdd:PLN02860  417 D-------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV---GVPDSRL 475
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2792-3213 2.38e-18

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 90.89  E-value: 2.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2792 LTPIQH--WFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELlwHVP 2869
Cdd:cd19533    4 LTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPI--RHI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2870 VQSFDECAELFAKA------QRSLDLEQGPLLRAVLVDgpAGEQRLL--LAIHHLVVDGVSWRVLLEDLQQVYRQFAEGA 2941
Cdd:cd19533   82 DLSGDPDPEGAAQQwmqedlRKPLPLDNDPLFRHALFT--LGDNRHFwyQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2942 EPALPAKTSaFRDWAGRLQAYAGSESLREELGWWQARLGGQPvEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApA 3021
Cdd:cd19533  160 PAPPAPFGS-FLDLVEEEQAYRQSERFERDRAFWTEQFEDLP-EPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAA-E 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3022 AYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREalfdDIDLTRSVGWFTSAYPLRLTPAqsPGESIKAIKEQLRAV 3101
Cdd:cd19533  237 AHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRL----GAAARQTPGMVANTLPLRLTVD--PQQTFAELVAQVSRE 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3102 PHKGLGYGVLRY-LADPAVRQAMAALPTAPITFNYLG-QFDQSFADALFQPLDQPTGPIhdeqaplpNELSVdgQVY--- 3176
Cdd:cd19533  311 LRSLLRHQRYRYeDLRRDLGLTGELHPLFGPTVNYMPfDYGLDFGGVVGLTHNLSSGPT--------NDLSI--FVYdrd 380
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597620 3177 -GGELVLRWTYSRERYDARTVNELAQAYLAELQALIEH 3213
Cdd:cd19533  381 dESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
693-946 2.50e-18

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 90.82  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  693 QSAAYNIPGGLRLRGELDEAALRASFQRLVERHEALRTRFLERD-GAALQRIDERGEFAWQFVDLAALAEHERAAAaaqr 771
Cdd:cd19545   18 QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDsGGLLQVVVKESPISWTESTSLDEYLEEDRAA---- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  772 reaeaqqPFDLeKGPLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPlelhYAEFAaw 851
Cdd:cd19545   94 -------PMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSR----FVKYL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  852 QRQWLDAGEGarqlaYWRERLGDTAPVleLATDHPRTARQASPAARYSLRVDEA--LARAIREAALdheasvfmwLLAAF 929
Cdd:cd19545  160 RQLDDEAAAE-----FWRSYLAGLDPA--VFPPLPSSRYQPRPDATLEHSISLPssASSGVTLATV---------LRAAW 223
                        250
                 ....*....|....*..
gi 15597620  930 QALLHRHSGQGEIRIGV 946
Cdd:cd19545  224 ALVLSRYTGSDDVVFGV 240
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
3280-3555 2.83e-18

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 90.32  E-value: 2.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3280 RIDSPLDPERFAAAWQAVVARHEALRASFVwNAGETMLQVI--HKPGRTRIEFLD-WSELpedgheerlqalhkrEREag 3356
Cdd:cd19537   31 RLSGDVDRDRLASAWNTVLARHRILRSRYV-PRDGGLRRSYssSPPRVQRVDTLDvWKEI---------------NRP-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3357 FDLLEQPPfhlrlIRLgearywFMMSNH------HILIDAWCRGLLMNDFFEIYSalGESRPanlPTPPRYRDYIAWlQR 3430
Cdd:cd19537   93 FDLEREDP-----IRV------FISPDTllvvmsHIICDLTTLQLLLREVSAAYN--GKLLP---PVRREYLDSTAW-SR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3431 QDLEQSRRWWSESLRGFerPTLVPSDRPFLREHAGESggmivgdRYTRLDAADGARLRELAQRYQLTVNTFAQAAWALTL 3510
Cdd:cd19537  156 PASPEDLDFWSEYLSGL--PLLNLPRRTSSKSYRGTS-------RVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALAL 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15597620 3511 RRFSGERDVLFGVTVAGRPVgmPEMQRTVGLFINSIPLRVQMPAA 3555
Cdd:cd19537  227 QDLSDRTDIVLGAPYLNRTS--EEDMETVGLFLEPLPIRIRFPSS 269
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
1125-1556 3.31e-18

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 91.96  E-value: 3.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1125 PARAWLPELLERQLAQSAERVAL--EWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAG 1202
Cdd:PLN02330   25 PDKLTLPDFVLQDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1203 GAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAeGVTPICLDSLKLD---NWPSQAPGLHLHGDNLAY----- 1274
Cdd:PLN02330  105 GVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGL-GLPVIVLGEEKIEgavNWKELLEAADRAGDTSDNeeilq 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1275 -----VIYTSGSTGQPKGVGNTHAALAERLqwMQATYTLdGDDVLMQKAPVS----FDVS--VWECFWPLVTGCRLVLAA 1343
Cdd:PLN02330  184 tdlcaLPFSSGTTGISKGVMLTHRNLVANL--CSSLFSV-GPEMIGQVVTLGlipfFHIYgiTGICCATLRNKGKVVVMS 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1344 PGEHRdpARLVELVRQfGVTTLHFVPPLLQLFIDEPGVAACG----SLRRLFSGGEALPAELRNRVLQRLPAVALHNRYG 1419
Cdd:PLN02330  261 RFELR--TFLNALITQ-EVSFAPIVPPIILNLVKNPIVEEFDlsklKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYG 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1420 PTE-TAINVTHWQCRAEDG--ERSPIGRPLGNVVCRVLDAEFNL-LPAGVAGELCIGGLGLARGYLGRPALSAERFVADP 1495
Cdd:PLN02330  338 LTEhSCITLTHGDPEKGHGiaKKNSVGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDG 417
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  1496 FsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:PLN02330  418 W-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVV 471
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
2210-2659 3.42e-18

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 91.38  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLL-- 2287
Cdd:cd05932    5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2288 --LSHAALFEALgeLPAGVARwCLEEDGPALDAEDP--------APL--AALSGPQHQAYLIYTSGSTGKPKGVAVSHGE 2355
Cdd:cd05932   85 gkLDDWKAMAPG--VPEGLIS-ISLPPPSAANCQYQwddliaqhPPLeeRPTRFPEQLATLIYTSGTTGQPKGVMLTFGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2356 IAMHCAAVIECFGMRAEDcelhfysinfdaaseRLLAPL-LCgarvvlraqgqwgaeEICELIRAEGVSILG-----FTP 2429
Cdd:cd05932  162 FAWAAQAGIEHIGTEEND---------------RMLSYLpLA---------------HVTERVFVEGGSLYGgvlvaFAE 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2430 SYGS-----QLAQ----------WLESQGR--------------QLPVRMCITGGEALTGEHLQRIRQAF---APAS--- 2474
Cdd:cd05932  212 SLDTfvedvQRARptlffsvprlWTKFQQGvqdkipqqklnlllKIPVVNSLVKRKVLKGLGLDQCRLAGcgsAPVPpal 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2475 ----------FFNAYGPTETVVMPLACLaPERLEEGAASVPIGSVVgarvayildadlalVPQGATGELYVGGAGLARGY 2544
Cdd:cd05932  292 lewyrslglnILEAYGMTENFAYSHLNY-PGRDKIGTVGNAGPGVE--------------VRISEDGEILVRSPALMMGY 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2545 HERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKI-RGFRIELGEIEARLLEHPQVREALVLALD 2623
Cdd:cd05932  357 YKDPEATAEAFTADGF-------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSG 429
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 15597620 2624 SPSGKQLAGYVASAVAEQDEDAQAALREALKTHLKQ 2659
Cdd:cd05932  430 LPAPLALVVLSEEARLRADAFARAELEASLRAHLAR 465
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
3864-4233 3.59e-18

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 88.93  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3864 LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDViAQTASQSFDISVWQFLAAPLFGARVAIVPNAvahdPQ 3943
Cdd:cd17630    2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDS-WLLSLPLYHVGGLAILVRSLLAGAELVLLER----NQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3944 GLLAHVGEQGITVLESVPSLIQGMLAE--ERQALDGLRWMLPTGEAMPPELARQWLKRypRIGLVNAYGPAECSDDVAFF 4021
Cdd:cd17630   77 ALAEDLAPPGVTHVSLVPTQLQRLLDSgqGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETASQVATK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4022 RVDLASTEStylpIGSPTDNNRLYLLGAgaddafelvplgavGELCVAGTGVGRGYVGDPLrtaqafvPHPFGAPGerLY 4101
Cdd:cd17630  155 RPDGFGRGG----VGVLLPGRELRIVED--------------GEIWVGGASLAMGYLRGQL-------VPEFNEDG--WF 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4102 RTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSAdsp 4180
Cdd:cd17630  208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVvGVPDEELGQRPVAVIVGRGPADPAE--- 284
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 4181 aglmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:cd17630  285 -------------LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1730-2043 3.63e-18

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 90.57  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1730 PLSYSQQRMWFLWQLEPDSPAYNVGGLARLSGPLDVARFEAALQALVQRHETLRTTFPSvDGV--PVQRVHGDGGLHMDW 1807
Cdd:cd19544    3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILW-EGLsePVQVVWRQAELPVEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1808 QDFSAlDRDSRQQhLQTLADSEAHRpFDLESGPLLRVCMVK-MAEREHYLVVTLHHIVTEGWAMDIFARELgalyEAFLD 1886
Cdd:cd19544   82 LTLDP-GDDALAQ-LRARFDPRRYR-LDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----QAILA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1887 DRESPLEPlPVQYLDYsVWQRewLESGERQRQLDYWKAQLGN-EHP-----LLELPGDrPRPPVQSHQgdlyrfDLSPEL 1960
Cdd:cd19544  155 GRAAALPP-PVPYRNF-VAQA--RLGASQAEHEAFFREMLGDvDEPtapfgLLDVQGD-GSDITEARL------ALDAEL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1961 AERVRRFNAARGLTmfmtmTATL-----AALLYRYSGQQDL--------RIGAPvanrirPESEGLIGAFLNTQVLRCRL 2027
Cdd:cd19544  224 AQRLRAQARRLGVS-----PASLfhlawALVLARCSGRDDVvfgtvlsgRMQGG------AGADRALGMFINTLPLRVRL 292
                        330
                 ....*....|....*.
gi 15597620 2028 DGQmSVGELLEQVRQT 2043
Cdd:cd19544  293 GGR-SVREAVRQTHAR 307
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
3863-4225 3.92e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 89.10  E-value: 3.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3863 NLAYVIYTSGSTGLPKGVMV--EQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVwQFLAAPLFGARVaiVPNAVaH 3940
Cdd:cd17638    1 DVSDIMFTSGTTGRSKGVMCahRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKA-GIVACLLTGATV--VPVAV-F 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3941 DPQGLLAHVGEQGITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAEC--- 4014
Cdd:cd17638   77 DVDAILEAIERERITVLPGPPTLFQSLLDHpgrKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAgva 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4015 -----SDDVaffrVDLASTESTYLPigsptdnnrlyllgagaddAFElVPLGAVGELCVAGTGVGRGYVGDPLRTAQAfv 4089
Cdd:cd17638  157 tmcrpGDDA----ETVATTCGRACP-------------------GFE-VRIADDGEVLVRGYNVMQGYLDDPEATAEA-- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4090 phpFGAPGerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVP 4169
Cdd:cd17638  211 ---IDADG--WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAV-----------IG--VP 272
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4170 ----GETPRSSADSPAGLMVEQgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKL 4225
Cdd:cd17638  273 dermGEVGKAFVVARPGVTLTE----EDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PRK07638 PRK07638
acyl-CoA synthetase; Validated
3727-4230 4.30e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 90.99  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGvGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIV 3806
Cdd:PRK07638   15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3807 ELSRTLVLVCTQAcreqalaLFDELGCVDRPRLLvWDEIQ-----------QGEGAEHDPqVYSGpqnlayviYTSGSTG 3875
Cdd:PRK07638   94 AISNADMIVTERY-------KLNDLPDEEGRVIE-IDEWKrmiekylptyaPIENVQNAP-FYMG--------FTSGSTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3876 LPKGVMVEQAGMLNNQLSKVPYLELDEND--VIAQTASQSFdisvwqFLAAPL----FGARVAIVPNAVahdPQGLLAHV 3949
Cdd:PRK07638  157 KPKAFLRAQQSWLHSFDCNVHDFHMKREDsvLIAGTLVHSL------FLYGAIstlyVGQTVHLMRKFI---PNQVLDKL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3950 GEQGITVLESVPSLIQGMLAEERqALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSddvafFRVDLASTE 4029
Cdd:PRK07638  228 ETENISVMYTVPTMLESLYKENR-VIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELS-----FVTALVDEE 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4030 STYLP--IGSPTDNNRLYLLGAGaddafelvplgavGELCVAGTgVGRGYVGDPLRTA----QAFVPHPFGAPGerlYRT 4103
Cdd:PRK07638  302 SERRPnsVGRPFHNVQVRICNEA-------------GEEVQKGE-IGTVYVKSPQFFMgyiiGGVLARELNADG---WMT 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4104 -GDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAvqeGANGKYLvgylvpGETPRssadspag 4182
Cdd:PRK07638  365 vRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI---GVPDSYW------GEKPV-------- 427
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 15597620  4183 LMVEQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK07638  428 AIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
2209-2644 4.38e-18

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 91.58  E-value: 4.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2209 GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL 2288
Cdd:PLN02330   53 GKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2289 SHAALFE----------ALGELP-AGVARWcleedGPALDAEDPAPLAALSGPQHQAYLI---YTSGSTGKPKGVAVSHG 2354
Cdd:PLN02330  133 TNDTNYGkvkglglpviVLGEEKiEGAVNW-----KELLEAADRAGDTSDNEEILQTDLCalpFSSGTTGISKGVMLTHR 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2355 E-IAMHCAAViecFGMRAEDCE----------LHFYSInfdaaSERLLAPLLCGARVVlrAQGQWGAEEICELIRAEGVS 2423
Cdd:PLN02330  208 NlVANLCSSL---FSVGPEMIGqvvtlglipfFHIYGI-----TGICCATLRNKGKVV--VMSRFELRTFLNALITQEVS 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2424 ILGFTPSYGSQLAQ---WLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPERLEEG 2500
Cdd:PLN02330  278 FAPIVPPIILNLVKnpiVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGI 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2501 AASVPIGSVVGARVAYILDADLAL-VPQGATGELYVGGAGLARGYHERPALSAERFVPDpfaaegGRLYrTGDLVRLCDN 2579
Cdd:PLN02330  358 AKKNSVGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDED------GWLH-TGDIGYIDDD 430
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2580 GQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVA--SAVAEQDED 2644
Cdd:PLN02330  431 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLpDEEAGEIPAACVVinPKAKESEED 498
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
3720-4327 4.60e-18

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 92.46  E-value: 4.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3720 EAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPT 3799
Cdd:COG3319    3 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3800 QRLTRIVELSRTLVLVCTQACREQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKG 3879
Cdd:COG3319   83 ALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3880 VMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQGITVLES 3959
Cdd:COG3319  163 VLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3960 VPSLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPT 4039
Cdd:COG3319  243 LLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGP 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4040 DNNRLYLLGAGADDAFELVPLGAVGelcVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVG 4119
Cdd:COG3319  323 GLLVLLVLLVLLLPLLLGVGGGGGG---GGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4120 RIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRSSADSPAglmveqgawferikQQLR 4199
Cdd:COG3319  400 RLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLL--------------LLLL 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4200 ADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQnqAYQAPRNELEETLARIWAEVLKVERVGVFDNFFELGGH 4279
Cdd:COG3319  466 LLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAA--AAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGG 543
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 4280 SLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESLAPSEISEQ 4327
Cdd:COG3319  544 SLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSP 591
PRK13382 PRK13382
bile acid CoA ligase;
3740-4232 4.77e-18

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 91.36  E-value: 4.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQ- 3818
Cdd:PRK13382   70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEe 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3819 --ACREQALAlfdelGCVDRPRLLVW-----DEIQQGEGAEHDPQ-VYSGPQNLAYVIYTSGSTGLPKGVMVEQ---AGM 3887
Cdd:PRK13382  150 fsATVDRALA-----DCPQATRIVAWtdedhDLTVEVLIAAHAGQrPEPTGRKGRVILLTSGTTGTPKGARRSGpggIGT 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3888 LNNQLSKVPyLELDENDVIAQTASQSFDISVWQFLAAplfgARVAIVPNAvAHDPQGLLAHVGEQGITVLESVPSLIQGM 3967
Cdd:PRK13382  225 LKAILDRTP-WRAEEPTVIVAPMFHAWGFSQLVLAAS----LACTIVTRR-RFDPEATLDLIDRHRATGLAVVPVMFDRI 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3968 L---AEERQALDG--LRWMLPTGEAMPPELARQWLKRYPRIgLVNAYGPAECSDDVAFFRVDLASTESTylpIGSPTDNN 4042
Cdd:PRK13382  299 MdlpAEVRNRYSGrsLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIATATPADLRAAPDT---AGRPAEGT 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4043 RLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYV-GDPLRTAQAFVPhpfgapgerlyrTGDLARRRADGVLEYVGRI 4121
Cdd:PRK13382  375 EIRIL----DQDFREVPTGEVGTIFVRNDTQFDGYTsGSTKDFHDGFMA------------SGDVGYLDENGRLFVVGRD 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4122 DHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGEtprssadspaglmvEQGAWFERIKQQLRA 4200
Cdd:PRK13382  439 DEMIVSGGENVYPIEVEKTLATHPDVAEAAViGVDDEQYGQRLAAFVVLKP--------------GASATPETLKQHVRD 504
                         490       500       510
                  ....*....|....*....|....*....|..
gi 15597620  4201 DLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK13382  505 NLANYKVPRDIVVLDELPRGATGKILRRELQA 536
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3740-4152 5.90e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 91.17  E-value: 5.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRL-GHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQ 3818
Cdd:PRK08314   37 SYRELLEEAERLaGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3819 ACREQALALFDELGC--------------------------------VDRPRLLVWDE-IQQGEGAehdPQVYSGPQNLA 3865
Cdd:PRK08314  117 ELAPKVAPAVGNLRLrhvivaqysdylpaepeiavpawlraepplqaLAPGGVVAWKEaLAAGLAP---PPHTAGPDDLA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3866 YVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQsFDISVWQ-FLAAPLF-GARVAIVP---NAVAH 3940
Cdd:PRK08314  194 VLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTGMVhSMNAPIYaGATVVLMPrwdREAAA 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3941 DpqgLLAHvgeQGITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPPELARQWLKRYpriGL--VNAYGPAECs 4015
Cdd:PRK08314  273 R---LIER---YRVTHWTNIPTMVVDFLASpglAERDLSSLRYIGGGGAAMPEAVAERLKELT---GLdyVEGYGLTET- 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4016 ddvaffrvdLASTEStylpigSPTDNNRLYLLGA---GAD------DAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQ 4086
Cdd:PRK08314  343 ---------MAQTHS------NPPDRPKLQCLGIptfGVDarvidpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAE 407
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4087 AFVPhpfgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:PRK08314  408 AFIE----IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACV 469
PRK07514 PRK07514
malonyl-CoA synthase; Validated
3718-4230 6.26e-18

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 90.71  E-value: 6.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRiAASCLE----QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3793
Cdd:PRK07514    5 LFDALRAAFADR-DAPFIEtpdgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3794 DPGHPTQRLTRIVELSRTLVLVCTQACREQALALFDELGCvdrPRLLVWDEIQQG---EGAEHDPQ----VYSGPQNLAY 3866
Cdd:PRK07514   84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGA---PHVETLDADGTGsllEAAAAAPDdfetVPRGADDLAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3867 VIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQtasqsfdisvwqflAAPLF---GARVAIVPNAVAH--- 3940
Cdd:PRK07514  161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIH--------------ALPIFhthGLFVATNVALLAGasm 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3941 ------DPQGLLAHVGEQgiTVLESVPSLIQGMLAEE---RQALDGLRwMLPTGEAmpPELA---RQW--------LKRY 4000
Cdd:PRK07514  227 iflpkfDPDAVLALMPRA--TVMMGVPTFYTRLLQEPrltREAAAHMR-LFISGSA--PLLAethREFqertghaiLERY 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4001 priGLvnaygpaecsddvaffrvdlasTEsTYLPIGSPTDNNRLyllgAGA--------------DDAFELVPLGAVGEL 4066
Cdd:PRK07514  302 ---GM----------------------TE-TNMNTSNPYDGERR----AGTvgfplpgvslrvtdPETGAELPPGEIGMI 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4067 CVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERAD 4146
Cdd:PRK07514  352 EVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPG 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4147 VREAAV-AVQEGANGKYLVGYLVPGetPRSSADSpaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKL 4225
Cdd:PRK07514  425 VVESAViGVPHPDFGEGVTAVVVPK--PGAALDE------------AAILAALKGRLARFKQPKRVFFVDELPRNTMGKV 490

                  ....*
gi 15597620  4226 DRKAL 4230
Cdd:PRK07514  491 QKNLL 495
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
2323-2658 6.72e-18

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 89.82  E-value: 6.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2323 PLAALSGPQHQAYLIY-TSGSTGKPKGVAVSHGEI---AMHCAAVIECFGMRAEDCELHFYS-------INFDAASERLl 2391
Cdd:COG1541   74 PFGLFAVPLEEIVRIHaSSGTTGKPTVVGYTRKDLdrwAELFARSLRAAGVRPGDRVQNAFGyglftggLGLHYGAERL- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2392 apllcGARVVLRAQGQwgAEEICELIRAEGVSILGFTPSYGSQLAQWLESQG---RQLPVRMCITGGEALTGEHLQRIRQ 2468
Cdd:COG1541  153 -----GATVIPAGGGN--TERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGidpRDLSLKKGIFGGEPWSEEMRKEIEE 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2469 AFApASFFNAYGPTEtvvmplaclaperleegaasvpIGSVVG----ARVAYILDADLAL-----------VPQGATGEL 2533
Cdd:COG1541  226 RWG-IKAYDIYGLTE----------------------VGPGVAyeceAQDGLHIWEDHFLveiidpetgepVPEGEEGEL 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2534 YVggAGLAR-GYherPALsaeRfvpdpfaaeggrlYRTGDLVRL----CDNG----QVEYV-GRIDHQVKIRGFRIELGE 2603
Cdd:COG1541  283 VV--TTLTKeAM---PLI---R-------------YRTGDLTRLlpepCPCGrthpRIGRIlGRADDMLIIRGVNVFPSQ 341
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2604 IEARLLEHPQVREALVLALDSPSGK-QLAGYVASAVAEQDEDAQAALREALKTHLK 2658
Cdd:COG1541  342 IEEVLLRIPEVGPEYQIVVDREGGLdELTVRVELAPGASLEALAEAIAAALKAVLG 397
PRK09274 PRK09274
peptide synthase; Provisional
3724-4172 7.21e-18

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 90.73  E-value: 7.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3724 AAHPQRIAASCLE----------QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPL 3793
Cdd:PRK09274   17 QERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3794 DPGHPTQRLTRIVELSRTlvlvctQACREQALA-----LF-------DELGCVDRPrlLVW-----DEIQQGEGAEHDPQ 3856
Cdd:PRK09274   97 DPGMGIKNLKQCLAEAQP------DAFIGIPKAhlarrLFgwgkpsvRRLVTVGGR--LLWggttlATLLRDGAAAPFPM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3857 VYSGPQNLAYVIYTSGSTGLPKGVmVEQAGMLNNQLskvpyleldendviaQTASQSFDISVWQF-LAA-PLF------- 3927
Cdd:PRK09274  169 ADLAPDDMAAILFTSGSTGTPKGV-VYTHGMFEAQI---------------EALREDYGIEPGEIdLPTfPLFalfgpal 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3928 GARvAIVPNAVAH-----DPQGLLAHVGEQGITVLESVPSLIQ--GMLAEERQ-ALDGLRWMLPTGEAMPPELA---RQW 3996
Cdd:PRK09274  233 GMT-SVIPDMDPTrpatvDPAKLFAAIERYGVTNLFGSPALLErlGRYGEANGiKLPSLRRVISAGAPVPIAVIerfRAM 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3997 LKRYPRIglVNAYGPAEC-------SDDVAFFRVDLASTESTYLpIGSPTDNNRLYLLGAGA------DDAFELvPLGAV 4063
Cdd:PRK09274  312 LPPDAEI--LTPYGATEAlpissieSREILFATRAATDNGAGIC-VGRPVDGVEVRIIAISDapipewDDALRL-ATGEI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4064 GELCVAGTGVGRGYVGDPLRTAQAFVPHPfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHE 4143
Cdd:PRK09274  388 GEIVVAGPMVTRSYYNRPEATRLAKIPDG---QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNT 464
                         490       500
                  ....*....|....*....|....*....
gi 15597620  4144 RADVREAAvavqegangkyLVGYLVPGET 4172
Cdd:PRK09274  465 HPGVKRSA-----------LVGVGVPGAQ 482
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
2204-2661 7.55e-18

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 91.22  E-value: 7.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2204 ALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAG-------GAYVPldpeyplERLQ 2276
Cdd:cd05967   75 PVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA-------KELA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2277 YMIEDSGVRLLLSHAALFE-------------AL---------------GELPAG---VARWcLEEDGPALDAE--DPAP 2323
Cdd:cd05967  148 SRIDDAKPKLIVTASCGIEpgkvvpykplldkALelsghkphhvlvlnrPQVPADltkPGRD-LDWSELLAKAEpvDCVP 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2324 LAAlsgpQHQAYLIYTSGSTGKPKGVAVSHGEiamHCAAVI----ECFGMRAEDCelhfysinFDAASER---------L 2390
Cdd:cd05967  227 VAA----TDPLYILYTSGTTGKPKGVVRDNGG---HAVALNwsmrNIYGIKPGDV--------WWAASDVgwvvghsyiV 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2391 LAPLLCGARVVLRA--------QGQWgaeeiCELIRAEGVSILgFT-----------PSYGSQLAQWLESQGRQLPVrmc 2451
Cdd:cd05967  292 YGPLLHGATTVLYEgkpvgtpdPGAF-----WRVIEKYQVNAL-FTaptairairkeDPDGKYIKKYDLSSLRTLFL--- 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2452 itGGEALTGEHLQRIRQAFaPASFFNAYGPTET---VVMPLACLAPERLEEGAASVPigsVVGARVAyILDADLALVPQG 2528
Cdd:cd05967  363 --AGERLDPPTLEWAENTL-GVPVIDHWWQTETgwpITANPVGLEPLPIKAGSPGKP---VPGYQVQ-VLDEDGEPVGPN 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2529 ATGELYVGGAgLARGYHERPALSAERFVPDPFAAEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARL 2608
Cdd:cd05967  436 ELGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2609 LEHPQVREALVLALDSPsgkqLAGYVASAVA---EQDEDAQAALREALKTHLKQQL 2661
Cdd:cd05967  514 LSHPAVAECAVVGVRDE----LKGQVPLGLVvlkEGVKITAEELEKELVALVREQI 565
PLN02574 PLN02574
4-coumarate--CoA ligase-like
2186-2689 7.72e-18

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 90.67  E-value: 7.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2186 DTLHGLFAArvAASPQAPALTFA--GQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGA 2262
Cdd:PLN02574   41 DAVSFIFSH--HNHNGDTALIDSstGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2263 YVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVA------------------RWCLEEDGPALdaedPAPL 2324
Cdd:PLN02574  119 VTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIgvpenydfdskriefpkfYELIKEDFDFV----PKPV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2325 AalsGPQHQAYLIYTSGSTGKPKGVAVSHGE-IAMhcaavIECFgMRAEDCE----------------LHFYSINFDAAS 2387
Cdd:PLN02574  195 I---KQDDVAAIMYSSGTTGASKGVVLTHRNlIAM-----VELF-VRFEASQyeypgsdnvylaalpmFHIYGLSLFVVG 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2388 erLLAplLCGARVVLRaqgQWGAEEICELIRAEGVS--------ILGFTPSYGSQLAQWLESqgrqlpVRMCITGGEALT 2459
Cdd:PLN02574  266 --LLS--LGSTIVVMR---RFDASDMVKVIDRFKVThfpvvppiLMALTKKAKGVCGEVLKS------LKQVSCGAAPLS 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2460 GEHLQRIRQAFAPASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDAdlALVPQGATGELYVGGAG 2539
Cdd:PLN02574  333 GKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDWSTG--CLLPPGNCGELWIQGPG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2540 LARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALV 2619
Cdd:PLN02574  411 VMKGYLNNPKATQSTIDKDGW-------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAV 483
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  2620 laldSPSGKQLAGYVASA-VAEQDEDAQAalREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PLN02574  484 ----TAVPDKECGEIPVAfVVRRQGSTLS--QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
1156-1594 9.32e-18

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 90.22  E-value: 9.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQahl 1235
Cdd:cd05932    9 WGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1236 ferlpgaegvtpicldslKLDNWPSQAPGL----------------------------------HLHG-DNLAYVIYTSG 1280
Cdd:cd05932   86 ------------------KLDDWKAMAPGVpeglisislpppsaancqyqwddliaqhppleerPTRFpEQLATLIYTSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1281 STGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVS--FDVSVWECFWpLVTGCRLVLAapgEHRDpaRLVELVR 1358
Cdd:cd05932  148 TTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAhvTERVFVEGGS-LYGGVLVAFA---ESLD--TFVEDVQ 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1359 QFGVTTLHFVPPLLQLF----IDEPGVAA---------CGSL--------------RRLFSGGEALPAEL----RNRVLQ 1407
Cdd:cd05932  222 RARPTLFFSVPRLWTKFqqgvQDKIPQQKlnlllkipvVNSLvkrkvlkglgldqcRLAGCGSAPVPPALlewyRSLGLN 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1408 RLPAvalhnrYGPTETaINVTHwQCRAEDGERSPIGRPLGNVVCRVLDaefnllpagvAGELCIGGLGLARGYLGRPALS 1487
Cdd:cd05932  302 ILEA------YGMTEN-FAYSH-LNYPGRDKIGTVGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEAT 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1488 AERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKL-RGFRIEPEEIQARLLAQPGVaQAVVVIREGVAGSQL 1566
Cdd:cd05932  364 AEAFTADGF-------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAPLA 435
                        490       500
                 ....*....|....*....|....*...
gi 15597620 1567 VGYYTGAVGAEAEAEQNQRLRAALQAEL 1594
Cdd:cd05932  436 LVVLSEEARLRADAFARAELEASLRAHL 463
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
2336-2623 9.72e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 87.94  E-value: 9.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2336 LIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCEL----HFYSINFDAAserLLAPLLCGARVVlrAQGQWGAE 2411
Cdd:cd17638    5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpFFHTFGYKAG---IVACLLTGATVV--PVAVFDVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2412 EICELIRAEGVSILGFTPS-YGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLA 2490
Cdd:cd17638   80 AILEAIERERITVLPGPPTlFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2491 claperlEEGAASVPIGSVVGARVAyilDADLALVPQGatgELYVGGAGLARGYHERPALSAERFVPDpfaaegGRLYrT 2570
Cdd:cd17638  160 -------RPGDDAETVATTCGRACP---GFEVRIADDG---EVLVRGYNVMQGYLDDPEATAEAIDAD------GWLH-T 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2571 GDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALD 2623
Cdd:cd17638  220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVP 272
PRK07867 PRK07867
acyl-CoA synthetase; Validated
1124-1645 1.52e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 89.74  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1124 EPARAWLPELLERqLAQSAERvALEWDGGSLGYAELHARANRLAHYLR---DKGVGPDVRVAIcaERSPQLLVGLLAIVK 1200
Cdd:PRK07867    1 TSSAPTVAELLLP-LAEDDDR-GLYFEDSFTSWREHIRGSAARAAALRarlDPTRPPHVGVLL--DNTPEFSLLLGAAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1201 AGGAYVPLDPDYPSERLAYMLADSGVELLLT---QAHLFERLPGaeGVTPICLDSLK----LDNWPSQAPGL-HLHGDNL 1272
Cdd:PRK07867   77 SGIVPVGLNPTRRGAALARDIAHADCQLVLTesaHAELLDGLDP--GVRVINVDSPAwadeLAAHRDAEPPFrVADPDDL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1273 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWP-LVTGCRLVLAApgehRDPA 1351
Cdd:PRK07867  155 FMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIALRR----KFSA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1352 -RLVELVRQFGVTTLHFVPPLLQLFIDEPGVA--ACGSLRRLFsGGEALPAELRnRVLQRLpAVALHNRYGPTETAINVT 1428
Cdd:PRK07867  231 sGFLPDVRRYGATYANYVGKPLSYVLATPERPddADNPLRIVY-GNEGAPGDIA-RFARRF-GCVVVDGFGSTEGGVAIT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1429 hwqcRAEDGERSPIGRPLGNVvcRVLD---------AEFNLLPAGVA----GELC-IGGLGLARGYLGRPALSAERFvad 1494
Cdd:PRK07867  308 ----RTPDTPPGALGPLPPGV--AIVDpdtgtecppAEDADGRLLNAdeaiGELVnTAGPGGFEGYYNDPEADAERM--- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1495 pfsAAGerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYYTGA 1573
Cdd:PRK07867  379 ---RGG--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEvAVYAVPDPVVGDQVMAALVLA 453
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  1574 VGAEAEAEQNQRLRAAlQAELPEYMVPTQLMRLAQMPLGPSGKLDTRAL-------PEPVWQqrehVEPRTELQRRIAA 1645
Cdd:PRK07867  454 PGAKFDPDAFAEFLAA-QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLsaegvdcADPVWW----IRRLTPSDYAALA 527
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
41-554 1.66e-17

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 88.73  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   41 LSYRDL-DLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAY----PPESARRhhqerllsiIADA 115
Cdd:cd05973    1 LTFGELrALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFtafgPKAIEHR---------LRTS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  116 EPRLVLTTADLRepllqmnaqlsaanapqllcvDQLDpavaeawDEPQVrpehiafLQYTSGSTALPKGVQVSHGNLVAN 195
Cdd:cd05973   72 GARLVVTDAANR---------------------HKLD-------SDPFV-------MMFTSGTTGLPKGVPVPLRALAAF 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  196 EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRYFLERPVRWLEaisQYGGTVSGGPDFAYRLCS 275
Cdd:cd05973  117 GAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIE---RLGVTNLAGSPTAYRLLM 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  276 ERVAESAlQRLDLSgWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVTG----------GQRGQGI 345
Cdd:cd05973  194 AAGAEVP-ARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDH------YGQTELGMVLANhhalehpvhaGSAGRAM 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  346 PALAVDGEALARNRIAEGegsvlmccgrsqpEHAVLIVDAASGEVLgddnvgeiWAAgpsiahGYWRNPEASAkafverD 425
Cdd:cd05973  266 PGWRVAVLDDDGDELGPG-------------EPGRLAIDIANSPLM--------WFR------GYQLPDTPAI------D 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  426 GRtWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIERTV-------ESEV---PSARKGR-VAAFAVTVDGEEG 493
Cdd:cd05973  313 GG-YYLTGDTVeFDPDGSFSFIGRADDVITMSGYRIGPFDVESALiehpavaEAAVigvPDPERTEvVKAFVVLRGGHEG 391
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  494 I-GIAAEIGRGVQKsvpaqelidsirQAVAEAYqeaPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05973  392 TpALADELQLHVKK------------RLSAHAY---PRTIHFVD--ELPKTPSGKIQRFLLR 436
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1130-1315 1.76e-17

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 89.93  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGP-DVrVAICAERSPQLLVGLLAIVKAGGAYVPL 1208
Cdd:PRK08279   39 LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKgDV-VALLMENRPEYLAAWLGLAKLGAVVALL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1209 DPDYPSERLAYMLADSGVELLLT---QAHLFERLP-------------GAEGVTPICLDSLK--LDNWPSQAPGLH--LH 1268
Cdd:PRK08279  118 NTQQRGAVLAHSLNLVDAKHLIVgeeLVEAFEEARadlarpprlwvagGDTLDDPEGYEDLAaaAAGAPTTNPASRsgVT 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15597620  1269 GDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLM 1315
Cdd:PRK08279  198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLY 244
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
2210-2623 2.16e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 88.57  E-value: 2.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLs 2289
Cdd:cd17640    4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 haalfealgelpagvarwcLEEDGPALdaedpaplaalsgpqhqAYLIYTSGSTGKPKGVAVSHGEIAmhcaaviecFGM 2369
Cdd:cd17640   83 -------------------VENDSDDL-----------------ATIIYTSGTTGNPKGVMLTHANLL---------HQI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2370 RaedcelHFYSINFDAASERLLAPL--------LCGARVVLraqgqWGAEEICELIRAEGVSILGFTPSY---------- 2431
Cdd:cd17640  118 R------SLSDIVPPQPGDRFLSILpiwhsyerSAEYFIFA-----CGCSQAYTSIRTLKDDLKRVKPHYivsvprlwes 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2432 ---GSQLAQWLESQGRQLPVRMCITGGE---ALTG-----EHLQRirqafapasFFNA--------YGPTETVVMpLACL 2492
Cdd:cd17640  187 lysGIQKQVSKSSPIKQFLFLFFLSGGIfkfGISGggalpPHVDT---------FFEAigievlngYGLTETSPV-VSAR 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2493 APERLEEGAASVPIGSVVgarvAYILDADL-ALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTG 2571
Cdd:cd17640  257 RLKCNVRGSVGRPLPGTE----IKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTG 325
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2572 DLVRLCDNGQVEYVGRI-DHQVKIRGFRIELGEIEARLLEHPQVREALVLALD 2623
Cdd:cd17640  326 DLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2335-2687 2.18e-17

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 87.44  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2335 YLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAEDCELHFYSINfDAASERLLAP--------------LLCGAR 2399
Cdd:cd05924    7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADfGTGEFTPSEDAHKAAAA-AAGTVMFPAPplmhgtgswtafggLLGGQT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2400 VVLRAQGqWGAEEICELIRAEGVSILGFT-PSYGSQLAQWLESQG-RQLP-VRMCITGGEALTGEHLQRIRQAFAPASFF 2476
Cdd:cd05924   86 VVLPDDR-FDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGpYDLSsLFAISSGGALLSPEVKQGLLELVPNITLV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2477 NAYGPTETVVMPLACLAPERLEEGAASVPIGSVVgarvayILDADLALVPQGATGELYVGGAGL-ARGYHERPALSAERF 2555
Cdd:cd05924  165 DAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV------VLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2556 VpdpfAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLAgyv 2634
Cdd:cd05924  239 P----EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERwGQEVV--- 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2635 asAVAEQDEDAQAALrEALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRR 2687
Cdd:cd05924  312 --AVVQLREGAGVDL-EELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
64-554 2.24e-17

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 89.68  E-value: 2.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAY----PPESARRhhqerllsiIADAEPRLVLT-TADLR-------EPLL 131
Cdd:cd05967  107 GDRVIIYMPMIPEAAIAMLACARIGAIHSVVFggfaAKELASR---------IDDAKPKLIVTaSCGIEpgkvvpyKPLL 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  132 QMNAQLSAANAPQLLCVDQLD-PAVAEA------WDE-----------PqVRPEHIAFLQYTSGSTALPKGVQV-SHGNL 192
Cdd:cd05967  178 DKALELSGHKPHHVLVLNRPQvPADLTKpgrdldWSEllakaepvdcvP-VAATDPLYILYTSGTTGKPKGVVRdNGGHA 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  193 VANEVLIRRGFGIGADDVIVSwlplYHDMGLIGG----LLQPIFSGVPCVLmspryFLERPVRWLEA------ISQYGGT 262
Cdd:cd05967  257 VALNWSMRNIYGIKPGDVWWA----ASDVGWVVGhsyiVYGPLLHGATTVL-----YEGKPVGTPDPgafwrvIEKYQVN 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  263 vsggpdfayRLCSERVAESALQRLDLSGwrvafsgsEPIRQDSLERFAEKFAA-SRFDASSffacYGLAEATLfvtggqr 341
Cdd:cd05967  328 ---------ALFTAPTAIRAIRKEDPDG--------KYIKKYDLSSLRTLFLAgERLDPPT----LEWAENTL------- 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  342 gqGIPALavD-------GEALARNRIAEGEGSV-LMCCGRSQPEHAVLIVDAAsGEVLGDDNVGEIWAAGP---SIAHGY 410
Cdd:cd05967  380 --GVPVI--DhwwqtetGWPITANPVGLEPLPIkAGSPGKPVPGYQVQVLDED-GEPVGPNELGNIVIKLPlppGCLLTL 454
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  411 WRNPEASAKAFVERDgRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------VPSARKG 479
Cdd:cd05967  455 WKNDERFKKLYLSKF-PGYYDTGDAGYKdEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHpavaecavvgVRDELKG 533
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  480 RVA-AFAVTVdgeEGIGIAAEigrGVQKsvpaqELIDSIRQ---AVAeayqeAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05967  534 QVPlGLVVLK---EGVKITAE---ELEK-----ELVALVREqigPVA-----AFRLVIFVK--RLPKTRSGKILRRTLR 594
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1130-1622 2.73e-17

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 88.89  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAqsAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPD----VRVAICAErspqLLVGLLAIVKAGgaY 1205
Cdd:PRK10946   27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGdtalVQLGNVAE----FYITFFALLKLG--V 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1206 VPLDPDYPSERL---AY--------MLADSGVELLLTQAHLFERLPGAEGVTPICLD----SLKLDNWPSQAPGLHLHG- 1269
Cdd:PRK10946   99 APVNALFSHQRSelnAYasqiepalLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLnddgEHSLDDAINHPAEDFTATp 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1270 ---DNLAYVIYTSGSTGQPKGVGNTH-------AALAERLQWMQATYTLdgddvLMQKAPVSFDVSVWECFWPLVTGCRL 1339
Cdd:PRK10946  179 spaDEVAFFQLSGGSTGTPKLIPRTHndyyysvRRSVEICGFTPQTRYL-----CALPAAHNYPMSSPGALGVFLAGGTV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1340 VLAA-PGehrdPARLVELVRQFGVTTLHFVPPLLQLF---IDEPGV-AACGSLRRLFSGGEALPAELRNRVlqrlPAV-- 1412
Cdd:PRK10946  254 VLAPdPS----ATLCFPLIEKHQVNVTALVPPAVSLWlqaIAEGGSrAQLASLKLLQVGGARLSETLARRI----PAElg 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1413 -ALHNRYGPTETAINVThwqcRAEDGERSPI---GRPL-GNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALS 1487
Cdd:PRK10946  326 cQLQQVFGMAEGLVNYT----RLDDSDERIFttqGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1488 AERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREgvagSQLV 1567
Cdd:PRK10946  402 ASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSME----DELM 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  1568 GYYTGAVGAEAEAEQNQRLRAALQAE-LPEYMVPTQLMRLAQMPLGPSGKLDTRAL 1622
Cdd:PRK10946  471 GEKSCAFLVVKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4245-4319 2.91e-17

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 79.13  E-value: 2.91e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 4245 APRNELEETLARIWAEVLKV--ERVGVFDNFF-ELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYIESL 4319
Cdd:COG0236    1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3718-4223 3.49e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 88.65  E-value: 3.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3798 PTQRLTRIVELSRTLVLVCTQACR------------EQALALFDELGCVDR-------PRLLVWDEIQQGEGAEHDP--Q 3856
Cdd:PRK06164   95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavpPDALPPLRAIAVVDDaadatpaPAPGARVQLFALPDPAPPAaaG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3857 VYSGPQNLAYVIYT-SGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVP 3935
Cdd:PRK06164  175 ERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEP 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3936 navAHDPQGLLAHVGEQGITVLESVPSLIQGMLAE--ERQALDGLRWM-----LPTGEAMPPElARQwlKRYPRIGLvna 4008
Cdd:PRK06164  255 ---VFDAARTARALRRHRVTHTFGNDEMLRRILDTagERADFPSARLFgfasfAPALGELAAL-ARA--RGVPLTGL--- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4009 YGPAECSDDVAFFRVDLASTEStYLPIGSPTDNNRLYLLGAGADDAfeLVPLGAVGELCVAGTGVGRGYVGDPLRTAQAF 4088
Cdd:PRK06164  326 YGSSEVQALVALQPATDPVSVR-IEGGGRPASPEARVRARDPQDGA--LLPDGESGEIEIRAPSLMRGYLDNPDATARAL 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4089 VPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREA-AVAVQEGANGKyLVGYL 4167
Cdd:PRK06164  403 TDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAqVVGATRDGKTV-PVAFV 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  4168 VPgeTPRSSADsPAGLMveqgAWferikqqLRADLPDYMVPLHWLVLDRMP--LNANG 4223
Cdd:PRK06164  475 IP--TDGASPD-EAGLM----AA-------CREALAGFKVPARVQVVEAFPvtESANG 518
PRK08315 PRK08315
AMP-binding domain protein; Validated
3717-4224 3.56e-17

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 88.71  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3717 RLFEAQVAAHPQRIAASCLEQ--RWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLD 3794
Cdd:PRK08315   20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3795 PGHPTQRLTRIVELS--RTLVLV-------------------CTQACREQALALFDELGCVDR------PRLLVWDEIQQ 3847
Cdd:PRK08315  100 PAYRLSELEYALNQSgcKALIAAdgfkdsdyvamlyelapelATCEPGQLQSARLPELRRVIFlgdekhPGMLNFDELLA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3848 GEGAEHDPQVYSGPQNLAY--VI---YTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAqtasqsfdISVwqfl 3922
Cdd:PRK08315  180 LGRAVDDAELAARQATLDPddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLC--------IPV---- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3923 aaPLF---------------GArvAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA---LDGLRwmlpT 3984
Cdd:PRK08315  248 --PLYhcfgmvlgnlacvthGA--TMVYPGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFArfdLSSLR----T 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3985 GeAM-----PPELARQWLKRYPRIGLVNAYGPAECS--------DDVAFFRVdlaSTESTYLP-----IGSPTDNnrlyl 4046
Cdd:PRK08315  320 G-IMagspcPIEVMKRVIDKMHMSEVTIAYGMTETSpvstqtrtDDPLEKRV---TTVGRALPhlevkIVDPETG----- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4047 lgagaddafELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPhpfgapgERLYRTGDLARRRADGVLEYVGRIDHQVk 4126
Cdd:PRK08315  391 ---------ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDA-------DGWMHTGDLAVMDEEGYVNIVGRIKDMI- 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4127 IRGfrielG------EIEARLHERADVREAAVavqegangkylVGylVP----GEtprssadspaglmvEQGAWF----- 4191
Cdd:PRK08315  454 IRG-----GeniyprEIEEFLYTHPKIQDVQV-----------VG--VPdekyGE--------------EVCAWIilrpg 501
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 15597620  4192 -----ERIKQQLRADLPDYMVPLHWLVLDRMPLNANGK 4224
Cdd:PRK08315  502 atlteEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3719-4209 3.96e-17

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 88.78  E-value: 3.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3719 FEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHP 3798
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3799 TQRLTRIVELSRTLVLVCTQACREqalaLFDEL-GCVDRPRLLVW---DEIQQGEGAE-----------HDPQVYSGPQ- 3862
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVE----AFEEArADLARPPRLWVaggDTLDDPEGYEdlaaaaagaptTNPASRSGVTa 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3863 -NLAYVIYTSGSTGLPKGVMVEQ----------AGMLNnqlskvpyleLDENDVIAQTA----SQSFDISVWQFLAAplf 3927
Cdd:PRK08279  199 kDTAFYIYTSGTTGLPKAAVMSHmrwlkamggfGGLLR----------LTPDDVLYCCLplyhNTGGTVAWSSVLAA--- 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3928 GARVAIV---------PNAVAHDPQgLLAHVGEQGITVLESVPSliqgmlAEERQalDGLRWMlpTGEAMPPELARQWLK 3998
Cdd:PRK08279  266 GATLALRrkfsasrfwDDVRRYRAT-AFQYIGELCRYLLNQPPK------PTDRD--HRLRLM--IGNGLRPDIWDEFQQ 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3999 RY--PRI-----------GLVNAYG--------PAECSDDVAFFRVDLASTEstylPIgsptdnnRlyllgaGADDAFEL 4057
Cdd:PRK08279  335 RFgiPRIlefyaasegnvGFINVFNfdgtvgrvPLWLAHPYAIVKYDVDTGE----PV-------R------DADGRCIK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4058 VPLGAVGELCVAGTGVGR--GYvGDPLRTAQAFVPHPFgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELG 4135
Cdd:PRK08279  398 VKPGEVGLLIGRITDRGPfdGY-TDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATT 475
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  4136 EIEARLHERADVREAAVavqegangkYlvGYLVPGetprssADSPAG---LMVEQGAWFE--RIKQQLRADLPDYMVPL 4209
Cdd:PRK08279  476 EVENALSGFPGVEEAVV---------Y--GVEVPG------TDGRAGmaaIVLADGAEFDlaALAAHLYERLPAYAVPL 537
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
18-466 4.07e-17

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 88.15  E-value: 4.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   18 RAVQEPERLALRFlaEDDgegvVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVP--- 93
Cdd:cd17655    6 QAEKTPDHTAVVF--EDQ----TLTYRELNERANQLARTLREKGVGPDTIVgIMAERSLEMIVGILGILKAGGAYLPidp 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 AYPpesarrhhQERLLSIIADAEPRLVLTTADLREPLLqmNAQLsaanapqllcVDQLDPAVAEAWD----EPQVRPEHI 169
Cdd:cd17655   80 DYP--------EERIQYILEDSGADILLTQSHLQPPIA--FIGL----------IDLLDEDTIYHEEsenlEPVSKSDDL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  170 AFLQYTSGSTALPKGVQVSHGNLVaNEV--LIRRGFGIGADDVIVsWLPLYHDMGlIGGLLQPIFSGVPCVLmSPRYFLE 247
Cdd:cd17655  140 AYVIYTSGSTGKPKGVMIEHRGVV-NLVewANKVIYQGEHLRVAL-FASISFDAS-VTEIFASLLSGNTLYI-VRKETVL 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  248 RPVRWLEAISQYGGTVSGGPDfayRLCSERVAESALQRLDLsgwRVAFSGSEPIRQDSLERFAEKFAASRfdasSFFACY 327
Cdd:cd17655  216 DGQALTQYIRQNRITIIDLTP---AHLKLLDAADDSEGLSL---KHLIVGGEALSTELAKKIIELFGTNP----TITNAY 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  328 GLAEAT------LFVTGGQRGQGIPAlavdGEALARNRIaegegSVLMCCGRSQPEhavlivdaasGEvlgddnVGEIWA 401
Cdd:cd17655  286 GPTETTvdasiyQYEPETDQQVSVPI----GKPLGNTRI-----YILDQYGRPQPV----------GV------AGELYI 340
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  402 AGPSIAHGYWRNPEASAKAFVE---RDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 466
Cdd:cd17655  341 GGEGVARGYLNRPELTAEKFVDdpfVPGERMYRTGDLArWLPDGNIEFLGRIDHQVKIRGYRIELGEIE 409
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
3850-4230 4.29e-17

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 88.40  E-value: 4.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3850 GAEHD-PQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL----ELDENDVIAQTASQSFDIsvWQFLAA 3924
Cdd:PRK08751  195 GRKHSmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLagtgKLEEGCEVVITALPLYHI--FALTAN 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3925 PLFGARVAIVPNAVAH--DPQGLLAHVGEQGITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPPELARQWlKR 3999
Cdd:PRK08751  273 GLVFMKIGGCNHLISNprDMPGFVKELKKTRFTAFTGVNTLFNGLLNTpgfDQIDFSSLKMTLGGGMAVQRSVAERW-KQ 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4000 YPRIGLVNAYGPAECSDDVAFFRVDLASTE-STYLPIGSpTDnnrlyllGAGADDAFELVPLGAVGELCVAGTGVGRGYV 4078
Cdd:PRK08751  352 VTGLTLVEAYGLTETSPAACINPLTLKEYNgSIGLPIPS-TD-------ACIKDDAGTVLAIGEIGELCIKGPQVMKGYW 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4079 GDPLRTAQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE-AAVAVQEG 4157
Cdd:PRK08751  424 KRPEETAKVM-------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAVGVPDE 496
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  4158 ANGKyLVGYLVPGETPRSSAdspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK08751  497 KSGE-IVKVVIVKKDPALTA--------------EDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3739-4237 4.49e-17

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 88.70  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3739 WSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHP-------------------- 3798
Cdd:cd05968   92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGkeaaatrlqdaeakalitad 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3799 -TQRLTRIVELSRTLVLVCTQACREQALALFDELGCVDRP---RLLVWDEIQQGEGAEHDPqvySGPQNLAYVIYTSGST 3874
Cdd:cd05968  172 gFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPakgRDLSYDEEKETAGDGAER---TESEDPLMIIYTSGTT 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3875 GLPKGVMVEQAGM-LNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAH-VGEQ 3952
Cdd:cd05968  249 GKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPKADRLWRmVEDH 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3953 GITVLESVPSLIQGMLAE-----ERQALDGLRWMLPTGEAMPPELARqWLKRYPRIG---LVNAYGPAECSDDV---AFF 4021
Cdd:cd05968  329 EITHLGLSPTLIRALKPRgdapvNAHDLSSLRVLGSTGEPWNPEPWN-WLFETVGKGrnpIINYSGGTEISGGIlgnVLI 407
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4022 RVDLASTESTYLPigsptdnnrlyllGAGA---DDAFELVPlGAVGELCVAGTGVG--RGYVGDPLRTAQAFVPHpfgap 4096
Cdd:cd05968  408 KPIKPSSFNGPVP-------------GMKAdvlDESGKPAR-PEVGELVLLAPWPGmtRGFWRDEDRYLETYWSR----- 468
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4097 GERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE-AAVAVQEGANGKYLVGYLV--PGETP 4173
Cdd:cd05968  469 FDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsAAIGVPHPVKGEAIVCFVVlkPGVTP 548
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 4174 rssadspaglmveQGAWFERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQ 4237
Cdd:cd05968  549 -------------TEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK 599
PLN02654 PLN02654
acetate-CoA ligase
1069-1622 4.52e-17

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 88.80  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1069 YAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDIAlvdaEQAAHLAEWGSAP-CE--------PAR-AWLP------- 1131
Cdd:PLN02654   15 FPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIA----SQFYWKQKWEGDEvCSenldvrkgPISiEWFKggktnic 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1132 -ELLERQL-AQSAERVALEWDG------GSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGG 1203
Cdd:PLN02654   91 yNCLDRNVeAGNGDKIAIYWEGnepgfdASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1204 AYVPLDPDYPSERLAYMLADSGVELLLTQA---------HLFERLPGA------EGVT-PICL-----DSLK-------- 1254
Cdd:PLN02654  171 VHSVVFAGFSAESLAQRIVDCKPKVVITCNavkrgpktiNLKDIVDAAldesakNGVSvGICLtyenqLAMKredtkwqe 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1255 ---------LDNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAAlaerlqWMqaTYTLDGDDVLMQKAPVSFDVS 1325
Cdd:PLN02654  251 grdvwwqdvVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGG------YM--VYTATTFKYAFDYKPTDVYWC 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1326 VWECFW----------PLVTGCRLVL--AAPgEHRDPARLVELVRQFGVTTLHFVPPLLQLFI---DEPGVA-ACGSLRR 1389
Cdd:PLN02654  323 TADCGWitghsyvtygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRhSRKSLRV 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1390 LFSGGEAL-PAELRnrvlqrlpavALHNRYGPTETAINVTHWQCRAEDGERSPI-----------GRPLGNVVCRVLDAE 1457
Cdd:PLN02654  402 LGSVGEPInPSAWR----------WFFNVVGDSRCPISDTWWQTETGGFMITPLpgawpqkpgsaTFPFFGVQPVIVDEK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1458 FNLLPAGVAGELCIGGL--GLARGYLGrpalSAERFVADPFSA-AGerLYRTGDRARWNADGVLEYLGRLDQQVKLRGFR 1534
Cdd:PLN02654  472 GKEIEGECSGYLCVKKSwpGAFRTLYG----DHERYETTYFKPfAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHR 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1535 IEPEEIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGP 1613
Cdd:PLN02654  546 IGTAEVESALVSHPQCAEAAVVgIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTR 625

                  ....*....
gi 15597620  1614 SGKLDTRAL 1622
Cdd:PLN02654  626 SGKIMRRIL 634
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
2191-2666 4.87e-17

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 87.74  E-value: 4.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2191 LFAARVAAS-PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2269
Cdd:cd12118    8 SFLERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2270 YPLERLQYMIEDSGVRLLL-SHAALFEALgelpagvarwcleedgpaLDAEDPAPLAALSGPQHQAY-LIYTSGSTGKPK 2347
Cdd:cd12118   88 LDAEEIAFILRHSEAKVLFvDREFEYEDL------------------LAEGDPDFEWIPPADEWDPIaLNYTSGTTGRPK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2348 GVAVSH-GEIAMHCAAVIEcFGMRAEDCELHFYSInFDAASERLL--APLLCGARVVLRaqgQWGAEEICELIRAEGVSI 2424
Cdd:cd12118  150 GVVYHHrGAYLNALANILE-WEMKQHPVYLWTLPM-FHCNGWCFPwtVAAVGGTNVCLR---KVDAKAIYDLIEKHKVTH 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2425 LGFTPSYGSQLAQWLESQGRQLP--VRMcITGGEALTGEHLQRIRQ-AFAPasfFNAYGPTETVVMPLACL-APE----R 2496
Cdd:cd12118  225 FCGAPTVLNMLANAPPSDARPLPhrVHV-MTAGAPPPAAVLAKMEElGFDV---THVYGLTETYGPATVCAwKPEwdelP 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2497 LEEGAAS-----VPIGSVVGARVayiLDADLAL-VPQ-GAT-GELYVGGAGLARGYHERPALSAERFvpdpfaaEGGrLY 2568
Cdd:cd12118  301 TEERARLkarqgVRYVGLEEVDV---LDPETMKpVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAF-------RGG-WF 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2569 RTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVASavaeqdEDAQA 2647
Cdd:cd12118  370 HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEKWGEVPCAFVEL------KEGAK 443
                        490
                 ....*....|....*....
gi 15597620 2648 ALREALKTHLKQQLPDYMV 2666
Cdd:cd12118  444 VTEEEIIAFCREHLAGFMV 462
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2822-3019 5.39e-17

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 86.93  E-value: 5.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2822 IDLGLLRKSLQRLVEQHDALRLAFRQVDGE----WLAQHRPLREqelLWHVPVQSFDECAELFAKAQRSLDLEQGPLLRA 2897
Cdd:cd19538   36 LDVQALQQALYDVVERHESLRTVFPEEDGVpyqlILEEDEATPK---LEIKEVDEEELESEINEAVRYPFDLSEEPPFRA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2898 VLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSES-----LREEL 2972
Cdd:cd19538  113 TLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLPVQYADYALWQQELLGDESdpdslIARQL 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15597620 2973 GWWQARLGGQP--VEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQA 3019
Cdd:cd19538  193 AYWKKQLAGLPdeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
160-452 6.36e-17

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 87.66  E-value: 6.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  160 DEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEV----LIRRGFGIGADDVIVSWLPLYHDM-------------- 221
Cdd:cd05927  107 PPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAgvfkILEILNKINPTDVYISYLPLAHIFervvealflyhgak 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  222 -----GLIGGL------LQP-IFSGVPCVLMspryflerpvRWLEAIsqYGGTVSGGP------DFAYRLCSERVAESAL 283
Cdd:cd05927  187 igfysGDIRLLlddikaLKPtVFPGVPRVLN----------RIYDKI--FNKVQAKGPlkrklfNFALNYKLAELRSGVV 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  284 QRL------------DLSGWRVAF--SGSEPIRQDSLERFAEKFaasrfdASSFFACYGLAEATlfvtggqrgqGIPALA 349
Cdd:cd05927  255 RASpfwdklvfnkikQALGGNVRLmlTGSAPLSPEVLEFLRVAL------GCPVLEGYGQTECT----------AGATLT 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  350 VDGEalarnriaegegSVLMCCGRSQPEHAVLIVDAASGE--VLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVErDGr 427
Cdd:cd05927  319 LPGD------------TSVGHVGGPLPCAEVKLVDVPEMNydAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDE-DG- 384
                        330       340
                 ....*....|....*....|....*.
gi 15597620  428 tWLRTGDLG-FLRDGELFVTGRLKDM 452
Cdd:cd05927  385 -WLHTGDIGeWLPNGTLKIIDRKKNI 409
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
2203-2689 6.67e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 87.90  E-value: 6.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2203 PALTFAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIED 2281
Cdd:PRK05677   41 PAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFND 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2282 SGVRLLL---SHAALFEALgeLP-AGVARWCLEEDG----------------------PALDAEDPAPL-AALS------ 2328
Cdd:PRK05677  121 SGAKALVclaNMAHLAEKV--LPkTGVKHVIVTEVAdmlpplkrllinavvkhvkkmvPAYHLPQAVKFnDALAkgagqp 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2329 ------GPQHQAYLIYTSGSTGKPKGVAVSHGEIAmhcAAVIECFGMRA----EDCEL--------HFYSINFDAaserl 2390
Cdd:PRK05677  199 vteanpQADDVAVLQYTGGTTGVAKGAMLTHRNLV---ANMLQCRALMGsnlnEGCEIliaplplyHIYAFTFHC----- 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2391 LAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILG----FTPSYGSQLAQWLESQGrqlpVRMCITGGEALTGEHLQRI 2466
Cdd:PRK05677  271 MAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGlntlFVALCNNEAFRKLDFSA----LKLTLSGGMALQLATAERW 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2467 RQAFAPAsFFNAYGPTETvvMPLACLAP-ERLEEGAASVPIGSVVgarvAYILDADLALVPQGATGELYVGGAGLARGYH 2545
Cdd:PRK05677  347 KEVTGCA-ICEGYGMTET--SPVVSVNPsQAIQVGTIGIPVPSTL----CKVIDDDGNELPLGEVGELCVKGPQVMKGYW 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2546 ERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVRE-ALVLALDS 2624
Cdd:PRK05677  420 QRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGVPDE 492
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  2625 PSGKQLAGYVASAVAEqdedaqAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK05677  493 KSGEAIKVFVVVKPGE------TLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
3863-4227 7.12e-17

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 85.15  E-value: 7.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3863 NLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAApLFGARVAIVPNAVahDP 3942
Cdd:cd17633    1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKF--NP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3943 QGLLAHVGEQGITVLESVPSLIQGMLAEERQALDgLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDDVAFFR 4022
Cdd:cd17633   78 KSWIRKINQYNATVIYLVPTMLQALARTLEPESK-IKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4023 VDLASTEStylpIGSPTDNNRLYLLGAGAddafelvplGAVGELCVAGTGVGRGYVgdplrTAQAFVPHPFgapgerlYR 4102
Cdd:cd17633  157 QESRPPNS----VGRPFPNVEIEIRNADG---------GEIGKIFVKSEMVFSGYV-----RGGFSNPDGW-------MS 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4103 TGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETprssADSPAg 4182
Cdd:cd17633  212 VGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK----LTYKQ- 286
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 15597620 4183 lmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDR 4227
Cdd:cd17633  287 -----------LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3722-4225 8.96e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 87.14  E-value: 8.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3722 QVAAH----PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGH 3797
Cdd:PRK07786   22 QLARHalmqPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3798 PTQRLTRIVELSRTLVLVCTQACREQALALFDE---------LGCVDRPRLLVWDEIQQGEGAEHDPqVYSGPQNLAYVI 3868
Cdd:PRK07786  102 TPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIvpllstvvvAGGSSDDSVLGYEDLLAEAGPAHAP-VDIPNDSPALIM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3869 YTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDI----SVWQFLaapLFGARVAIVPNAvAHDPQG 3944
Cdd:PRK07786  181 YTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIagigSMLPGL---LLGAPTVIYPLG-AFDPGQ 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3945 LLAHVGEQGITVLESVPSLIQGMLAEERQ-----ALDGLRWmlptGEA-MPPELARQWLKRYPRIGLVNAYGPAECSDDV 4018
Cdd:PRK07786  257 LLDVLEAEKVTGIFLVPAQWQAVCAEQQArprdlALRVLSW----GAApASDTLLRQMAATFPEAQILAAFGQTEMSPVT 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4019 AFFRVD--LASTESTYLPIgsPTDNNRLyllgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgAP 4096
Cdd:PRK07786  333 CMLLGEdaIRKLGSVGKVI--PTVAARV------VDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4097 GerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQegANGKYlvgylvpGETPRSS 4176
Cdd:PRK07786  399 G--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGR--ADEKW-------GEVPVAV 467
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597620  4177 A---DSPAGLMVEQGAWFerikqqLRADLPDYMVPLHWLVLDRMPLNANGKL 4225
Cdd:PRK07786  468 AavrNDDAALTLEDLAEF------LTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK07638 PRK07638
acyl-CoA synthetase; Validated
19-560 1.00e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 86.76  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    19 AVQEPERLALRFLAEddgegvVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
Cdd:PRK07638   11 ASLQPNKIAIKENDR------VLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDI-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    99 sarRHHQERLLSIIADAEPRLVLTTADLREPLlqmnaqlSAANAPQLLcVDQLDPAVAEAWDE--PQVRPEHIAF-LQYT 175
Cdd:PRK07638   83 ---KWKQDELKERLAISNADMIVTERYKLNDL-------PDEEGRVIE-IDEWKRMIEKYLPTyaPIENVQNAPFyMGFT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   176 SGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLmspRYFLerPVRWLEA 255
Cdd:PRK07638  152 SGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLM---RKFI--PNQVLDK 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   256 ISQ------YggTVSGGPDFAYRLcsERVAESALqrldlsgwRVAFSGSEpirqdsLERFAEKFAASRFDASSFFACYGL 329
Cdd:PRK07638  227 LETenisvmY--TVPTMLESLYKE--NRVIENKM--------KIISSGAK------WEAEAKEKIKNIFPYAKLYEFYGA 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   330 AEATlFVTggqrgqgipalavdgeALARNRIAEGEGSVlmccGRsqPEHAVLI-VDAASGEVLGDDNVGEIWAAGPSIAH 408
Cdd:PRK07638  289 SELS-FVT----------------ALVDEESERRPNSV----GR--PFHNVQVrICNEAGEEVQKGEIGTVYVKSPQFFM 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   409 GYwrnpEASAKAFVERDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIERtVESEVPSARKGRVAAFAVT 487
Cdd:PRK07638  346 GY----IIGGVLARELNADGWMTVRDVGYEdEEGFIYIVGREKNMILFGGINIFPEEIES-VLHEHPAVDEIVVIGVPDS 420
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   488 VDGEEGIGIaaeigrgVQKSVPAQELIDSIRQAVAeAYQeAPKVVALLNpgALPKTSSGKLQRSACRLRLEDG 560
Cdd:PRK07638  421 YWGEKPVAI-------IKGSATKQQLKSFCLQRLS-SFK-IPKEWHFVD--EIPYTNSGKIARMEAKSWIENQ 482
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
2186-2644 1.58e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 86.62  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2186 DTLHGLFAARvaASPQAPALTFAGQTLSYAELDARSNRLARVLRS-HGVGPEVRVGLALERSLEMVVGLLAILKAGGAYV 2264
Cdd:PRK13388    3 DTIAQLLRDR--AGDDTIAVRYGDRTWTWREVLAEAAARAAALIAlADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2265 PLDPEYPLERLQYMIEDSGVRLLLS---HAALFEALgELPaGVARwcLEEDGPAL-----DAEDPAPLAALsGPQHQAYL 2336
Cdd:PRK13388   81 GLNTTRRGAALAADIRRADCQLLVTdaeHRPLLDGL-DLP-GVRV--LDVDTPAYaelvaAAGALTPHREV-DAMDPFML 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2337 IYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED---CELHFYSINFDAAserLLAPLLC-GARVVLRAqgQWGAEE 2412
Cdd:PRK13388  156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDvcyVSMPLFHSNAVMA---GWAPAVAsGAAVALPA--KFSASG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2413 ICELIRAEGVSILGFTpsyGSQLAQWLESQGR----QLPVRMCItGGEAlTGEHLQRIRQAFApASFFNAYGPTETVVM- 2487
Cdd:PRK13388  231 FLDDVRRYGATYFNYV---GKPLAYILATPERpddaDNPLRVAF-GNEA-SPRDIAEFSRRFG-CQVEDGYGSSEGAVIv 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2488 ------PLACLApeRLEEGAASVPIGSVVGARVAyILDADLALV-PQGATGELY-VGGAGLARGYHERPALSAERFvpdp 2559
Cdd:PRK13388  305 vrepgtPPGSIG--RGAPGVAIYNPETLTECAVA-RFDAHGALLnADEAIGELVnTAGAGFFEGYYNNPEATAERM---- 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2560 faaEGGRlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQlagyVASAV 2638
Cdd:PRK13388  378 ---RHGM-YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVpDERVGDQ----VMAAL 449

                  ....*.
gi 15597620  2639 AEQDED 2644
Cdd:PRK13388  450 VLRDGA 455
PRK07529 PRK07529
AMP-binding domain protein; Validated
2163-2662 1.62e-16

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 86.93  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2163 PLFAAEERKQLLLAGTAGEAGLQDTLHGLFAARVAASPQAPALTF--------AGQTLSYAELDARSNRLARVLRSHGVG 2234
Cdd:PRK07529    2 PAFATLADIEAIEAVPLAARDLPASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2235 PEVRVGLALERSLEMVVGLLAILKAGGAyVPLDPEYPLERLQYMIEDSGVRLLLSHAALF---------EALGELPA--- 2302
Cdd:PRK07529   82 PGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLGPFPgtdiwqkvaEVLAALPElrt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2303 -----------GVARWCLEEDGPALDAEDPAPLAALS-------------GPQHQAYLIYTSGSTGKPKGVAVSHG-EIA 2357
Cdd:PRK07529  161 vvevdlarylpGPKRLAVPLIRRKAHARILDFDAELArqpgdrlfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGnEVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2358 MHCAAViECFGMRAED---CELHFYSINfdAASERLLAPLLCGARVVLRA-QGQWGAE---EICELIRAEGVSILGFTPS 2430
Cdd:PRK07529  241 NAWLGA-LLLGLGPGDtvfCGLPLFHVN--ALLVTGLAPLARGAHVVLATpQGYRGPGviaNFWKIVERYRINFLSGVPT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2431 YGSQLAqwlesqgrQLPV--------RMCITGGEALTGEHLQRIRQAFApASFFNAYGPTETvvmplACLAPERLEEGaa 2502
Cdd:PRK07529  318 VYAALL--------QVPVdghdisslRYALCGAAPLPVEVFRRFEAATG-VRIVEGYGLTEA-----TCVSSVNPPDG-- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2503 SVPIGSvVGARVAY------ILDADLALV---PQGATGELYVGGAGLARGYherpaLSAERfvpDPFAAEGGRLYRTGDL 2573
Cdd:PRK07529  382 ERRIGS-VGLRLPYqrvrvvILDDAGRYLrdcAVDEVGVLCIAGPNVFSGY-----LEAAH---NKGLWLEDGWLNTGDL 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2574 VRLCDNGQVEYVGRidhqVK---IR-GFRIELGEIEARLLEHPQVreALVLALDSPSGKqlAGYVASAVAEQDEDAQAAL 2649
Cdd:PRK07529  453 GRIDADGYFWLTGR----AKdliIRgGHNIDPAAIEEALLRHPAV--ALAAAVGRPDAH--AGELPVAYVQLKPGASATE 524
                         570
                  ....*....|...
gi 15597620  2650 REaLKTHLKQQLP 2662
Cdd:PRK07529  525 AE-LLAFARDHIA 536
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
2187-2625 1.63e-16

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 86.27  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2187 TLHGLFAARVAASPQAPALTF---AG--QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGG 2261
Cdd:PRK08008    8 HLRQMWDDLADVYGHKTALIFessGGvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2262 AYVPLDPEYPLERLQYMIEDSGVRLLLSHAA---LFEALGELPAG------VARWCLEEDGPALD-----AEDPAPL--- 2324
Cdd:PRK08008   88 IMVPINARLLREESAWILQNSQASLLVTSAQfypMYRQIQQEDATplrhicLTRVALPADDGVSSftqlkAQQPATLcya 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2325 AALSgPQHQAYLIYTSGSTGKPKGVAVSHGEI-------AMHCAaviecfgMRAEDCELHF---YSINFDAASerLLAPL 2394
Cdd:PRK08008  168 PPLS-TDDTAEILFTSGTTSRPKGVVITHYNLrfagyysAWQCA-------LRDDDVYLTVmpaFHIDCQCTA--AMAAF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2395 LCGARVVL----RAQGQWGaeEICELiRA---EGVSILGFTpsygsQLAQWLESQGRQLPVR-----MCITGGEALTGEh 2462
Cdd:PRK08008  238 SAGATFVLlekySARAFWG--QVCKY-RAtitECIPMMIRT-----LMVQPPSANDRQHCLRevmfyLNLSDQEKDAFE- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2463 lQRIRqafapASFFNAYGPTETVVmplaCLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGG-AG-- 2539
Cdd:PRK08008  309 -ERFG-----VRLLTSYGMTETIV----GIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGkt 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2540 LARGYHERPALSAERFVPDpfaaegGRLYrTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALV 2619
Cdd:PRK08008  379 IFKEYYLDPKATAKVLEAD------GWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451

                  ....*.
gi 15597620  2620 LALDSP 2625
Cdd:PRK08008  452 VGIKDS 457
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
3860-4143 1.76e-16

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 86.41  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3860 GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIaqtasQSF--DISVWQFLAAPLFgARVAIVPNA 3937
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVM-----MSFlpPFHAYGFNSCTLF-PLLSGVPVV 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3938 VAHDP---QGLLAHVGEQGITVLESVP---SLIQGMLAEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGP 4011
Cdd:PRK06334  255 FAYNPlypKKIVEMIDEAKVTFLGSTPvffDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGT 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4012 AECSDDVAFFRVDLASTESTylpIGSPTDNNRLYLLgagADDAFELVPLGAVGELCVAGTGVGRGYVG-DPlrtAQAFVP 4090
Cdd:PRK06334  335 TECSPVITINTVNSPKHESC---VGMPIRGMDVLIV---SEETKVPVSSGETGLVLTRGTSLFSGYLGeDF---GQGFVE 405
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  4091 hpfgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHE 4143
Cdd:PRK06334  406 ----LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3252-3677 1.84e-16

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 85.38  E-value: 1.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3252 PLTPMQEgLLLHTLLEPGTgiYYMQDRY-RIDSPLDPERFAAAWQAVVARHEALRASFVWNAGETMlQVIHKP--GRTRI 3328
Cdd:cd19534    3 PLTPIQR-WFFEQNLAGRH--HFNQSVLlRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQ-QRIRGDveELFRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3329 EFLDWSELPEDghEERLQALhkREREAGFDLLEQPPFHLRLIRLGEARYWFMMSNHHILIDA--WcRgLLMNDFFEIYSA 3406
Cdd:cd19534   79 EVVDLSSLAQA--AAIEALA--AEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsW-R-ILLEDLEAAYEQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3407 LGESRPANLPTPPRYRDYIAWLQRQ----DLEQSRRWWSESLRGFERPtlVPSDRPFLREHAGEsggmivgdRYTRLDAA 3482
Cdd:cd19534  153 ALAGEPIPLPSKTSFQTWAELLAEYaqspALLEELAYWRELPAADYWG--LPKDPEQTYGDART--------VSFTLDEE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3483 DGARL-RELAQRYQLTVNTFAQAAWALTLRRFSGERDVLfgVTVA--GRPVGMPEMQ--RTVGLFINSIPLRVQMPAAG- 3556
Cdd:cd19534  223 ETEALlQEANAAYRTEINDLLLAALALAFQDWTGRAPPA--IFLEghGREEIDPGLDlsRTVGWFTSMYPVVLDLEASEd 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3557 ---QRCTVREWLNRLFERNLE---LReheHLPLVAIQESSELPKGQPLFDSLFVFE----NAPVEVSVLDRAQSlNASSD 3626
Cdd:cd19534  301 lgdTLKRVKEQLRRIPNKGIGygiLR---YLTPEGTKRLAFHPQPEISFNYLGQFDqgerDDALFVSAVGGGGS-DIGPD 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597620 3627 SGRTHTnFPLTVVCYpGDDLGLHLSYDQRYFEAPTVERLLGEFKRLLLALA 3677
Cdd:cd19534  377 TPRFAL-LDINAVVE-GGQLVITVSYSRNMYHEETIQQLADSYKEALEALI 425
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3737-4205 1.94e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 85.59  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRivelsrtlvlvC 3816
Cdd:cd05910    1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQ-----------C 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3817 TQacreqalalfdelgcvdrprllvwdeiqqgegaEHDPQVYSG-PQNL--AYVIYTSGSTGLPKGVmVEQAGMLNNQLs 3893
Cdd:cd05910   70 LQ---------------------------------EAEPDAFIGiPKADepAAILFTSGSTGTPKGV-VYRHGTFAAQI- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3894 kvpyleldenDVIAQT---ASQSFDISVwqFLAAPLFGARV---AIVPnAVAH------DPQGLLAHVGEQGITVLESVP 3961
Cdd:cd05910  115 ----------DALRQLygiRPGEVDLAT--FPLFALFGPALgltSVIP-DMDPtrparaDPQKLVGAIRQYGVSIVFGSP 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3962 SLIQGML---AEERQALDGLRWMLPTGEAMPPELARQwLKRY--PRIGLVNAYGPAECSDdVAFFRVDLASTESTYLP-- 4034
Cdd:cd05910  182 ALLERVArycAQHGITLPSLRRVLSAGAPVPIALAAR-LRKMlsDEAEILTPYGATEALP-VSSIGSRELLATTTAATsg 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4035 -----IGSPTDNNRLYLLGAGA------DDAFELvPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHpfgaPGER-LYR 4102
Cdd:cd05910  260 gagtcVGRPIPGVRVRIIEIDDepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDD----NSEGfWHR 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4103 TGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAvavqegangkyLVGYLVPGET-------PRS 4175
Cdd:cd05910  335 MGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA-----------LVGVGKPGCQlpvlcvePLP 403
                        490       500       510
                 ....*....|....*....|....*....|
gi 15597620 4176 SADSPAGlmveqgawfeRIKQQLRADLPDY 4205
Cdd:cd05910  404 GTITPRA----------RLEQELRALAKDY 423
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
2174-2634 2.12e-16

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 86.04  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2174 LLAGTAGEAGLQdtlhglFAARVAASPQAPALTFA--GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVV 2251
Cdd:cd17642   11 LEDGTAGEQLHK------AMKRYASVPGTIAFTDAhtGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2252 GLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALgelpAGVAR--------------------WCLEE 2311
Cdd:cd17642   85 PVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKV----LNVQKklkiiktiiildskedykgyQCLYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2312 -----DGPALDAEDPAPLAALSGPQhQAYLIYTSGSTGKPKGVAVSHGEIAM---HCAAVIECFGMRAEDCELHFYSINF 2383
Cdd:cd17642  161 fitqnLPPGFNEYDFKPPSFDRDEQ-VALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPFHH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2384 DAASERLLAPLLCGARVVLRAQgqWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCI-TGGEALTGEH 2462
Cdd:cd17642  240 GFGMFTTLGYLICGFRVVLMYK--FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIaSGGAPLSKEV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2463 LQRIRQAFAPASFFNAYGPTETVVMPLacLAPERLEEGAASvpiGSVVGARVAYILDADLA-LVPQGATGELYVGGAGLA 2541
Cdd:cd17642  318 GEAVAKRFKLPGIRQGYGLTETTSAIL--ITPEGDDKPGAV---GKVVPFFYAKVVDLDTGkTLGPNERGELCVKGPMIM 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2542 RGYHERPALSAERFVPDpfaaegGRLyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLA 2621
Cdd:cd17642  393 KGYVNNPEATKALIDKD------GWL-HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
                        490
                 ....*....|...
gi 15597620 2622 LDSPSGKQLAGYV 2634
Cdd:cd17642  466 IPDEDAGELPAAV 478
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
13-552 2.32e-16

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 85.30  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   13 QALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHAQLGDR--AVLLFPSgPDYVAAFFGCLYAGVI 90
Cdd:cd17645    2 QLFEEQVERTPDHVAVVD------RGQSLTYKQLNEKANQLARHLRGKGVKPDDqvGIMLDKS-LDMIAAILGVLKAGGA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   91 AVPA---YPPEsarrhhqeRLLSIIADAEPRLVLTtadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPE 167
Cdd:cd17645   75 YVPIdpdYPGE--------RIAYMLADSSAKILLT------------------------------------------NPD 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  168 HIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDmGLIGGLLQPIFSG--VPCVLMSPRYF 245
Cdd:cd17645  105 DLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFD-ASAWEIFPHLTAGaaLHVVPSERRLD 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  246 LERPVRWLEaisQYGGTVSGGPdfayrlcsERVAESALQrLDLSGWRVAFSGSepirqDSLERFAEKfaasrfdASSFFA 325
Cdd:cd17645  184 LDALNDYFN---QEGITISFLP--------TGAAEQFMQ-LDNQSLRVLLTGG-----DKLKKIERK-------GYKLVN 239
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  326 CYGLAEATLFVTGGQRGQGIPALAVdGEALARNRI-AEGEGSVLmccgrsQPEHAvlivdaasgevlgddnVGEIWAAGP 404
Cdd:cd17645  240 NYGPTENTVVATSFEIDKPYANIPI-GKPIDNTRVyILDEALQL------QPIGV----------------AGELCIAGE 296
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  405 SIAHGYWRNPEASAKAFV---ERDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIertvESEVPSARKGR 480
Cdd:cd17645  297 GLARGYLNRPELTAEKFIvhpFVPGERMYRTGDLAkFLPDGNIEFLGRLDQQVKIRGYRIEPGEI----EPFLMNHPLIE 372
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  481 VAAFAVTVDGEEGIGIAAEIgrGVQKSVPAQELIDSIRQAVAEAYqeAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd17645  373 LAAVLAKEDADGRKYLVAYV--TAPEEIPHEELREWLKNDLPDYM--IPTYFVHLK--ALPLTANGKVDRKA 438
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
6-440 2.51e-16

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 86.09  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     6 ELPTTLVQALRRRAVQEPERLalrFLAE--DDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFpSGPDYVAAF-- 81
Cdd:PRK08180   36 DYPRRLTDRLVHWAQEAPDRV---FLAErgADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMIL-SGNSIEHALla 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    82 FGCLYAGVIAVPAYPPESAR-------RHHQERL----------------LSIIADAEPRLVLTTADLREPLLQMNAQLS 138
Cdd:PRK08180  112 LAAMYAGVPYAPVSPAYSLVsqdfgklRHVLELLtpglvfaddgaafaraLAAVVPADVEVVAVRGAVPGRAATPFAALL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   139 AANAPqllcvdqldPAVAEAWDepQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADD--VIVSWLP 216
Cdd:PRK08180  192 ATPPT---------AAVDAAHA--AVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLP 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   217 LYH------DMGLI---GGLL-----QPIFSGVPCVL-----MSPRYFLERPVRWlEAISQYggtvsggpdfayrlcSER 277
Cdd:PRK08180  261 WNHtfggnhNLGIVlynGGTLyiddgKPTPGGFDETLrnlreISPTVYFNVPKGW-EMLVPA---------------LER 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   278 ---VAESALQRLDLsgwrVAFSG---SEPIRqDSLERFAEkfaASRFDASSFFACYGLAE---ATLFVTGGQRGQGipal 348
Cdd:PRK08180  325 daaLRRRFFSRLKL----LFYAGaalSQDVW-DRLDRVAE---ATCGERIRMMTGLGMTEtapSATFTTGPLSRAG---- 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   349 avdgealarnriaegegsvlmCCGRSQPEHAVLIVDAasgevlgDDNVgEIWAAGPSIAHGYWRNPEASAKAFVErDGrt 428
Cdd:PRK08180  393 ---------------------NIGLPAPGCEVKLVPV-------GGKL-EVRVKGPNVTPGYWRAPELTAEAFDE-EG-- 440
                         490
                  ....*....|..
gi 15597620   429 WLRTGDLGFLRD 440
Cdd:PRK08180  441 YYRSGDAVRFVD 452
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
3843-4230 3.04e-16

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 85.59  E-value: 3.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3843 DEIQQGEGAEHDPqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLE--LDENDVIAQTASQSFDISVWQ 3920
Cdd:PRK05677  189 DALAKGAGQPVTE-ANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsnLNEGCEILIAPLPLYHIYAFT 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3921 F--LAAPLFGARVAIVPNAvaHDPQGLLAHVGEQGITVLESVPSLIQGML-AEERQALD--GLRWMLPTGEAMPPELARQ 3995
Cdd:PRK05677  268 FhcMAMMLIGNHNILISNP--RDLPAMVKELGKWKFSGFVGLNTLFVALCnNEAFRKLDfsALKLTLSGGMALQLATAER 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3996 WlKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPtdnnrlylLGAGADDAFELVPLGAVGELCVAGTGVGR 4075
Cdd:PRK05677  346 W-KEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPST--------LCKVIDDDGNELPLGEVGELCVKGPQVMK 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4076 GYVGDPLRTAQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE-AAVAV 4154
Cdd:PRK05677  417 GYWQRPEATDEIL-------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGV 489
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  4155 QEGANGKYLVGYLV--PGETPRSsadspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK05677  490 PDEKSGEAIKVFVVvkPGETLTK----------------EQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
174-546 6.15e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 82.35  E-value: 6.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  174 YTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdmglIGgllqpifsgvpcVLMspryflerpvrWL 253
Cdd:cd17636    7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFH----IG------------TLM-----------FT 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  254 EAISQYGGTVSggpdFAYRLCSERVAEsALQRLDLSGwrvAFsgsepIRQDSLERFAEKFAASRFDASSFFACYGLAEAT 333
Cdd:cd17636   60 LATFHAGGTNV----FVRRVDAEEVLE-LIEAERCTH---AF-----LLPPTIDQIVELNADGLYDLSSLRSSPAAPEWN 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  334 LFVT---------GGQRGQ----GIPALA-VDGEALARNriaegegsvlmccGRSQPEHAVLIVDAASGEVlGDDNVGEI 399
Cdd:cd17636  127 DMATvdtspwgrkPGGYGQtevmGLATFAaLGGGAIGGA-------------GRPSPLVQVRILDEDGREV-PDGEVGEI 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  400 WAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGfLR--DGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----- 472
Cdd:cd17636  193 VARGPTVMAGYWNRPEVNARRT--RGG--WHHTNDLG-RRepDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHpavad 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  473 -----VPSARKGR-VAAFAVTVDGEegigiaaeigrgvqkSVPAQELIDSIRQAVAeAYQEaPKVVALLNpgALPKTSSG 546
Cdd:cd17636  268 aavigVPDPRWAQsVKAIVVLKPGA---------------SVTEAELIEHCRARIA-SYKK-PKSVEFAD--ALPRTAGG 328
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2798-3218 8.72e-16

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 83.46  E-value: 8.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2798 WFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFrQVDGEWLAQHRPlreQELLWHVPVQSFDEC- 2876
Cdd:cd20483   12 WFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAY-FEGDDFGEQQVL---DDPSFHLIVIDLSEAa 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2877 ---AELFAKAQRS----LDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPA-LPAK 2948
Cdd:cd20483   88 dpeAALDQLVRNLrrqeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLAtVPPP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2949 TSAFRDWAGRLQAYAGSESLREELGWWQARLGGQPVEWP------CDRPQGDNREALaeSVSLRLDP---QRTRQLLQQA 3019
Cdd:cd20483  168 PVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDASKllpfakAERPPVKDYERS--TVEATLDKellARMKRICAQH 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3020 ---PAAYrtqvndlLLTALARVLCRWSGQPSTLVQL----EGHGrealfddiDLTRSVGWFTSAYPLRLT--PAQSPGES 3090
Cdd:cd20483  246 avtPFMF-------LLAAFRAFLYRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCRmdCDMSFDDL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3091 IKAIKEQ-LRAVPHKGLGYGVLryLADPAVRQAMAALPTAPITFNYL--GQFDQ-SFADALFQPLDQptgpihdEQAPLP 3166
Cdd:cd20483  311 LESTKTTcLEAYEHSAVPFDYI--VDALDVPRSTSHFPIGQIAVNYQvhGKFPEyDTGDFKFTDYDH-------YDIPTA 381
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597620 3167 NELSVDGQVYG-GELVLRWTYSRERYDARTVNELAQAYlaelQALIEHCLEDG 3218
Cdd:cd20483  382 CDIALEAEEDPdGGLDLRLEFSTTLYDSADMERFLDNF----VTFLTSVIRDH 430
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2338-2686 8.93e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 82.33  E-value: 8.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2338 YTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED---CELHFYSINFDAASerLLAPLLCGARVVLRAQGqWGAEEIC 2414
Cdd:cd05917    9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlcIPVPLFHCFGSVLG--VLACLTHGATMVFPSPS-FDPLAVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2415 ELIRAEGVSILGFTPS-YGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVMPLACLA 2493
Cdd:cd05917   86 EAIEKEKCTALHGVPTmFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQTRT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2494 PERLEEGAASVpiGSVVGARVAYILDADLALVPQ-GATGELYVGGAGLARGYHERPALSAErfvpdpfAAEGGRLYRTGD 2572
Cdd:cd05917  166 DDSIEKRVNTV--GRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAE-------AIDGDGWLHTGD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2573 LVRLCDNGQVEYVGRIDHQVkIRGFR-IELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasavaeQDEDAQAALR 2650
Cdd:cd05917  237 LAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVpDERYGEEVCAWI------RLKEGAELTE 309
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 15597620 2651 EALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDR 2686
Cdd:cd05917  310 EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
64-527 9.37e-16

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 83.67  E-value: 9.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP---PESARR--HHQERLLSIIA--DAEPRLVLTTADlrEPLLQMNAQ 136
Cdd:cd05932   31 GSKIALISKNCAEWFITDLAIWMAGHISVPLYPtlnPDTIRYvlEHSESKALFVGklDDWKAMAPGVPE--GLISISLPP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  137 LSAANapqllCVDQLDPAVAEA---WDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLV-ANEVLIRRgFGIGADDVIV 212
Cdd:cd05932  109 PSAAN-----CQYQWDDLIAQHpplEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAwAAQAGIEH-IGTEENDRML 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  213 SWLPLYH-------DMG-LIGGLL----QPIFSGVPCVLMS-PRYFLERPVRWleAISQYGGTVSGGPDFAYRLCSERVA 279
Cdd:cd05932  183 SYLPLAHvtervfvEGGsLYGGVLvafaESLDTFVEDVQRArPTLFFSVPRLW--TKFQQGVQDKIPQQKLNLLLKIPVV 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  280 ESALQR-----LDLSGWRVAFSGSEPIRQDSLERFaekfaasRFDASSFFACYGLAEATLFVTGGQRGqgipalavdgea 354
Cdd:cd05932  261 NSLVKRkvlkgLGLDQCRLAGCGSAPVPPALLEWY-------RSLGLNILEAYGMTENFAYSHLNYPG------------ 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  355 laRNRIaegeGSVlmccGRSQPEHAVLIvdaasgevlGDDnvGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGD 434
Cdd:cd05932  322 --RDKI----GTV----GNAGPGVEVRI---------SED--GEILVRSPALMMGYYKDPEATAEAFTA-DG--FLRTGD 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  435 LGFL-RDGELFVTGRLKDML-IVRGHNLYPQDIERTVesevpsARKGRVAAFAVTvdgeeGIGIAAEIGRGVQKSVPAQE 512
Cdd:cd05932  378 KGELdADGNLTITGRVKDIFkTSKGKYVAPAPIENKL------AEHDRVEMVCVI-----GSGLPAPLALVVLSEEARLR 446
                        490
                 ....*....|....*
gi 15597620  513 LIDSIRQAVAEAYQE 527
Cdd:cd05932  447 ADAFARAELEASLRA 461
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3709-4233 1.04e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 83.94  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3709 YPLEQG----YVRlfeAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSF 3784
Cdd:PRK06178   28 YPHGERplteYLR---AWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGIL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3785 KAGAGYLPLDPghptqrLTRIVELSRTL------VLVC--------TQACREQAL------ALFDEL---------GCVD 3835
Cdd:PRK06178  105 KLGAVHVPVSP------LFREHELSYELndagaeVLLAldqlapvvEQVRAETSLrhvivtSLADVLpaeptlplpDSLR 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3836 RPRLLVWDEI-----QQGEGAEhDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPY-LELDENDVIAQT 3909
Cdd:PRK06178  179 APRLAAAGAIdllpaLRACTAP-VPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVaVVGGEDSVFLSF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3910 ASQsFDISVWQF-LAAPLF-GARVAIVPNavaHDPQGLLAHVGEQGITVLE-SVPSLIQGMLAEERQALDgLRWMLPTGE 3986
Cdd:PRK06178  258 LPE-FWIAGENFgLLFPLFsGATLVLLAR---WDAVAFMAAVERYRVTRTVmLVDNAVELMDHPRFAEYD-LSSLRQVRV 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3987 A-----MPPELARQWLKRYPRIGLVNAYGPAE---CSDDVAFFRVDLASTESTYLPIGSPTdnnrlyllgAGAD------ 4052
Cdd:PRK06178  333 VsfvkkLNPDYRQRWRALTGSVLAEAAWGMTEthtCDTFTAGFQDDDFDLLSQPVFVGLPV---------PGTEfkicdf 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4053 DAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapgERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRI 4132
Cdd:PRK06178  404 ETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR--------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSV 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4133 ELGEIEARLHERADVREAAVAVQEGAN-GKYLVGYLVpgetPRSSAD-SPAGLMveqgAWferikqqLRADLPDYMVPlH 4210
Cdd:PRK06178  476 FPSEVEALLGQHPAVLGSAVVGRPDPDkGQVPVAFVQ----LKPGADlTAAALQ----AW-------CRENMAVYKVP-E 539
                         570       580
                  ....*....|....*....|...
gi 15597620  4211 WLVLDRMPLNANGKLDRKALPAL 4233
Cdd:PRK06178  540 IRIVDALPMTATGKVRKQDLQAL 562
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
1156-1556 1.08e-15

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 83.67  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH 1234
Cdd:cd05928   44 FRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1235 LferLPGAEGVTPICLD-SLKL-------DNWPS------QAPGLHL---HGDNLAYVIY-TSGSTGQPKGVGNTHAALA 1296
Cdd:cd05928  124 L---APEVDSVASECPSlKTKLlvseksrDGWLNfkellnEASTEHHcveTGSQEPMAIYfTSGTTGSPKMAEHSHSSLG 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1297 ERLQwMQATYTLDgddvlMQKAPVSFDVS--------VWECFWPLVTG-CRLVLAAPgeHRDPARLVELVRQFGVTTLHF 1367
Cdd:cd05928  201 LGLK-VNGRYWLD-----LTASDIMWNTSdtgwiksaWSSLFEPWIQGaCVFVHHLP--RFDPLVILKTLSSYPITTFCG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1368 VPPLLQLFIDEPGVA-ACGSLRRLFSGGEALPAELRNRvLQRLPAVALHNRYGPTETA-INVTHWQCRAEDGErspIGRP 1445
Cdd:cd05928  273 APTVYRMLVQQDLSSyKFPSLQHCVTGGEPLNPEVLEK-WKAQTGLDIYEGYGQTETGlICANFKGMKIKPGS---MGKA 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1446 LGNVVCRVLDAEFNLLPAGVAGELCI-----GGLGLARGYLGRPALSAERFVADpfsaagerLYRTGDRARWNADGVLEY 1520
Cdd:cd05928  349 SPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMDEDGYFWF 420
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15597620 1521 LGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:cd05928  421 MGRADDVINSSGYRIGPFEVESALIEHPAVVESAVV 456
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
2196-2661 1.19e-15

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 83.84  E-value: 1.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2196 VAASPQAPALTFAG------QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAG-------GA 2262
Cdd:TIGR02188   67 LEARPDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGaihsvvfGG 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2263 YVPldpeyplERLQYMIEDSGVRLLLS-------------HAALFEALGELP-------------AGVARWC-------- 2308
Cdd:TIGR02188  147 FSA-------EALADRINDAGAKLVITadeglrggkviplKAIVDEALEKCPvsvehvlvvrrtgNPVVPWVegrdvwwh 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2309 -LEEDGPA------LDAEDPAplaalsgpqhqaYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAED---CEL- 2376
Cdd:TIGR02188  220 dLMAKASAycepepMDSEDPL------------FILYTSGSTGKPKGVLHTTGGYLLYAAMTMKyVFDIKDGDifwCTAd 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2377 ------HFYSInfdaaserlLAPLLCGARVVL-------RAQGQWgaeeiCELIRAEGVSILgftpsYGSQLA-QWLESQ 2442
Cdd:TIGR02188  288 vgwitgHSYIV---------YGPLANGATTVMfegvptyPDPGRF-----WEIIEKHKVTIF-----YTAPTAiRALMRL 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2443 GRQLP-------VRMCITGGEALTGE----HLQRIRQAFAPasFFNAYGPTET---VVMPLACLAPerLEEGAASVPIGS 2508
Cdd:TIGR02188  349 GDEWVkkhdlssLRLLGSVGEPINPEawmwYYKVVGKERCP--IVDTWWQTETggiMITPLPGATP--TKPGSATLPFFG 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2509 VVGArvayILDADLALVP-QGATGELYVGGA--GLARGYHERPalsaERFVPDPFAAEGGrLYRTGDLVRLCDNGQVEYV 2585
Cdd:TIGR02188  425 IEPA----VVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPG-YYFTGDGARRDKDGYIWIT 495
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620   2586 GRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP-SGKQLAGYVasaVAEQDEDAQAALREALKTHLKQQL 2661
Cdd:TIGR02188  496 GRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDiKGQAIYAFV---TLKDGYEPDDELRKELRKHVRKEI 569
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
3736-4152 1.47e-15

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 83.41  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3736 EQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPL----DPGHPTQRLtrivELSRT 3811
Cdd:PRK04319   71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDRL----EDSEA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3812 LVLVCTQACREQALAlfDELGCVdRPRLLVWDEIQQGEG--------AEHDPQ---VYSGPQNLAYVIYTSGSTGLPKGV 3880
Cdd:PRK04319  147 KVLITTPALLERKPA--DDLPSL-KHVLLVGEDVEEGPGtldfnalmEQASDEfdiEWTDREDGAILHYTSGSTGKPKGV 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3881 MVEQAGMLNNQLSKVPYLELDENDVIAQTAS------QSFDIsvwqflAAPLFgARVAIVPNAVAHDPQGLLAHVGEQGI 3954
Cdd:PRK04319  224 LHVHNAMLQHYQTGKYVLDLHEDDVYWCTADpgwvtgTSYGI------FAPWL-NGATNVIDGGRFSPERWYRILEDYKV 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3955 TVLESVPSLIQgML----AE--ERQALDGLRWMLPTGEAMPPELARqWLKRY--PRI----------GLVNAYGPAecsd 4016
Cdd:PRK04319  297 TVWYTAPTAIR-MLmgagDDlvKKYDLSSLRHILSVGEPLNPEVVR-WGMKVfgLPIhdnwwmtetgGIMIANYPA---- 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4017 dvafFRVDLAStestylpIGSPtdnnrlyLLGAGA---DDAFELVPLGAVGELCVAgTG---VGRGYVGDPLRTAQAFVP 4090
Cdd:PRK04319  371 ----MDIKPGS-------MGKP-------LPGIEAaivDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAG 431
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  4091 HpfgapgerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:PRK04319  432 D--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3718-4108 1.53e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 83.56  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAascLEQR------W---SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGA 3788
Cdd:PRK12582   54 LLAKWAAEAPDRPW---LAQRepghgqWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3789 GYLPLDPGHPT-----QRLTRIVELSR-TLVLVCTQACREQALALFDELGcvdrPRLLVWDEIQQGEGAEHDPQVYS--- 3859
Cdd:PRK12582  131 PAAPVSPAYSLmshdhAKLKHLFDLVKpRVVFAQSGAPFARALAALDLLD----VTVVHVTGPGEGIASIAFADLAAtpp 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3860 -----------GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIaqtaSQSFDISVWQFlaapLFG 3928
Cdd:PRK12582  207 taavaaaiaaiTPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP----PVSLDWMPWNH----TMG 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3929 ARVAIVPNAVAH-----DPQGLLAHVGEQGI--------TVLESVPSLIqGMLAEERQAldglrwmlptgeamPPELARQ 3995
Cdd:PRK12582  279 GNANFNGLLWGGgtlyiDDGKPLPGMFEETIrnlreispTVYGNVPAGY-AMLAEAMEK--------------DDALRRS 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3996 WLKRYPRIGlvnaYGPAECSDDVAFFRVDLA---------------STESTYLPIGSPTDNNRLYLLGAGADD-AFELVP 4059
Cdd:PRK12582  344 FFKNLRLMA----YGGATLSDDLYERMQALAvrttghripfytgygATETAPTTTGTHWDTERVGLIGLPLPGvELKLAP 419
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 15597620  4060 LGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLAR 4108
Cdd:PRK12582  420 VGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAAR 461
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
15-449 1.61e-15

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 83.25  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   15 LRRRAVQEPERLalrFLAEDDGEGV--VLSYRDLDLRARSIAAALQAHAQLGDRAVLLFP-SGPDYVAAFFGCLYAGVIA 91
Cdd:cd05921    1 LAHWARQAPDRT---WLAEREGNGGwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSgNSIEHALMALAAMYAGVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   92 VPAYPPESARRHHQERLLSIIADAEPRLVL------------TTADLREPLLQMNAQLSAANAPQLLCVDQLDP--AVAE 157
Cdd:cd05921   78 APVSPAYSLMSQDLAKLKHLFELLKPGLVFaqdaapfaralaAIFPLGTPLVVSRNAVAGRGAISFAELAATPPtaAVDA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  158 AWDepQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADD--VIVSWLPLYHDMG--------LIGGL 227
Cdd:cd05921  158 AFA--AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGgnhnfnlvLYNGG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  228 LQPIFSGVPcvlmSPRYFlERPVRWLEAIS-QYGGTVSGGPDFayrLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSL 306
Cdd:cd05921  236 TLYIDDGKP----MPGGF-EETLRNLREISpTVYFNVPAGWEM---LVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVW 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  307 ERFAEkfaasrfdassffacygLAEATLfvtggqrGQGIPALAVDGEalarnriAEGEGSVLMCCG-RSQPEHAVLIVDA 385
Cdd:cd05921  308 DRLQA-----------------LAVATV-------GERIPMMAGLGA-------TETAPTATFTHWpTERSGLIGLPAPG 356
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  386 ASGEVLGDDNVGEIWAAGPSIAHGYWRNPEASAKAFVErDGrtWLRTGDLGFLRDGE-----LFVTGRL 449
Cdd:cd05921  357 TELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDE-EG--FYCLGDAAKLADPDdpakgLVFDGRV 422
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
1275-1618 1.98e-15

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 80.78  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1275 VIYTSGSTGQPKGVGNTHAAL-AERLQWMqATYTLDGDDVLMQKAPVsFDVsvwecfwplvTGCRLVLA---APG----- 1345
Cdd:cd17637    5 IIHTAAVAGRPRGAVLSHGNLiAANLQLI-HAMGLTEADVYLNMLPL-FHI----------AGLNLALAtfhAGGanvvm 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1346 EHRDPARLVELVRQFGVTTLHFVPPLLQLFID--EPGVAACGSLRrLFSGGEAlPAelrnrVLQRLPAV---ALHNRYGP 1420
Cdd:cd17637   73 EKFDPAEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSLR-HVLGLDA-PE-----TIQRFEETtgaTFWSLYGQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1421 TETAINVTHWQCRAEDGErspIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADpfsaag 1500
Cdd:cd17637  146 TETSGLVTLSPYRERPGS---AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG------ 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1501 erLYRTGDRARWNADGVLEYLGRLDQQ--VKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLvGYYTGAV---- 1574
Cdd:cd17637  217 --WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI---GVPDPKW-GEGIKAVcvlk 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 15597620 1575 -GAEAEAEQnqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLD 1618
Cdd:cd17637  291 pGATLTADE---LIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
166-554 2.02e-15

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 82.92  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   166 PEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHdmglIGGL---LQPIFSGVpCVLMSP 242
Cdd:PLN02860  171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCH----IGGLssaLAMLMVGA-CHVLLP 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   243 RyFLERPVrwLEAISQYGGT----VsggPDFAYRLCSerVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRF 318
Cdd:PLN02860  246 K-FDAKAA--LQAIKQHNVTsmitV---PAMMADLIS--LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKL 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   319 dassfFACYGLAEAT---LFVTGGQRGQGIPALAVDGEALARNRIAEGEGSVlmCCGRSQPEHAVLIVDAASgevlgdDN 395
Cdd:PLN02860  318 -----FSAYGMTEACsslTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGV--CVGKPAPHVELKIGLDES------SR 384
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   396 VGEIWAAGPSIAHGYWRNPEASAKAFVeRDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIE-------- 466
Cdd:PLN02860  385 VGRILTRGPHVMLGYWGQNSETASVLS-NDG--WLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEavlsqhpg 461
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   467 --RTVESEVPSARKGR-VAAFAVTVDGEEGIGIAAEIGRGvQKSVPAQELIDSIRQAVAEAYQeAPKVVaLLNPGALPKT 543
Cdd:PLN02860  462 vaSVVVVGVPDSRLTEmVVACVRLRDGWIWSDNEKENAKK-NLTLSSETLRHHCREKNLSRFK-IPKLF-VQWRKPFPLT 538
                         410
                  ....*....|.
gi 15597620   544 SSGKLQRSACR 554
Cdd:PLN02860  539 TTGKIRRDEVR 549
PRK07638 PRK07638
acyl-CoA synthetase; Validated
2199-2689 2.12e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 82.52  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2199 SPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEvRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY-PLERLQy 2277
Cdd:PRK07638   14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWkQDELKE- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2278 miedsgvRLLLSHAALFEA----LGELPAGVAR-WCLEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVS 2352
Cdd:PRK07638   92 -------RLAISNADMIVTerykLNDLPDEEGRvIEIDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2353 HgEIAMH---CAAviECFGMRAEDCEL--------HFYsinFDAASErllapLLCGARVVLraQGQWGAEEICELIRAEG 2421
Cdd:PRK07638  165 Q-QSWLHsfdCNV--HDFHMKREDSVLiagtlvhsLFL---YGAIST-----LYVGQTVHL--MRKFIPNQVLDKLETEN 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2422 VSILGFTPSYGSQLAQwlESQGRQLPVRMcITGGEALTGEHLQRIRQAFAPASFFNAYGPTETVVmpLACLAPERLEEGA 2501
Cdd:PRK07638  232 ISVMYTVPTMLESLYK--ENRVIENKMKI-ISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF--VTALVDEESERRP 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2502 ASV--PIGSVVgarvAYILDADLALVPQGATGELYVGGAGLARGYherpaLSAERFVPDPFAAEggrlYRT-GDLVRLCD 2578
Cdd:PRK07638  307 NSVgrPFHNVQ----VRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG----WMTvRDVGYEDE 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2579 NGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPsgkqLAGYVASAVAEQDEDAQAalreaLKTHLK 2658
Cdd:PRK07638  374 EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS----YWGEKPVAIIKGSATKQQ-----LKSFCL 444
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  2659 QQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK07638  445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
1134-1588 2.23e-15

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 83.27  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1134 LERQLAQSAERVALEWDGGSLG------YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLA---------I 1198
Cdd:PRK00174   73 LDRHLKTRGDKVAIIWEGDDPGdsrkitYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsV 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1199 VKAGgayvpldpdYPSERLAYMLADSGVELLLTQAHLFER-------------LPGAEGV----------TPICLDSLKl 1255
Cdd:PRK00174  153 VFGG---------FSAEALADRIIDAGAKLVITADEGVRGgkpiplkanvdeaLANCPSVekvivvrrtgGDVDWVEGR- 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1256 DNW--------PSQAPGLHLHGDNLAYVIYTSGSTGQPKGV-----G-NTHAALAerlqwMQATYTLDGDDVlmqkapvs 1321
Cdd:PRK00174  223 DLWwhelvagaSDECEPEPMDAEDPLFILYTSGSTGKPKGVlhttgGyLVYAAMT-----MKYVFDYKDGDV-------- 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1322 fdvsvwecFW-----------------PLVTGCRLVL--AAPgEHRDPARLVELVRQFGVTTLHFVPPLLQLFI----DE 1378
Cdd:PRK00174  290 --------YWctadvgwvtghsyivygPLANGATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMkegdEH 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1379 PGVAACGSLRRLFSGGEALPAElrnrvlqrlpavA---LHNRYGPTETAINVTHWQcrAEDGER--SPI----------- 1442
Cdd:PRK00174  361 PKKYDLSSLRLLGSVGEPINPE------------AwewYYKVVGGERCPIVDTWWQ--TETGGImiTPLpgatplkpgsa 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1443 GRPLGNVVCRVLDAEFNLLPAGVAGELCIGGL--GLARGYLGRPalsaERFVADPFSAAGERlYRTGDRARWNADGVLEY 1520
Cdd:PRK00174  427 TRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKGM-YFTGDGARRDEDGYYWI 501
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  1521 LGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIR-EGVAGSQLVGYYTGAVGAEAEAEQNQRLRA 1588
Cdd:PRK00174  502 TGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpDDIKGQGIYAFVTLKGGEEPSDELRKELRN 570
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
4026-4321 2.65e-15

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 79.79  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4026 ASTESTYLPIGSPTDNNRLYLLGAGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFGAPGERLYRTGD 4105
Cdd:COG3433    7 PPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4106 LARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGetprssadsPAGLMV 4185
Cdd:COG3433   87 LLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVA---------ALDGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4186 EQGAWFERIKQqlradLPDYMVPLHWLVLDRMPLNANGKLDRKALPALDIGQMQNQAYQAP---RNELEETLARIWAEVL 4262
Cdd:COG3433  158 AAAALAALDKV-----PPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaleTALTEEELRADVAELL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 4263 KV--ERVGVFDNFFELGGHSLLATQIASRVQKAlQRNVPLRAMFECTTVEELASYIESLAP 4321
Cdd:COG3433  233 GVdpEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQA 292
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
1156-1635 3.22e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 82.45  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML--ADSGVELL-LTQ 1232
Cdd:PRK07008   42 YRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVnhAEDRYVLFdLTF 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1233 AHLFE----RLPGAEGVTPIC-LDSLKLDNWPSQAPGLHLHGDNLAY------------VIYTSGSTGQPKGVGNTH--- 1292
Cdd:PRK07008  122 LPLVDalapQCPNVKGWVAMTdAAHLPAGSTPLLCYETLVGAQDGDYdwprfdenqassLCYTSGTTGNPKGALYSHrst 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1293 ------AALAERLqwmqatyTLDGDDVLMQKAPVsFDVSVWECFW--PLvTGCRLVLaaPGEHRDPARLVELVRQFGVTT 1364
Cdd:PRK07008  202 vlhaygAALPDAM-------GLSARDAVLPVVPM-FHVNAWGLPYsaPL-TGAKLVL--PGPDLDGKSLYELIEAERVTF 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1365 LHFVPPLLQLFID--EPGVAACGSLRRLFSGGEALPAELRnRVLQRLPAVALHNRYGPTE-----TAINVTHWQCRAEDG 1437
Cdd:PRK07008  271 SAGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPPAMI-RTFEDEYGVEVIHAWGMTEmsplgTLCKLKWKHSQLPLD 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1438 ERSPI----GRPLGNVVCRVLDAEFNLLP-AGVA-GELCIGGLGLARGYLGRPalsaerfvADPFSaagERLYRTGDRAR 1511
Cdd:PRK07008  350 EQRKLlekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRGD--------ASPLV---DGWFPTGDVAT 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1512 WNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQA----------------VVVIREG--VAGSQLVGYYTGA 1573
Cdd:PRK07008  419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAaciacahpkwderpllVVVKRPGaeVTREELLAFYEGK 498
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  1574 VGaeaeaeqnqrlraalqaelpEYMVPTQLMRLAQMPLGPSGKLDTRALPEpvwQQREHVEP 1635
Cdd:PRK07008  499 VA--------------------KWWIPDDVVFVDAIPHTATGKLQKLKLRE---QFRDYVLP 537
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
37-239 3.66e-15

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 81.95  E-value: 3.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   37 EGVVLSYRDLDLRARSI--AAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGViaVPAYPPESARRhhqERLLSIIAD 114
Cdd:cd05938    2 EGETYTYRDVDRRSNQAarALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGC--PVAFLNTNIRS---KSLLHCFRC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  115 AEPRLVLTTADLRE-------PLLQMNAQ---LSAANAPQllCVDQLDPAVAEAWDEP-------QVRPEHIAFLQYTSG 177
Cdd:cd05938   77 CGAKVLVVAPELQEaveevlpALRADGVSvwyLSHTSNTE--GVISLLDKVDAASDEPvpaslraHVTIKSPALYIYTSG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620  178 STALPKGVQVSHGNLVANEVLIRRgFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL 239
Cdd:cd05938  155 TTGLPKAARISHLRVLQCSGFLSL-CGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVL 215
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
2187-2688 3.78e-15

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 82.48  E-value: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2187 TLHGLFAARVAASPQAPA---LTFAGQT------LSYAELDARSNRLARVLRSHgVGPEVRVGLALERSLEMVVGLLAIL 2257
Cdd:PRK12476   35 TLISLIERNIANVGDTVAyryLDHSHSAagcaveLTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2258 KAGGAYVPL-DPEYP--LERLQYMIEDSGVRLLLSHAALFEALGELPAGVARwcleEDGPALDAED--PAPLAALSGPQH 2332
Cdd:PRK12476  114 KAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPR----LRRPRVIAIDaiPDSAGESFVPVE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2333 Q-----AYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRaeDCELHFYS---INFDAASERLLAPLLCGARVVL-- 2402
Cdd:PRK12476  190 LdtddvSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLL--DRNTHGVSwlpLYHDMGLSMIGFPAVYGGHSTLms 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2403 -----RAQGQWgaeeICEL-IRAEGVSILGFTPSYGSQLA--QWLESQGRQLPVR--MCITGGEALTGEHLQRIRQAFAP 2472
Cdd:PRK12476  268 ptafvRRPQRW----IKALsEGSRTGRVVTAAPNFAYEWAaqRGLPAEGDDIDLSnvVLIIGSEPVSIDAVTTFNKAFAP 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2473 asffnaYGPTETVVMP----------LACLAP-----------ERLEEGAA------------SVPIGSVVGARVAYILD 2519
Cdd:PRK12476  344 ------YGLPRTAFKPsygiaeatlfVATIAPdaepsvvyldrEQLGAGRAvrvaadapnavaHVSCGQVARSQWAVIVD 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2520 ADL-ALVPQGATGELYVGGAGLARGYHERPALSAERF-------VPDPF----AAEGGRLYRTGDLVRLCDnGQVEYVGR 2587
Cdd:PRK12476  418 PDTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrLAEGShadgAADDGTWLRTGDLGVYLD-GELYITGR 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2588 IDHQVKIRGFRIELGEIEARLLE-HPQVREALVLALDSPS--GKQLAGYVASAVAEQDEDAQAALrEALKTHLKQQLPDY 2664
Cdd:PRK12476  497 IADLIVIDGRNHYPQDIEATVAEaSPMVRRGYVTAFTVPAedNERLVIVAERAAGTSRADPAPAI-DAIRAAVSRRHGLA 575
                         570       580
                  ....*....|....*....|....
gi 15597620  2665 MVPAHLLLLASLPLTANGKLDRRA 2688
Cdd:PRK12476  576 VADVRLVPAGAIPRTTSGKLARRA 599
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
2176-2689 3.85e-15

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 82.23  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2176 AGTAGEAGLQD--TLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVG 2252
Cdd:PRK08751   13 AGVAAEIDLEQfrTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2253 LLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS---------------------HAALFEALGELPAGVARWCLE- 2310
Cdd:PRK08751   93 TFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVidnfgttvqqviadtpvkqviTTGLGDMLGFPKAALVNFVVKy 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2311 ----------------EDGPALDAEDPAPLAALSgPQHQAYLIYTSGSTGKPKGVAVSHGEIA---MHCAAVIECFGMRA 2371
Cdd:PRK08751  173 vkklvpeyringairfREALALGRKHSMPTLQIE-PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmQQAHQWLAGTGKLE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2372 EDCE-----LHFYSInFDAASERLLAPLLCGA-RVVLRAQGQWGAeeICELIRAEGVSILGFTPSYGSQLAQWLESQGRQ 2445
Cdd:PRK08751  252 EGCEvvitaLPLYHI-FALTANGLVFMKIGGCnHLISNPRDMPGF--VKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDF 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2446 LPVRMCITGGEALTGEHLQRIRQAfAPASFFNAYGPTETvvMPLACLAPERLEE--GAASVPIGSVVgarvAYILDADLA 2523
Cdd:PRK08751  329 SSLKMTLGGGMAVQRSVAERWKQV-TGLTLVEAYGLTET--SPAACINPLTLKEynGSIGLPIPSTD----ACIKDDAGT 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2524 LVPQGATGELYVGGAGLARGYHERPALSAErfVPDpfaAEGgrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGE 2603
Cdd:PRK08751  402 VLAIGEIGELCIKGPQVMKGYWKRPEETAK--VMD---ADG--WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNE 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2604 IEARLLEHPQVREalVLALDSPSGKqlAGYVASAVAEQDEDAQAAlrEALKTHLKQQLPDYMVPAHLLLLASLPLTANGK 2683
Cdd:PRK08751  475 IEDVIAMMPGVLE--VAAVGVPDEK--SGEIVKVVIVKKDPALTA--EDVKAHARANLTGYKQPRIIEFRKELPKTNVGK 548

                  ....*.
gi 15597620  2684 LDRRAL 2689
Cdd:PRK08751  549 ILRREL 554
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
164-550 4.21e-15

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 80.96  E-value: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  164 VRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGF---GIGADDVIVSWLPlyhdMGL-IGGLlqpIF------S 233
Cdd:COG1541   80 VPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLraaGVRPGDRVQNAFG----YGLfTGGL---GLhygaerL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  234 GVPCVLMSPryflERPVRWLEAISQYGGTV-SGGPDFAYRLCseRVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEK 312
Cdd:COG1541  153 GATVIPAGG----GNTERQLRLMQDFGPTVlVGTPSYLLYLA--EVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEER 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  313 FAASRFDassffaCYGLAEATlfvtggqrgqgiPALAVDGEALARNRIaeGEGSVLmccgrsqPEhavlIVDAASGEVLG 392
Cdd:COG1541  227 WGIKAYD------IYGLTEVG------------PGVAYECEAQDGLHI--WEDHFL-------VE----IIDPETGEPVP 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  393 DDNVGEIwaagpsiahgywrnpeasakafV----ERDG----RtwLRTGDLGFLRDGE----------LFVTGRLKDMLI 454
Cdd:COG1541  276 EGEEGEL----------------------VvttlTKEAmpliR--YRTGDLTRLLPEPcpcgrthpriGRILGRADDMLI 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  455 VRGHNLYPQDIErtvesEVPSARKGRVAAFAVTVDGEEG---IGIAAEIGRGVQksvpaqelIDSIRQAVAEAYQEAPKV 531
Cdd:COG1541  332 IRGVNVFPSQIE-----EVLLRIPEVGPEYQIVVDREGGldeLTVRVELAPGAS--------LEALAEAIAAALKAVLGL 398
                        410       420
                 ....*....|....*....|..
gi 15597620  532 ---VALLNPGALPKtSSGKLQR 550
Cdd:COG1541  399 raeVELVEPGSLPR-SEGKAKR 419
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
8-224 5.47e-15

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 81.84  E-value: 5.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     8 PTTLVQALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLY 86
Cdd:PRK08279   36 KRSLGDVFEEAAARHPDRPALLF------EDQSISYAELNARANRYAHWAAARgVGKGDVVALLMENRPEYLAAWLGLAK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    87 AGVIAvpayppeSARRHHQ--ERLLSIIADAEPRLVLTTADLREPLLQMNAQLsaANAPQLLCVDQLDPAVAEAWDE--- 161
Cdd:PRK08279  110 LGAVV-------ALLNTQQrgAVLAHSLNLVDAKHLIVGEELVEAFEEARADL--ARPPRLWVAGGDTLDDPEGYEDlaa 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   162 -------------PQVRPEHIAFLQYTSGSTALPKGVQVSHGnlvanevliR-----RGFG----IGADDVIVSWLPLYH 219
Cdd:PRK08279  181 aaagapttnpasrSGVTAKDTAFYIYTSGTTGLPKAAVMSHM---------RwlkamGGFGgllrLTPDDVLYCCLPLYH 251

                  ....*
gi 15597620   220 DMGLI 224
Cdd:PRK08279  252 NTGGT 256
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
2329-2620 6.24e-15

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 81.40  E-value: 6.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2329 GPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHF----YSINFDAASerlLAPLLCGARVVLrA 2404
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFlppfHAYGFNSCT---LFPLLSGVPVVF-A 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2405 QGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTE 2483
Cdd:PRK06334  257 YNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPsLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTE 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2484 -TVVMPLACLAPERLEEgAASVPIGsvvGARVAYILDADLALVPQGATGELYVGGAGLARGYHERpalsaerfvpDP--- 2559
Cdd:PRK06334  337 cSPVITINTVNSPKHES-CVGMPIR---GMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGE----------DFgqg 402
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  2560 FAAEGGRL-YRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEH---PQVREALVL 2620
Cdd:PRK06334  403 FVELGGETwYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPL 467
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
1156-1594 7.41e-15

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 81.11  E-value: 7.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGV--GPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQA 1233
Cdd:cd05927    8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaeGVTPICLDSLKldNWPSQAPGLHLHG--DNLAYVIYTSGSTGQPKGVGNTHAALAErlqwmqatyTLDGD 1311
Cdd:cd05927   88 ----------GVKVYSLEEFE--KLGKKNKVPPPPPkpEDLATICYTSGTTGNPKGVMLTHGNIVS---------NVAGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1312 DVLMQKAPVSFDVSVWECFWPL--------VTGCRLVLAAPGEHR-DPARLVELVRQFGVTTLHFVPPLLQLFIDE--PG 1380
Cdd:cd05927  147 FKILEILNKINPTDVYISYLPLahifervvEALFLYHGAKIGFYSgDIRLLLDDIKALKPTVFPGVPRVLNRIYDKifNK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1381 VAACGSLRR-LFSGG-EALPAELRNRVLQRLP------------AVALHNR----------------------------Y 1418
Cdd:cd05927  227 VQAKGPLKRkLFNFAlNYKLAELRSGVVRASPfwdklvfnkikqALGGNVRlmltgsaplspevleflrvalgcpvlegY 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1419 GPTET--AINVTHwqcraeDGERSP--IGRPLGNVVCRVLD-AEFNLLPAGV--AGELCIGGLGLARGYLGRPALSAERF 1491
Cdd:cd05927  307 GQTECtaGATLTL------PGDTSVghVGGPLPCAEVKLVDvPEMNYDAKDPnpRGEVCIRGPNVFSGYYKDPEKTAEAL 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1492 VADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKL-RGFRIEPEEIQARLLAQPGVAQ-------------AVVVI 1557
Cdd:cd05927  381 DEDGW-------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQifvygdslksflvAIVVP 453
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 15597620 1558 REGV----AGSQLvgyytGAVGAEAEAEQNQRLRAALQAEL 1594
Cdd:cd05927  454 DPDVlkewAASKG-----GGTGSFEELCKNPEVKKAILEDL 489
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
2207-2666 7.50e-15

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 80.55  E-value: 7.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2207 FAGQTLSYAELDARSNRLARVLRS-HGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVR 2285
Cdd:cd05937    1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2286 LLLShaalfealgelpagvarwcleedgpalDAEDPAplaalsgpqhqaYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE 2365
Cdd:cd05937   81 FVIV---------------------------DPDDPA------------ILIYTSGTTGLPKAAAISWRRTLVTSNLLSH 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2366 CFGMRAED----CELHFYSinfDAASERLLAPLLCGARVVLRAQgqWGAEEICELIRAEGVSILgftpSYGSQLAQWL-- 2439
Cdd:cd05937  122 DLNLKNGDrtytCMPLYHG---TAAFLGACNCLMSGGTLALSRK--FSASQFWKDVRDSGATII----QYVGELCRYLls 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2440 ---ESQGRQLPVRMCItgGEALTGEHLQRIRQAFAPASFFNAYGPTETVvmplacLAPERLEEGAASvpIGSVV--GARV 2514
Cdd:cd05937  193 tppSPYDRDHKVRVAW--GNGLRPDIWERFRERFNVPEIGEFYAATEGV------FALTNHNVGDFG--AGAIGhhGLIR 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2515 AYILDADLALV---------------------PQGATGELYV----GGAGLARGYHERPALSAERFVPDPFAaEGGRLYR 2569
Cdd:cd05937  263 RWKFENQVVLVkmdpetddpirdpktgfcvraPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFR-KGDIYFR 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2570 TGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASAVAEQDEDAQAAL 2649
Cdd:cd05937  342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEFT 421
                        490
                 ....*....|....*..
gi 15597620 2650 REALKTHLKQQLPDYMV 2666
Cdd:cd05937  422 KSLLASLARKNLPSYAV 438
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3740-4230 1.16e-14

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 79.87  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQA 3819
Cdd:cd05973    2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3820 CREQalalFDElgcvdrprllvwdeiqqgegaehDPQVYsgpqnlayvIYTSGSTGLPKGVMVEqagmLNNQLSKVPYLE 3899
Cdd:cd05973   82 NRHK----LDS-----------------------DPFVM---------MFTSGTTGLPKGVPVP----LRALAAFGAYLR 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3900 ----LDENDVIAQTASQSFDISVWQFLAAPLfGARVAIVPNAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLA---EER 3972
Cdd:cd05973  122 davdLRPEDSFWNAADPGWAYGLYYAITGPL-ALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAagaEVP 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3973 QALDG-LRWMLPTGEAMPPELARqWLKRYPRIGLVNAYGPAEcsddVAFFrvdLASTESTYLPI-----GSPTDNNRLYL 4046
Cdd:cd05973  201 ARPKGrLRRVSSAGEPLTPEVIR-WFDAALGVPIHDHYGQTE----LGMV---LANHHALEHPVhagsaGRAMPGWRVAV 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4047 LgagADDAFELVPlgavGELCVAGTGVGRgyvgDPLRTAQAFVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVK 4126
Cdd:cd05973  273 L---DDDGDELGP----GEPGRLAIDIAN----SPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVIT 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4127 IRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSADSPAGLMveqgawfERIKQQLRAdlpdY 4205
Cdd:cd05973  342 MSGYRIGPFDVESALIEHPAVAEAAViGVPDPERTEVVKAFVVLRGGHEGTPALADELQ-------LHVKKRLSA----H 410
                        490       500
                 ....*....|....*....|....*
gi 15597620 4206 MVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05973  411 AYPRTIHFVDELPKTPSGKIQRFLL 435
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
2212-2656 1.17e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 80.86  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2212 LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL-----ERLQYMIEDSGVRL 2286
Cdd:PRK12582   81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRV 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2287 LLS-HAALFE-ALGELPAGVARWcLEEDGPAlDAEDPAPLAALS---------------GPQHQAYLIYTSGSTGKPKGV 2349
Cdd:PRK12582  161 VFAqSGAPFArALAALDLLDVTV-VHVTGPG-EGIASIAFADLAatpptaavaaaiaaiTPDTVAKYLFTSGSTGMPKAV 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2350 AVSHGeiaMHCAAVIECFGMRAEDCE------LHFYSINFDAASERLLAPLLCGARVVLRAQGQWGAEEICELIRA-EGV 2422
Cdd:PRK12582  239 INTQR---MMCANIAMQEQLRPREPDppppvsLDWMPWNHTMGGNANFNGLLWGGGTLYIDDGKPLPGMFEETIRNlREI 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2423 S--ILGFTPSYGSQLAQWLESQ---GRQLPVRMCIT--GGEALTGEHLQRIrQAFAPAS------FFNAYGPTETvvMPL 2489
Cdd:PRK12582  316 SptVYGNVPAGYAMLAEAMEKDdalRRSFFKNLRLMayGGATLSDDLYERM-QALAVRTtghripFYTGYGATET--APT 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2490 ACL---APERleEGAASVPIGSVvgarvayildaDLALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggr 2566
Cdd:PRK12582  393 TTGthwDTER--VGLIGLPLPGV-----------ELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------ 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2567 lYRTGDLVRLCDNGQVE----YVGRIDHQVKI-RGFRIELGEIEARLLE--HPQVREALVLALD----------SPSG-K 2628
Cdd:PRK12582  454 -YRLGDAARFVDPDDPEkgliFDGRVAEDFKLsTGTWVSVGTLRPDAVAacSPVIHDAVVAGQDrafigllawpNPAAcR 532
                         490       500       510
                  ....*....|....*....|....*....|.
gi 15597620  2629 QLAGYvASAVAEQ---DEDAQAALREALKTH 2656
Cdd:PRK12582  533 QLAGD-PDAAPEDvvkHPAVLAILREGLSAH 562
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
2194-2634 1.24e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 80.05  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2194 ARVAasPQAPALTFA--GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP 2271
Cdd:PRK13390    7 AQIA--PDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2272 LERLQYMIEDSGVRLLLSHAAL----FEALGELPAGVArWCLEEDGPAlDAEdpAPLAALSGPQHQ----AYLIYTSGST 2343
Cdd:PRK13390   85 APEADYIVGDSGARVLVASAALdglaAKVGADLPLRLS-FGGEIDGFG-SFE--AALAGAGPRLTEqpcgAVMLYSSGTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2344 GKPKGV--------AVSHGEIAMHCAAVIecFGMRAEDcelhfysINFDAASERLLAPL-LCGarvVLRAQGqwGAEEIC 2414
Cdd:PRK13390  161 GFPKGIqpdlpgrdVDAPGDPIVAIARAF--YDISESD-------IYYSSAPIYHAAPLrWCS---MVHALG--GTVVLA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2415 EliRAEGVSILGFTPSYGSQLAQWLESqgrqLPVRMCITGGEALTGEHLQRIR---QAFAPAS--------------FFN 2477
Cdd:PRK13390  227 K--RFDAQATLGHVERYRITVTQMVPT----MFVRLLKLDADVRTRYDVSSLRaviHAAAPCPvdvkhamidwlgpiVYE 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2478 AYGPTETVVMPLAClAPERLEEGAAsvpIG-SVVGArvAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFV 2556
Cdd:PRK13390  301 YYSSTEAHGMTFID-SPDWLAHPGS---VGrSVLGD--LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQH 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2557 P-DPFAAEggrlyrTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLAGYV 2634
Cdd:PRK13390  375 PaHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEmGEQVKAVI 448
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1634-1710 1.40e-14

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 71.42  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1634 EPRTELQRRIAAIWSEVLGLP--RVGLRDDFF-ELGGHSLLATRIVSRTRQACDVELPLRALFEASELEAFCEQVRAAQA 1710
Cdd:COG0236    1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
2207-2373 1.45e-14

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 80.03  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2207 FAGQTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVR 2285
Cdd:cd05938    1 FEGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2286 LLLSHAALFEALGE-LPA----GVARWCLEEDGP---------ALDAE-DPAPLAALSGPQH---QAYLIYTSGSTGKPK 2347
Cdd:cd05938   81 VLVVAPELQEAVEEvLPAlradGVSVWYLSHTSNtegvislldKVDAAsDEPVPASLRAHVTiksPALYIYTSGTTGLPK 160
                        170       180
                 ....*....|....*....|....*.
gi 15597620 2348 GVAVSHGEIAMhCAAVIECFGMRAED 2373
Cdd:cd05938  161 AARISHLRVLQ-CSGFLSLCGVTADD 185
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
36-556 1.67e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 79.74  E-value: 1.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    36 GEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGV--IAVPAY--PPESARrhhqerlls 110
Cdd:PRK13391   20 STGEVVTYRELDERSNRLAHLFRSLgLKRGDHVAIFMENNLRYLEVCWAAERSGLyyTCVNSHltPAEAAY--------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   111 IIADAEPRLVLTTADLREPllqmnAQLSAANAPQL-LCV-----------DQLDPAVAEAWDEPqVRPEHI-AFLQYTSG 177
Cdd:PRK13391   91 IVDDSGARALITSAAKLDV-----ARALLKQCPGVrHRLvldgdgelegfVGYAEAVAGLPATP-IADESLgTDMLYSSG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   178 STALPKGV--QVSHGNLVAN---EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQpIFSGVPCVLMspryflER--PV 250
Cdd:PRK13391  165 TTGRPKGIkrPLPEQPPDTPlplTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLV-IRLGGTVIVM------EHfdAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   251 RWLEAISQYGGTVSG-GPDFAYRLCseRVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGL 329
Cdd:PRK13391  238 QYLALIEEYGVTHTQlVPTMFSRML--KLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEY------YAA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   330 AEATLFVtggqrgqgipalAVDG-EALARnriaegEGSVlmccGRsqPEHAVLIVDAASGEVLGDDNVGEIWAAGPSiAH 408
Cdd:PRK13391  310 TEGLGFT------------ACDSeEWLAH------PGTV----GR--AMFGDLHILDDDGAELPPGEPGTIWFEGGR-PF 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   409 GYWRNPEASAKAfveRDGR-TWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIER--TVESEVPSArkgrvAAF 484
Cdd:PRK13391  365 EYLNDPAKTAEA---RHPDgTWSTVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENllITHPKVADA-----AVF 436
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620   485 AVTVD--GEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVaeAYQEAPKVVALLNpgALPKTSSGKLQRSACRLR 556
Cdd:PRK13391  437 GVPNEdlGEEVKAVVQPVDGVDPGPALAAELIAFCRQRL--SRQKCPRSIDFED--ELPRLPTGKLYKRLLRDR 506
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
2199-2623 1.74e-14

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 79.53  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2199 SPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYM 2278
Cdd:PRK09029   16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2279 IEDSGVR--LLLSHAALFEALGELPAgvarwcleedgPALDAEDPAPLAalsgPQHQAYLIYTSGSTGKPKGVAVSHgei 2356
Cdd:PRK09029   96 LPSLTLDfaLVLEGENTFSALTSLHL-----------QLVEGAHAVAWQ----PQRLATMTLTSGSTGLPKAAVHTA--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2357 AMHCAAviecfgmrAED-CELhfysINFDAASERLLA-P-------------LLCGARVVLRAQGQwgaeeiceLIRA-E 2420
Cdd:PRK09029  158 QAHLAS--------AEGvLSL----MPFTAQDSWLLSlPlfhvsgqgivwrwLYAGATLVVRDKQP--------LEQAlA 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2421 GVSILGFTPsygSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQ----AFApasffnAYGPTE---TVVMPLAcla 2493
Cdd:PRK09029  218 GCTHASLVP---TQLWRLLDNRSEPLSLKAVLLGGAAIPVELTEQAEQqgirCWC------GYGLTEmasTVCAKRA--- 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2494 perleEGAASVpiGSVVGARvayildaDLALVpqgaTGELYVGGAGLARGYherpalsaerfvpdpfaaeggrlYRTGDL 2573
Cdd:PRK09029  286 -----DGLAGV--GSPLPGR-------EVKLV----DGEIWLRGASLALGY-----------------------WRQGQL 324
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  2574 VRLCD--------------NGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALD 2623
Cdd:PRK09029  325 VPLVNdegwfatrdrgewqNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1122-1512 1.75e-14

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 80.31  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1122 PCEPARAWLPELLERQLAQSAERVAL-------EWDGgsLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVG 1194
Cdd:PRK08180   33 PLGDYPRRLTDRLVHWAQEAPDRVFLaergadgGWRR--LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1195 LLAIVKAGGAYVPLDPDY--PS---ERLAYML---------ADSGVE-------LLLTQAHLFERLPGAEGVTPICLDSL 1253
Cdd:PRK08180  111 ALAAMYAGVPYAPVSPAYslVSqdfGKLRHVLelltpglvfADDGAAfaralaaVVPADVEVVAVRGAVPGRAATPFAAL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1254 KLDNWPSQAPGLH--LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDD--VLMQKAPvsfdvsvwec 1329
Cdd:PRK08180  191 LATPPTAAVDAAHaaVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLP---------- 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1330 fWPLVTGCR----LVLAAPGEHR-D-----PARLVELVRQFG--VTTLHF-VPP----LLQLFIDEPGVAAC--GSLRRL 1390
Cdd:PRK08180  261 -WNHTFGGNhnlgIVLYNGGTLYiDdgkptPGGFDETLRNLReiSPTVYFnVPKgwemLVPALERDAALRRRffSRLKLL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1391 FSGGEALPAELRNRvLQRLPAVALHNR------YGPTETAINVT--HWQcraedGERS-PIGRPL-GNVVCrvldaefnL 1460
Cdd:PRK08180  340 FYAGAALSQDVWDR-LDRVAEATCGERirmmtgLGMTETAPSATftTGP-----LSRAgNIGLPApGCEVK--------L 405
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597620  1461 LPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARW 1512
Cdd:PRK08180  406 VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVRF 450
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
2188-2654 2.09e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 79.66  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2188 LHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2267
Cdd:PRK13383   37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2268 PEYPLERLQYMIEDSGVRLLLSHAALFEALgelpAGVARWCLEEDGPALDAEDPAPLAALSGPQHQAYLiyTSGSTGKPK 2347
Cdd:PRK13383  117 TEFRSDALAAALRAHHISTVVADNEFAERI----AGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLL--TSGTTGKPK 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2348 GV----AVSHGeIAMHCAAVIEC---FGMRAEDCELHFYSINFDAaserLLAPLLCGARVVLRAqgQWGAEEI---CELI 2417
Cdd:PRK13383  191 GVprapQLRSA-VGVWVTILDRTrlrTGSRISVAMPMFHGLGLGM----LMLTIALGGTVLTHR--HFDAEAAlaqASLH 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2418 RAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPAsFFNAYGPTETVVMPLAclAPERL 2497
Cdd:PRK13383  264 RADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALA--TPADL 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2498 EEGAASVpiGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHErpalSAERFVPDPFAAeggrlyrTGDLVRLC 2577
Cdd:PRK13383  341 RDAPETV--GKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDGMTS-------TGDMGYLD 407
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2578 DNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLAGYVAsAVAEQDEDAqAALREALK 2654
Cdd:PRK13383  408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVpDERFGHRLAAFVV-LHPGSGVDA-AQLRDYLK 483
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3866-4226 2.32e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 78.19  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3866 YVIYTSGSTGLPKGVMVEQA---GMLNNQLSKVPYLELDENDVIAQTASQ----SFDI-------SVWQFLAAPLFGARV 3931
Cdd:cd05924    7 YILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFTPSEDAHKAAAAAagtvMFPApplmhgtGSWTAFGGLLGGQTV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3932 AIVpnAVAHDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA-----LDGLRWMLPTGEAMPPELARQWLKRYPRIGLV 4006
Cdd:cd05924   87 VLP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDagpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4007 NAYGPAEcsddvaffrvdlASTESTYLPIGSPTDNNRLYLLGAG---ADDAFELVPLGAVGELCVAGTG-VGRGYVGDPL 4082
Cdd:cd05924  165 DAFGSSE------------TGFTGSGHSAGSGPETGPFTRANPDtvvLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4083 RTAQAFVPhpfgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVA-VQEGANGK 4161
Cdd:cd05924  233 KTAETFPE----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVgRPDERWGQ 308
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620 4162 YLVGYLvpgetprsSADSPAGLMVEQgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLD 4226
Cdd:cd05924  309 EVVAVV--------QLREGAGVDLEE------LREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK05857 PRK05857
fatty acid--CoA ligase;
1131-1636 2.61e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 79.28  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1131 PELLERQLAQSAER---VALE-WDGGS-LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAY 1205
Cdd:PRK05857   14 STVLDRVFEQARQQpeaIALRrCDGTSaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1206 VPLDPDYPSERLAYM--LADSGVELLLTQAHL-FERLPGAEGVTPICLDSLKLD----------NWPSQAPGLHlhGDNL 1272
Cdd:PRK05857   94 VMADGNLPIAAIERFcqITDPAAALVAPGSKMaSSAVPEALHSIPVIAVDIAAVtresehsldaASLAGNADQG--SEDP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1273 AYVIYTSGSTGQPKGV---GNTHAAL-----AERLQWM-----QATYTldgddvlmqKAPVSFDVSVWECFWPLVTGCRL 1339
Cdd:PRK05857  172 LAMIFTSGTTGEPKAVllaNRTFFAVpdilqKEGLNWVtwvvgETTYS---------PLPATHIGGLWWILTCLMHGGLC 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1340 VLAapGEHrdPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACG--SLRRLFSGG-EALPAELRnrvLQRLPAVALHN 1416
Cdd:PRK05857  243 VTG--GEN--TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVR---FIEATGVRTAQ 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1417 RYGPTETAINVThwqCRAEDG------ERSPIGRPLGNVvcrvldaEFNLLPAGVAGELCIGGLGLAR------------ 1478
Cdd:PRK05857  316 VYGLSETGCTAL---CLPTDDgsivkiEAGAVGRPYPGV-------DVYLAATDGIGPTAPGAGPSASfgtlwikspanm 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1479 -GYLGRPALSAERFVadpfsaagERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVI 1557
Cdd:PRK05857  386 lGYWNNPERTAEVLI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYE 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1558 REGVAGSQLVGYY---TGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHVE 1634
Cdd:PRK05857  458 IPDEEFGALVGLAvvaSAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVV 537

                  ..
gi 15597620  1635 PR 1636
Cdd:PRK05857  538 VR 539
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
2210-2621 3.11e-14

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 78.80  E-value: 3.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGgayVPLDPEYplerlqymieDSgvrllLS 2289
Cdd:cd17639    4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVY----------AT-----LG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 HAALFEALGElpAGVArwCLEEDGpalDAEDPAplaalsgpqhqayLI-YTSGSTGKPKGVAVSHGEIAMHCAAVIECFG 2368
Cdd:cd17639   66 EDALIHSLNE--TECS--AIFTDG---KPDDLA-------------CImYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVP 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2369 --MRAEDC-----------ELHFYSINFDA------ASERLLAPLL----CGARVVLRAQGQWGAEEICELIRA---EGV 2422
Cdd:cd17639  126 elLGPDDRylaylplahifELAAENVCLYRggtigyGSPRTLTDKSkrgcKGDLTEFKPTLMVGVPAIWDTIRKgvlAKL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2423 SILG------FTPSYGSQLAQWLESQG------------RQL---PVRMCITGGEALTGEHLQRIRQAFAPasFFNAYGP 2481
Cdd:cd17639  206 NPMGglkrtlFWTAYQSKLKALKEGPGtplldelvfkkvRAAlggRLRYMLSGGAPLSADTQEFLNIVLCP--VIQGYGL 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2482 TETVVMplACLA-PERLEEGAASVPIGSVVGARV-----AYILDADLalvPQGatgELYVGGAGLARGYHERPALSAERF 2555
Cdd:cd17639  284 TETCAG--GTVQdPGDLETGRVGPPLPCCEIKLVdweegGYSTDKPP---PRG---EILIRGPNVFKGYYKNPEKTKEAF 355
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 2556 VPDpfaaeggRLYRTGDLVRLCDNGQVEYVGRIDHQVKIR-GFRIELGEIEARLLEHPQVREALVLA 2621
Cdd:cd17639  356 DGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
24-550 3.44e-14

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 79.17  E-value: 3.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    24 ERLALRFLAEDDGEGvvLSYRDLD---------LRARSIAAalqahaqlGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP- 93
Cdd:PRK04319   59 DKVALRYLDASRKEK--YTYKELKelsnkfanvLKELGVEK--------GDRVFIFMPRIPELYFALLGALKNGAIVGPl 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    94 --AYPPESARrhhqERLlsiiADAEPRLVLTTADLREpllqmnaQLSAANAPQL---LCVDQ----------LDPAVAEA 158
Cdd:PRK04319  129 feAFMEEAVR----DRL----EDSEAKVLITTPALLE-------RKPADDLPSLkhvLLVGEdveegpgtldFNALMEQA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   159 WDE---PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIvsWLPLyhDMGLIGGLLQPIFS-- 233
Cdd:PRK04319  194 SDEfdiEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDVY--WCTA--DPGWVTGTSYGIFApw 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   234 --GVPCVLMSPRYfleRPVRWLEAISQYGGTVSGGPDFAYRLCSeRVAESALQRLDLSGWRVAFSGSEPIRQDSLeRFAE 311
Cdd:PRK04319  270 lnGATNVIDGGRF---SPERWYRILEDYKVTVWYTAPTAIRMLM-GAGDDLVKKYDLSSLRHILSVGEPLNPEVV-RWGM 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   312 KFAASRFDASsffacYGLAEatlfvTGGQRGQGIPALAVDgealarnriaegEGSvlMccGRSQPEHAVLIVDAAsGEVL 391
Cdd:PRK04319  345 KVFGLPIHDN-----WWMTE-----TGGIMIANYPAMDIK------------PGS--M--GKPLPGIEAAIVDDQ-GNEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   392 GDDNVGEI-----WaagPSIAHGYWRNPEASAKAFVerDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDI 465
Cdd:PRK04319  398 PPNRMGNLaikkgW---PSMMRGIWNNPEKYESYFA--GD--WYVSGDSAYMdEDGYFWFQGRVDDVIKTSGERVGPFEV 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   466 E-RTVE----SEV-----PSARKG-RVAAFAVTVDGEEgigiaaeigrgvqksvPAQELIDSIRQAVAE--AYQEAPKVV 532
Cdd:PRK04319  471 EsKLMEhpavAEAgvigkPDPVRGeIIKAFVALRPGYE----------------PSEELKEEIRGFVKKglGAHAAPREI 534
                         570
                  ....*....|....*...
gi 15597620   533 ALLNpgALPKTSSGKLQR 550
Cdd:PRK04319  535 EFKD--KLPKTRSGKIMR 550
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
23-554 3.63e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 78.90  E-value: 3.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    23 PERLALrFLAEddgEGVVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAG--VIAVPAY--PP 97
Cdd:PRK13390   11 PDRPAV-IVAE---TGEQVSYRQLDDDSAALARVLYDAgLRTGDVVALLSDNSPEALVVLWAALRSGlyITAINHHltAP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    98 ESArrhhqerllSIIADAEPRLVLTTADLREPLLQMNA--QLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHiAFLQYT 175
Cdd:PRK13390   87 EAD---------YIVGDSGARVLVASAALDGLAAKVGAdlPLRLSFGGEIDGFGSFEAALAGAGPRLTEQPCG-AVMLYS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   176 SGSTALPKGVQVSHGNLVANE-----VLIRRG-FGIGADDVIVSWLPLYHdmgliggllqpifsgvpcvlmspryflERP 249
Cdd:PRK13390  157 SGTTGFPKGIQPDLPGRDVDApgdpiVAIARAfYDISESDIYYSSAPIYH---------------------------AAP 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   250 VRWLEAISQYGGTVSGGPDF----------AYRLCSERVAESALQRL-----------DLSGWRVAFSGSEPIRQDSLER 308
Cdd:PRK13390  210 LRWCSMVHALGGTVVLAKRFdaqatlghveRYRITVTQMVPTMFVRLlkldadvrtryDVSSLRAVIHAAAPCPVDVKHA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   309 FAEKFAASRFDASSFFACYGLAeatlFVTGGQ--RGQGipalAVDGEALARNRIAEGEGSvlmccgrsqpehavlivDAA 386
Cdd:PRK13390  290 MIDWLGPIVYEYYSSTEAHGMT----FIDSPDwlAHPG----SVGRSVLGDLHICDDDGN-----------------ELP 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   387 SGEVlgddnvGEIWAAGPSIAHGYWRNPEASAKAfvERDGRT-WLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQD 464
Cdd:PRK13390  345 AGRI------GTVYFERDRLPFRYLNDPEKTAAA--QHPAHPfWTTVGDLGSVdEDGYLYLADRKSFMIISGGVNIYPQE 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   465 IERTVESEvPSARKgrVAAFAVTvDGEEGIGIAA--EIGRGVQKSVP-AQELIDSIRQAVaeAYQEAPKVVALLNpgALP 541
Cdd:PRK13390  417 TENALTMH-PAVHD--VAVIGVP-DPEMGEQVKAviQLVEGIRGSDElARELIDYTRSRI--AHYKAPRSVEFVD--ELP 488
                         570
                  ....*....|...
gi 15597620   542 KTSSGKLQRSACR 554
Cdd:PRK13390  489 RTPTGKLVKGLLR 501
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
1157-1637 3.93e-14

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 78.92  E-value: 3.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1157 AELHARAnRLAHYLRDKGVGPDVRVAIcaERSPQLLVGLLAIVKAGGAYVPLDPdypSERLAYMLAD---SGVELLLTQA 1233
Cdd:PRK13388   34 AEAAARA-AALIALADPDRPLHVGVLL--GNTPEMLFWLAAAALGGYVLVGLNT---TRRGAALAADirrADCQLLVTDA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1234 HLFERLPGAE--GVTPICLDSlkldnwPSQAPGLHLHG----------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQW 1301
Cdd:PRK13388  108 EHRPLLDGLDlpGVRVLDVDT------PAYAELVAAAGaltphrevdaMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1302 MQATYTLDGDDVLMQKAPVSFDVSVWECFWP-LVTGCRLVLAApgeHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPG 1380
Cdd:PRK13388  182 LTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPA---KFSASGFLDDVRRYGATYFNYVGKPLAYILATPE 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1381 VA--ACGSLRRLFsGGEALP---AELRNRVlqrlpAVALHNRYGPTETAINVThwqcRAEDGERSPIGRPLGNVV----- 1450
Cdd:PRK13388  259 RPddADNPLRVAF-GNEASPrdiAEFSRRF-----GCQVEDGYGSSEGAVIVV----REPGTPPGSIGRGAPGVAiynpe 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1451 ----CRV--LDAEFNLL-PAGVAGELC-IGGLGLARGYLGRPALSAERFvadpfsAAGerLYRTGDRARWNADGVLEYLG 1522
Cdd:PRK13388  329 tlteCAVarFDAHGALLnADEAIGELVnTAGAGFFEGYYNNPEATAERM------RHG--MYWSGDLAYRDADGWIYFAG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1523 RLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVV-VIREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAAlQAELPEYMVPT 1601
Cdd:PRK13388  401 RTADWMRVDGENLSAAPIERILLRHPAINRVAVyAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAA-QPDLGTKAWPR 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 15597620  1602 QLMRLAQMPLGPSGKLDTRAL---------PEPVWQQREHVEPRT 1637
Cdd:PRK13388  480 YVRIAADLPSTATNKVLKRELiaqgwatgdPVTLWVRRGGPAYRL 524
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3716-4230 4.37e-14

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 78.91  E-value: 4.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3716 VRLFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:PRK07059   26 ADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3796 GHPTQRLTR---------IVEL---SRTL--VLVCTQACREQALALFDELG--------CVDRPRLLV--W--------- 3842
Cdd:PRK07059  106 LYTPRELEHqlkdsgaeaIVVLenfATTVqqVLAKTAVKHVVVASMGDLLGfkghivnfVVRRVKKMVpaWslpghvrfn 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3843 DEIQQGEGAEHDPqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLskvpyleldENDVIAQTASQSF-DISVWQF 3921
Cdd:PRK07059  186 DALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL---------QMEAWLQPAFEKKpRPDQLNF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3922 LAA-PLF---------------GARVAIVPNAvaHDPQGLLAHVGEQGITVLESVPSLIQGML-AEERQALD--GLRWML 3982
Cdd:PRK07059  256 VCAlPLYhifaltvcgllgmrtGGRNILIPNP--RDIPGFIKELKKYQVHIFPAVNTLYNALLnNPDFDKLDfsKLIVAN 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3983 PTGEAMPPELARQWLKRyPRIGLVNAYGPAECSDDVAFFRVDLAS-TESTYLPIGSPTDNNRlyllgagaDDAFELVPLG 4061
Cdd:PRK07059  334 GGGMAVQRPVAERWLEM-TGCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIR--------DDDGNDLPLG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4062 AVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARL 4141
Cdd:PRK07059  405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4142 HERADVRE-AAVAVQEGANGKYLVGYLV---PGETPrssadspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRM 4217
Cdd:PRK07059  478 ASHPGVLEvAAVGVPDEHSGEAVKLFVVkkdPALTE------------------EDVKAFCKERLTNYKRPKFVEFRTEL 539
                         570
                  ....*....|...
gi 15597620  4218 PLNANGKLDRKAL 4230
Cdd:PRK07059  540 PKTNVGKILRREL 552
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
80-556 4.40e-14

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 78.59  E-value: 4.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    80 AFFGCLYAgVIAVPAYPPESARRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQ----LSAANAPQLLCVDQLDPAV 155
Cdd:PRK12406   48 AFFEAAYA-AMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALPAgvtvLSVPTPPEIAAAYRISPAL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   156 A----------------EAWDEPQVrpEHIAFLQYTSGSTALPKGVQVSHGN---LVANEVLIRRGFGIGADDVIVSWLP 216
Cdd:PRK12406  127 LtppagaidwegwlaqqEPYDGPPV--PQPQSMIYTSGTTGHPKGVRRAAPTpeqAAAAEQMRALIYGLKPGIRALLTGP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   217 LYHDMGLIGGLLQPIFSGVpCVLMsPRYfleRPVRWLEAISQYG-GTVSGGPDFAYRLCseRVAESALQRLDLSGWRVAF 295
Cdd:PRK12406  205 LYHSAPNAYGLRAGRLGGV-LVLQ-PRF---DPEELLQLIERHRiTHMHMVPTMFIRLL--KLPEEVRAKYDVSSLRHVI 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   296 SGSEPIRQDSlerfaeKFAASRFDASSFFACYGLAEAtlfvtggqrgqGIPALAVDGEALARnriaegEGSVlmccGRSQ 375
Cdd:PRK12406  278 HAAAPCPADV------KRAMIEWWGPVIYEYYGSTES-----------GAVTFATSEDALSH------PGTV----GKAA 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   376 PEHAVLIVDAaSGEVLGDDNVGEIWAAGPSIAH-GYWRNPEASAKafVERDGrtWLRTGDLGFL-RDGELFVTGRLKDML 453
Cdd:PRK12406  331 PGAELRFVDE-DGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--IDRGG--FITSGDVGYLdADGYLFLCDRKRDMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   454 IVRGHNLYPQDIErTVESEVPSARKgrVAAFavtvdgeegiGIA-AEIGRGVQKSVPAQELI----DSIRQAVAE--AYQ 526
Cdd:PRK12406  406 ISGGVNIYPAEIE-AVLHAVPGVHD--CAVF----------GIPdAEFGEALMAVVEPQPGAtldeADIRAQLKArlAGY 472
                         490       500       510
                  ....*....|....*....|....*....|
gi 15597620   527 EAPKVVALLNpgALPKTSSGKLQRSacRLR 556
Cdd:PRK12406  473 KVPKHIEIMA--ELPREDSGKIFKR--RLR 498
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
1275-1556 4.70e-14

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 76.57  E-value: 4.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1275 VIYTSGSTGQPKGVGNTHAAL---AERLQWMQAtytLDGDDVLMQKAPVsFDVSVWECFWP-LVTGCRLVLAApgeHRDP 1350
Cdd:cd17636    5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtFHAGGTNVFVR---RVDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1351 ARLVELVRQFGVTtLHFVPPLLQLFIDEPGVAACGSLRRLFSGgeALPAELRNRVLQRLPAVALHNR-YGPTE-TAINVT 1428
Cdd:cd17636   78 EEVLELIEAERCT-HAFLLPPTIDQIVELNADGLYDLSSLRSS--PAAPEWNDMATVDTSPWGRKPGgYGQTEvMGLATF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1429 HWQCRaedGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVAdpfsaageRLYRTGD 1508
Cdd:cd17636  155 AALGG---GAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--------GWHHTND 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 1509 RARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVV 1556
Cdd:cd17636  224 LGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3717-4232 4.71e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 78.11  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3717 RLFEAQVAAHPQRIAASCLEQR-WSYAELNRRANRLGHALRAAGvgidqPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:PRK07787    3 SLNPAAVAAAADIADAVRIGGRvLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3796 GHPTQRLTRIVELSR-TLVLVCTQAcreqalalfdelGCVDRPRLLVwDEIQQGEGAEHDPqvysGPQNLAYVIYTSGST 3874
Cdd:PRK07787   78 DSGVAERRHILADSGaQAWLGPAPD------------DPAGLPHVPV-RLHARSWHRYPEP----DPDAPALIVYTSGTT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3875 GLPKGVMVEQAGMLNNQlskvpyleldenDVIAQTasqsfdisvWQFLAA-------PLFGARVAI--------VPNAVA 3939
Cdd:PRK07787  141 GPPKGVVLSRRAIAADL------------DALAEA---------WQWTADdvlvhglPLFHVHGLVlgvlgplrIGNRFV 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3940 H----DPQGLlAHVGEQGITVLESVPSLIQGMLA--EERQALDGLRwMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAE 4013
Cdd:PRK07787  200 HtgrpTPEAY-AQALSEGGTLYFGVPTVWSRIAAdpEAARALRGAR-LLVSGSAALPVPVFDRLAALTGHRPVERYGMTE 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4014 CSDDVAFfRVDLASTESTylpIGSPTDNNRLYLLgagaDDAFELVPLG--AVGELCVAGTGVGRGYVGDPLRTAQAFVPH 4091
Cdd:PRK07787  278 TLITLST-RADGERRPGW---VGLPLAGVETRLV----DEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTAD 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4092 PFgapgerlYRTGDLARRRADGVLEYVGR--IDhQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLV 4168
Cdd:PRK07787  350 GW-------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVvGVPDDDLGQRIVAYVV 421
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  4169 PGETPrsSADSPAGLMVEQGAWFERiKQQLRadlpdymvplhwlVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK07787  422 GADDV--AADELIDFVAQQLSVHKR-PREVR-------------FVDALPRNAMGKVLKKQLLS 469
PLN02736 PLN02736
long-chain acyl-CoA synthetase
165-466 4.74e-14

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 78.99  E-value: 4.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   165 RPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHD-------MGLIGGLLQPIFSGVPC 237
Cdd:PLN02736  219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIyervnqiVMLHYGVAVGFYQGDNL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   238 VLMS------PRYFLERPVRWLEAISQYGGTV-SGGP------DFAYR-----LCSERVAESALQRLDLS------GWRV 293
Cdd:PLN02736  299 KLMDdlaalrPTIFCSVPRLYNRIYDGITNAVkESGGlkerlfNAAYNakkqaLENGKNPSPMWDRLVFNkikaklGGRV 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   294 AF--SGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVTGGQRGqgipalavdgealarNRIAEGEGSVLMCC 371
Cdd:PLN02736  379 RFmsSGASPLSPDVMEFLRICFGGRVLEG------YGMTETSCVISGMDEG---------------DNLSGHVGSPNPAC 437
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   372 grsqpehAVLIVDAASGEVLGDDNV---GEIWAAGPSIAHGYWRNpEASAKAFVERDGrtWLRTGDLG-FLRDGELFVTG 447
Cdd:PLN02736  438 -------EVKLVDVPEMNYTSEDQPyprGEICVRGPIIFKGYYKD-EVQTREVIDEDG--WLHTGDIGlWLPGGRLKIID 507
                         330       340
                  ....*....|....*....|
gi 15597620   448 RLKDML-IVRGHNLYPQDIE 466
Cdd:PLN02736  508 RKKNIFkLAQGEYIAPEKIE 527
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
1423-1711 5.14e-14

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 75.94  E-value: 5.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1423 TAINVTHWQCRAEDGERSPIGRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFSAAGER 1502
Cdd:COG3433    1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1503 LYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAGSQLVGYYTGAVGAEAEAEq 1582
Cdd:COG3433   81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAA- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1583 nqrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHVEP-------RTELQRRIAAIWSEVLGLP- 1654
Cdd:COG3433  160 ---AALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAAspapaleTALTEEELRADVAELLGVDp 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 1655 -RVGLRDDFFELGGHSLLATRIVSRTRQAcDVELPLRALFEASELEAFCEQVRAAQAA 1711
Cdd:COG3433  237 eEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAA 293
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
15-550 7.21e-14

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 77.72  E-value: 7.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   15 LRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAA-LQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
Cdd:cd12118   10 LERAAAVYPDRTSIVY------GDRRYTWRQTYDRCRRLASAlAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   94 AyppesARRHHQERLLSIIADAEPRLVLTTADLR-EPLLQMNaqlsaanapqllcvdqlDPAvaEAWDEPQVRPEHIAfL 172
Cdd:cd12118   84 L-----NTRLDAEEIAFILRHSEAKVLFVDREFEyEDLLAEG-----------------DPD--FEWIPPADEWDPIA-L 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  173 QYTSGSTALPKGVQVSHgnlvanevlirRGFGIGADDVIVSW-----------LPLYHDMGLIGGLLQPIFSGVPCVLMS 241
Cdd:cd12118  139 NYTSGTTGRPKGVVYHH-----------RGAYLNALANILEWemkqhpvylwtLPMFHCNGWCFPWTVAAVGGTNVCLRK 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  242 PRYflerPVRWlEAISQYGGT-VSGGPDFAYRLCSERvaESALQRLDlsgWRVAF--SGSEPIrqdslERFAEKFAASRF 318
Cdd:cd12118  208 VDA----KAIY-DLIEKHKVThFCGAPTVLNMLANAP--PSDARPLP---HRVHVmtAGAPPP-----AAVLAKMEELGF 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  319 DASSffaCYGLAEATLFVTGGQRGQGIPALAVDGEALARNRiaEGEGSVLMccgrsqpeHAVLIVDAASGE-VLGD-DNV 396
Cdd:cd12118  273 DVTH---VYGLTETYGPATVCAWKPEWDELPTEERARLKAR--QGVRYVGL--------EEVDVLDPETMKpVPRDgKTI 339
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  397 GEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIERT------- 468
Cdd:cd12118  340 GEIVFRGNIVMKGYLKNPEATAEAF--RGG--WFHSGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEVEGVlykhpav 415
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  469 VESEV---PSARKGRVA-AFAVTVDGeegigiaaeigrgvqKSVPAQELIDSIRQAVAeAYqEAPKVVALlnpGALPKTS 544
Cdd:cd12118  416 LEAAVvarPDEKWGEVPcAFVELKEG---------------AKVTEEEIIAFCREHLA-GF-MVPKTVVF---GELPKTS 475

                 ....*.
gi 15597620  545 SGKLQR 550
Cdd:cd12118  476 TGKIQK 481
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
1270-1553 8.75e-14

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 77.55  E-value: 8.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1270 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPvSFDVSVWEC--FWPLVTGCRLVLAApgEH 1347
Cdd:PRK06334  183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAYGFNSctLFPLLSGVPVVFAY--NP 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1348 RDPARLVELVRQFGVTTLHFVPPLLQLFID--EPGVAACGSLRRLFSGGEALPAELRNRVLQRLPAVALHNRYGPTETAI 1425
Cdd:PRK06334  260 LYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSP 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1426 NVThwqcraEDGERSP-----IGRPLGNVVCRVLDAEFNL-LPAGVAGELCIGGLGLARGYLGrpALSAERFVadpfSAA 1499
Cdd:PRK06334  340 VIT------INTVNSPkhescVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLG--EDFGQGFV----ELG 407
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620  1500 GERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQA 1553
Cdd:PRK06334  408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA 461
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
74-681 9.83e-14

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 78.57  E-value: 9.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     74 GPDYVAAFFGCLYAG----VIAvPAYPPesARrhhQERLLSIiadAEPR--LVLTTA---------------DLRE--PL 130
Cdd:TIGR03443  305 GVDLVVAVMGVLKAGatfsVID-PAYPP--AR---QTIYLSV---AKPRalIVIEKAgtldqlvrdyidkelELRTeiPA 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    131 LQMNAQLS-AANAPQLLCVDQLDPAVAEAwDEPQ---VRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIG 206
Cdd:TIGR03443  376 LALQDDGSlVGGSLEGGETDVLAPYQALK-DTPTgvvVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLS 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    207 ADD--VIVSWL---PLYHDMgligglLQPIFSGVPcVLMSPRYFLERPVRWLEAISQYGGTVSGgpdfayrlcservAES 281
Cdd:TIGR03443  455 ENDkfTMLSGIahdPIQRDM------FTPLFLGAQ-LLVPTADDIGTPGRLAEWMAKYGATVTH-------------LTP 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    282 ALQRLdLSGWRVA---------FSGSEPIRQD--SLERFAEKFaasrfdasSFFACYGLAEAtlfvtggQRGQG---IPA 347
Cdd:TIGR03443  515 AMGQL-LSAQATTpipslhhafFVGDILTKRDclRLQTLAENV--------CIVNMYGTTET-------QRAVSyfeIPS 578
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    348 LAVDGEALARNRIaegegsvLMCCGRSQPEHAVLIVD-------AASGEVlgddnvGEIWAAGPSIAHGYWRNPEASAKA 420
Cdd:TIGR03443  579 RSSDSTFLKNLKD-------VMPAGKGMKNVQLLVVNrndrtqtCGVGEV------GEIYVRAGGLAEGYLGLPELNAEK 645
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    421 FV-----------ERDGRT-------WL-------RTGDLG-FLRDGELFVTGRLKDMLIVRG--------------HNL 460
Cdd:TIGR03443  646 FVnnwfvdpshwiDLDKENnkperefWLgprdrlyRTGDLGrYLPDGNVECCGRADDQVKIRGfrielgeidthlsqHPL 725
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    461 YPQDI---------ERTVESE-VPSARKGRVAAFAVTVDGEEGIGIaaeIGRGVQKSvpaQELIDSIRQAVAE--AYQEA 528
Cdd:TIGR03443  726 VRENVtlvrrdkdeEPTLVSYiVPQDKSDELEEFKSEVDDEESSDP---VVKGLIKY---RKLIKDIREYLKKklPSYAI 799
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    529 PKVVALLNpgALPKTSSGKLQRSAcrLRLEDGSLdsyalfpgLQAVQEAQPPAGDDELL----ARIGEIWkarLGV---- 600
Cdd:TIGR03443  800 PTVIVPLK--KLPLNPNGKVDKPA--LPFPDTAQ--------LAAVAKNRSASAADEEFteteREIRDLW---LELlpnr 864
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    601 -AQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFEAPTLQAFSATVAR-----QLAAGLPAEAPMAHLPRGVD 674
Cdd:TIGR03443  865 pATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRlkkgeELADEGDSEIEEEETVLELD 944

                   ....*..
gi 15597620    675 LPQSAAQ 681
Cdd:TIGR03443  945 YAKDAKT 951
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3861-4235 1.05e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 75.98  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3861 PQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAqTASQSFDI--SVWQFLAAPLFGARVAIVPNAV 3938
Cdd:cd05944    1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLL-CGLPLFHVngSVVTLLTPLASGAHVVLAGPAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3939 AHDP---QGLLAHVGEQGITVLESVPSLIQGMLAEERQA-LDGLRWMLPTGEAMPPELARQWLKRyPRIGLVNAYGPAEC 4014
Cdd:cd05944   80 YRNPglfDNFWKLVERYRITSLSTVPTVYAALLQVPVNAdISSLRFAMSGAAPLPVELRARFEDA-TGLPVVEGYGLTEA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4015 SDDVAffrvdlASTESTYLPIGS-----PTDNNRLYLLGAGADDAFELVPlGAVGELCVAGTGVGRGYVgDPLRTAQAFV 4089
Cdd:cd05944  159 TCLVA------VNPPDGPKRPGSvglrlPYARVRIKVLDGVGRLLRDCAP-DEVGEICVAGPGVFGGYL-YTEGNKNAFV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4090 phpfgapGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGAN-GKYLVGY-- 4166
Cdd:cd05944  231 -------ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHaGELPVAYvq 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 4167 LVPGETprssadspaglmVEQGAWFERIKQQL--RAdlpdyMVPLHWLVLDRMPLNANGKLDRKALPALDI 4235
Cdd:cd05944  304 LKPGAV------------VEEEELLAWARDHVpeRA-----AVPKHIEVLEELPVTAVGKVFKPALRADAI 357
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
3709-4230 1.10e-13

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 77.18  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3709 YPLEQGYVR--LFEA--QVAAHPQRIA--ASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVG 3782
Cdd:cd17642    9 YPLEDGTAGeqLHKAmkRYASVPGTIAftDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3783 SFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQACREQALALFDELGCVDRprLLVWDEIQQGEG--------AEHD 3854
Cdd:cd17642   89 GLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKT--IIILDSKEDYKGyqclytfiTQNL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3855 P---QVYS-------GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNN-QLSKVPYLEldeNDVIAQTASqsfdISVWQF-- 3921
Cdd:cd17642  167 PpgfNEYDfkppsfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARfSHARDPIFG---NQIIPDTAI----LTVIPFhh 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3922 -------LAAPLFGARVAIVPNavaHDPQGLLAHVGEQGITVLESVPSLIqGMLAE----ERQALDGLRWMLPTGEAMPP 3990
Cdd:cd17642  240 gfgmfttLGYLICGFRVVLMYK---FEEELFLRSLQDYKVQSALLVPTLF-AFFAKstlvDKYDLSNLHEIASGGAPLSK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3991 ELARQWLKRYPRIGLVNAYGpaecsddvaffrvdlaSTESTYLPIGSPTDNNRLYLLGagaddafELVPLGAV------- 4063
Cdd:cd17642  316 EVGEAVAKRFKLPGIRQGYG----------------LTETTSAILITPEGDDKPGAVG-------KVVPFFYAkvvdldt 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4064 ---------GELCVAGTGVGRGYVGDPLRTAQAFVPhpfgapgERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIEL 4134
Cdd:cd17642  373 gktlgpnerGELCVKGPMIMKGYVNNPEATKALIDK-------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPP 445
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4135 GEIEARLHERADVREAAVA--VQEGAngkylvgylvpGETPrssadsPAGLMVEQGAWF-ERIKQQLRAdlpDYMVPLHW 4211
Cdd:cd17642  446 AELESILLQHPKIFDAGVAgiPDEDA-----------GELP------AAVVVLEAGKTMtEKEVMDYVA---SQVSTAKR 505
                        570       580
                 ....*....|....*....|....
gi 15597620 4212 L-----VLDRMPLNANGKLDRKAL 4230
Cdd:cd17642  506 LrggvkFVDEVPKGLTGKIDRRKI 529
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
2212-2596 1.10e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 77.85  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2212 LSYAELDARSN----RLARVLRshgvgPEVRVGLALERSLEMVVGLLAILKAGGAYVPL-DPEYP--LERLQYMIEDSGV 2284
Cdd:PRK07769   56 LTWSQFGARNRavgaRLQQVTK-----PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTP 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2285 RLLLSHAALFEALGELPAGVARwcleEDGP---ALDAEDPAPLAALSGPQHQ----AYLIYTSGSTGKPKGVAVSHGEIA 2357
Cdd:PRK07769  131 SAILTTTDSAEGVRKFFRARPA----KERPrviAVDAVPDEVGATWVPPEANedtiAYLQYTSGSTRIPAGVQITHLNLP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2358 MHCAAVIECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVL-------RAQGQWgaeeICELIRAEGVSILGFT-- 2428
Cdd:PRK07769  207 TNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFmspaafvRRPGRW----IRELARKPGGTGGTFSaa 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2429 PSYGSQLAqwlesQGRQLP-----------VRMCITGGEALTGEHLQRIRQAFAPasffnaYGPTETVVMPLACLA---- 2493
Cdd:PRK07769  283 PNFAFEHA-----AARGLPkdgeppldlsnVKGLLNGSEPVSPASMRKFNEAFAP------YGLPPTAIKPSYGMAeatl 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2494 -----------------------------PERLEEGAASVPIGSVVGARVAYILDADLAL-VPQGATGELYVGGAGLARG 2543
Cdd:PRK07769  352 fvsttpmdeeptviyvdrdelnagrfvevPADAPNAVAQVSAGKVGVSEWAVIVDPETASeLPDGQIGEIWLHGNNIGTG 431
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  2544 YHERPALSAERF-------VPDPFA---AEGGRLYRTGDLVRLCDnGQVEYVGRIDHQVKIRG 2596
Cdd:PRK07769  432 YWGKPEETAATFqnilksrLSESHAegaPDDALWVRTGDYGVYFD-GELYITGRVKDLVIIDG 493
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
1149-1600 1.11e-13

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 77.52  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1149 WDGGS---LGYAELHARANRLAHYLRDK-GVGPDVRVAI----CAERspqlLVGLLAIVKAGGAYVPLDPDYPSERLAYM 1220
Cdd:PRK05620   31 WGGAEqeqTTFAAIGARAAALAHALHDElGITGDQRVGSmmynCAEH----LEVLFAVACMGAVFNPLNKQLMNDQIVHI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1221 LADSGVELLLTQAHLFERL-------PGAEGVTPICLDSLK------------------LDNWPSQAPGLHLHGDNLAYV 1275
Cdd:PRK05620  107 INHAEDEVIVADPRLAEQLgeilkecPCVRAVVFIGPSDADsaaahmpegikvysyealLDGRSTVYDWPELDETTAAAI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1276 IYTSGSTGQPKGVGNTHAALaerlqWMQATyTLDGDDVLMQKAPVSF--DVSVWECF-W--PL---VTGCRLVLaaPGEH 1347
Cdd:PRK05620  187 CYSTGTTGAPKGVVYSHRSL-----YLQSL-SLRTTDSLAVTHGESFlcCVPIYHVLsWgvPLaafMSGTPLVF--PGPD 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1348 RDPARLVELVRQFGVTTLHFVPPL-LQLFI----DEPGVAacgSLRRLFSGGEALPAELRNrvlqrlpavALHNRYGpte 1422
Cdd:PRK05620  259 LSAPTLAKIIATAMPRVAHGVPTLwIQLMVhylkNPPERM---SLQEIYVGGSAVPPILIK---------AWEERYG--- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1423 taINVTH-WQCRaedgERSPIG---RPLGNV------VCRVLDAEFnllPAGV-----------------AGELCIGGLG 1475
Cdd:PRK05620  324 --VDVVHvWGMT----ETSPVGtvaRPPSGVsgearwAYRVSQGRF---PASLeyrivndgqvmestdrnEGEIQVRGNW 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1476 LARGYLGRPA----LSAERFVADPFSAAGERL-----YRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLA 1546
Cdd:PRK05620  395 VTASYYHSPTeeggGAASTFRGEDVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMA 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  1547 QPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVP 1600
Cdd:PRK05620  475 APEVVECAVIgYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLP 529
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
41-552 1.37e-13

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 76.74  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   41 LSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVP---AYPpesarrhhQERLLSIIADAE 116
Cdd:cd17650   13 LTYRELNERANQLARTLRGLGVAPGSVVgVCADRSLDAIVGLLAVLKAGGAYVPidpDYP--------AERLQYMLEDSG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  117 PRLVLTtadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEHIAFLQYTSGSTALPKGVQVSHGNLVANE 196
Cdd:cd17650   85 AKLLLT------------------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAA 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  197 VLIRRGFGIGADDV-IVSWLPLYHDMgLIGGLLQPIFSG---VPCvlmsPRYFLERPVRWLEAISQYGGTVSggpDFAYR 272
Cdd:cd17650  123 HAWRREYELDSFPVrLLQMASFSFDV-FAGDFARSLLNGgtlVIC----PDEVKLDPAALYDLILKSRITLM---ESTPA 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  273 LCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDASSffacYGLAEATLFVTGGQRGQGipalavdg 352
Cdd:cd17650  195 LIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINS----YGVTEATIDSTYYEEGRD-------- 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  353 ealarnriaEGEGSVLMCCGRSQPEHAVLIVDAASGEV-LGddNVGEIWAAGPSIAHGYWRNPEASAKAFVER---DGRT 428
Cdd:cd17650  263 ---------PLGDSANVPIGRPLPNTAMYVLDERLQPQpVG--VAGELYIGGAGVARGYLNRPELTAERFVENpfaPGER 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  429 WLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIErTVESEVPSARKgrvAAFAVTVDGEEGIGIAAEIgrgvqks 507
Cdd:cd17650  332 MYRTGDLArWRADGNVELLGRVDHQVKIRGFRIELGEIE-SQLARHPAIDE---AVVAVREDKGGEARLCAYV------- 400
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620  508 VPAQEL-IDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSA 552
Cdd:cd17650  401 VAAATLnTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2703-2771 1.56e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 68.34  E-value: 1.56e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 2703 APRSVLEQQLAGVWREVLNV--ERVGLGDNFF-ELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQSLAA 2771
Cdd:COG0236    1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEeFGIELPDTELFEYPTVADLAD 73
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
1156-1555 1.58e-13

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 76.87  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGgayVPLDPDYPS---ERLAYMLADSGVELLLTq 1232
Cdd:cd17639    8 YAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYATlgeDALIHSLNETECSAIFT- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1233 ahlferlpgaegvtpicldslklDNWPsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAerlqwmQATYTLDG-- 1310
Cdd:cd17639   84 -----------------------DGKP----------DDLACIMYTSGSTGNPKGVMLTHGNLV------AGIAGLGDrv 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1311 ------DDVLMQKAPVS--FDVSVWECFwpLVTGCRLVLAAP---------GEHRD-----PARLV------ELVRQFGV 1362
Cdd:cd17639  125 pellgpDDRYLAYLPLAhiFELAAENVC--LYRGGTIGYGSPrtltdkskrGCKGDltefkPTLMVgvpaiwDTIRKGVL 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1363 TTLHFVPPLL-QLF----------IDE-PGVAAC-------------GSLRRLFSGGEALPAELrnrvlQRLPAVALH-- 1415
Cdd:cd17639  203 AKLNPMGGLKrTLFwtayqsklkaLKEgPGTPLLdelvfkkvraalgGRLRYMLSGGAPLSADT-----QEFLNIVLCpv 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1416 -NRYGPTETAIN--VTHWqcraEDGERSPIGRPLGNVVCRVLDAE------FNLLPAGvagELCIGGLGLARGYLGRPAL 1486
Cdd:cd17639  278 iQGYGLTETCAGgtVQDP----GDLETGRVGPPLPCCEIKLVDWEeggystDKPPPRG---EILIRGPNVFKGYYKNPEK 350
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1487 SAERFvadpfsaAGERLYRTGDRARWNADGVLEYLGRLDQQVKLR-GFRIEPEEIQARLLAQPGVAQAVV 1555
Cdd:cd17639  351 TKEAF-------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICV 413
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
3740-4232 1.64e-13

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 77.38  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPG-HPTQRLTRIVELSRTLVLVCTQ 3818
Cdd:PRK06060   32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPElHRDDHALAARNTEPALVVTSDA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3819 ACREqalalFDELGCVDRPRLLvwDEIQQGEGAEHDPqvySGPQNLAYVIYTSGSTGLPKGVMVEQA-------GMLNNQ 3891
Cdd:PRK06060  112 LRDR-----FQPSRVAEAAELM--SEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHAdpltfvdAMCRKA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3892 LSKVPyleldeNDVIAQTASQSFDI----SVWQFLAAplfGARVAIVPNAVAHDPQGLLAHVGEQgiTVLESVPSLIQGM 3967
Cdd:PRK06060  182 LRLTP------EDTGLCSARMYFAYglgnSVWFPLAT---GGSAVINSAPVTPEAAAILSARFGP--SVLYGVPNFFARV 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3968 L-AEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAEC-----SDDVAFFRVdlaSTESTYLPigsPTDN 4041
Cdd:PRK06060  251 IdSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVgqtfvSNRVDEWRL---GTLGRVLP---PYEI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4042 NRLYLLGAGADDAFElvplgavGELCVAGTGVGRGYVG--DPLRTAQAFVphpfgapgerlyRTGDLARRRADGVLEYVG 4119
Cdd:PRK06060  325 RVVAPDGTTAGPGVE-------GDLWVRGPAIAKGYWNrpDSPVANEGWL------------DTRDRVCIDSDGWVTYRC 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4120 RIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGetprssadSPAGLmveQGAWFERIKQQL 4198
Cdd:PRK06060  386 RADDTEVIGGVNVDPREVERLIIEDEAVAEAAVvAVRESTGASTLQAFLVAT--------SGATI---DGSVMRDLHRGL 454
                         490       500       510
                  ....*....|....*....|....*....|....
gi 15597620  4199 RADLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK06060  455 LNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
2335-2686 2.24e-13

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 74.36  E-value: 2.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2335 YLIYTSGSTGKPKGVAvshgeiamhcaaviecfgmRAEDCELHFYSINFD----AASERLLAP---------------LL 2395
Cdd:cd17633    4 YIGFTSGTTGLPKAYY-------------------RSERSWIESFVCNEDlfniSGEDAILAPgplshslflygaisaLY 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2396 CGARVVLraQGQWGAEEICELIRAEGVSILGFTPSygsQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFAPASF 2475
Cdd:cd17633   65 LGGTFIG--QRKFNPKSWIRKINQYNATVIYLVPT---MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2476 FNAYGPTETVVmpLACLAPERLEE-GAASVPIGSVVgarvAYILDADlalvpQGATGELYVGGAGLARGYherpaLSAER 2554
Cdd:cd17633  140 IEFYGTSELSF--ITYNFNQESRPpNSVGRPFPNVE----IEIRNAD-----GGEIGKIFVKSEMVFSGY-----VRGGF 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2555 FVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAgyV 2634
Cdd:cd17633  204 SNPDGW-------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA--V 274
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15597620 2635 ASAVAEQdedaqaALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDR 2686
Cdd:cd17633  275 ALYSGDK------LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3737-4225 2.53e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 76.10  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDpghptQRLTR-----IVELSRT 3811
Cdd:PRK08276   10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPIN-----WHLTAaeiayIVDDSGA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3812 LVLVCTQACREQALALFDELGCVDRPRLLV---------WDEIQQGEGAEHDPQVYSGpqnlAYVIYTSGSTGLPKGVmv 3882
Cdd:PRK08276   85 KVLIVSAALADTAAELAAELPAGVPLLLVVagpvpgfrsYEEALAAQPDTPIADETAG----ADMLYSSGTTGRPKGI-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3883 eqagmlnnqlsKVPYLELDENDVIAQ-TASQSFDISVWQ----FLAAPLFGA---RVAIVPNAVAH--------DPQGLL 3946
Cdd:PRK08276  159 -----------KRPLPGLDPDEAPGMmLALLGFGMYGGPdsvyLSPAPLYHTaplRFGMSALALGGtvvvmekfDAEEAL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3947 AHVGEQGITVLESVPSLIQGMLA---EERQALD--GLRWMLPTGEAMPPELARQWLKRYPRIglVNAYgpaecsddvaff 4021
Cdd:PRK08276  228 ALIERYRVTHSQLVPTMFVRMLKlpeEVRARYDvsSLRVAIHAAAPCPVEVKRAMIDWWGPI--IHEY------------ 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4022 rvdLASTESTYLPIGSPTDnnrlYLLGAGA------------DDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFV 4089
Cdd:PRK08276  294 ---YASSEGGGVTVITSED----WLAHPGSvgkavlgevrilDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4090 PHpfgapgeRLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVP 4169
Cdd:PRK08276  367 PH-------GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV-----------FG--VP 426
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4170 ----GET------PRSSADSPAGLMVEQGAWferikqqLRADLPDYMVPLHWLVLDRMPLNANGKL 4225
Cdd:PRK08276  427 deemGERvkavvqPADGADAGDALAAELIAW-------LRGRLAHYKCPRSIDFEDELPRTPTGKL 485
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
3724-4108 2.60e-13

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 76.32  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3724 AAHPQRIaasCLEQR-----W---SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3795
Cdd:cd05921    6 RQAPDRT---WLAERegnggWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3796 -----GHPTQRLTRIVE-LSRTLVLVCTQACREQALALFDELG---------CVDRPRLLVWDEIQQGEGAEHDPQVYS- 3859
Cdd:cd05921   83 ayslmSQDLAKLKHLFElLKPGLVFAQDAAPFARALAAIFPLGtplvvsrnaVAGRGAISFAELAATPPTAAVDAAFAAv 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3860 GPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKvpyleLDENDVIAQTASQSFDISVWQFlaapLFGARVAIvpNAVA 3939
Cdd:cd05921  163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAML-----EQTYPFFGEEPPVLVDWLPWNH----TFGGNHNF--NLVL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3940 HD------------PQGL---LAHVGEQGITVLESVP----SLIQGMLAEE---RQALDGLRWMLPTGEAMPP------- 3990
Cdd:cd05921  232 YNggtlyiddgkpmPGGFeetLRNLREISPTVYFNVPagweMLVAALEKDEalrRRFFKRLKLMFYAGAGLSQdvwdrlq 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3991 ELARQWLKRypRIGLVNAYGPAECSdDVAFFRVDLASTESTylpIGSPTDNNRLyllgagaddafELVPLGAVGELCVAG 4070
Cdd:cd05921  312 ALAVATVGE--RIPMMAGLGATETA-PTATFTHWPTERSGL---IGLPAPGTEL-----------KLVPSGGKYEVRVKG 374
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597620 4071 TGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLAR 4108
Cdd:cd05921  375 PNVTPGYWRQPELTAQAFDEEGF-------YCLGDAAK 405
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
149-554 2.87e-13

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 75.88  E-value: 2.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  149 DQLDPAVAEAWDepqvrpehiafLQYTSGSTALPKGVQVSH-GNLVANEVLI--RRGFGIGADDVIVSWLPLYHDMGLIG 225
Cdd:cd05929  118 ETPIEDEAAGWK-----------MLYSGGTTGRPKGIKRGLpGGPPDNDTLMaaALGFGPGADSVYLSPAPLYHAAPFRW 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  226 GLLQpIFSGVPCVLMsPRYfleRPVRWLEAISQYGGT-VSGGPDFAYRLCseRVAESALQRLDLSGWRVAFSGSEP---- 300
Cdd:cd05929  187 SMTA-LFMGGTLVLM-EKF---DPEEFLRLIERYRVTfAQFVPTMFVRLL--KLPEAVRNAYDLSSLKRVIHAAAPcppw 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  301 IRQDSLERFAEKFaasrfdassfFACYGlaeatlfvtgGQRGQGIpaLAVDGEALARNRiaegeGSVlmccGRSQpEHAV 380
Cdd:cd05929  260 VKEQWIDWGGPII----------WEYYG----------GTEGQGL--TIINGEEWLTHP-----GSV----GRAV-LGKV 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  381 LIVDAAsGEVLGDDNVGEIWAAGPSiAHGYWRNPEASAKAfveRDGRTWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHN 459
Cdd:cd05929  308 HILDED-GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAA---RNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVN 382
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  460 LYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGeegigiaaeigrGVQKSVPAQELIDSIRQAVAEayQEA 528
Cdd:cd05929  383 IYPQEIENALIAHpkvldaavvgVPDEELGqRVHAVVQPAPG------------ADAGTALAEELIAFLRDRLSR--YKC 448
                        410       420
                 ....*....|....*....|....*.
gi 15597620  529 PKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05929  449 PRSIEFVA--ELPRDDTGKLYRRLLR 472
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3724-4224 3.09e-13

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 75.80  E-value: 3.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3724 AAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLT 3803
Cdd:cd12118   15 AVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3804 RIVELSRTLVLVCTQACR-EQALALFDElgcvdrprllvWDEIQQGEGaEHDPQVYSgpqnlayviYTSGSTGLPKGVMV 3882
Cdd:cd12118   95 FILRHSEAKVLFVDREFEyEDLLAEGDP-----------DFEWIPPAD-EWDPIALN---------YTSGTTGRPKGVVY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3883 EQAGMLNNQLSKVPYLELDENDVIAQTASQsFDISVWQFL-AAPLFGARVAIVPNAvahDPQGLLAHVGEQGITVLESVP 3961
Cdd:cd12118  154 HHRGAYLNALANILEWEMKQHPVYLWTLPM-FHCNGWCFPwTVAAVGGTNVCLRKV---DAKAIYDLIEKHKVTHFCGAP 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3962 ---SLIQGMLAEERQALDGLRWMLPTGEAMPPELarqwLKRYPRIG--LVNAYGPAECSDDVAffrVDLASTESTYLPig 4036
Cdd:cd12118  230 tvlNMLANAPPSDARPLPHRVHVMTAGAPPPAAV----LAKMEELGfdVTHVYGLTETYGPAT---VCAWKPEWDELP-- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4037 sPTDNNRL-------YLLGAGAD----DAFELVPLGA--VGELCVAGTGVGRGYVGDPLRTAQAFvphpfgAPGerLYRT 4103
Cdd:cd12118  301 -TEERARLkarqgvrYVGLEEVDvldpETMKPVPRDGktIGEIVFRGNIVMKGYLKNPEATAEAF------RGG--WFHS 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4104 GDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGylVP----GETPRssads 4179
Cdd:cd12118  372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV-----------VA--RPdekwGEVPC----- 433
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 4180 pAGLMVEQG--AWFERIKQQLRADLPDYMVPLHwLVLDRMPLNANGK 4224
Cdd:cd12118  434 -AFVELKEGakVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGK 478
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
3845-4230 3.47e-13

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 76.01  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3845 IQQGEGAEHDPqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSkvpyleldendVIAQTASQSFDisvwqflAA 3924
Cdd:PRK12492  191 LRQGRGLSLKP-VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQ-----------VRACLSQLGPD-------GQ 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3925 PLF--GARVAIVPNAVAH-------------------------DPQGLLAHVGEQGITVLESVPSLIQGMLAE-ERQALD 3976
Cdd:PRK12492  252 PLMkeGQEVMIAPLPLYHiyaftancmcmmvsgnhnvlitnprDIPGFIKELGKWRFSALLGLNTLFVALMDHpGFKDLD 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3977 --GLRWMLPTGEAMPPELARQWlKRYPRIGLVNAYGPAECSDDVAffrVDLASTESTYLPIGSPTDNNRLYLLGagaDDA 4054
Cdd:PRK12492  332 fsALKLTNSGGTALVKATAERW-EQLTGCTIVEGYGLTETSPVAS---TNPYGELARLGTVGIPVPGTALKVID---DDG 404
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4055 FELvPLGAVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIEL 4134
Cdd:PRK12492  405 NEL-PLGERGELCIKGPQVMKGYWQQPEATAEAL-------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYP 476
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4135 GEIEARLHERADVRE-AAVAVQEGANGKYLVGYLVPGEtprssadspAGLMVEQgawferIKQQLRADLPDYMVPLHWLV 4213
Cdd:PRK12492  477 NEIEDVVMAHPKVANcAAIGVPDERSGEAVKLFVVARD---------PGLSVEE------LKAYCKENFTGYKVPKHIVL 541
                         410
                  ....*....|....*..
gi 15597620  4214 LDRMPLNANGKLDRKAL 4230
Cdd:PRK12492  542 RDSLPMTPVGKILRREL 558
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
2213-2689 3.95e-13

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 75.58  E-value: 3.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2213 SYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHA 2291
Cdd:cd05928   43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2292 ALFEAL----GELPAGVARWCLEE---DG-----PALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMH 2359
Cdd:cd05928  123 ELAPEVdsvaSECPSLKTKLLVSEksrDGwlnfkELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLG 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2360 CAAVIECF-GMRAEDCelhFYSIN----FDAASERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQ 2434
Cdd:cd05928  203 LKVNGRYWlDLTASDI---MWNTSdtgwIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRM 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2435 LAQWLESQGRQLPVRMCITGGEALTGEHLQRIRqAFAPASFFNAYGPTETVvmpLACLAPERLEegaasVPIGSVVGARV 2514
Cdd:cd05928  280 LVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWK-AQTGLDIYEGYGQTETG---LICANFKGMK-----IKPGSMGKASP 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2515 AY---ILDADLALVPQGATGELYVggaglaRGYHERPALSAERFVPDP---FAAEGGRLYRTGDLVRLCDNGQVEYVGRI 2588
Cdd:cd05928  351 PYdvqIIDDNGNVLPPGTEGDIGI------RVKPIRPFGLFSGYVDNPektAATIRGDFYLTGDRGIMDEDGYFWFMGRA 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2589 DHQVKIRGFRIELGEIEARLLEHPQVRE-ALVLALDSPSGKQLAGYVASAVAEQDEDAQAALREaLKTHLKQQLPDYMVP 2667
Cdd:cd05928  425 DDVINSSGYRIGPFEVESALIEHPAVVEsAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKE-LQQHVKSVTAPYKYP 503
                        490       500
                 ....*....|....*....|..
gi 15597620 2668 AHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05928  504 RKVEFVQELPKTVTGKIQRNEL 525
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
3740-4230 4.12e-13

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 75.59  E-value: 4.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRLGHALRAA-GVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQ 3818
Cdd:PRK05620   40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3819 ACREQALALFDELGCVDRPRLLVWDEIQqgEGAEHDPQ----------------VYSGPQ----NLAYVIYTSGSTGLPK 3878
Cdd:PRK05620  120 RLAEQLGEILKECPCVRAVVFIGPSDAD--SAAAHMPEgikvysyealldgrstVYDWPEldetTAAAICYSTGTTGAPK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3879 GVMVEQAGMLNNQLSkvpyleLDENDVIAQTASQSFDISV-------WQF-LAAPLFGARVaIVPNAVAHDPQglLAHVG 3950
Cdd:PRK05620  198 GVVYSHRSLYLQSLS------LRTTDSLAVTHGESFLCCVpiyhvlsWGVpLAAFMSGTPL-VFPGPDLSAPT--LAKII 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3951 EQGIT-VLESVPSL-IQGMLAEERQALD--GLRWMLPTGEAMPPELARQWLKRYPrIGLVNAYGPAECSddvaffrvdlA 4026
Cdd:PRK05620  269 ATAMPrVAHGVPTLwIQLMVHYLKNPPErmSLQEIYVGGSAVPPILIKAWEERYG-VDVVHVWGMTETS----------P 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4027 STESTYLPIGSPTDNNRLYLLGAG---ADDAFELVPLGAV--------GELCVAGTGVGRGYVGDPLRT----AQAFVPH 4091
Cdd:PRK05620  338 VGTVARPPSGVSGEARWAYRVSQGrfpASLEYRIVNDGQVmestdrneGEIQVRGNWVTASYYHSPTEEgggaASTFRGE 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4092 PFGAPGERL-----YRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylVGY 4166
Cdd:PRK05620  418 DVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV-----------IGY 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  4167 LVP--GETPRSSADSPAGL-MVEQGAwfERIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK05620  487 PDDkwGERPLAVTVLAPGIePTRETA--ERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
9-550 4.13e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 75.42  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     9 TTLVQALRRRAVQEPERLALrflAEDDGegvVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYA 87
Cdd:PRK13383   35 TNPYTLLAVTAARWPGRTAI---IDDDG---ALSYRELQRATESLARRLTRDGVAPGRAVgVMCRNGRGFVTAVFAVGLL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    88 GVIAVP------AYPPESARRHHQERllSIIADAEprlvlttadlrepllqMNAQLSAANAPQLLcvdqLDPAVAEAWD- 160
Cdd:PRK13383  109 GADVVPistefrSDALAAALRAHHIS--TVVADNE----------------FAERIAGADDAVAV----IDPATAGAEEs 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   161 --EPQVRPE-HIAFLqyTSGSTALPKGV----QVSHGNLVANEVLIRRGFGIGADdvIVSWLPLYHDMGLiGGLLQPIFS 233
Cdd:PRK13383  167 ggRPAVAAPgRIVLL--TSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGSR--ISVAMPMFHGLGL-GMLMLTIAL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   234 GvpCVLMSPRYFlERPVRWLEAISQYGGTVSGGPDFAYRLCSerVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKF 313
Cdd:PRK13383  242 G--GTVLTHRHF-DAEAALAQASLHRADAFTAVPVVLARILE--LPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   314 AASRFDAssffacYGLAEAtlfvtggqrgqGIPALAVDGEalarnrIAEGEGSVlmccGRSQPEHAVLIVDAaSGEVLGD 393
Cdd:PRK13383  317 GDILYNG------YGSTEV-----------GIGALATPAD------LRDAPETV----GKPVAGCPVRILDR-NNRPVGP 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   394 DNVGEIWAAGPSIAHGYwrnPEASAKAFVerDGRTwlRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIERTVESE 472
Cdd:PRK13383  369 RVTGRIFVGGELAGTRY---TDGGGKAVV--DGMT--STGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAH 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   473 ----------VPSARKG-RVAAFAVTVDGEEgigiaaeigrgvqksVPAQELIDSIRQAVAEAyqEAPKVVALLnpGALP 541
Cdd:PRK13383  442 pavadnavigVPDERFGhRLAAFVVLHPGSG---------------VDAAQLRDYLKDRVSRF--EQPRDINIV--SSIP 502

                  ....*....
gi 15597620   542 KTSSGKLQR 550
Cdd:PRK13383  503 RNPTGKVLR 511
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1115-1511 5.04e-13

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 75.16  E-value: 5.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1115 LAEWgsAPCEPARAWLPElleRQLAQSAERVAlewdggslgYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVG 1194
Cdd:cd05921    1 LAHW--ARQAPDRTWLAE---REGNGGWRRVT---------YAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALM 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1195 LLAIVKAGGAYVPLDPDYpserlAYMLADsgvelLLTQAHLFERL-PG---AEGVTPI--CLDSLKLDNWPSQAPGLHLH 1268
Cdd:cd05921   67 ALAAMYAGVPAAPVSPAY-----SLMSQD-----LAKLKHLFELLkPGlvfAQDAAPFarALAAIFPLGTPLVVSRNAVA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1269 G---------------------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVlmqkaPVS 1321
Cdd:cd05921  137 GrgaisfaelaatpptaavdaafaavgpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVL 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1322 FDVSVWECFWPLVTGCRLVLAAPGE-HRD-----PARLVELVRQFG--VTTLHFVPP-----LLQLFIDEPGVAAC--GS 1386
Cdd:cd05921  212 VDWLPWNHTFGGNHNFNLVLYNGGTlYIDdgkpmPGGFEETLRNLReiSPTVYFNVPagwemLVAALEKDEALRRRffKR 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1387 LRRLFSGGEALPAELRNRvLQRLP------AVALHNRYGPTETA--INVTHWqcraeDGERSP-IGRPLGNVvcrvldaE 1457
Cdd:cd05921  292 LKLMFYAGAGLSQDVWDR-LQALAvatvgeRIPMMAGLGATETAptATFTHW-----PTERSGlIGLPAPGT-------E 358
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597620 1458 FNLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRAR 1511
Cdd:cd05921  359 LKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF-------YCLGDAAK 405
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
3867-4227 5.39e-13

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 73.45  E-value: 5.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3867 VIYTSGSTGLPKGVMVEQAGM---LNNQLSKVpyLELDENDVIAQTASQSFDISVWQFLAAPLFGArvAIVPNAVAHDPQ 3943
Cdd:cd17635    6 VIFTSGTTGEPKAVLLANKTFfavPDILQKEG--LNWVVGDVTYLPLPATHIGGLWWILTCLIHGG--LCVTGGENTTYK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3944 GLLAHVGEQGITVLESVPSL---IQGMLAEERQALDGLRwMLPTGEAMPPELARQWLKRYPRIGLVNAYGPAECSDdVAF 4020
Cdd:cd17635   82 SLFKILTTNAVTTTCLVPTLlskLVSELKSANATVPSLR-LIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGT-ALC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4021 FRVDLASTESTylPIGSPTDNNRLYLlgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapGERL 4100
Cdd:cd17635  160 LPTDDDSIEIN--AVGRPYPGVDVYL----AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4101 YrTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANgkylVGYLVpgetprssadsp 4180
Cdd:cd17635  227 N-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEE----FGELV------------ 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15597620 4181 aGLMVEQGAWFER-----IKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDR 4227
Cdd:cd17635  290 -GLAVVASAELDEnairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
2224-2622 6.35e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 74.84  E-value: 6.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2224 LARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL-----SHAALFEALG 2298
Cdd:PLN02860   45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVtdetcSSWYEELQND 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2299 ELPAGVARWCLEEDGP-----ALDAEDPAPLAALSG----------PQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAV 2363
Cdd:PLN02860  125 RLPSLMWQVFLESPSSsvfifLNSFLTTEMLKQRALgtteldyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2364 IECFGMRAEDCELHFYSINFDAASERLLAPLLCGARVVLRAqgQWGAEEICELIRAEGVSILGFTP-------SYGSQLA 2436
Cdd:PLN02860  205 IAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLP--KFDAKAALQAIKQHNVTSMITVPammadliSLTRKSM 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2437 QWLESQGrqlpVRMCITGGEALTGEHLQRIRQAFAPASFFNAYGPTET----VVMPL----------ACLAPERLEEGAA 2502
Cdd:PLN02860  283 TWKVFPS----VRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcsslTFMTLhdptlespkqTLQTVNQTKSSSV 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2503 SVPIGSVVGARVAYIldaDLALVPQGA--TGELYVGGAGLARGYHERPALSAERFVPDPFAAeggrlyrTGDLVRLCDNG 2580
Cdd:PLN02860  359 HQPQGVCVGKPAPHV---ELKIGLDESsrVGRILTRGPHVMLGYWGQNSETASVLSNDGWLD-------TGDIGWIDKAG 428
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 15597620  2581 QVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL 2622
Cdd:PLN02860  429 NLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
2821-3044 7.25e-13

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 74.00  E-value: 7.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2821 AIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQEL-LWHVPVQSFDECAELFAKAQRSLDLEQGPLLRAVL 2899
Cdd:cd19540   35 ALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPdLTVVDVTEDELAARLAEAARRGFDLTAELPLRARL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2900 VDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSES-----LREELGW 2974
Cdd:cd19540  115 FRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLPVQYADYALWQRELLGDEDdpdslAARQLAY 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620 2975 WQARLGGQP--VEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQApAAYRTQVNDLLLTALARVLCRWSG 3044
Cdd:cd19540  195 WRETLAGLPeeLELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA-REHGATLFMVLHAALAVLLSRLGA 265
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
2201-2659 8.90e-13

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 74.39  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2201 QAPALTFAGQ--------TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2272
Cdd:cd05921    7 QAPDRTWLAEregnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2273 -----ERLQYMIEDSGVRLLL-SHAALFE-ALGE-LPAGVARWCLEEDGPALDA------------EDPAPLAALSGPQH 2332
Cdd:cd05921   87 msqdlAKLKHLFELLKPGLVFaQDAAPFArALAAiFPLGTPLVVSRNAVAGRGAisfaelaatpptAAVDAAFAAVGPDT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2333 QAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED--CELHFYSINFDAASERLLAPLLCGARVVLRAQGQWGA 2410
Cdd:cd05921  167 VAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDGKPMP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2411 EEICELIR--AEGVSILGFT-PSYGSQLAQWLEsQGRQL------PVRMCITGGEALTGEHLQRIrQAFAPAS------F 2475
Cdd:cd05921  247 GGFEETLRnlREISPTVYFNvPAGWEMLVAALE-KDEALrrrffkRLKLMFYAGAGLSQDVWDRL-QALAVATvgeripM 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2476 FNAYGPTETVvmPLACLAPERLEE-GAASVPIGSVvgarvayildaDLALVPQGATGELYVGGAGLARGYHERPALSAER 2554
Cdd:cd05921  325 MAGLGATETA--PTATFTHWPTERsGLIGLPAPGT-----------ELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQA 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2555 FVPDPFaaeggrlYRTGDLVRLCDNGQVE----YVGRIDHQVKIR-GFRIELGEIEARLLEH--PQVREALV-------- 2619
Cdd:cd05921  392 FDEEGF-------YCLGDAAKLADPDDPAkglvFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHDAVVagedraev 464
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 15597620 2620 ---LALDSPSGKQLAGYVASAVAE--QDEDAQAALREALKTHLKQ 2659
Cdd:cd05921  465 galVFPDLLACRRLVGLQEASDAEvlRHAKVRAAFRDRLAALNGE 509
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
13-554 9.54e-13

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 74.45  E-value: 9.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   13 QALRRRAVQEPERLALRFLAEDdGEGVVLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
Cdd:cd05968   65 QLLDKWLADTRTRPALRWEGED-GTSRTLTYGELLYEVkRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   92 VP---AYPPESARrhhqerllSIIADAEPRLvLTTADL-----REPLLQMNAQLSAANAPQ---LLCVDQLDPAVAEA-- 158
Cdd:cd05968  144 VPifsGFGKEAAA--------TRLQDAEAKA-LITADGftrrgREVNLKEEADKACAQCPTvekVVVVRHLGNDFTPAkg 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  159 ----WDE---------PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVL-IRRGFGIGADDvIVSWLPlyhDMG-- 222
Cdd:cd05968  215 rdlsYDEeketagdgaERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGD-LLTWFT---DLGwm 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  223 -----LIGGLLQP----IFSGVPCvlmspryfLERPVRWLEAISQYGGTVSGGPDFAYRLCSERvAESALQRLDLSGWRV 293
Cdd:cd05968  291 mgpwlIFGGLILGatmvLYDGAPD--------HPKADRLWRMVEDHEITHLGLSPTLIRALKPR-GDAPVNAHDLSSLRV 361
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  294 AFSGSEPIRQDSLERFAEKFAASRFDASSFfacYGLAEATLFVTGGQRGQGIPALAVDGealarnriaegegsvlmccgr 373
Cdd:cd05968  362 LGSTGEPWNPEPWNWLFETVGKGRNPIINY---SGGTEISGGILGNVLIKPIKPSSFNG--------------------- 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  374 SQPEHAVLIVDAASGEVlgDDNVGE--IWAAGPSIAHGYWRNPEASAKAFVERDGRTWLRtGDLGFL-RDGELFVTGRLK 450
Cdd:cd05968  418 PVPGMKADVLDESGKPA--RPEVGElvLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVH-GDFAYYdEEGYFYILGRSD 494
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  451 DMLIVRGHNLYPQDIE-------RTVESE---VPSARKGRV-AAFAVTVDGEEgigiaaeigrgvqksvPAQELIDSIRQ 519
Cdd:cd05968  495 DTINVAGKRVGPAEIEsvlnahpAVLESAaigVPHPVKGEAiVCFVVLKPGVT----------------PTEALAEELME 558
                        570       580       590
                 ....*....|....*....|....*....|....*
gi 15597620  520 AVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACR 554
Cdd:cd05968  559 RVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1148-1508 9.54e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 74.59  E-value: 9.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1148 EWDG--GSLGYAELHARANRLAHYLRDKGVGPDvRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPS---ERLAYMLA 1222
Cdd:PRK05850   28 DPAGvaETLTWSQLYRRTLNVAEELRRHGSTGD-RAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1223 DSGVELLLTQ-------AHLFERLPGAEGVTPICLDSLKLDNWPSQAPGLHLHgDNLAYVIYTSGSTGQPKGVGNTHAAL 1295
Cdd:PRK05850  107 DTSPSVVLTTsavvddvTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDL-PSTAYLQYTSGSTRTPAGVMVSHRNV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1296 AERLQWMQATYTLDGDDVlmqkAPVSFDVSVWECFW-----------PLVTGCRLVLAAP-GEHRDPARLVELVRQFGvt 1363
Cdd:PRK05850  186 IANFEQLMSDYFGDTGGV----PPPDTTVVSWLPFYhdmglvlgvcaPILGGCPAVLTSPvAFLQRPARWMQLLASNP-- 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1364 tlhfvppllQLFIDEPGVA----------------ACGSLRRLFSGGEAL-PAELRnRVLQR-----LPAVALHNRYGPT 1421
Cdd:PRK05850  260 ---------HAFSAAPNFAfelavrktsdddmaglDLGGVLGIISGSERVhPATLK-RFADRfapfnLRETAIRPSYGLA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1422 E-----------TAINVTHWQ-----------CRAEDG--------ERSPIgrplgnvvCRVLDAEFNL-LPAGVAGELC 1470
Cdd:PRK05850  330 EatvyvatrepgQPPESVRFDyeklsaghakrCETGGGtplvsygsPRSPT--------VRIVDPDTCIeCPAGTVGEIW 401
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 15597620  1471 IGGLGLARGYLGRPALSAERF---VADPfSA---AGERLyRTGD 1508
Cdd:PRK05850  402 VHGDNVAAGYWQKPEETERTFgatLVDP-SPgtpEGPWL-RTGD 443
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
3749-4171 1.10e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 74.39  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3749 NRLGHALRAAGVGIDQ------PVALLAERGLDLLGMIVGSFKAGAGYLPLD----PGHpTQRLTRIVELSRTLVLVCTQ 3818
Cdd:PRK12476   72 TQLGVRLRAVGARLQQvagpgdRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGH-AERLDTALRDAEPTVVLTTT 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3819 ACREQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVpyL 3898
Cdd:PRK12476  151 AAAEAVEGFLRNLPRLRRPRVIAIDAIPDSAGESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMI--L 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3899 ELDENDVIAQTAS-----QSFDISVWQFLAapLFGARVAIV-PNAVAHDPQGLLAHVGEQGIT--VLESVPSL-----IQ 3965
Cdd:PRK12476  228 SIDLLDRNTHGVSwlplyHDMGLSMIGFPA--VYGGHSTLMsPTAFVRRPQRWIKALSEGSRTgrVVTAAPNFayewaAQ 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3966 GMLAEERQALDGLRWMLPTG-EAMPPELARQWLKRY-----PRIGLVNAYGPAECSDDVA------------FFRVDLAS 4027
Cdd:PRK12476  306 RGLPAEGDDIDLSNVVLIIGsEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFVAtiapdaepsvvyLDREQLGA 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4028 TESTYLPIGSP---------TDNNRLYLLGAGADDAFELvPLGAVGELCVAGTGVGRGYVGDPLRTAQAFV--------- 4089
Cdd:PRK12476  386 GRAVRVAADAPnavahvscgQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlae 464
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4090 -PHPFGAPGERLY-RTGDLARRRaDGVLEYVGRIDHQVKIRGFRIELGEIEarlherADVREAAVAVQEGangkYLVGYL 4167
Cdd:PRK12476  465 gSHADGAADDGTWlRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIE------ATVAEASPMVRRG----YVTAFT 533

                  ....
gi 15597620  4168 VPGE 4171
Cdd:PRK12476  534 VPAE 537
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
3736-4169 1.54e-12

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 73.55  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLV 3815
Cdd:cd17640    3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3816 ctqacreqalalfdelgcvdrprllvwdeiqqgegaehdpqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKV 3895
Cdd:cd17640   83 -----------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLS 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3896 PYLELDENDV---------IAQTASQSFdisvwqflaapLFGARVAIVPNAVAHDPQGlLAHVGEQgitVLESVPSL--- 3963
Cdd:cd17640  122 DIVPPQPGDRflsilpiwhSYERSAEYF-----------IFACGCSQAYTSIRTLKDD-LKRVKPH---YIVSVPRLwes 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3964 ----IQGMLAEE---RQALDG-------LRWMLPTGEAMPPELARqwlkRYPRIG--LVNAYGPAECSDDVAFFRVDLAS 4027
Cdd:cd17640  187 lysgIQKQVSKSspiKQFLFLfflsggiFKFGISGGGALPPHVDT----FFEAIGieVLNGYGLTETSPVVSARRLKCNV 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4028 TESTYLPIgsptdnnrlyllgagADDAFELV--------PLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapger 4099
Cdd:cd17640  263 RGSVGRPL---------------PGTEIKIVdpegnvvlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------ 321
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620 4100 lYRTGDLARRRADGVLEYVGRI-DHQVKIRGFRIELGEIEARLhERADVREAAVAVqeGANGKYLVGYLVP 4169
Cdd:cd17640  322 -FNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEAL-MRSPFIEQIMVV--GQDQKRLGALIVP 388
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3725-4233 1.69e-12

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 73.49  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3725 AHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQpVALL-----AERGLDLLGMivgsFKAGAgyLPLDPGHPT 3799
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGD-TALVqlgnvAEFYITFFAL----LKLGV--APVNALFSH 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3800 QRL---TRIVELSRTLVLvctqACREQAL----ALFDELGcVDRPRLLVW----DEIQQG------EGAEHDPQVYSGPQ 3862
Cdd:PRK10946  108 QRSelnAYASQIEPALLI----ADRQHALfsddDFLNTLV-AEHSSLRVVlllnDDGEHSlddainHPAEDFTATPSPAD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3863 NLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDEND--VIAQTASQSFDISVWQFLAAPLFGARVAIvpnavAH 3940
Cdd:PRK10946  183 EVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTryLCALPAAHNYPMSSPGALGVFLAGGTVVL-----AP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3941 DPQGLL--AHVGEQGITVLESVPS-----LIQGMLAEERQALDGLRWMLPTGEAMPPELARqwlkRYPRI---------- 4003
Cdd:PRK10946  258 DPSATLcfPLIEKHQVNVTALVPPavslwLQAIAEGGSRAQLASLKLLQVGGARLSETLAR----RIPAElgcqlqqvfg 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4004 ---GLVNaYGPAECSDDVAFfrvdlaSTESTylPIgSPTDNNRLyllgagADDAFELVPLGAVGELCVAGTGVGRGYVGD 4080
Cdd:PRK10946  334 maeGLVN-YTRLDDSDERIF------TTQGR--PM-SPDDEVWV------ADADGNPLPQGEVGRLMTRGPYTFRGYYKS 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4081 PLRTAQAFVPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAA-VAVQEGAN 4159
Cdd:PRK10946  398 PQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAlVSMEDELM 470
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  4160 GKYLVGYLVPGETPRSSAdspaglmveqgawferIKQQLRAD-LPDYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:PRK10946  471 GEKSCAFLVVKEPLKAVQ----------------LRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
2336-2629 1.75e-12

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 71.95  E-value: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2336 LIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCEL------HFYSINFdaaserLLAPLLCGARVVLRAQGQwg 2409
Cdd:cd17636    5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLnsgplfHIGTLMF------TLATFHAGGTNVFVRRVD-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2410 AEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQL----------PVRMCITGGEALTGEHLqrirqafapasffNAY 2479
Cdd:cd17636   77 AEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLsslrsspaapEWNDMATVDTSPWGRKP-------------GGY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2480 GPTEtvVMPLACLApeRLEEGAASVPIGSVVGARVaYILDADLALVPQGATGELYVGGAGLARGYHERPALSAERFVpdp 2559
Cdd:cd17636  144 GQTE--VMGLATFA--ALGGGAIGGAGRPSPLVQV-RILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--- 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2560 faaegGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQ 2629
Cdd:cd17636  216 -----GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ 280
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
8-222 2.17e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 73.54  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     8 PTTLVQALRRRAVQEPERLALRFLAEDDGEGVVLSYRDLDLRARSIAAALQAHAQLGDRAVLLFpSGPDYVAAF--FGCL 85
Cdd:PRK12582   48 PRSIPHLLAKWAAEAPDRPWLAQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMIL-SGNSIEHALmtLAAM 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    86 YAGVIAVPAYPPESARRHHQERLLSIIADAEPRLVLT------TADLREPLLQMNAQLSAANAP--------QLLCVDQL 151
Cdd:PRK12582  127 QAGVPAAPVSPAYSLMSHDHAKLKHLFDLVKPRVVFAqsgapfARALAALDLLDVTVVHVTGPGegiasiafADLAATPP 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620   152 DPAVAEAWDepQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADD---VIVSWLPLYHDMG 222
Cdd:PRK12582  207 TAAVAAAIA--AITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMG 278
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2198-2689 2.17e-12

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 73.10  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2198 ASPQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGgaYVPLDPEYPLERLQY 2277
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSEL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2278 -----------MIEDSGVRLLLSHAALFEALGELPAgVARWCLEEDGPALD-----AEDPAPLAALSGPQHQ-AYLIYTS 2340
Cdd:PRK10946  113 nayasqiepalLIADRQHALFSDDDFLNTLVAEHSS-LRVVLLLNDDGEHSlddaiNHPAEDFTATPSPADEvAFFQLSG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2341 GSTGKPKGVAVSHGEIAMHCAAVIECFGMRAED---CEL---HfysiNFDAASERLLAPLLCGARVVLRAQGqwGAEEIC 2414
Cdd:PRK10946  192 GSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTrylCALpaaH----NYPMSSPGALGVFLAGGTVVLAPDP--SATLCF 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2415 ELIRAEGVSILGFTPS-------------YGSQL----------AQWLESQGRQLPvrmcitggeALTGEHLQrirQAFA 2471
Cdd:PRK10946  266 PLIEKHQVNVTALVPPavslwlqaiaeggSRAQLaslkllqvggARLSETLARRIP---------AELGCQLQ---QVFG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2472 PASFFNAY----GPTETVVMPLAClaperleegaasvPIGSVVGARVAyilDADLALVPQGATGELYVGGAGLARGYHER 2547
Cdd:PRK10946  334 MAEGLVNYtrldDSDERIFTTQGR-------------PMSPDDEVWVA---DADGNPLPQGEVGRLMTRGPYTFRGYYKS 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2548 PALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVRE-ALVLALDSPS 2626
Cdd:PRK10946  398 PQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHaALVSMEDELM 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  2627 GKQLAGYVASavaeqdedaqaalREALKT-----HLKQQ-LPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK10946  471 GEKSCAFLVV-------------KEPLKAvqlrrFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK08308 PRK08308
acyl-CoA synthetase; Validated
1180-1623 2.71e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 72.38  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1180 RVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQahlferlpgaEGVTPIcldsLKLDNWP 1259
Cdd:PRK08308   34 RFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYG----------ESDFTK----LEAVNYL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1260 SQAPGLhlhgdnlayVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPVSFDvsvwecfWPLVTGcrl 1339
Cdd:PRK08308  100 AEEPSL---------LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHS-------YGLICG--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1340 VLAAPGE--------HRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPgvAACGSLRRLFSGGEALPAELrnrvLQRLPA 1411
Cdd:PRK08308  161 VLAALTRgskpviitNKNPKFALNILRNTPQHILYAVPLMLHILGRLL--PGTFQFHAVMTSGTPLPEAW----FYKLRE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1412 VALH--NRYGPTETA-INVTHWQCRAEDgerspIGRPLGNVVCRVLDAEfnllpaGVAGELCIgglglargylgrpalsa 1488
Cdd:PRK08308  235 RTTYmmQQYGCSEAGcVSICPDMKSHLD-----LGNPLPHVSVSAGSDE------NAPEEIVV----------------- 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1489 erfvadpfsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIR-EGVAGSQLv 1567
Cdd:PRK08308  287 ---------KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGkDPVAGERV- 356
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  1568 gyyTGAVGAEAEAEQNQrLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALP 1623
Cdd:PRK08308  357 ---KAKVISHEEIDPVQ-LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
1156-1600 3.15e-12

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 72.46  E-value: 3.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRD-KGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLtqah 1234
Cdd:cd05937    8 YSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1235 lferlpgaegVTPicldslkldnwpsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVL 1314
Cdd:cd05937   84 ----------VDP----------------------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRT 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1315 MQKAPV----SFDVSVWEC-----------------FWPLV--TG----------CRLVLAAPGEHRDPARLVELV---- 1357
Cdd:cd05937  132 YTCMPLyhgtAAFLGACNClmsggtlalsrkfsasqFWKDVrdSGatiiqyvgelCRYLLSTPPSPYDRDHKVRVAwgng 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1358 ----------RQFGVTTLHfvppllQLFIDEPGVAAcgsLRRLFSGGEALPAELRNRVLQRLpavALHNRYGPTETAINV 1427
Cdd:cd05937  212 lrpdiwerfrERFNVPEIG------EFYAATEGVFA---LTNHNVGDFGAGAIGHHGLIRRW---KFENQVVLVKMDPET 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1428 THWQCRAEDG--ERSPIGRPlGNVVCRVldaefNLLPagvagelciggLGLARGYLGRPALSAERFVADPFSAaGERLYR 1505
Cdd:cd05937  280 DDPIRDPKTGfcVRAPVGEP-GEMLGRV-----PFKN-----------REAFQGYLHNEDATESKLVRDVFRK-GDIYFR 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1506 TGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVagsqLVGYYTGAVGAEAEAEQNQ- 1584
Cdd:cd05937  342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY---GV----KVPGHDGRAGCAAITLEESs 414
                        490       500
                 ....*....|....*....|....*
gi 15597620 1585 ---------RLRAALQAELPEYMVP 1600
Cdd:cd05937  415 avpteftksLLASLARKNLPSYAVP 439
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4252-4311 3.15e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 64.12  E-value: 3.15e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620   4252 ETLARIWAEVLKV--ERVGVFDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEE 4311
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
2186-2689 3.39e-12

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 72.78  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2186 DTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVLRShGVGPEV--RVGLALERSLEMVVGLLAILKAGGAY 2263
Cdd:PRK08974   23 QSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQN-GLGLKKgdRVALMMPNLLQYPIALFGILRAGMIV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2264 VPLDPEYPLERLQYMIEDSGVR--LLLSHAA---------------LFEALGE-LPAG-------VARWcLEEDGPALDA 2318
Cdd:PRK08974  102 VNVNPLYTPRELEHQLNDSGAKaiVIVSNFAhtlekvvfktpvkhvILTRMGDqLSTAkgtlvnfVVKY-IKRLVPKYHL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2319 EDPAPL-AALS-GPQHQ-----------AYLIYTSGSTGKPKGVAVSHGEI---AMHCAAVIECF---GMRAEDCELHFY 2379
Cdd:PRK08974  181 PDAISFrSALHkGRRMQyvkpelvpedlAFLQYTGGTTGVAKGAMLTHRNMlanLEQAKAAYGPLlhpGKELVVTALPLY 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2380 SInFdAASERLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSqlaqWLESQG-RQL---PVRMCITGG 2455
Cdd:PRK08974  261 HI-F-ALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNA----LLNNEEfQELdfsSLKLSVGGG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2456 -----------EALTGEHLqrirqafapasfFNAYGPTETVvmPLACLAPERLEEGAASvpIGSVVGARVAYILDADLAL 2524
Cdd:PRK08974  335 mavqqavaerwVKLTGQYL------------LEGYGLTECS--PLVSVNPYDLDYYSGS--IGLPVPSTEIKLVDDDGNE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2525 VPQGATGELYVGGAGLARGYHERPALSAErFVPDPFAAeggrlyrTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEI 2604
Cdd:PRK08974  399 VPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2605 EARLLEHPQVREALVLALDSPSGKQLagyVASAVAEQDEdaqAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKL 2684
Cdd:PRK08974  471 EDVVMLHPKVLEVAAVGVPSEVSGEA---VKIFVVKKDP---SLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544

                  ....*
gi 15597620  2685 DRRAL 2689
Cdd:PRK08974  545 LRREL 549
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
3740-4157 4.09e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 72.09  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCtqa 3819
Cdd:cd05914    9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3820 creqalalfdelgcvdrprllvwdeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLE 3899
Cdd:cd05914   86 ---------------------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3900 LDENDVI------AQTASQSFDisvwqFLAAPLFGARVAI---VPNAVAHDPQgllahvgEQGITVLESVPSLIQGM--- 3967
Cdd:cd05914  127 LGKGDKIlsilplHHIYPLTFT-----LLLPLLNGAHVVFldkIPSAKIIALA-------FAQVTPTLGVPVPLVIEkif 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3968 ----------------LAEE-----------RQALDG----LRWMLPTGEAMPPELARQWLKryprIGL--VNAYGPAEC 4014
Cdd:cd05914  195 kmdiipkltlkkfkfkLAKKinnrkirklafKKVHEAfggnIKEFVIGGAKINPDVEEFLRT----IGFpyTIGYGMTET 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4015 SDDVAFF---RVDLASTestylpiGSPTDNnrlylLGAGADDAfelVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPh 4091
Cdd:cd05914  271 APIISYSppnRIRLGSA-------GKVIDG-----VEVRIDSP---DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK- 334
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 4092 pfgapgERLYRTGDLARRRADGVLEYVGRIDHQ-VKIRGFRIELGEIEARLHERADVREAAVAVQEG 4157
Cdd:cd05914  335 ------DGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK 395
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
3736-4152 4.17e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 72.11  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALR-AAGVGIDQPVALLAERGLDLLGMIVGSFKAGagyLPLDPGhptqrltrIVELSRTLVL 3814
Cdd:cd05928   39 EVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTG---LVFIPG--------TIQLTAKDIL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3815 VCTQACREQALALFDELG-CVD---------RPRLLVWDEIQQG---------EGAEHDPQVYSGPQNLAYVIYTSGSTG 3875
Cdd:cd05928  108 YRLQASKAKCIVTSDELApEVDsvasecpslKTKLLVSEKSRDGwlnfkellnEASTEHHCVETGSQEPMAIYFTSGTTG 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3876 LPKgvMVEQAGMLNNQLSKV---PYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAVAHDPQGLLAHVGEQ 3952
Cdd:cd05928  188 SPK--MAEHSHSSLGLGLKVngrYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSY 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3953 GITVLESVPSLIQgMLAEE---RQALDGLRWMLPTGEAMPPELARQWlKRYPRIGLVNAYGPAECSDDVAFFRVdlASTE 4029
Cdd:cd05928  266 PITTFCGAPTVYR-MLVQQdlsSYKFPSLQHCVTGGEPLNPEVLEKW-KAQTGLDIYEGYGQTETGLICANFKG--MKIK 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4030 STYLPIGSPTDNNRLyllgagADDAFELVPLGAVGELCV-----AGTGVGRGYVGDPLRTAQAFvphpfgaPGErLYRTG 4104
Cdd:cd05928  342 PGSMGKASPPYDVQI------IDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATI-------RGD-FYLTG 407
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 4105 DLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:cd05928  408 DRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAV 455
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
2194-2652 4.68e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 72.34  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2194 ARVAASPQAPaltfagQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLE 2273
Cdd:PRK07768   18 GMVTGEPDAP------VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2274 RLQYMIEDSGVRLLLSHAAL------FEALGELPAGVA-RWCLEEDgpALDAEDPAPLaaLSGPQHQAYLIYTSGSTGKP 2346
Cdd:PRK07768   92 DLAVWAEDTLRVIGMIGAKAvvvgepFLAAAPVLEEKGiRVLTVAD--LLAADPIDPV--ETGEDDLALMQLTSGSTGSP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2347 KGVAVSHGEIAMHCAAVIEcfgmraedcelhfySINFDAASERLLA----------------PLLCGARVV-------LR 2403
Cdd:PRK07768  168 KAVQITHGNLYANAEAMFV--------------AAEFDVETDVMVSwlplfhdmgmvgfltvPMYFGAELVkvtpmdfLR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2404 AQGQWGaeeicELI-RAEGVSILGFTPSYgSQLAQWLESQGRQLP-----VRMCITGGEALTGEHLQRI-----RQAFAP 2472
Cdd:PRK07768  234 DPLLWA-----ELIsKYRGTMTAAPNFAY-ALLARRLRRQAKPGAfdlssLRFALNGAEPIDPADVEDLldagaRFGLRP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2473 ASFFNAYGPTETVV----------MPLACLAPERLEEGAASVPIGSVVGARVAY-----------ILDADLALVPQGATG 2531
Cdd:PRK07768  308 EAILPAYGMAEATLavsfspcgagLVVDEVDADLLAALRRAVPATKGNTRRLATlgpplpglevrVVDEDGQVLPPRGVG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2532 ELYVGGAGLARGYherpaLSAERFVPdpfAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEH 2611
Cdd:PRK07768  388 VIELRGESVTPGY-----LTMDGFIP---AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARV 459
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 15597620  2612 PQVREALVLA--LDSPSGKQLAGYVASAVAEQDEDAQAALREA 2652
Cdd:PRK07768  460 EGVRPGNAVAvrLDAGHSREGFAVAVESNAFEDPAEVRRIRHQ 502
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2793-3103 6.04e-12

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 70.79  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2793 TPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQhRPLREQELLWHVpVQS 2872
Cdd:cd19545    5 TPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQ-VVVKESPISWTE-STS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2873 FDECAELFAkaQRSLDLEQgPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAegaepalPAKTSAF 2952
Cdd:cd19545   83 LDEYLEEDR--AAPMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEP-------VPQPPPF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2953 RDWagrlQAYAGSESLREELGWWQARLGG-QPVEWPCD---RPQGDNREALaesvslrldpQRTRQLLQQAPAAYRTQVn 3028
Cdd:cd19545  153 SRF----VKYLRQLDDEAAAEFWRSYLAGlDPAVFPPLpssRYQPRPDATL----------EHSISLPSSASSGVTLAT- 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 3029 dLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDltRSVGWFTSAYPLR--LTPAQSPGESIKAIKEQL-RAVPH 3103
Cdd:cd19545  218 -VLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIE--QIVGPTIATVPLRvrIDPEQSVEDFLQTVQKDLlDMIPF 292
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
3751-4169 6.40e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 72.07  E-value: 6.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3751 LGHALRAAGVGIDQ---P---VALLAERGLDLLGMIVGSFKAGAGYLPL----DPGHpTQRLTRIVELSRTLVLVCTQAC 3820
Cdd:PRK07769   61 FGARNRAVGARLQQvtkPgdrVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGH-VGRLHAVLDDCTPSAILTTTDS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3821 REQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPqVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLEL 3900
Cdd:PRK07769  140 AEGVRKFFRARPAKERPRVIAVDAVPDEVGATWVP-PEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3901 DENDVIAQTASQSFDISVWQFLAAPLFGARVAIV-PNAVAHDPQ---GLLAHVGEQGITVLESVPSL------IQGMLAE 3970
Cdd:PRK07769  219 QEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMsPAAFVRRPGrwiRELARKPGGTGGTFSAAPNFafehaaARGLPKD 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3971 ERQALD--GLRWMLPTGEAMPPELARQWLKRYPRIGLVN-----AYGPAEC--------SDDVA-FFRVDLASTESTYLP 4034
Cdd:PRK07769  299 GEPPLDlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpSYGMAEAtlfvsttpMDEEPtVIYVDRDELNAGRFV 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4035 IGSPTDNNRLYLLGAG------------ADDAFELvPLGAVGELCVAGTGVGRGYVGDPLRTAQAF---------VPHPF 4093
Cdd:PRK07769  379 EVPADAPNAVAQVSAGkvgvsewavivdPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlsESHAE 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4094 GAP-GERLYRTGDLArRRADGVLEYVGRIDHQVKIRGfrielgeieaRLHERADV----REAAVAVQEGangkYLVGYLV 4168
Cdd:PRK07769  458 GAPdDALWVRTGDYG-VYFDGELYITGRVKDLVIIDG----------RNHYPQDLeytaQEATKALRTG----YVAAFSV 522

                  .
gi 15597620  4169 P 4169
Cdd:PRK07769  523 P 523
PRK13382 PRK13382
bile acid CoA ligase;
141-550 6.65e-12

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 71.71  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   141 NAPQLLCVDQLDPAVAEawDEPQVRPEHIAFLQYTSGSTALPKGVQVSH--GNLVANEVLIRRGFGIGADDVIVSwlPLY 218
Cdd:PRK13382  172 DEDHDLTVEVLIAAHAG--QRPEPTGRKGRVILLTSGTTGTPKGARRSGpgGIGTLKAILDRTPWRAEEPTVIVA--PMF 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   219 HDMGLIGGLLQPIFSgvpCVLMSPRYFleRPVRWLEAISQYGGTVSGGPDFAYRLCSERVAEsALQRLDLSGWRVAFSGS 298
Cdd:PRK13382  248 HAWGFSQLVLAASLA---CTIVTRRRF--DPEATLDLIDRHRATGLAVVPVMFDRIMDLPAE-VRNRYSGRSLRFAAASG 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   299 EPIRQDSLERFAEKFAasrfDAssFFACYGLAEATLFVTGGQRG-QGIPALAvdgealarNRIAEG-EGSVLMCCGRSQP 376
Cdd:PRK13382  322 SRMRPDVVIAFMDQFG----DV--IYNNYNATEAGMIATATPADlRAAPDTA--------GRPAEGtEIRILDQDFREVP 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   377 EhavlivdaasGEVlgddnvGEIWAAGPSIAHGYwrnPEASAKAFveRDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIV 455
Cdd:PRK13382  388 T----------GEV------GTIFVRNDTQFDGY---TSGSTKDF--HDG--FMASGDVGYLDEnGRLFVVGRDDEMIVS 444
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   456 RGHNLYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGeegigiaaeigrgvqksvpAQELIDSIRQAVAE- 523
Cdd:PRK13382  445 GGENVYPIEVEKTLATHpdvaeaavigVDDEQYGqRLAAFVVLKPG-------------------ASATPETLKQHVRDn 505
                         410       420
                  ....*....|....*....|....*...
gi 15597620   524 -AYQEAPKVVALLnpGALPKTSSGKLQR 550
Cdd:PRK13382  506 lANYKVPRDIVVL--DELPRGATGKILR 531
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
1154-1608 6.97e-12

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 71.23  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQA 1233
Cdd:cd05940    4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaegvtpicldslkldnwpsqapglhlhgdnlAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDV 1313
Cdd:cd05940   84 ---------------------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1314 LMQKAPVSFDVSVWECFWP-LVTGCRLVLaapGEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAA--CGSLRRL 1390
Cdd:cd05940  125 LYTCLPLYHSTALIVGWSAcLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTerKHKVRMI 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1391 FsgGEALPAELRNRVLQRLPAVALHNRYGPTETAINVTHWqcraeDGERSPIGR--PLGNVVCRVLDAEFNL-------- 1460
Cdd:cd05940  202 F--GNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF-----FGKPGAIGRnpSLLRKVAPLALVKYDLesgepird 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1461 -------LPAGVAGELC--IGGLGLARGYLGrPALSAERFVADPFsAAGERLYRTGDRARWNADGVLEYLGRLDQQVKLR 1531
Cdd:cd05940  275 aegrcikVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWK 352
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1532 GFRIEPEEIQARLLAQPGVAQAVVVireGVAgsqlVGYYTGAVG------AEAEAEQNQRLRAALQAELPEYMVPTQLmR 1605
Cdd:cd05940  353 GENVSTTEVAAVLGAFPGVEEANVY---GVQ----VPGTDGRAGmaaivlQPNEEFDLSALAAHLEKNLPGYARPLFL-R 424

                 ...
gi 15597620 1606 LAQ 1608
Cdd:cd05940  425 LQP 427
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1125-1621 7.96e-12

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 71.70  E-value: 7.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1125 PARAWLPELLERQLAQSAERVA---LEWDGGSLGYA------ELHARANRLAHYLRdKGVGPDVRVAICAERSPQLLVGL 1195
Cdd:PRK12476   31 PPGTTLISLIERNIANVGDTVAyryLDHSHSAAGCAveltwtQLGVRLRAVGARLQ-QVAGPGDRVAILAPQGIDYVAGF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1196 LAIVKAGGAYVPL-DPDYP--SERLAYMLADSGVELLLTQA-------HLFERLPGAEGVTPICLDSLKLDNWPSQAPgL 1265
Cdd:PRK12476  110 FAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTaaaeaveGFLRNLPRLRRPRVIAIDAIPDSAGESFVP-V 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1266 HLHGDNLAYVIYTSGSTGQPKGVGNTH-AALAERLQWMQATYTLDGDDVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAP 1344
Cdd:PRK12476  189 ELDTDDVSHLQYTSGSTRPPVGVEITHrAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSP 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1345 GEH-RDPARLVELVRQfGVTTlhfvpplLQLFIDEPGVA-ACGSLRRLFSGGEALpaELRNRVL---------------- 1406
Cdd:PRK12476  269 TAFvRRPQRWIKALSE-GSRT-------GRVVTAAPNFAyEWAAQRGLPAEGDDI--DLSNVVLiigsepvsidavttfn 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1407 -----QRLPAVALHNRYGPTETAINVTHWQCRAE------DGERSPIGRPL---------------GNVV----CRVLDA 1456
Cdd:PRK12476  339 kafapYGLPRTAFKPSYGIAEATLFVATIAPDAEpsvvylDREQLGAGRAVrvaadapnavahvscGQVArsqwAVIVDP 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1457 EF-NLLPAGVAGELCIGGLGLARGYLGRPALSAERFVADPFS-----------AAGERLYRTGDRARWnADGVLEYLGRL 1524
Cdd:PRK12476  419 DTgAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSrlaegshadgaADDGTWLRTGDLGVY-LDGELYITGRI 497
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1525 DQQVKLRGFRIEPEEIQARllaqpgVAQAVVVIREG---------VAGSQLVGYYTGAVGA-EAE-AEQNQRLRAALQAe 1593
Cdd:PRK12476  498 ADLIVIDGRNHYPQDIEAT------VAEASPMVRRGyvtaftvpaEDNERLVIVAERAAGTsRADpAPAIDAIRAAVSR- 570
                         570       580       590
                  ....*....|....*....|....*....|.
gi 15597620  1594 lpEYMVPTQLMRLAQ---MPLGPSGKLDTRA 1621
Cdd:PRK12476  571 --RHGLAVADVRLVPagaIPRTTSGKLARRA 599
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
2203-2689 8.42e-12

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 71.20  E-value: 8.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2203 PALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDS 2282
Cdd:PRK07059   40 PAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2283 GVRLL------------------LSH---AALFEALG--------------------ELPAGVARWCLEEDGPALDAEdP 2321
Cdd:PRK07059  120 GAEAIvvlenfattvqqvlaktaVKHvvvASMGDLLGfkghivnfvvrrvkkmvpawSLPGHVRFNDALAEGARQTFK-P 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2322 APLaalsGPQHQAYLIYTSGSTGKPKGVAVSHGEIAmhcAAVIE-------CFGMRAED------CELHFYSInFDAASE 2388
Cdd:PRK07059  199 VKL----GPDDVAFLQYTGGTTGVSKGATLLHRNIV---ANVLQmeawlqpAFEKKPRPdqlnfvCALPLYHI-FALTVC 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2389 RLLApLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQwleSQGRQL---PVRMCITGGEALTgEHLQR 2465
Cdd:PRK07059  271 GLLG-MRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN---PDFDKLdfsKLIVANGGGMAVQ-RPVAE 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2466 IRQAFAPASFFNAYGPTETVvmPLACLAPERLEE--GAASVPIGSVVGArvayILDADLALVPQGATGELYVGGAGLARG 2543
Cdd:PRK07059  346 RWLEMTGCPITEGYGLSETS--PVATCNPVDATEfsGTIGLPLPSTEVS----IRDDDGNDLPLGEPGEICIRGPQVMAG 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2544 YHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL- 2622
Cdd:PRK07059  420 YWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVp 492
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  2623 DSPSGKQlagyVASAVAEQDedaQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK07059  493 DEHSGEA----VKLFVVKKD---PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
64-554 9.06e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 71.34  E-value: 9.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESAR----RHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLSA 139
Cdd:cd05928   67 GDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKdilyRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  140 ANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNL-VANEVLIRRGFGIGADDVIvsWlpLY 218
Cdd:cd05928  147 KSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIM--W--NT 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  219 HDMGLIGGLLQPIFSGVP---CVLMS--PRYfleRPVRWLEAISQYGGTVSGGPDFAYRLcserVAESALQRLDLSGWRV 293
Cdd:cd05928  223 SDTGWIKSAWSSLFEPWIqgaCVFVHhlPRF---DPLVILKTLSSYPITTFCGAPTVYRM----LVQQDLSSYKFPSLQH 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  294 AFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEaTLFVTGGQRGQGIPAlavdgealarnriaegeGSVlmccGR 373
Cdd:cd05928  296 CVTGGEPLNPEVLEKWKAQTGLDIYEG------YGQTE-TGLICANFKGMKIKP-----------------GSM----GK 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  374 SQPEHAVLIVDaASGEVLGDDNVGEIWA-AGP----SIAHGYWRNPEASAKafVERdGRTWLrTGDLGFL-RDGELFVTG 447
Cdd:cd05928  348 ASPPYDVQIID-DNGNVLPPGTEGDIGIrVKPirpfGLFSGYVDNPEKTAA--TIR-GDFYL-TGDRGIMdEDGYFWFMG 422
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  448 RLKDMLIVRGHNLYPQDIERT-------VESEVPSA----RKGRVAAFAVtvdgeegigIAAEIgrgvqKSVPAQELIDS 516
Cdd:cd05928  423 RADDVINSSGYRIGPFEVESAliehpavVESAVVSSpdpiRGEVVKAFVV---------LAPQF-----LSHDPEQLTKE 488
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15597620  517 IRQAVAE--AYQEAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:cd05928  489 LQQHVKSvtAPYKYPRKVEFVQ--ELPKTVTGKIQRNELR 526
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
14-550 9.06e-12

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 71.44  E-value: 9.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   14 ALRRRAVQEPERLALRFLAEDDGEGVVLSYRDLD---------LRARSIAAalqahaqlGDRAVLLFPSGPDYVAAFFGC 84
Cdd:cd05966   58 CLDRHLKERGDKVAIIWEGDEPDQSRTITYRELLrevcrfanvLKSLGVKK--------GDRVAIYMPMIPELVIAMLAC 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   85 LYAGVI--AVPA-YPPESARrhhqERllsiIADAEPRLVLTtAD--LR--EPL-LQMNAQLSAANAPQL---LCVDQLDP 153
Cdd:cd05966  130 ARIGAVhsVVFAgFSAESLA----DR----INDAQCKLVIT-ADggYRggKVIpLKEIVDEALEKCPSVekvLVVKRTGG 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  154 AV----------------AEAWDEP-QVRPEHIAFLQYTSGSTALPKGVQVSH-GNLVANEVLIRRGFGIGADDVivswl 215
Cdd:cd05966  201 EVpmtegrdlwwhdlmakQSPECEPeWMDSEDPLFILYTSGSTGKPKGVVHTTgGYLLYAATTFKYVFDYHPDDI----- 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  216 plY---HDMGLIGG----LLQPIFSGVPCVLM--SPRYflERPVRWLEAISQYGGTVSGGPDFAYRLCSeRVAESALQRL 286
Cdd:cd05966  276 --YwctADIGWITGhsyiVYGPLANGATTVMFegTPTY--PDPGRYWDIVEKHKVTIFYTAPTAIRALM-KFGDEWVKKH 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  287 DLSGWRVAFSGSEPIRQDSLERFAEKFAASRfdassffaC-----YGLAEatlfvTGGQRGQGIPALavdgealarnrIA 361
Cdd:cd05966  351 DLSSLRVLGSVGEPINPEAWMWYYEVIGKER--------CpivdtWWQTE-----TGGIMITPLPGA-----------TP 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  362 EGEGSvlmcCGRSQPEHAVLIVDAASGEVLGDDN----VGEIWaagPSIAHGYWRNPEASAKAFVERDGRTWLrTGDlGF 437
Cdd:cd05966  407 LKPGS----ATRPFFGIEPAILDEEGNEVEGEVEgylvIKRPW---PGMARTIYGDHERYEDTYFSKFPGYYF-TGD-GA 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  438 LRD--GELFVTGRLKDMLIVRGHNLYPQDIERTV-------ESEV---PSARKGR-VAAFAVTVDGEEgigiaaeigrgv 504
Cdd:cd05966  478 RRDedGYYWITGRVDDVINVSGHRLGTAEVESALvahpavaEAAVvgrPHDIKGEaIYAFVTLKDGEE------------ 545
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597620  505 qksvPAQELIDSIRQAVAE-----AyqeAPKVValLNPGALPKTSSGKLQR 550
Cdd:cd05966  546 ----PSDELRKELRKHVRKeigpiA---TPDKI--QFVPGLPKTRSGKIMR 587
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
165-456 1.27e-11

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 70.92  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   165 RPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGF-GIGADDVIVSWLPLYHDMGL------------IG------ 225
Cdd:PLN02387  248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELaaesvmaavgaaIGygsplt 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   226 ----------------GLLQP-IFSGVPCVLMSPRYFLERPVrwleaiSQYGGTVSGGPDFAY--RLCS----------- 275
Cdd:PLN02387  328 ltdtsnkikkgtkgdaSALKPtLMTAVPAILDRVRDGVRKKV------DAKGGLAKKLFDIAYkrRLAAiegswfgawgl 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   276 ERVAESALQ----RLDLSGwRVAF--SGSEPIRQDSlERFAEkfaasrfdassffACYGlaeatlfVTGGQrGQGIPala 349
Cdd:PLN02387  402 EKLLWDALVfkkiRAVLGG-RIRFmlSGGAPLSGDT-QRFIN-------------ICLG-------APIGQ-GYGLT--- 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   350 vdgEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNV---GEIWAAGPSIAHGYWRNPEASAKAF-VERD 425
Cdd:PLN02387  456 ---ETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVYkVDER 532
                         330       340       350
                  ....*....|....*....|....*....|..
gi 15597620   426 GRTWLRTGDLG-FLRDGELFVTGRLKDmlIVR 456
Cdd:PLN02387  533 GMRWFYTGDIGqFHPDGCLEIIDRKKD--IVK 562
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
3838-4152 1.34e-11

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 70.74  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3838 RLLVWDEIQQGEGAEHDPQVYsGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL-ELDENDVIAQTAsqsfDI 3916
Cdd:TIGR02188  214 RDVWWHDLMAKASAYCEPEPM-DSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVfDIKDGDIFWCTA----DV 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3917 SvW-----QFLAAPLF-GARVAIVPNAVAHDPQGLLAHVGEQ-GITVLESVPSLIQGMLAE-----ERQALDGLRWMLPT 3984
Cdd:TIGR02188  289 G-WitghsYIVYGPLAnGATTVMFEGVPTYPDPGRFWEIIEKhKVTIFYTAPTAIRALMRLgdewvKKHDLSSLRLLGSV 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   3985 GEAMPPElARQWLKRYpriglvnaYGPAECSDDVAFFRVDLASTESTYLPIGSPTD--NNRLYLLGAGA----DDAFELV 4058
Cdd:TIGR02188  368 GEPINPE-AWMWYYKV--------VGKERCPIVDTWWQTETGGIMITPLPGATPTKpgSATLPFFGIEPavvdEEGNPVE 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4059 PLGAVGELCVAGT--GVGRGYVGDPLRTAQAFVPHpfgAPGerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGE 4136
Cdd:TIGR02188  439 GPGEGGYLVIKQPwpGMLRTIYGDHERFVDTYFSP---FPG--YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAE 513
                          330
                   ....*....|....*.
gi 15597620   4137 IEARLHERADVREAAV 4152
Cdd:TIGR02188  514 IESALVSHPAVAEAAV 529
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2710-2768 1.36e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.20  E-value: 1.36e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620   2710 QQLAGVWREVLNV--ERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQS 2768
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARlEEEFGVEIPPSDLFEHPTLAE 62
PLN02246 PLN02246
4-coumarate--CoA ligase
3718-4232 1.48e-11

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 70.39  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFE--AQVAAHPQRIAASCLEQrWSYAELNRRANRLGHALRAAGVGIDQPVALL----AERGLDLLGmivgSFKAGAGYL 3791
Cdd:PLN02246   29 CFErlSEFSDRPCLIDGATGRV-YTYADVELLSRRVAAGLHKLGIRQGDVVMLLlpncPEFVLAFLG----ASRRGAVTT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3792 PLDPGHPTQRLTRIVELSRTLVLVcTQACREQALALFDELG-----CVDRPR---LLVWDEIQQGEGAEhdPQVYSGPQN 3863
Cdd:PLN02246  104 TANPFYTPAEIAKQAKASGAKLII-TQSCYVDKLKGLAEDDgvtvvTIDDPPegcLHFSELTQADENEL--PEVEISPDD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3864 LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKV----PYLELDENDVIAqTASQSFDI----SVwqFLAAPLFGARVAIVP 3935
Cdd:PLN02246  181 VVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVdgenPNLYFHSDDVIL-CVLPMFHIyslnSV--LLCGLRVGAAILIMP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3936 NavaHDPQGLLAHVGEQGITVLESVPSLIQGML---AEERQALDGLRWMLPTGEAMPPELARQWLKRYPRIGLVNAYGPA 4012
Cdd:PLN02246  258 K---FEIGALLELIQRHKVTIAPFVPPIVLAIAkspVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4013 EC----SDDVAF----FRVDLASTestylpiGSPTDNNRLYLLGAgadDAFELVPLGAVGELCVAGTGVGRGYVGDPLRT 4084
Cdd:PLN02246  335 EAgpvlAMCLAFakepFPVKSGSC-------GTVVRNAELKIVDP---ETGASLPRNQPGEICIRGPQIMKGYLNDPEAT 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4085 AQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYL 4163
Cdd:PLN02246  405 ANTI-------DKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVvPMKDEVAGEVP 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  4164 VGYLVPGETPRSSADSPAGLMVEQGAWFERIKQQlradlpdYMVplhwlvlDRMPLNANGKLDRKALPA 4232
Cdd:PLN02246  478 VAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKV-------FFV-------DSIPKAPSGKILRKDLRA 532
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1641-1700 1.49e-11

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 62.20  E-value: 1.49e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620   1641 RRIAAIWSEVLGLP--RVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELEA 1700
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3720-4230 1.63e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 70.45  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3720 EAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPT 3799
Cdd:PRK06710   31 EQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3800 QRLTRIVELSRTLVLVCT-----QACREQALALFDELgCVDR-------PRLLVWDEIQQGEG----------------- 3850
Cdd:PRK06710  111 RELEYQLHDSGAKVILCLdlvfpRVTNVQSATKIEHV-IVTRiadflpfPKNLLYPFVQKKQSnlvvkvsesetihlwns 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3851 --AEHDP--QVYSGPQN-LAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYL----ELDEN--------DVIAQTAsqS 3913
Cdd:PRK06710  190 veKEVNTgvEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLynckEGEEVvlgvlpffHVYGMTA--V 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3914 FDISVWQflaaplfGARVAIVPNavaHDPQGLLAHVGEQGITVLESVPSLIQGMLAE---ERQALDGLRWMLPTGEAMPP 3990
Cdd:PRK06710  268 MNLSIMQ-------GYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpllKEYDISSIRACISGSAPLPV 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3991 ELARQWlKRYPRIGLVNAYGPAECSddvaffrvdlASTESTYL-------PIGSPTDNN--RLYLLGAGaddafELVPLG 4061
Cdd:PRK06710  338 EVQEKF-ETVTGGKLVEGYGLTESS----------PVTHSNFLwekrvpgSIGVPWPDTeaMIMSLETG-----EALPPG 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4062 AVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgapGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARL 4141
Cdd:PRK06710  402 EIGEIVVKGPQIMKGYWNKPEETAAVL--------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4142 HERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSAdspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPLN 4220
Cdd:PRK06710  474 YEHEKVQEVVTiGVPDPYRGETVKAFVVLKEGTECSE--------------EELNQFARKYLAAYKVPKVYEFRDELPKT 539
                         570
                  ....*....|
gi 15597620  4221 ANGKLDRKAL 4230
Cdd:PRK06710  540 TVGKILRRVL 549
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
17-556 1.88e-11

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 70.22  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   17 RRAVQEPERLALRFlAEDDGEGVVLSYRDL-DLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAy 95
Cdd:cd05970   25 AMAKEYPDKLALVW-CDDAGEERIFTFAELaDYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   96 ppesarrHHQERLLSI---IADAEPRLVLTTAdlrEPLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDE---------PQ 163
Cdd:cd05970  103 -------THQLTAKDIvyrIESADIKMIVAIA---EDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDfrkliknasPD 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  164 VRPEH---------IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVS----------WLPLYHDMglI 224
Cdd:cd05970  173 FERPTansypcgedILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTvadtgwgkavWGKIYGQW--I 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  225 GGllqpifsgvpCVLMSPRYFLERPVRWLEAISQYGGTVSGGPDFAYRLcserVAESALQRLDLSGWRVAFSGSEPIRQD 304
Cdd:cd05970  251 AG----------AAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRF----LIREDLSRYDLSSLRYCTTAGEALNPE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  305 SLERFAEKFAASRFDAssffacYGLAEATLFVTG--------GQRGQGIPALAVDgeALARNriaegegsvlmccGRSQP 376
Cdd:cd05970  317 VFNTFKEKTGIKLMEG------FGQTETTLTIATfpwmepkpGSMGKPAPGYEID--LIDRE-------------GRSCE 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  377 --EHAVLIVDAASGEVLGddnvgeiwaagpsIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFL-RDGELFVTGRLKDML 453
Cdd:cd05970  376 agEEGEIVIRTSKGKPVG-------------LFGGYYKDAEKTAEVW--HDG--YYHTGDAAWMdEDGYLWFVGRTDDLI 438
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  454 IVRGHNLYPQDIERTVESEvPSarkgrVAAFAVT--VDGEEGIGIAAEI--GRGVQksvPAQELIDSIRQAVAE--AYQE 527
Cdd:cd05970  439 KSSGYRIGPFEVESALIQH-PA-----VLECAVTgvPDPIRGQVVKATIvlAKGYE---PSEELKKELQDHVKKvtAPYK 509
                        570       580
                 ....*....|....*....|....*....
gi 15597620  528 APKVVALLNpgALPKTSSGKLQRSACRLR 556
Cdd:cd05970  510 YPRIVEFVD--ELPKTISGKIRRVEIRER 536
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
2213-2625 2.40e-11

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 69.78  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2213 SYAELDARSNRLARVLRSHGVGPEVRVG-LA--LERSLEMVVGLLAIlkaGGAYVPLDPEYPLERLQYMI---EDSGVRL 2286
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVAtIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVVIT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2287 LLSHAALFEAL-GELPAgVARWCLEEDgpalDAEDPAP-----------LAALSG--------PQHQAYLIYTSGSTGKP 2346
Cdd:PRK06018  118 DLTFVPILEKIaDKLPS-VERYVVLTD----AAHMPQTtlknavayeewIAEADGdfawktfdENTAAGMCYTSGTTGDP 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2347 KGVAVSHGEIAMHC--AAVIECFGMRAEDCEL--------HFYSINFDAASErllapllcGARVVLRAQGQWGAeEICEL 2416
Cdd:PRK06018  193 KGVLYSHRSNVLHAlmANNGDALGTSAADTMLpvvplfhaNSWGIAFSAPSM--------GTKLVMPGAKLDGA-SVYEL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2417 IRAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTgehlQRIRQAFAP--ASFFNAYGPTETVVM-PLACL 2492
Cdd:PRK06018  264 LDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPhLKMVVCGGSAMP----RSMIKAFEDmgVEVRHAWGMTEMSPLgTLAAL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2493 APE------------RLEEGAASvpigsvVGARVAYILDADLALVPQG-ATGELYVGGAGLARGYH--ERPALSAERFvp 2557
Cdd:PRK06018  340 KPPfsklpgdarldvLQKQGYPP------FGVEMKITDDAGKELPWDGkTFGRLKVRGPAVAAAYYrvDGEILDDDGF-- 411
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2558 dpfaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP 2625
Cdd:PRK06018  412 ----------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP 469
PRK08315 PRK08315
AMP-binding domain protein; Validated
2184-2369 2.56e-11

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 69.84  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2184 LQDTLHGLFAARVAASPQAPALTFAGQTL--SYAELDARSNRLARVLRSHGVGPEVRVGL-ALERSlEMVVGLLAILKAG 2260
Cdd:PRK08315   14 LEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIwAPNVP-EWVLTQFATAKIG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2261 GAYVPLDPEYPLERLQYMIEDSGVRLLLS----------------------------HAALFEAL-------GELPAGVA 2305
Cdd:PRK08315   93 AILVTINPAYRLSELEYALNQSGCKALIAadgfkdsdyvamlyelapelatcepgqlQSARLPELrrviflgDEKHPGML 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2306 RWC-LEEDGPALDAEDPAPLAA-LSgpQHQAYLI-YTSGSTGKPKGVAVSHGEI---------AMH-------CAAV--I 2364
Cdd:PRK08315  173 NFDeLLALGRAVDDAELAARQAtLD--PDDPINIqYTSGTTGFPKGATLTHRNIlnngyfigeAMKlteedrlCIPVplY 250

                  ....*
gi 15597620  2365 ECFGM 2369
Cdd:PRK08315  251 HCFGM 255
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
3867-4152 2.58e-11

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 68.45  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3867 VIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDViaqtasqsfdisvwqFLAA-PLF--------------GARV 3931
Cdd:cd17637    5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADV---------------YLNMlPLFhiaglnlalatfhaGGAN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3932 AIVPnavAHDPQGLLAHVGEQGITVLESVPSlIQGMLAEERQA----LDGLRwmLPTG-EAmpPELARQWLKRYPRIGLV 4006
Cdd:cd17637   70 VVME---KFDPAEALELIEEEKVTLMGSFPP-ILSNLLDAAEKsgvdLSSLR--HVLGlDA--PETIQRFEETTGATFWS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4007 nAYGPAECSDDVAFFRVDLASTEStylpiGSPTDNNRLYLlgagADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQ 4086
Cdd:cd17637  142 -LYGQTETSGLVTLSPYRERPGSA-----GRPGPLVRVRI----VDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAY 211
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4087 AFvphpfgapgeR--LYRTGDLARRRADGVLEYVGRIDHQ--VKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:cd17637  212 TF----------RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCV 271
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
584-657 3.00e-11

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 62.18  E-value: 3.00e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  584 DELLARIGEIWKARLGV--AQVAPRDHFFL-LGGNSIGAAQVVAQVRDSLGVALDLRQLFEAPTLQAFSATVARQLA 657
Cdd:COG0236    4 EELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
41-548 3.14e-11

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 68.97  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   41 LSYRDLDLRARSIAA--ALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPpesarrhhQERLLSIIADA 115
Cdd:cd17648   13 LTYRELNERANRLAHylLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPidpSYP--------DERIQFILEDT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  116 EPRLVLTTadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvrPEHIAFLQYTSGSTALPKGVQVSHGNLVAN 195
Cdd:cd17648   85 GARVVITN------------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  196 EV-LIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPRyFLERPVRWLEAISQYGGT-VSGGPdfayrl 273
Cdd:cd17648  123 RTsLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDE-MRFDPDRFYAYINREKVTyLSGTP------ 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  274 cservaeSALQRLDLSgwrvafsgsepiRQDSLERF---AEKFAASRFDA--SSF----FACYGLAEATLFvtggqrgqg 344
Cdd:cd17648  196 -------SVLQQYDLA------------RLPHLKRVdaaGEEFTAPVFEKlrSRFagliINAYGPTETTVT--------- 247
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  345 ipalavdgealARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEV-LGddNVGEIWAAGPSIAHGYWRNPEASAKAFVE 423
Cdd:cd17648  248 -----------NHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVpVG--AVGELYLGGDGVARGYLNRPELTAERFLP 314
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  424 ---------RDGR--TWLRTGDLG-FLRDGELFVTGRlKDMLI-VRGHNLYPQDIERTVeSEVPSARKGRVAAFAVTVDG 490
Cdd:cd17648  315 npfqteqerARGRnaRLYKTGDLVrWLPSGELEYLGR-NDFQVkIRGQRIEPGEVEAAL-ASYPGVRECAVVAKEDASQA 392
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  491 EEGIgIAAEIGRGV--QKSVPAQELIDSIRQAVAEaYQEAPKVVALLNpgaLPKTSSGKL 548
Cdd:cd17648  393 QSRI-QKYLVGYYLpePGHVPESDLLSFLRAKLPR-YMVPARLVRLEG---IPVTINGKL 447
PRK07867 PRK07867
acyl-CoA synthetase; Validated
3736-4232 3.51e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 69.32  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3736 EQRWSYAELNRRANRLGHALRAAgVGIDQP--VALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLV 3813
Cdd:PRK07867   26 DSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3814 LVCTQACREQALALFDELGCVDRPRLLVWDEIQQGEGAEHDPQVYSgPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLS 3893
Cdd:PRK07867  105 VLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRVAD-PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVM 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3894 KVPYLELDENDVIaqtasqsfdisvwqFLAAPLF---------------GARVAIVPNAVAhdpQGLLAHVGEQGITVLE 3958
Cdd:PRK07867  184 LAQRFGLGPDDVC--------------YVSMPLFhsnavmagwavalaaGASIALRRKFSA---SGFLPDVRRYGATYAN 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3959 SVPSLIQGMLAEERQALDG---LRWMLPTgEAMPPELARqWLKRYPrIGLVNAYGPAECSddVAFFRVDLASTEStylpI 4035
Cdd:PRK07867  247 YVGKPLSYVLATPERPDDAdnpLRIVYGN-EGAPGDIAR-FARRFG-CVVVDGFGSTEGG--VAITRTPDTPPGA----L 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4036 GSPTDNNRLYLLGAGA-------DDAFELVPLGAVGELC-VAGTGVGRGYVGDPlrtaqafvphpfGAPGERL----YRT 4103
Cdd:PRK07867  318 GPLPPGVAIVDPDTGTecppaedADGRLLNADEAIGELVnTAGPGGFEGYYNDP------------EADAERMrggvYWS 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4104 GDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSADSPAG 4182
Cdd:PRK07867  386 GDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVyAVPDPVVGDQVMAALVLAPGAKFDPDAFAE 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620  4183 LMVEQgawferikqqlrADLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK07867  466 FLAAQ------------PDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
3867-4152 3.82e-11

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 67.71  E-value: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3867 VIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAqTASQSFDISVWQF-LAAPLFGARVAIVPNAvahDPQGL 3945
Cdd:cd17636    5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFL-NSGPLFHIGTLMFtLATFHAGGTNVFVRRV---DAEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3946 LAHVGEQGITVLESVPSLIQGML---AEERQALDGLRWM--LPTGEAMPPELARQWlKRYPRiglvnAYGPAECSDDVAF 4020
Cdd:cd17636   81 LELIEAERCTHAFLLPPTIDQIVelnADGLYDLSSLRSSpaAPEWNDMATVDTSPW-GRKPG-----GYGQTEVMGLATF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4021 --FRVDLASTEstylpiGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapgE 4098
Cdd:cd17636  155 aaLGGGAIGGA------GRPSPLVQVRIL----DEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--------G 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597620 4099 RLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:cd17636  217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
PRK07788 PRK07788
acyl-CoA synthetase; Validated
19-550 4.14e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 69.19  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    19 AVQEPERLALrflAEDDGEgvvLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PA 94
Cdd:PRK07788   59 ARRAPDRAAL---IDERGT---LTYAELDEQSNALARGLLALgVRAGDGVAVLARNHRGFVLALYAAGKVGARIIllnTG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    95 YPP----ESARRhhqERLLSIIADAE--PRLVLTTADL-REPLLQMNAQLSAANAPQllcVDQLDPAVAEAWDEPQVRPE 167
Cdd:PRK07788  133 FSGpqlaEVAAR---EGVKALVYDDEftDLLSALPPDLgRLRAWGGNPDDDEPSGST---DETLDDLIAGSSTAPLPKPP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   168 -HIAFLQYTSGSTALPKGVQVSHGNLVAN--EVLIRRGFGIGADDVIVSwlPLYHDMGLigGLLQPIFsGVPCVLMSPRY 244
Cdd:PRK07788  207 kPGGIVILTSGTTGTPKGAPRPEPSPLAPlaGLLSRVPFRAGETTLLPA--PMFHATGW--AHLTLAM-ALGSTVVLRRR 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   245 FleRPVRWLEAISQYGGT---VSggPDFAYRLCseRVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAs 321
Cdd:PRK07788  282 F--DPEATLEDIAKHKATalvVV--PVMLSRIL--DLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNL- 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   322 sffacYGLAEATLfvtggqrgqgipALAVDGEALARNriaegEGSVlmccGRSQPEHAVLIVDAASGEVLGDDnVGEIWA 401
Cdd:PRK07788  355 -----YGSTEVAF------------ATIATPEDLAEA-----PGTV----GRPPKGVTVKILDENGNEVPRGV-VGRIFV 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   402 AGPSIAHGYW--RNPEasakafvERDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIErtvesEVPSARK 478
Cdd:PRK07788  408 GNGFPFEGYTdgRDKQ-------IIDG--LLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVE-----DLLAGHP 473
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   479 GRVAAFAVTVDGEE-GIGIAAEIGRGVQKSVPAQELIDSIRQAVAEayQEAPKVVALLNpgALPKTSSGKLQR 550
Cdd:PRK07788  474 DVVEAAVIGVDDEEfGQRLRAFVVKAPGAALDEDAIKDYVRDNLAR--YKVPRDVVFLD--ELPRNPTGKVLK 542
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
1278-1560 4.23e-11

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 68.64  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1278 TSGSTGQPKGVGNTHAALaERLQWMQA-TYTLDG---DDVLMqkapVSFDVSVWECFWPLVTGCR----LVLAA-PGehr 1348
Cdd:COG1541   91 SSGTTGKPTVVGYTRKDL-DRWAELFArSLRAAGvrpGDRVQ----NAFGYGLFTGGLGLHYGAErlgaTVIPAgGG--- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1349 DPARLVELVRQFGVTTLHFVPP-LLQL--FIDEPGV-AACGSLRRLFSGGEALPAELRNRVLQRLPAVAlHNRYGPTETA 1424
Cdd:COG1541  163 NTERQLRLMQDFGPTVLVGTPSyLLYLaeVAEEEGIdPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKA-YDIYGLTEVG 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1425 INVThWQCRAEDG----ErspigrplGNVVCRVLDAE-FNLLPAGVAGELCIGGLG-----LARgylgrpalsaerfvad 1494
Cdd:COG1541  242 PGVA-YECEAQDGlhiwE--------DHFLVEIIDPEtGEPVPEGEEGELVVTTLTkeampLIR---------------- 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1495 pfsaagerlYRTGDRARWNAD------------GVleyLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQA--VVVIREG 1560
Cdd:COG1541  297 ---------YRTGDLTRLLPEpcpcgrthprigRI---LGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREG 364
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
2213-2625 4.89e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 68.96  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2213 SYAELDARSNRLARVLRSHGVGPEVRVG-LALE--RSLEMVVGllaILKAGGAYVPLDPEYPLERLQYMI---EDSGVRL 2286
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALGVEPGDRVGtLAWNgyRHLEAYYG---VSGSGAVCHTINPRLFPEQIAYIVnhaEDRYVLF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2287 LLSHAALFEALGELPAGVARWCLEEDGPALDAeDPAPL---AALSGPQHQAY------------LIYTSGSTGKPKGVAV 2351
Cdd:PRK07008  118 DLTFLPLVDALAPQCPNVKGWVAMTDAAHLPA-GSTPLlcyETLVGAQDGDYdwprfdenqassLCYTSGTTGNPKGALY 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2352 SHGEIAMHC--AAVIECFGMRAEDCEL------HF--YSINFDAAserllaplLCGARVVLRAQGQWGAeEICELIRAEG 2421
Cdd:PRK07008  197 SHRSTVLHAygAALPDAMGLSARDAVLpvvpmfHVnaWGLPYSAP--------LTGAKLVLPGPDLDGK-SLYELIEAER 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2422 VSILGFTPSYGSQLAQWLESQGRQL-PVRMCITGGEALTGEHLQRIRQAFApASFFNAYGPTEtvVMPLACLApeRLEEG 2500
Cdd:PRK07008  268 VTFSAGVPTVWLGLLNHMREAGLRFsTLRRTVIGGSACPPAMIRTFEDEYG-VEVIHAWGMTE--MSPLGTLC--KLKWK 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2501 AASVPI----------GSVVGARVAYILDADLALVPQG--ATGELYVGGAGLARGYherpalsaerfvpdpFAAEGGRLY 2568
Cdd:PRK07008  343 HSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWVIDRY---------------FRGDASPLV 407
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597620  2569 R----TGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSP 2625
Cdd:PRK07008  408 DgwfpTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
3814-4120 4.99e-11

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 68.78  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3814 LVCTQACREQAL---ALFDELG-----------------CVDRPRLLVWDEI-QQGEGAEHDPqVYSGPQNLAYVIYTSG 3872
Cdd:cd05927   46 IISELACYAYSLvtvPLYDTLGpeaieyilnhaeisivfCDAGVKVYSLEEFeKLGKKNKVPP-PPPKPEDLATICYTSG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3873 STGLPKGVMVEQAGMLNNQLSKVPYLE----LDENDViaqtasqsfDIS------------VWQFLAaplFGARVAIVPN 3936
Cdd:cd05927  125 TTGNPKGVMLTHGNIVSNVAGVFKILEilnkINPTDV---------YISylplahifervvEALFLY---HGAKIGFYSG 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3937 avahDPQGLLAHVGEQGITVLESVPSLIQ-------------GMLAEE-------------------------------- 3971
Cdd:cd05927  193 ----DIRLLLDDIKALKPTVFPGVPRVLNriydkifnkvqakGPLKRKlfnfalnyklaelrsgvvraspfwdklvfnki 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3972 RQALDG-LRWMLPTGEAMPPELARqWLKRYPRIGLVNAYGPAECSDDVAFFRVDlastESTYLPIGSPTDNN--RL---- 4044
Cdd:cd05927  269 KQALGGnVRLMLTGSAPLSPEVLE-FLRVALGCPVLEGYGQTECTAGATLTLPG----DTSVGHVGGPLPCAevKLvdvp 343
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620 4045 ---YllgagadDAFELVPlgaVGELCVAGTGVGRGYVGDPLRTAQAFvphpfgaPGERLYRTGDLARRRADGVLEYVGR 4120
Cdd:cd05927  344 emnY-------DAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEAL-------DEDGWLHTGDIGEWLPNGTLKIIDR 405
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
691-970 5.64e-11

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 68.23  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  691 DPQSAAYNIPGGLRL--RGELDeaALRASFQRLVERHEALRTRFLERD-GAALQRIDERGEFAWQFVDLaalAEHERAAA 767
Cdd:cd19544   18 AEEGDPYLLRSLLAFdsRARLD--AFLAALQQVIDRHDILRTAILWEGlSEPVQVVWRQAELPVEELTL---DPGDDALA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  768 AAQRREAEAQQPFDLEKGPLLRVSLVRlDEQEHQLWVTL--HHIVADGWSLNLLLDEFSRLYAeacgGQPADLAPLeLHY 845
Cdd:cd19544   93 QLRARFDPRRYRLDLRQAPLLRAHVAE-DPANGRWLLLLlfHHLISDHTSLELLLEEIQAILA----GRAAALPPP-VPY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  846 AEFAAwqrQWLDAGEGARQLAYWRERLGD----TAP--VLELATDhprtarqASPAARYSLRVDEALARAIREAALDHE- 918
Cdd:cd19544  167 RNFVA---QARLGASQAEHEAFFREMLGDvdepTAPfgLLDVQGD-------GSDITEARLALDAELAQRLRAQARRLGv 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620  919 --ASVFMwllAAFQALLHRHSGQGEI--------RI-GVPSANRQrletqglVGFFINTLVLR 970
Cdd:cd19544  237 spASLFH---LAWALVLARCSGRDDVvfgtvlsgRMqGGAGADRA-------LGMFINTLPLR 289
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
1130-1556 5.76e-11

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 68.54  E-value: 5.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1130 LPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRD-----KGvgpDvRVAICAersPQLL---VGLLAIVKA 1201
Cdd:PRK08974   25 LVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNglglkKG---D-RVALMM---PNLLqypIALFGILRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1202 GGAYVPLDPDYPSERLAYMLADSGVELLLTQ---AHLFERLPGAEGVTPICLDSL------------------------- 1253
Cdd:PRK08974   98 GMIVVNVNPLYTPRELEHQLNDSGAKAIVIVsnfAHTLEKVVFKTPVKHVILTRMgdqlstakgtlvnfvvkyikrlvpk 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1254 -KLDNWPSQAPGLH-----------LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYT---LDGDDVLMQKA 1318
Cdd:PRK08974  178 yHLPDAISFRSALHkgrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpllHPGKELVVTAL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1319 PVS--FDVSVWECFWPLVTGCRLVLAAPgehRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAAC--GSLRRLFSGG 1394
Cdd:PRK08974  258 PLYhiFALTVNCLLFIELGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGG 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1395 EALPAELRNRvLQRLPAVALHNRYGPTETA--INVTHWQCRAEDGErspIGRPLGNVVCRVLDAEFNLLPAGVAGELCIG 1472
Cdd:PRK08974  335 MAVQQAVAER-WVKLTGQYLLEGYGLTECSplVSVNPYDLDYYSGS---IGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1473 GLGLARGYLGRPALSAErFVADPFSAagerlyrTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQ 1552
Cdd:PRK08974  411 GPQVMLGYWQRPEATDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482

                  ....
gi 15597620  1553 AVVV 1556
Cdd:PRK08974  483 VAAV 486
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
2210-2625 6.38e-11

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 68.60  E-value: 6.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRL--- 2286
Cdd:cd17641   10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVvia 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2287 --------LLSHAALFEALGEL----PAGVARWC---------LEEDGPALDAEDP----APLAALSgPQHQAYLIYTSG 2341
Cdd:cd17641   90 edeeqvdkLLEIADRIPSVRYViycdPRGMRKYDdprlisfedVVALGRALDRRDPglyeREVAAGK-GEDVAVLCTTSG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2342 STGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHF--------------------YSINFDAASERLLAPLL-CGARV 2400
Cdd:cd17641  169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVlplpwigeqmysvgqalvcgFIVNFPEEPETMMEDLReIGPTF 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2401 VLRAQGQWgaEEICELIRAE--------------GVSIL---------GFTPSYGSQLAQWLesqGRQL----------- 2446
Cdd:cd17641  249 VLLPPRVW--EGIAADVRARmmdatpfkrfmfelGMKLGlraldrgkrGRPVSLWLRLASWL---ADALlfrplrdrlgf 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2447 -PVRMCITGGEALTGEHLqrirqafapaSFFNA--------YGPTETVvmplaclaperleeGAASV-PIGSVVGARVAY 2516
Cdd:cd17641  324 sRLRSAATGGAALGPDTF----------RFFHAigvplkqlYGQTELA--------------GAYTVhRDGDVDPDTVGV 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2517 ILDAdlALVPQGATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRI-DHQVKIR 2595
Cdd:cd17641  380 PFPG--TEVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSD 450
                        490       500       510
                 ....*....|....*....|....*....|
gi 15597620 2596 GFRIELGEIEARLLEHPQVREALVLALDSP 2625
Cdd:cd17641  451 GTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
23-552 6.48e-11

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 68.27  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   23 PERLALRFLAEDdgegvvLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpesar 101
Cdd:cd17656    2 PDAVAVVFENQK------LTYRELNERSNQLARFLREKGVKKDSIVaIMMERSAEMIVGILGILKAGGAFVPIDP----- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  102 RHHQERLLSIIADAEPRLVLTTADLREPLLQmnaqlsaaNAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTAL 181
Cdd:cd17656   71 EYPEERRIYIMLDSGVRVVLTQRHLKSKLSF--------NKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  182 PKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMgliggLLQPIFSGvpcvlmspryflerpvrWLeaisqYGG 261
Cdd:cd17656  143 PKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDV-----CYQEIFST-----------------LL-----SGG 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  262 TVsggpdfayrlcseRVAESALQRlDLSGWrVAFSGSEPIRQDSLERFAEKFAASRFDA-SSFFACygLAEAtlfVTGGQ 340
Cdd:cd17656  196 TL-------------YIIREETKR-DVEQL-FDLVKRHNIEVVFLPVAFLKFIFSEREFiNRFPTC--VKHI---ITAGE 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  341 RGQgIPALAVdgEALAR------NRIAEGEGSVL-MCCGRSQPEHA-------------VLIVDAAsGEVLGDDNVGEIW 400
Cdd:cd17656  256 QLV-ITNEFK--EMLHEhnvhlhNHYGPSETHVVtTYTINPEAEIPelppigkpisntwIYILDQE-QQLQPQGIVGELY 331
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  401 AAGPSIAHGYWRNPEASAKAFV----ERDGRTWlRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIErtvesevps 475
Cdd:cd17656  332 ISGASVARGYLNRQELTAEKFFpdpfDPNERMY-RTGDLArYLPDGNIEFLGRADHQVKIRGYRIELGEIE--------- 401
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  476 arkgrvaafaVTVDGEEGIGIAAEIGRGVQKS--------VPAQELIDS-IRQAVAEAYQEAPKVVALLNPGALPKTSSG 546
Cdd:cd17656  402 ----------AQLLNHPGVSEAVVLDKADDKGekylcayfVMEQELNISqLREYLAKQLPEYMIPSFFVPLDQLPLTPNG 471

                 ....*.
gi 15597620  547 KLQRSA 552
Cdd:cd17656  472 KVDRKA 477
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
13-552 8.33e-11

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 67.85  E-value: 8.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   13 QALRRRAVQEPERLALRFlaeddgEGVVLSYRDLDLRARSIAAALQAHAQLGDRAV-LLFPSGPDYVAAFFGCLYAG--- 88
Cdd:cd17644    4 QLFEEQVERTPDAVAVVF------EDQQLTYEELNTKANQLAHYLQSLGVKSESLVgICVERSLEMIIGLLAILKAGgay 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   89 VIAVPAYPpesarrhhQERLLSIIADAEPRLVLTtadlrepllqmnaqlsaanapqllcvdqldpavaeawdepqvRPEH 168
Cdd:cd17644   78 VPLDPNYP--------QERLTYILEDAQISVLLT------------------------------------------QPEN 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  169 IAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMsPRYFLER 248
Cdd:cd17644  108 LAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLVLR-PEEMRSS 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  249 PVRWLEAISQYGGTVSggpDFAYRLCSERVAESALQRLDL-SGWRVAFSGSEPIRQDSLERFAEKFAasrfDASSFFACY 327
Cdd:cd17644  186 LEDFVQYIQQWQLTVL---SLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVG----NFIQLINVY 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  328 GLAEATLFVTggqrgqgIPALAVDGEAlARNRIAegegsvlmcCGRSQPEHAVLIVDAASGEV-LGddNVGEIWAAGPSI 406
Cdd:cd17644  259 GPTEATIAAT-------VCRLTQLTER-NITSVP---------IGRPIANTQVYILDENLQPVpVG--VPGELHIGGVGL 319
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  407 AHGYWRNPEASAKAFV-----ERDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIErTVESEVPSARKgr 480
Cdd:cd17644  320 ARGYLNRPELTAEKFIshpfnSSESERLYKTGDLArYLPDGNIEYLGRIDNQVKIRGFRIELGEIE-AVLSQHNDVKT-- 396
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  481 vaafAVTVDGEEGIGIAaeigRGVQKSVPAQELIDSI---RQAVAEAYQE--APKVVALLNpgALPKTSSGKLQRSA 552
Cdd:cd17644  397 ----AVVIVREDQPGNK----RLVAYIVPHYEESPSTvelRQFLKAKLPDymIPSAFVVLE--ELPLTPNGKIDRRA 463
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
1270-1633 8.72e-11

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 68.58  E-value: 8.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1270 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVLMQKAPV--SFDVSVwECFWPLVTGCRLVLAAPGEH 1347
Cdd:PRK08043  365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1348 RdpaRLV-ELVRQ------FGVTTL-----HFVPPLlqlfidepgvaACGSLRRLFSGGEALpAELRNRVLQRLPAVALH 1415
Cdd:PRK08043  444 Y---RIVpELVYDrnctvlFGTSTFlgnyaRFANPY-----------DFARLRYVVAGAEKL-QESTKQLWQDKFGLRIL 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1416 NRYGPTETA----INVthwqcraedgersPIGRPLGNVVCRVLDAEFNLLP-AGVA--GELCIGGLGLARGYL--GRP-- 1484
Cdd:PRK08043  509 EGYGVTECApvvsINV-------------PMAAKPGTVGRILPGMDARLLSvPGIEqgGRLQLKGPNIMNGYLrvEKPgv 575
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1485 --ALSAErfvadpfSAAGER---LYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEI-QARLLAQPGVAQAVVVIR 1558
Cdd:PRK08043  576 leVPTAE-------NARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVeQLALGVSPDKQHATAIKS 648
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  1559 EGVAGSQLVGYYTgavgaEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQREHV 1633
Cdd:PRK08043  649 DASKGEALVLFTT-----DSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQHD 718
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
2212-2587 9.18e-11

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 68.01  E-value: 9.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2212 LSYAELDARSNRLARVLRSHGV--GPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS 2289
Cdd:cd05927    6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 HAAL-------FEALGElpagvarwcleedgpalDAEDPAPLAAlsgPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAA 2362
Cdd:cd05927   86 DAGVkvysleeFEKLGK-----------------KNKVPPPPPK---PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2363 VIECFG----MRAEDCEL------HFYsinfdaasERL-LAPLLC-GARVvlraqGQWG------AEEICEL-------- 2416
Cdd:cd05927  146 VFKILEilnkINPTDVYIsylplaHIF--------ERVvEALFLYhGAKI-----GFYSgdirllLDDIKALkptvfpgv 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2417 ----------IRAeGVSILG------FTPSYGSQLAQWLESQGRQLP-----------------VRMCITGGEALTGEHL 2463
Cdd:cd05927  213 prvlnriydkIFN-KVQAKGplkrklFNFALNYKLAELRSGVVRASPfwdklvfnkikqalggnVRLMLTGSAPLSPEVL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2464 QRIRQAFApASFFNAYGPTEtvvmplaCLAPerleeGAASVP----IGSvVGARVAYIlDADLALVPQ--------GATG 2531
Cdd:cd05927  292 EFLRVALG-CPVLEGYGQTE-------CTAG-----ATLTLPgdtsVGH-VGGPLPCA-EVKLVDVPEmnydakdpNPRG 356
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2532 ELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGR 2587
Cdd:cd05927  357 EVCIRGPNVFSGYYKDPEKTAEALDEDGW-------LHTGDIGEWLPNGTLKIIDR 405
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
2831-3045 1.16e-10

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 67.08  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2831 LQRLVEQHDALRLAFRqvdgeWLAQHRP----LREQELLWH-VPVQSFDECAE----LFAKAQRSLDLEQGPLLRAVLVD 2901
Cdd:cd19544   45 LQQVIDRHDILRTAIL-----WEGLSEPvqvvWRQAELPVEeLTLDPGDDALAqlraRFDPRRYRLDLRQAPLLRAHVAE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2902 GPAGEQRLL-LAIHHLVVDGVSWRVLLEDLQqvyrQFAEGAEPALPAKTSaFRDWAGrlQAYAGSESLREElGWWQARLG 2980
Cdd:cd19544  120 DPANGRWLLlLLFHHLISDHTSLELLLEEIQ----AILAGRAAALPPPVP-YRNFVA--QARLGASQAEHE-AFFREMLG 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2981 GqpVEWPC-----DRPQGDNREalAESVSLRLDPQRTRQLLQQA------PAAyrtqvndLLLTALARVLCRWSGQ 3045
Cdd:cd19544  192 D--VDEPTapfglLDVQGDGSD--ITEARLALDAELAQRLRAQArrlgvsPAS-------LFHLAWALVLARCSGR 256
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
41-498 1.80e-10

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 66.68  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   41 LSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAvpayppesarrhhqerllsiiadaeprl 119
Cdd:cd05939    4 WTFRELNEYSNKVANFFQAQgYRSGDVVALFMENRLEFVALWLGLAKIGVET---------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  120 VLTTADLREPLLQMNAQLSAANApqlLCVDQLDPAVAEAWDEPQVRP----EHIAFLQYTSGSTALPKGVQVSHGNLVAN 195
Cdd:cd05939   56 ALINSNLRLESLLHCITVSKAKA---LIFNLLDPLLTQSSTEPPSQDdvnfRDKLFYIYTSGTTGLPKAAVIVHSRYYRI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  196 EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MSPRYFLERPVRWLEAISQYGGTVSggpdfAYR 272
Cdd:cd05939  133 AAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIrkkFSASNFWDDCVKYNCTIVQYIGEIC-----RYL 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  273 LCSERVAESALQRLdlsgwRVAFSGSepIRQDSLERFaekfaASRFDASSFFACYGLAEATLFVTGgqrgqgipalaVDG 352
Cdd:cd05939  208 LAQPPSEEEQKHNV-----RLAVGNG--LRPQIWEQF-----VRRFGIPQIGEFYGATEGNSSLVN-----------IDN 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  353 EALArnriaegegsvlmcCG---RSQPE-HAVLI--VDAASGEVLGDDN--------------VGEIWAAGPSIA-HGYw 411
Cdd:cd05939  265 HVGA--------------CGfnsRILPSvYPIRLikVDEDTGELIRDSDglcipcqpgepgllVGKIIQNDPLRRfDGY- 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  412 RNPEASAKAFVerdgRTWLRTGDLGFL------RD--GELFVTGRLKDMLIVRGHNLYPQDIERTVEsevPSARKGRVAA 483
Cdd:cd05939  330 VNEGATNKKIA----RDVFKKGDSAFLsgdvlvMDelGYLYFKDRTGDTFRWKGENVSTTEVEGILS---NVLGLEDVVV 402
                        490
                 ....*....|....*.
gi 15597620  484 FAVTVDGEEG-IGIAA 498
Cdd:cd05939  403 YGVEVPGVEGrAGMAA 418
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
1365-1631 1.88e-10

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 66.56  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1365 LHFVPPLLQLFIDEPGvaacGSLRR----LFSGGEALPAELRNRVLQRLPaVALhnRYGPTETAINVThwQCRAED---G 1437
Cdd:PRK07445  211 LSLVPTQLQRLLQLRP----QWLAQfrtiLLGGAPAWPSLLEQARQLQLR-LAP--TYGMTETASQIA--TLKPDDflaG 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1438 ERSpIGRPLGNVVCRvldaefnlLPAGVAGELCIGGLGLARGYLgrPALSAERfvadpfsaageRLYRTGDRARWNADGV 1517
Cdd:PRK07445  282 NNS-SGQVLPHAQIT--------IPANQTGNITIQAQSLALGYY--PQILDSQ-----------GIFETDDLGYLDAQGY 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1518 LEYLGRLDQQVKLRGFRIEPEEIQARLLAQpGVAQAVVVIreGVA----GSQLVGYYTGAVGAEAEAEqnqrLRAALQAE 1593
Cdd:PRK07445  340 LHILGRNSQKIITGGENVYPAEVEAAILAT-GLVQDVCVL--GLPdphwGEVVTAIYVPKDPSISLEE----LKTAIKDQ 412
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 15597620  1594 LPEYMVPTQLMRLAQMPLGPSGKLDTRALPEPVWQQRE 1631
Cdd:PRK07445  413 LSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
1155-1617 2.64e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 66.56  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1155 GYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH 1234
Cdd:PRK07768   31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1235 L------FERLP---GAEGVTPICLDSLkldnWPSQAPGLHLHG-DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQA 1304
Cdd:PRK07768  111 AvvvgepFLAAApvlEEKGIRVLTVADL----LAADPIDPVETGeDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1305 TYTLDGD-DVLMQKAPVSFDVSVWECFW-PLVTGCRLVLAAPGEH-RDPARLVELVRQFGVTTL---HFVPPLLQLFI-- 1376
Cdd:PRK07768  187 AAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPMDFlRDPLLWAELISKYRGTMTaapNFAYALLARRLrr 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1377 -DEPGVAACGSLRRLFSGGEAL-PAELRNRVLQ----RLPAVALHNRYGPTETAINVTHWQC------------------ 1432
Cdd:PRK07768  267 qAKPGAFDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPEAILPAYGMAEATLAVSFSPCgaglvvdevdadllaalr 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1433 RAEDGERSPI------GRPLGNVVCRVLDAEFNLLPAGVAGELCIGGLGLARGYLgrpalsaerfVADPFSAAGERL--Y 1504
Cdd:PRK07768  347 RAVPATKGNTrrlatlGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL----------TMDGFIPAQDADgwL 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1505 RTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQArllaqpgVAQAVVVIREGVAGSqlVGYYTG------AVGAE- 1577
Cdd:PRK07768  417 DTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIER-------AAARVEGVRPGNAVA--VRLDAGhsregfAVAVEs 487
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 15597620  1578 ---AEAEQNQRLRAALQAELPEY--MVPTQLMRLA--QMPLGPSGKL 1617
Cdd:PRK07768  488 nafEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLGpgSIPKTPSGKL 534
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3736-4217 2.72e-10

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 66.22  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAgylpldpghptqrltrIVELSRTLVlv 3815
Cdd:cd05940    1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA----------------VAALINYNL-- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3816 ctqacREQALAlfdelGCVD--RPRLLVWDeiqqgegaehdpqvysgpqnLAYVIYTSGSTGLPKGVMVEQ--------- 3884
Cdd:cd05940   63 -----RGESLA-----HCLNvsSAKHLVVD--------------------AALYIYTSGTTGLPKAAIISHrrawrggaf 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3885 -AGMLNNQLSKVPYLELDENDVIAQTasqsfdISVWQFLAAplfGARVAIV---------PNAVAHDpqgllahvgeqgI 3954
Cdd:cd05940  113 fAGSGGALPSDVLYTCLPLYHSTALI------VGWSACLAS---GATLVIRkkfsasnfwDDIRKYQ------------A 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3955 TVLESVPSLIQGMLAEERQALD---GLRWMLptGEAMPPELARQWLKRY--PRIglVNAYGPAECsdDVAFFRVD----L 4025
Cdd:cd05940  172 TIFQYIGELCRYLLNQPPKPTErkhKVRMIF--GNGLRPDIWEEFKERFgvPRI--AEFYAATEG--NSGFINFFgkpgA 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4026 ASTESTYLPIGSP-------TDNNRLYllgAGADDAFELVPLGAVGELCVAGTGVGR--GYVgDPLRTAQAFVPHPFgAP 4096
Cdd:cd05940  246 IGRNPSLLRKVAPlalvkydLESGEPI---RDAEGRCIKVPRGEPGLLISRINPLEPfdGYT-DPAATEKKILRDVF-KK 320
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4097 GERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkYlvGYLVPGETPRSS 4176
Cdd:cd05940  321 GDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV---------Y--GVQVPGTDGRAG 389
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 15597620 4177 AdspAGLMVEQGAWF--ERIKQQLRADLPDYMVPLHWLVLDRM 4217
Cdd:cd05940  390 M---AAIVLQPNEEFdlSALAAHLEKNLPGYARPLFLRLQPEM 429
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
588-647 2.97e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 58.73  E-value: 2.97e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620    588 ARIGEIWKARLGVA--QVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFEAPTLQA 647
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
3855-4169 3.01e-10

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 66.23  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3855 PQVYSgpQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQL-SKVPYLEL----DENDVIAQTASQSFDISVWQFLAAPLfGA 3929
Cdd:PRK08974  201 PELVP--EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqAKAAYGPLlhpgKELVVTALPLYHIFALTVNCLLFIEL-GG 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3930 RVAIVPNAvaHDPQGLLAHVGEQGITVLESVPSLIQGML-AEERQALDGLRWMLPTGEAMPPE--LARQWlKRYPRIGLV 4006
Cdd:PRK08974  278 QNLLITNP--RDIPGFVKELKKYPFTAITGVNTLFNALLnNEEFQELDFSSLKLSVGGGMAVQqaVAERW-VKLTGQYLL 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4007 NAYGPAECSDDVAFFRVDLASTESTylpIGSPTDNNRLYLLgagaDDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQ 4086
Cdd:PRK08974  355 EGYGLTECSPLVSVNPYDLDYYSGS---IGLPVPSTEIKLV----DDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4087 AFvphpfgapGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVRE-AAVAVQEGANG----- 4160
Cdd:PRK08974  428 VI--------KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEvAAVGVPSEVSGeavki 499
                         330       340
                  ....*....|....*....|....*...
gi 15597620  4161 -------------------KYLVGYLVP 4169
Cdd:PRK08974  500 fvvkkdpslteeelithcrRHLTGYKVP 527
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
40-498 3.35e-10

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 65.84  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   40 VLSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVpayppesarrhhqerllsiiadaepr 118
Cdd:cd05940    3 ALTYAELDAMAnRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAA-------------------------- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  119 lvLTTADLR-EPLLQmnaqlsaanapqllCVDQLDPA--VAEAwdepqvrpehiAFLQYTSGSTALPKGVQVSHGNLVAN 195
Cdd:cd05940   57 --LINYNLRgESLAH--------------CLNVSSAKhlVVDA-----------ALYIYTSGTTGLPKAAIISHRRAWRG 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  196 EVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MSPRYFLERPVRWLEAISQYGGTVSggpdfAYR 272
Cdd:cd05940  110 GAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFSASNFWDDIRKYQATIFQYIGELC-----RYL 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  273 LCSERVAESALQRLdlsgwRVAFSGSepIRQDSLERFAEKFAASR---FDA-----SSFFACYGLAEATLFVTGGQRGQG 344
Cdd:cd05940  185 LNQPPKPTERKHKV-----RMIFGNG--LRPDIWEEFKERFGVPRiaeFYAategnSGFINFFGKPGAIGRNPSLLRKVA 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  345 IPALA-VDGEALARNRIAEGegsvlmCCGRSQPEHavlivdaaSGEVlgddnVGEIWAAGPSIahGYWRNPEASAKAF-- 421
Cdd:cd05940  258 PLALVkYDLESGEPIRDAEG------RCIKVPRGE--------PGLL-----ISRINPLEPFD--GYTDPAATEKKILrd 316
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  422 VERDGRTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVeSEVPSARKGRVaaFAVTVDGEEG-IGIAA 498
Cdd:cd05940  317 VFKKGDAWFNTGDLmRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVL-GAFPGVEEANV--YGVQVPGTDGrAGMAA 392
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
129-467 4.04e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 65.66  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   129 PLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGAD 208
Cdd:PRK09029   97 PSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   209 DvivSWL---PLYHDMGLigGLLQpifsgvpcvlmspryflerpvRWLEAisqyGGT--VSGGPDFAY------------ 271
Cdd:PRK09029  177 D---SWLlslPLFHVSGQ--GIVW---------------------RWLYA----GATlvVRDKQPLEQalagcthaslvp 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   272 ----RLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFaekfaasrfdassffaC-YGLAEATLFVTggqrgqgip 346
Cdd:PRK09029  227 tqlwRLLDNRSEPLSLKAVLLGGAAIPVELTEQAEQQGIRCW----------------CgYGLTEMASTVC--------- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   347 ALAVDGEAlarnriaeGEGSVLmccgrsqPEHAVLIVDaasgevlgddnvGEIWAAGPSIAHGYWRNPEAsaKAFVERDG 426
Cdd:PRK09029  282 AKRADGLA--------GVGSPL-------PGREVKLVD------------GEIWLRGASLALGYWRQGQL--VPLVNDEG 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 15597620   427 rtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIER 467
Cdd:PRK09029  333 --WFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIER 371
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
2317-2614 4.65e-10

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 65.34  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2317 DAEDPAPLAALSGPQHQAYLIY-TSGSTGKPKGVAVSHGEIAMHC---AAVIECFGMRAEDCELHFYS-------INFDA 2385
Cdd:cd05913   63 DLRDNYPFGLFAVPREKVVRIHaSSGTTGKPTVVGYTKNDLDVWAelvARCLDAAGVTPGDRVQNAYGyglftggLGFHY 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2386 ASERLlapllcGARVV----LRAQGQWgaeeicELIRAEGVSILGFTPSYGSQLAQWLESQG---RQLPVRMCITGGEAL 2458
Cdd:cd05913  143 GAERL------GALVIpaggGNTERQL------QLIKDFGPTVLCCTPSYALYLAEEAEEEGidpRELSLKVGIFGAEPW 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2459 TGEHLQRIRQAFaPASFFNAYGPTETVVMPLACLAPERLE----EGAASVPIgsvvgarvayILDADLALVPQGATGELy 2534
Cdd:cd05913  211 TEEMRKRIERRL-GIKAYDIYGLTEIIGPGVAFECEEKDGlhiwEDHFIPEI----------IDPETGEPVPPGEVGEL- 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2535 vggaglargyherpalsaerfVPDPFAAEGGRL--YRTGDLVRL----CDNGQV-----EYVGRIDHQVKIRGFRIELGE 2603
Cdd:cd05913  279 ---------------------VFTTLTKEAMPLirYRTRDITRLlpgpCPCGRThrridRITGRSDDMLIIRGVNVFPSQ 337
                        330
                 ....*....|.
gi 15597620 2604 IEARLLEHPQV 2614
Cdd:cd05913  338 IEDVLLKIPGL 348
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
1144-1618 5.31e-10

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 66.14  E-value: 5.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1144 RVALE-WDGGSLGYAELHARANRLAHYLRdKGVGPDVRVAICAERSPQLLVGLLAIVKAGgaYVPLDPDY---PSERLAY 1219
Cdd:PRK06814  648 KLAVEdPVNGPLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAG--RVPAMINFsagIANILSA 724
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1220 MLAdSGVELLLT------QAHLFERLPG-AEGVTPICLDSLK------------LDNWPSQAPGLHLHGDNLAYVIYTSG 1280
Cdd:PRK06814  725 CKA-AQVKTVLTsrafieKARLGPLIEAlEFGIRIIYLEDVRaqigladkikglLAGRFPLVYFCNRDPDDPAVILFTSG 803
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1281 STGQPKGVGNTHAA-LAERLQwMQATYTLDGDDVLMQKAPVsfdvsvWECF-------WPLVTGCRLVLAAPGEHrdpAR 1352
Cdd:PRK06814  804 SEGTPKGVVLSHRNlLANRAQ-VAARIDFSPEDKVFNALPV------FHSFgltgglvLPLLSGVKVFLYPSPLH---YR 873
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1353 LV-ELVRQFGVTTLHFVPPLLQlfidepGVAACG------SLRRLFSGGEALPAELRNRVLQRLpAVALHNRYGPTET-- 1423
Cdd:PRK06814  874 IIpELIYDTNATILFGTDTFLN------GYARYAhpydfrSLRYVFAGAEKVKEETRQTWMEKF-GIRILEGYGVTETap 946
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1424 --AINvTHWQCRAedgerSPIGRPLGNVvcrvldaEFNLLP-AGV--AGELCIGGLGLARGYLgrpalSAER-FVADPFS 1497
Cdd:PRK06814  947 viALN-TPMHNKA-----GTVGRLLPGI-------EYRLEPvPGIdeGGRLFVRGPNVMLGYL-----RAENpGVLEPPA 1008
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1498 aagERLYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIE---PEEIQARLlaQPGVAQAVVVIREGVAGSQLVGYYTGAv 1574
Cdd:PRK06814 1009 ---DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISlaaVEELAAEL--WPDALHAAVSIPDARKGERIILLTTAS- 1082
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 15597620  1575 gaeaEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGKLD 1618
Cdd:PRK06814 1083 ----DATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
1156-1556 5.97e-10

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 65.52  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAH- 1234
Cdd:cd17641   14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDEe 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1235 ----LFERLPGAEGVTPICL---------DSLKLdNWPSQA-----------PGLH------LHGDNLAYVIYTSGSTGQ 1284
Cdd:cd17641   94 qvdkLLEIADRIPSVRYVIYcdprgmrkyDDPRL-ISFEDVvalgraldrrdPGLYerevaaGKGEDVAVLCTTSGTTGK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1285 PKGVGNTHAALAER---------------------LQW-MQATYTL-------------DGDDVLMQK----AP--VSFD 1323
Cdd:cd17641  173 PKLAMLSHGNFLGHcaaylaadplgpgdeyvsvlpLPWiGEQMYSVgqalvcgfivnfpEEPETMMEDlreiGPtfVLLP 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1324 VSVWECFWPLVTgCRLVLAAPGEHRDPARLVELVRQFGVTTLHFVPPLLQLFI--------------DEPGVAACgslRR 1389
Cdd:cd17641  253 PRVWEGIAADVR-ARMMDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLaswladallfrplrDRLGFSRL---RS 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1390 LFSGGEALPAELRnRVLQRLpAVALHNRYGPTETAINVThwQCRAEDGERSPIGRPLGNVVCRVLDAefnllpagvaGEL 1469
Cdd:cd17641  329 AATGGAALGPDTF-RFFHAI-GVPLKQLYGQTELAGAYT--VHRDGDVDPDTVGVPFPGTEVRIDEV----------GEI 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1470 CIGGLGLARGYLGRPALSAERFVADPFsaagerlYRTGDRARWNADGVLEYLGRLDQQVKL-RGFRIEPEEIQARLLAQP 1548
Cdd:cd17641  395 LVRSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSP 467

                 ....*...
gi 15597620 1549 GVAQAVVV 1556
Cdd:cd17641  468 YIAEAVVL 475
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
169-552 7.54e-10

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 64.30  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   169 IAFLQYTSGSTALPKGVQVSHGNLVAN-EVLIRRGFGIGaddvivSWL---PLYHdmglIGG---LLQPIFSGV-PCVLM 240
Cdd:PRK07824   37 VALVVATSGTTGTPKGAMLTAAALTASaDATHDRLGGPG------QWLlalPAHH----IAGlqvLVRSVIAGSePVELD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   241 SPRYF----LERPVRWLEAISQYGGTVSGGPDFAYRlcsERVAESALQRLDlsgwrVAFSGSEPIRQDSLERFAEKfaas 316
Cdd:PRK07824  107 VSAGFdptaLPRAVAELGGGRRYTSLVPMQLAKALD---DPAATAALAELD-----AVLVGGGPAPAPVLDAAAAA---- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   317 rfdASSFFACYGLAEATlfvtGGQRGQGIPalaVDGealARNRIAEGEgsvlmccgrsqpehavlivdaasgevlgddnv 396
Cdd:PRK07824  175 ---GINVVRTYGMSETS----GGCVYDGVP---LDG---VRVRVEDGR-------------------------------- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   397 geIWAAGPSIAHGYwRNPEaSAKAFVERdgrTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVeSEVPSA 476
Cdd:PRK07824  210 --IALGGPTLAKGY-RNPV-DPDPFAEP---GWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAAL-ATHPAV 281
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620   477 RKgrVAAFAVTvDGEEGIGIAAeigrGVQKSVPAQELIDSIRQAVAEAYQ--EAPKVVALLNpgALPKTSSGKLQRSA 552
Cdd:PRK07824  282 AD--CAVFGLP-DDRLGQRVVA----AVVGDGGPAPTLEALRAHVARTLDrtAAPRELHVVD--ELPRRGIGKVDRRA 350
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
164-502 9.14e-10

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 64.38  E-value: 9.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  164 VRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVpCVLMSPR 243
Cdd:cd05937   84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGG-TLALSRK 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  244 YFLERpvRWLEAISqyggtvSGGPDFAYrlcserVAEsaLQRLDLSG----------WRVAFSGSepIRQDSLERFAEKF 313
Cdd:cd05937  163 FSASQ--FWKDVRD------SGATIIQY------VGE--LCRYLLSTppspydrdhkVRVAWGNG--LRPDIWERFRERF 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  314 AASrfDASSFFACyglAEATLFVTGGQRGQ-GIPALAVDGeALARNRIAEGEGSVLMccgrsQPEHAVLIVDAASG--EV 390
Cdd:cd05937  225 NVP--EIGEFYAA---TEGVFALTNHNVGDfGAGAIGHHG-LIRRWKFENQVVLVKM-----DPETDDPIRDPKTGfcVR 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  391 LGDDNVGEIWAAGP----SIAHGYWRNPEASAKAFVE---RDGRTWLRTGDLgfLR---DGELFVTGRLKDMLIVRGHNL 460
Cdd:cd05937  294 APVGEPGEMLGRVPfknrEAFQGYLHNEDATESKLVRdvfRKGDIYFRTGDL--LRqdaDGRWYFLDRLGDTFRWKSENV 371
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 15597620  461 YPQDIeRTVESEVPSARKGRVaaFAVTVDGEEG-IGIAAEIGR 502
Cdd:cd05937  372 STTEV-ADVLGAHPDIAEANV--YGVKVPGHDGrAGCAAITLE 411
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
3861-4154 1.05e-09

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 64.43  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3861 PQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVPNAV- 3938
Cdd:cd05908  105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIaGMNQYLMPTRLf 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3939 AHDPQGLLAHVGEQGITVLESvPS----LIQGMLAEERQA---LDGLRWMLPTGEAMPPELARQWLKRYPRIGL-----V 4006
Cdd:cd05908  185 IRRPILWLKKASEHKATIVSS-PNfgykYFLKTLKPEKANdwdLSSIRMILNGAEPIDYELCHEFLDHMSKYGLkrnaiL 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4007 NAYGPAECSDDVAFFRVDLASTEST----YLPIGSP------TDNNRLYLLGAG----------ADDAFELVPLGAVGEL 4066
Cdd:cd05908  264 PVYGLAEASVGASLPKAQSPFKTITlgrrHVTHGEPepevdkKDSECLTFVEVGkpidetdiriCDEDNKILPDGYIGHI 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4067 CVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRaDGVLEYVGRIDHQVKIRGFRIELGEIEARLHERAD 4146
Cdd:cd05908  344 QIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG 415

                 ....*...
gi 15597620 4147 VREAAVAV 4154
Cdd:cd05908  416 VELGRVVA 423
prpE PRK10524
propionyl-CoA synthetase; Provisional
1134-1622 1.08e-09

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 64.58  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1134 LERQLAQSAERVALEWDGGSLG------YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLA---------- 1197
Cdd:PRK10524   59 VDRHLAKRPEQLALIAVSTETDeertytFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLAcarigaihsv 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1198 ---------------------IVKA-----GGAYVPLDP---------DYPSER-------LAYMLADSGVELL---LTQ 1232
Cdd:PRK10524  139 vfggfashslaariddakpvlIVSAdagsrGGKVVPYKPlldeaialaQHKPRHvllvdrgLAPMARVAGRDVDyatLRA 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1233 AHLFERLPgaegvtPICLDSlkldNWPSqapglhlhgdnlaYVIYTSGSTGQPKGV----GNTHAALAERLQwmqatYTL 1308
Cdd:PRK10524  219 QHLGARVP------VEWLES----NEPS-------------YILYTSGTTGKPKGVqrdtGGYAVALATSMD-----TIF 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1309 DGddvlmQKAPVSFDVSvwECFW----------PLVTGCRLVLAAPGEHR-DPARLVELVRQFGVTTLHFVPPLLQLFID 1377
Cdd:PRK10524  271 GG-----KAGETFFCAS--DIGWvvghsyivyaPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTAIRVLKK 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1378 EPgvAAC------GSLRRLFSGGEALPAELRNRVLQRLPAVALHNrYGPTETAINVTHWQCRAEDGER---SPiGRPLGN 1448
Cdd:PRK10524  344 QD--PALlrkhdlSSLRALFLAGEPLDEPTASWISEALGVPVIDN-YWQTETGWPILAIARGVEDRPTrlgSP-GVPMYG 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1449 VVCRVLD-AEFNLLPAGVAGELCIGGlGLARGYLGRPALSAERFVADPFSAAGERLYRTGDRARWNADGVLEYLGRLDQQ 1527
Cdd:PRK10524  420 YNVKLLNeVTGEPCGPNEKGVLVIEG-PLPPGCMQTVWGDDDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDV 498
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1528 VKLRGFRIEPEEIQARLLAQPGVAQ-AVVVIREGVAGSQLVGYytgAVGAEAEAEQNQRLRAALQAELPEyMVPTQLMRL 1606
Cdd:PRK10524  499 INVAGHRLGTREIEESISSHPAVAEvAVVGVKDALKGQVAVAF---VVPKDSDSLADREARLALEKEIMA-LVDSQLGAV 574
                         570       580
                  ....*....|....*....|....*
gi 15597620  1607 A---------QMPLGPSGKLDTRAL 1622
Cdd:PRK10524  575 ArparvwfvsALPKTRSGKLLRRAI 599
PLN02479 PLN02479
acetate-CoA ligase
3718-4232 1.30e-09

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 64.48  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3718 LFEAQVAAHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAER---------GLDLLGMIVGSFKaga 3788
Cdd:PLN02479   25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNipamyeahfGVPMAGAVVNCVN--- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3789 gyLPLDpghpTQRLTRIVELSRTLVLVCTQ---ACREQALALFDE--LGCVDRPRLLV-WDEIQQGEGAEH--------- 3853
Cdd:PLN02479  102 --IRLN----APTIAFLLEHSKSEVVMVDQeffTLAEEALKILAEkkKSSFKPPLLIViGDPTCDPKSLQYalgkgaiey 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3854 -------DPQ-VYSGPQNLAYVI---YTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQsFDISVWQF- 3921
Cdd:PLN02479  176 ekfletgDPEfAWKPPADEWQSIalgYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPM-FHCNGWCFt 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3922 --LAApLFGARVAIvpNAVAhdPQGLLAHVGEQGITVLESVP----SLIQGMLAEERQALDGLRWMLPTGEAMPPELARQ 3995
Cdd:PLN02479  255 wtLAA-LCGTNICL--RQVT--AKAIYSAIANYGVTHFCAAPvvlnTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3996 WLKRYPRI----GLVNAYGPAEcsddvaffrVDLASTESTYLPigsPTDNNRL-------YLLGAGAD--DAFELVPLGA 4062
Cdd:PLN02479  330 MSEKGFRVthtyGLSETYGPST---------VCAWKPEWDSLP---PEEQARLnarqgvrYIGLEGLDvvDTKTMKPVPA 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4063 ----VGELCVAGTGVGRGYVGDPLRTAQAFvphpfgAPGerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIE 4138
Cdd:PLN02479  398 dgktMGEIVMRGNMVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVE 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4139 ARLHERADVREAAVAVQEGAN-GKYLVGYLvpgeTPRSSADSPaglmvEQGAWFERIKQQLRADLPDYMVPLHwLVLDRM 4217
Cdd:PLN02479  470 NVVYTHPAVLEASVVARPDERwGESPCAFV----TLKPGVDKS-----DEAALAEDIMKFCRERLPAYWVPKS-VVFGPL 539
                         570
                  ....*....|....*
gi 15597620  4218 PLNANGKLDRKALPA 4232
Cdd:PLN02479  540 PKTATGKIQKHVLRA 554
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
3725-4232 1.39e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 64.28  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3725 AHPQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGiDQP--VALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRL 3802
Cdd:PRK13388   13 AGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADP-DRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3803 TRIVELSRTLVLVCTQACReqalALFDELGCVDRPRLLV----WDEIQQGEGAEHdPQVYSGPQNLAYVIYTSGSTGLPK 3878
Cdd:PRK13388   92 AADIRRADCQLLVTDAEHR----PLLDGLDLPGVRVLDVdtpaYAELVAAAGALT-PHREVDAMDPFMLIFTSGTTGAPK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3879 GVMVEQAGMLNNQLSKVPYLELDENDVIaqtasqsfdisvwqFLAAPLF---------------GARVAIVPNAVAhdpQ 3943
Cdd:PRK13388  167 AVRCSHGRLAFAGRALTERFGLTRDDVC--------------YVSMPLFhsnavmagwapavasGAAVALPAKFSA---S 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3944 GLLAHVGEQGITVLESVPSLIQGMLAEERQALDG---LRWMLPTgEAMPPELArQWLKRYpRIGLVNAYGPAEcsDDVAF 4020
Cdd:PRK13388  230 GFLDDVRRYGATYFNYVGKPLAYILATPERPDDAdnpLRVAFGN-EASPRDIA-EFSRRF-GCQVEDGYGSSE--GAVIV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4021 FRVDLASTEStylpIGSPTDNNRLYLLGAGADDA---FE-----LVPLGAVGELC-VAGTGVGRGYVGDPlrtaqafvph 4091
Cdd:PRK13388  305 VREPGTPPGS----IGRGAPGVAIYNPETLTECAvarFDahgalLNADEAIGELVnTAGAGFFEGYYNNP---------- 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4092 pfGAPGERL----YRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylvgYL 4167
Cdd:PRK13388  371 --EATAERMrhgmYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAV-------------YA 435
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  4168 VPgeTPRSSADSPAGLMVEQGAWF--ERIKQQLRA--DLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK13388  436 VP--DERVGDQVMAALVLRDGATFdpDAFAAFLAAqpDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
PLN03102 PLN03102
acyl-activating enzyme; Provisional
172-554 1.45e-09

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 64.27  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   172 LQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSGVP-CV--LMSPRYFler 248
Cdd:PLN03102  191 LNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSvCMrhVTAPEIY--- 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   249 pvrwlEAISQYGGTvsggpdfaYRLCSERVAESALQ--RLDLSGW----RVAFSGSEPirQDSLERFAEKFAASRFDAss 322
Cdd:PLN03102  268 -----KNIEMHNVT--------HMCCVPTVFNILLKgnSLDLSPRsgpvHVLTGGSPP--PAALVKKVQRLGFQVMHA-- 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   323 ffacYGLAEATlfvtggqrgqgipalavdgealarnriaegeGSVLMCCGRSQ----PEHAVLIVDAASG-EVLGDDNV- 396
Cdd:PLN03102  331 ----YGLTEAT-------------------------------GPVLFCEWQDEwnrlPENQQMELKARQGvSILGLADVd 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   397 -----------------GEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGH 458
Cdd:PLN03102  376 vknketqesvprdgktmGEIVIKGSSIMKGYLKNPKATSEAF--KHG--WLNTGDVGVIHpDGHVEIKDRSKDIIISGGE 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   459 NL-----------YPQDIERTVESeVPSARKGRV-AAFAVTVDGEEGigiaaeIGRGVQKSVPAQ-ELIDSIRQAVAEAY 525
Cdd:PLN03102  452 NIssvevenvlykYPKVLETAVVA-MPHPTWGETpCAFVVLEKGETT------KEDRVDKLVTRErDLIEYCRENLPHFM 524
                         410       420
                  ....*....|....*....|....*....
gi 15597620   526 qeAPKVVALLNpgALPKTSSGKLQRSACR 554
Cdd:PLN03102  525 --CPRKVVFLQ--ELPKNGNGKILKPKLR 549
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
10-492 1.75e-09

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 63.93  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    10 TLVQALRRRAVQEPERLALRFlaeDDGEGVV--LSYRDLDLRA-RSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLY 86
Cdd:PRK08008    8 HLRQMWDDLADVYGHKTALIF---ESSGGVVrrYSYLELNEEInRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    87 AGVIAVPAyppeSARRHHQERLLsIIADAEPRLVLTTADLRePLLQMNAQLSAANAPQLLCVDQLDPAVAEAWDEPQVRP 166
Cdd:PRK08008   85 IGAIMVPI----NARLLREESAW-ILQNSQASLLVTSAQFY-PMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   167 EHIAFLQY--------------TSGSTALPKGVQVSHGNLV------ANEVLIRrgfgigADDVIVSWLPLYH-DMGLIG 225
Cdd:PRK08008  159 QQPATLCYapplstddtaeilfTSGTTSRPKGVVITHYNLRfagyysAWQCALR------DDDVYLTVMPAFHiDCQCTA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   226 GLlqPIFS-GVPCVLM---SPRYFlerpvrWlEAISQYGGTVSGG-PDFAYRLCSERVAESALQ-RLDLSGWRVAFSGSE 299
Cdd:PRK08008  233 AM--AAFSaGATFVLLekySARAF------W-GQVCKYRATITECiPMMIRTLMVQPPSANDRQhCLREVMFYLNLSDQE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   300 piRQDSLERFAekfaasrfdaSSFFACYGLAEATLFVTGGQRGQ-------GIPALAVdgEAlarnRIAEGEGSVLmccg 372
Cdd:PRK08008  304 --KDAFEERFG----------VRLLTSYGMTETIVGIIGDRPGDkrrwpsiGRPGFCY--EA----EIRDDHNRPL---- 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   373 rsqpehavlivdaASGEVlgddnvGEIW---AAGPSIAHGYWRNPEASAKAFvERDGrtWLRTGDLGFL-RDGELFVTGR 448
Cdd:PRK08008  362 -------------PAGEI------GEICikgVPGKTIFKEYYLDPKATAKVL-EADG--WLHTGDTGYVdEEGFFYFVDR 419
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620   449 LKDMLIVRGHNLYPQDIERTVESE----------VP-SARKGRVAAFAVTVDGEE 492
Cdd:PRK08008  420 RCNMIKRGGENVSCVELENIIATHpkiqdivvvgIKdSIRDEAIKAFVVLNEGET 474
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2810-3047 1.78e-09

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 64.30  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2810 WNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQVDGEWLAQHRPLREQELLWHVPVQSFDE-----CAELFAKAQ 2884
Cdd:PRK10252   30 WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEIIDLRTQPDphaaaQALMQADLQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2885 RSLDLEQG-PLLRAVLVDgpAGEQRLL--LAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAepalPAKTSAFRDWAGRL-- 2959
Cdd:PRK10252  110 QDLRVDSGkPLVFHQLIQ--LGDNRWYwyQRYHHLLVDGFSFPAITRRIAAIYCAWLRGE----PTPASPFTPFADVVee 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2960 -QAYAGSESLREELGWWQARLGGQP--VEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTqvnDLLLTALA 3036
Cdd:PRK10252  184 yQRYRASEAWQRDAAFWAEQRRQLPppASLSPAPLPGRSASADILRLKLEFTDGAFRQLAAQASGVQRP---DLALALVA 260
                         250
                  ....*....|.
gi 15597620  3037 RVLCRWSGQPS 3047
Cdd:PRK10252  261 LWLGRLCGRMD 271
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
1156-1624 1.93e-09

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 63.62  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYML---ADSGVELLLTQ 1232
Cdd:PRK06018   42 YAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIInhaEDRVVITDLTF 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1233 AHLFE----RLPGAEGVT----------PICLDSLKLDNWPSQAPGLHLHGD----NLAYVIYTSGSTGQPKGVGNTHaa 1294
Cdd:PRK06018  122 VPILEkiadKLPSVERYVvltdaahmpqTTLKNAVAYEEWIAEADGDFAWKTfdenTAAGMCYTSGTTGDPKGVLYSH-- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1295 laeRLQWMQATYTLDGD-------DVLMQKAPVsFDVSVWE-CFWPLVTGCRLVLaaPGEHRDPARLVELVRQFGVTTLH 1366
Cdd:PRK06018  200 ---RSNVLHALMANNGDalgtsaaDTMLPVVPL-FHANSWGiAFSAPSMGTKLVM--PGAKLDGASVYELLDTEKVTFTA 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1367 FVPPLLQLFID--EPGVAACGSLRRLFSGGEALPAELRnRVLQRLPAVALHnRYGPTETAINVT---------HWQCRAE 1435
Cdd:PRK06018  274 GVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMPRSMI-KAFEDMGVEVRH-AWGMTEMSPLGTlaalkppfsKLPGDAR 351
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1436 DGERSPIGRPLGNVVCRVLDAEFNLLP--AGVAGELCIGGLGLARGYLGrpaLSAERFVADPFsaagerlYRTGDRARWN 1513
Cdd:PRK06018  352 LDVLQKQGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGPAVAAAYYR---VDGEILDDDGF-------FDTGDVATID 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1514 ADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQ------LVgyytgAVGAEAEAEQNQRLR 1587
Cdd:PRK06018  422 AYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI---GVYHPKwderplLI-----VQLKPGETATREEIL 493
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 15597620  1588 AALQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALPE 1624
Cdd:PRK06018  494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
PRK05857 PRK05857
fatty acid--CoA ligase;
2200-2697 2.01e-09

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 63.49  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2200 PQAPALTFAGQT--LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP---LER 2274
Cdd:PRK05857   28 PEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPiaaIER 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2275 LQYMIEDSGVRLL----LSHAALFEALGELPAGVARWCLEEDGPALDAEDPAPLAAL-SGPQHQAYLIYTSGSTGKPKGV 2349
Cdd:PRK05857  108 FCQITDPAAALVApgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNAdQGSEDPLAMIFTSGTTGEPKAV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2350 AVSHgEIAMHCAAVIECFGMRAEDCelhfysinfdAASERLLAPL------------LCGARVVLRAQGQWGAEEICELI 2417
Cdd:PRK05857  188 LLAN-RTFFAVPDILQKEGLNWVTW----------VVGETTYSPLpathigglwwilTCLMHGGLCVTGGENTTSLLEIL 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2418 RAEGVSILGFTPSYGSQLAQWLESQGRQLP-VRMCITGGEALTGEHLQRIRQAFAPASFFnaYGPTETVVMPLaCLAPE- 2495
Cdd:PRK05857  257 TTNAVATTCLVPTLLSKLVSELKSANATVPsLRLVGYGGSRAIAADVRFIEATGVRTAQV--YGLSETGCTAL-CLPTDd 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2496 ----RLEEGAASVPIGSVVgarvAYILDADLA--LVPQGAT----GELYVGGAGLARGYHERPALSAERFVpdpfaaEGg 2565
Cdd:PRK05857  334 gsivKIEAGAVGRPYPGVD----VYLAATDGIgpTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLI------DG- 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2566 rLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEaRLLEH-PQVREALVLALDSPSGKQLAGYVASAVAEQDED 2644
Cdd:PRK05857  403 -WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEFGALVGLAVVASAELDES 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  2645 AQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPApdpALN 2697
Cdd:PRK05857  481 AARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAA---AAT 530
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1156-1616 2.26e-09

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 63.83  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPS----ERL------------AY 1219
Cdd:cd05943  101 WAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVpgvlDRFgqiepkvlfavdAY 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1220 MLADSGVELLLTQAHLFERLPGAEGVtpICLDSLKLD---NWPSQAPGLHLHG-----------------DNLAYVIYTS 1279
Cdd:cd05943  181 TYNGKRHDVREKVAELVKGLPSLLAV--VVVPYTVAAgqpDLSKIAKALTLEDflatgaagelefeplpfDHPLYILYSS 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1280 GSTGQPKGVgnTHAALAERLQWMQAtYTLDGDdvlMQKAPVSFDVSVweCFW--------PLVTGCRLVL--AAPGeHRD 1349
Cdd:cd05943  259 GTTGLPKCI--VHGAGGTLLQHLKE-HILHCD---LRPGDRLFYYTT--CGWmmwnwlvsGLAVGATIVLydGSPF-YPD 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1350 PARLVELVRQFGVTTL----HFVPPLLQLFIDEPGVAACGSLRRLFSGGEALPAELRNRVLQRL-PAVALHNRYGPTETA 1424
Cdd:cd05943  330 TNALWDLADEEGITVFgtsaKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIkPDVLLASISGGTDII 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1425 invthwQCRAEDGERSPIGRplGNVVCRVLDAEFNLLP------AGVAGELCIgglglARGYLGRPAlsaeRFVADPfsa 1498
Cdd:cd05943  410 ------SCFVGGNPLLPVYR--GEIQCRGLGMAVEAFDeegkpvWGEKGELVC-----TKPFPSMPV----GFWNDP--- 469
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1499 AGER-----------LYRTGDRARWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVIREGVAG-SQL 1566
Cdd:cd05943  470 DGSRyraayfakypgVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGdERV 549
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 15597620 1567 VGYYTGAVGAEAEAEQNQRLRAALQAELPEYMVPTQLMRLAQMPLGPSGK 1616
Cdd:cd05943  550 ILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
3842-4181 2.68e-09

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 63.26  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3842 WDEIQqgegAEHDP---QVYSGPQNLAYVIYTSGSTGLPKGVM-------------VEQAGMLNNQ--LSKVPYLELDEN 3903
Cdd:cd05932  118 WDDLI----AQHPPleeRPTRFPEQLATLIYTSGTTGQPKGVMltfgsfawaaqagIEHIGTEENDrmLSYLPLAHVTER 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3904 DVIAQTASQS-----FDISVWQFLAaPLFGARVAI---VPNAVAHDPQGLLAHVGEQGITVLESVP---SLIQgmlaeeR 3972
Cdd:cd05932  194 VFVEGGSLYGgvlvaFAESLDTFVE-DVQRARPTLffsVPRLWTKFQQGVQDKIPQQKLNLLLKIPvvnSLVK------R 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3973 QALDGL-----RWMLPTGEAMPPELarqwLKRYPRIGL--VNAYGPAEcsddvaffrvdlastESTYLPIGSPTDNNRLY 4045
Cdd:cd05932  267 KVLKGLgldqcRLAGCGSAPVPPAL----LEWYRSLGLniLEAYGMTE---------------NFAYSHLNYPGRDKIGT 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4046 LLGAGADDAfelVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQV 4125
Cdd:cd05932  328 VGNAGPGVE---VRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF-------LRTGDKGELDADGNLTITGRVKDIF 397
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 4126 KI-RGFRIELGEIEARLHERADVREAAVAvqeGANGKYLVGYLVPGETPRSSADSPA 4181
Cdd:cd05932  398 KTsKGKYVAPAPIENKLAEHDRVEMVCVI---GSGLPAPLALVVLSEEARLRADAFA 451
PRK08162 PRK08162
acyl-CoA synthetase; Validated
379-554 2.96e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 63.04  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   379 AVLIVDAASGEVLGDDN--VGEIWAAGPSIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIV 455
Cdd:PRK08162  369 GVTVLDPDTMQPVPADGetIGEIMFRGNIVMKGYLKNPKATEEAF--AGG--WFHTGDLAVLHpDGYIKIKDRSKDIIIS 444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   456 RGHNLypqdieRTVESEVPSARKGRVAAFAVTVDGEEGIGIA----AEIGRGVqkSVPAQELIDSIRQAVAeAYQeAPKV 531
Cdd:PRK08162  445 GGENI------SSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVpcafVELKDGA--SATEEEIIAHCREHLA-GFK-VPKA 514
                         170       180
                  ....*....|....*....|...
gi 15597620   532 VALlnpGALPKTSSGKLQRSACR 554
Cdd:PRK08162  515 VVF---GELPKTSTGKIQKFVLR 534
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
3738-4154 3.11e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 63.09  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3738 RWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDpgHPTQR----------LTRIVE 3807
Cdd:PRK07768   29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLH--QPTPRtdlavwaedtLRVIGM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3808 LSRTLVLVctQACREQALALFDELGCvdrpRLLVWDEIQQGEGAEhdpQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGM 3887
Cdd:PRK07768  107 IGAKAVVV--GEPFLAAAPVLEEKGI----RVLTVADLLAADPID---PVETGEDDLALMQLTSGSTGSPKAVQITHGNL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3888 LNNQLSKVPYLELD-ENDVIAQTASQSFDISVWQFLAAPL-FGAR-VAIVPNAVAHDPQGLLAHVGEQGITVLeSVPSLI 3964
Cdd:PRK07768  178 YANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMyFGAElVKVTPMDFLRDPLLWAELISKYRGTMT-AAPNFA 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3965 QGMLAE--ERQALDG------LRWMLPTGEAMPPELARQWLKRYPRIGL-----VNAYGPAECSDDVAFFRV-------- 4023
Cdd:PRK07768  257 YALLARrlRRQAKPGafdlssLRFALNGAEPIDPADVEDLLDAGARFGLrpeaiLPAYGMAEATLAVSFSPCgaglvvde 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4024 ---DLASTESTYLPIGSPtDNNRLYLLG--------AGADDAFELVPLGAVGELCVAGTGVGRGYVgdplrTAQAFVPhp 4092
Cdd:PRK07768  337 vdaDLLAALRRAVPATKG-NTRRLATLGpplpglevRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFIP-- 408
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  4093 fgAPGER-LYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEaRLHERAD-VREA-AVAV 4154
Cdd:PRK07768  409 --AQDADgWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE-RAAARVEgVRPGnAVAV 470
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
3839-4152 4.28e-09

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 62.51  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3839 LLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISV 3918
Cdd:PLN02860  149 FLTTEMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGL 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3919 WQFLAAPLFGARVAIVPNavaHDPQGLLAHVGEQGITVLESVPSLIQGMLA-----EERQALDGLRWMLPTGEAMPPELA 3993
Cdd:PLN02860  229 SSALAMLMVGACHVLLPK---FDAKAALQAIKQHNVTSMITVPAMMADLISltrksMTWKVFPSVRKILNGGGSLSSRLL 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3994 RQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLASTESTYLPIGSPTDNNRLYL----------------LGAGADDAFEl 4057
Cdd:PLN02860  306 PDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVhqpqgvcvgkpaphveLKIGLDESSR- 384
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4058 vplgaVGELCVAGTGVGRGYVGDPLRTAQAfvphpfgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEI 4137
Cdd:PLN02860  385 -----VGRILTRGPHVMLGYWGQNSETASV-------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEV 452
                         330
                  ....*....|....*
gi 15597620  4138 EARLHERADVREAAV 4152
Cdd:PLN02860  453 EAVLSQHPGVASVVV 467
PRK05857 PRK05857
fatty acid--CoA ligase;
3740-4232 6.02e-09

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 61.95  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQA 3819
Cdd:PRK05857   43 RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3820 CREQALALFDELGCVdrPRLLVWDEIQQGEGAEHDPQVY------SGPQNLAYVIYTSGSTGLPKGVMVEqagmlNNQLS 3893
Cdd:PRK05857  123 SKMASSAVPEALHSI--PVIAVDIAAVTRESEHSLDAASlagnadQGSEDPLAMIFTSGTTGEPKAVLLA-----NRTFF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3894 KVPyleldenDVIAQTASQSFDISVWQFLAAPLFGARVA---IVPNAVAHDpqGLLAHVGEQGITVLES----------- 3959
Cdd:PRK05857  196 AVP-------DILQKEGLNWVTWVVGETTYSPLPATHIGglwWILTCLMHG--GLCVTGGENTTSLLEIlttnavattcl 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3960 VPSLIQGMLAEERQA---LDGLRWMLPTG-----------EAMPPELARQWlkrypriGLVNAYGPAEC--SDDVAFFRV 4023
Cdd:PRK05857  267 VPTLLSKLVSELKSAnatVPSLRLVGYGGsraiaadvrfiEATGVRTAQVY-------GLSETGCTALClpTDDGSIVKI 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4024 DLAStestylpIGSPTDNNRLYLLGAGADD--AFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVphpfgapgERLY 4101
Cdd:PRK05857  340 EAGA-------VGRPYPGVDVYLAATDGIGptAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLI--------DGWV 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4102 RTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVpgeTPRSSADSPA 4181
Cdd:PRK05857  405 NTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAV---VASAELDESA 481
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15597620  4182 GLMVEQgawfeRIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK05857  482 ARALKH-----TIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAA 527
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
1130-1600 6.57e-09

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 62.09  E-value: 6.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1130 LPELLERQLAQSAERVALEWDGGSLG--------------------YAELHARANRLAHYLR-DKGVGPDVRVAICAERS 1188
Cdd:cd17632   24 LAQIIATVMTGYADRPALGQRATELVtdpatgrttlrllprfetitYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1189 PQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELL-LTQAHL------------------F------------- 1236
Cdd:cd17632  104 PDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLaVSAEHLdlaveavleggtpprlvvFdhrpevdahraal 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1237 ----ERLPG-AEGVTPICLDSLKL-DNWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAErlQWMQATYTLDG 1310
Cdd:cd17632  184 esarERLAAvGIPVTTLTLIAVRGrDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVAT--FWLKVSSIQDI 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1311 D---DVLMQKAPVSFDVSVWECFWPLVTGCRLVLAAPGehrDPARLVE---LVRQfgvTTLHFVPP----LLQLFIDEpg 1380
Cdd:cd17632  262 RppaSITLNFMPMSHIAGRISLYGTLARGGTAYFAAAS---DMSTLFDdlaLVRP---TELFLVPRvcdmLFQRYQAE-- 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1381 vaacgSLRRLFSGGEA------LPAELRNRVL----------------------QRLPAVALHNRYGPTETAINVThwqc 1432
Cdd:cd17632  334 -----LDRRSVAGADAetlaerVKAELRERVLggrllaavcgsaplsaemkafmESLLDLDLHDGYGSTEAGAVIL---- 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1433 raeDGErspIGRPlgnvvcRVLDAEFNLLPA-GV--------AGELCIGGLGLARGYLGRPALSAERFVADPFsaagerl 1503
Cdd:cd17632  405 ---DGV---IVRP------PVLDYKLVDVPElGYfrtdrphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------- 465
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1504 YRTGD-RARWNADGvLEYLGRLDQQVKL-RGFRIEPEEIQARLLAQPGVAQ-------------AVVVIREgvagsqlvg 1568
Cdd:cd17632  466 YRTGDvMAELGPDR-LVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQifvygnserayllAVVVPTQ--------- 535
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 15597620 1569 yytGAVGAEAEAEQNQRLRAALQ-----AELPEYMVP 1600
Cdd:cd17632  536 ---DALAGEDTARLRAALAESLQriareAGLQSYEIP 569
PLN03102 PLN03102
acyl-activating enzyme; Provisional
3852-4230 7.72e-09

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 61.96  E-value: 7.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3852 EHDPQVYSgpqnlayviYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQsFDISVWQFL--AAPLFGA 3929
Cdd:PLN03102  185 EHDPISLN---------YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPM-FHCNGWTFTwgTAARGGT 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3930 RVAIVPNAVAHDPQGLLAHvgeqGITVLESVPSLIQGMLAEER--QALDGLRWMLPTGEAMPPELArqwLKRYPRIG--L 4005
Cdd:PLN03102  255 SVCMRHVTAPEIYKNIEMH----NVTHMCCVPTVFNILLKGNSldLSPRSGPVHVLTGGSPPPAAL---VKKVQRLGfqV 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4006 VNAYGPAECSDDVAFFRvdlASTESTYLPigsptDNNRLYL--------LGAGADD-----AFELVPLGA--VGELCVAG 4070
Cdd:PLN03102  328 MHAYGLTEATGPVLFCE---WQDEWNRLP-----ENQQMELkarqgvsiLGLADVDvknkeTQESVPRDGktMGEIVIKG 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4071 TGVGRGYVGDPLRTAQAFvPHPFgapgerlYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREA 4150
Cdd:PLN03102  400 SSIMKGYLKNPKATSEAF-KHGW-------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4151 AV-AVQEGANGKYLVGYLVPGETPRSSADSPAGLMVEQGAWFErikqQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKA 4229
Cdd:PLN03102  472 AVvAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDLIE----YCRENLPHFMCPRKVVFLQELPKNGNGKILKPK 547

                  .
gi 15597620  4230 L 4230
Cdd:PLN03102  548 L 548
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2809-3105 8.80e-09

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 61.17  E-value: 8.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2809 HWNQALLlQPRQAIDLGLLRKSLQRLVEQHDALRLAFrqvdgEWLAQHRPLR----EQELLWHV---PVQSFDECAELFA 2881
Cdd:cd19547   24 YFNQNVL-ELVGGTDEDVLREAWRRVADRYEILRTGF-----TWRDRAEPLQyvrdDLAPPWALldwSGEDPDRRAELLE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2882 K-----AQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEPALpAKTSAFRDWA 2956
Cdd:cd19547   98 RlladdRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQL-SPCRPYRDYV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2957 G--RLQAYAGSESLReelgWWQ---ARLGGQPV-EWPCDrpqgdnREALAESVSLRLDPQRTRqLLQQAPAAYRTQVNDL 3030
Cdd:cd19547  177 RwiRARTAQSEESER----FWReylRDLTPSPFsTAPAD------REGEFDTVVHEFPEQLTR-LVNEAARGYGVTTNAI 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620 3031 LLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDLTrsVGWFTSAYPL--RLTPAQSPGESIKAIKEQLRAVPHKG 3105
Cdd:cd19547  246 SQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHM--VGIFINTIPLriRLDPDQTVTGLLETIHRDLATTAAHG 320
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2185-2685 1.10e-08

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 61.91  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2185 QDTLHGLFAARVAAS----PQAPALT-FAGQTLSYAELDARSNRLARVLRsHGVGPEVRVGLALERSLEMVVGLLAILKA 2259
Cdd:PRK06814  627 SDYDRTLFEALIEAAkihgFKKLAVEdPVNGPLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSA 705
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2260 GgaYVPLdpeyplerlqyMIEDS-------------GVRLLLSHAALFEA--LGELPAGVAR-----WcLEEDGPALDAE 2319
Cdd:PRK06814  706 G--RVPA-----------MINFSagianilsackaaQVKTVLTSRAFIEKarLGPLIEALEFgiriiY-LEDVRAQIGLA 771
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2320 DP--------APLAALSG--PQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCA---AVIECFGM-RAEDCELHFYSINFDA 2385
Cdd:PRK06814  772 DKikgllagrFPLVYFCNrdPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAqvaARIDFSPEdKVFNALPVFHSFGLTG 851
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2386 AserLLAPLLCGARVVL-------RAqgqwgaeeICELIRAEGVSILGFTPSYGSQLAQWLESQG-RQLpvRMCITGGEA 2457
Cdd:PRK06814  852 G---LVLPLLSGVKVFLypsplhyRI--------IPELIYDTNATILFGTDTFLNGYARYAHPYDfRSL--RYVFAGAEK 918
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2458 LTgehlQRIRQAFAPA---SFFNAYGPTETVvmP-LACLAPERLEEGAasvpigsvVGaRVAYILDADLALVP---QGat 2530
Cdd:PRK06814  919 VK----EETRQTWMEKfgiRILEGYGVTETA--PvIALNTPMHNKAGT--------VG-RLLPGIEYRLEPVPgidEG-- 981
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2531 GELYVGGAGLARGYherpaLSAER---FVPDPfaaEGgrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEAr 2607
Cdd:PRK06814  982 GRLFVRGPNVMLGY-----LRAENpgvLEPPA---DG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE- 1050
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2608 llehpqvreaLVLALDSpsgkqlaGYVASAVAEQDE----------DAQAALREALKTHLK-QQLPDYMVPAHLLLLASL 2676
Cdd:PRK06814 1051 ----------LAAELWP-------DALHAAVSIPDArkgeriilltTASDATRAAFLAHAKaAGASELMVPAEIITIDEI 1113

                  ....*....
gi 15597620  2677 PLTANGKLD 2685
Cdd:PRK06814 1114 PLLGTGKID 1122
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1136-1312 1.38e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 61.28  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1136 RQLAQSAERVALEWDggsLGYAELHAR----ANRLAHYLRdkgvgPDVRVAICAERSPQLLVGLLAIVKAGGAYVPL-DP 1210
Cdd:PRK07769   41 RFLDFSTERDGVARD---LTWSQFGARnravGARLQQVTK-----PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1211 DYP--SERLAYMLADSGVELLLTQA-------HLFERLPGAEGVTPICLDSLKLDNWPSQAPgLHLHGDNLAYVIYTSGS 1281
Cdd:PRK07769  113 AEPghVGRLHAVLDDCTPSAILTTTdsaegvrKFFRARPAKERPRVIAVDAVPDEVGATWVP-PEANEDTIAYLQYTSGS 191
                         170       180       190
                  ....*....|....*....|....*....|.
gi 15597620  1282 TGQPKGVGNTHAALAERLqwMQATYTLDGDD 1312
Cdd:PRK07769  192 TRIPAGVQITHLNLPTNV--LQVIDALEGQE 220
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
2531-2689 1.55e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 60.06  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2531 GELYVGGAGLARGYHERPalsaerfVPDPFAAEGgrLYRTGDLVRLcDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLE 2610
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPV-------DPDPFAEPG--WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2611 HPQVREALVLALDSPSGKQ--LAGYVASAvaeqdedAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRA 2688
Cdd:PRK07824  278 HPAVADCAVFGLPDDRLGQrvVAAVVGDG-------GPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRA 350

                  .
gi 15597620  2689 L 2689
Cdd:PRK07824  351 L 351
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
2201-2367 1.66e-08

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 60.66  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2201 QAPALTFAGQ--------TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2272
Cdd:PRK08180   51 EAPDRVFLAErgadggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2273 -----ERLQYMIEdsgvrlLLSHAALFEALGELPAGVARWCLEEDGPALDAEDPA------PLAAL-------------- 2327
Cdd:PRK08180  131 vsqdfGKLRHVLE------LLTPGLVFADDGAAFARALAAVVPADVEVVAVRGAVpgraatPFAALlatpptaavdaaha 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 15597620  2328 -SGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECF 2367
Cdd:PRK08180  205 aVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF 245
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
783-1314 2.21e-08

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 61.04  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  783 EKGPLLRVSLVRLDEQEHQlwvTLHHIVADGWSLNLLLDeFSRLYAEAcGGQPADLAPlelhYAefaaWQRQWLD--AGE 860
Cdd:COG3321  813 AAGDAVVLPSLRRGEDELA---QLLTALAQLWVAGVPVD-WSALYPGR-GRRRVPLPT----YP----FQREDAAaaLLA 879
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  861 GARQLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQG 940
Cdd:COG3321  880 AALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAA 959
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  941 EIRIGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQLFQVLFN 1020
Cdd:COG3321  960 EAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAA 1039
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1021 HQQRDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRC 1100
Cdd:COG3321 1040 AAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAA 1119
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1101 LGDIALVDAEQAAHLAEWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVR 1180
Cdd:COG3321 1120 AAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAA 1199
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1181 VAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQAHLFERLPGAEGVTPICLDSLKLDNWPS 1260
Cdd:COG3321 1200 LLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAA 1279
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597620 1261 QAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYTLDGDDVL 1314
Cdd:COG3321 1280 AAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
3737-4230 2.29e-08

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 60.08  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVC 3816
Cdd:PRK08008   36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3817 TqacrEQALALFDELG----------CVDRPRL------LVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGV 3880
Cdd:PRK08008  116 S----AQFYPMYRQIQqedatplrhiCLTRVALpaddgvSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3881 MVEQAGMLNNQLSKVPYLELDENDVIAqTASQSFDISvWQFLAA-PLF--GARVAIVPNAVAhdpQGLLAHVGEQGITVL 3957
Cdd:PRK08008  192 VITHYNLRFAGYYSAWQCALRDDDVYL-TVMPAFHID-CQCTAAmAAFsaGATFVLLEKYSA---RAFWGQVCKYRATIT 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3958 ESVPSLIQGML-----AEERQ-ALDGLRWMLPTGEAMppelARQWLKRYpRIGLVNAYGpaecsddvaffrvdlaSTEST 4031
Cdd:PRK08008  267 ECIPMMIRTLMvqppsANDRQhCLREVMFYLNLSDQE----KDAFEERF-GVRLLTSYG----------------MTETI 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4032 YLPIG-SPTDNNRLYLLG-AG-------ADDAFELVPLGAVGELC---VAGTGVGRGYVGDPLRTAQAFVPhpfgapgER 4099
Cdd:PRK08008  326 VGIIGdRPGDKRRWPSIGrPGfcyeaeiRDDHNRPLPAGEIGEICikgVPGKTIFKEYYLDPKATAKVLEA-------DG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4100 LYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-----AVQEGANGKYLVgyLVPGETpr 4174
Cdd:PRK08008  399 WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvgikdSIRDEAIKAFVV--LNEGET-- 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4175 ssadspagLMVEQgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK08008  475 --------LSEEE------FFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
3736-4152 2.79e-08

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 60.27  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVGIDQPVALlaergldllgmivgsfkagagYLPLDP-------------------- 3795
Cdd:cd05966   82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAI---------------------YMPMIPelviamlacarigavhsvvf 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3796 -GHPTQRLT-RIVELSRTLVLVCTQACR-----------EQALalfDELGCVDR---------------PRLLVWDEIQQ 3847
Cdd:cd05966  141 aGFSAESLAdRINDAQCKLVITADGGYRggkviplkeivDEAL---EKCPSVEKvlvvkrtggevpmteGRDLWWHDLMA 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3848 GEGAEHDPQVYSgPQNLAYVIYTSGSTGLPKGVMVEQAG-MLNNQLSKVPYLELDENDVIAQTAsqsfDISvW-----QF 3921
Cdd:cd05966  218 KQSPECEPEWMD-SEDPLFILYTSGSTGKPKGVVHTTGGyLLYAATTFKYVFDYHPDDIYWCTA----DIG-WitghsYI 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3922 LAAPLF-GARVAI---VPNAvaHDPQGLLAHVGEQGITVLESVPSLI-----QGMLAEERQALDGLRWMLPTGEAMPPEl 3992
Cdd:cd05966  292 VYGPLAnGATTVMfegTPTY--PDPGRYWDIVEKHKVTIFYTAPTAIralmkFGDEWVKKHDLSSLRVLGSVGEPINPE- 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3993 ARQWLKRYprIGLvnaygpaecsddvafFRVDLAST----ES-----TYLPIGSPTD--NNRLYLLGAGA---DDAFELV 4058
Cdd:cd05966  369 AWMWYYEV--IGK---------------ERCPIVDTwwqtETggimiTPLPGATPLKpgSATRPFFGIEPailDEEGNEV 431
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4059 PLGAVGELCVAGT--GVGRGYVGDPLRTAQAFVpHPFgaPGerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGE 4136
Cdd:cd05966  432 EGEVEGYLVIKRPwpGMARTIYGDHERYEDTYF-SKF--PG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAE 506
                        490
                 ....*....|....*.
gi 15597620 4137 IEARLHERADVREAAV 4152
Cdd:cd05966  507 VESALVAHPAVAEAAV 522
PLN02479 PLN02479
acetate-CoA ligase
152-556 3.28e-08

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 59.86  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   152 DPAVAeaWDEPQVRPEHIAfLQYTSGSTALPKGVQVSH--GNLVANEVLIRRGFGIGAddvIVSW-LPLYHDMGLIGGLL 228
Cdd:PLN02479  183 DPEFA--WKPPADEWQSIA-LGYTSGTTASPKGVVLHHrgAYLMALSNALIWGMNEGA---VYLWtLPMFHCNGWCFTWT 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   229 QPIFSGVPCVLmspRYFLERPVrwLEAISQYGGT-VSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLE 307
Cdd:PLN02479  257 LAALCGTNICL---RQVTAKAI--YSAIANYGVThFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFAMS 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   308 RFAEKFAASrfdassffacYGLAEatlfvTGGQrgQGIPALAVDGEAL---ARNRIAEGEGSvlmccgRSQPEHAVLIVD 384
Cdd:PLN02479  332 EKGFRVTHT----------YGLSE-----TYGP--STVCAWKPEWDSLppeEQARLNARQGV------RYIGLEGLDVVD 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   385 AASGEVLGDD--NVGEIWAAGPSIAHGYWRNPEASAKAFverdGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLY 461
Cdd:PLN02479  389 TKTMKPVPADgkTMGEIVMRGNMVMKGYLKNPKANEEAF----ANGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENIS 464
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   462 PQDIERTV-------ESEV---PSARKGRVAAFAVT----VDGEEGIGIAAEIGRGVQKSVPAQELidsirqavaeayqe 527
Cdd:PLN02479  465 SLEVENVVythpavlEASVvarPDERWGESPCAFVTlkpgVDKSDEAALAEDIMKFCRERLPAYWV-------------- 530
                         410       420
                  ....*....|....*....|....*....
gi 15597620   528 aPKVVALlnpGALPKTSSGKLQRSACRLR 556
Cdd:PLN02479  531 -PKSVVF---GPLPKTATGKIQKHVLRAK 555
PLN03102 PLN03102
acyl-activating enzyme; Provisional
2336-2689 5.40e-08

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 59.26  E-value: 5.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2336 LIYTSGSTGKPKGVAVSH-GEIAMHCAAVIecfGMRAEDCELHFYSI---NFDAASERLLAPLLCGARVVLRaqgQWGAE 2411
Cdd:PLN03102  191 LNYTSGTTADPKGVVISHrGAYLSTLSAII---GWEMGTCPVYLWTLpmfHCNGWTFTWGTAARGGTSVCMR---HVTAP 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2412 EICELIRAEGVSILGFTPSYGSQLAQW--LESQGRQLPVRMcITGGEALTGEHLQRIRQ-AFapaSFFNAYGPTETVVMP 2488
Cdd:PLN03102  265 EIYKNIEMHNVTHMCCVPTVFNILLKGnsLDLSPRSGPVHV-LTGGSPPPAALVKKVQRlGF---QVMHAYGLTEATGPV 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2489 LACLAPE---RLEEGAaSVPIGSVVGARVAYILDAD------LALVPQ-GAT-GELYVGGAGLARGYHERPALSAERFvp 2557
Cdd:PLN03102  341 LFCEWQDewnRLPENQ-QMELKARQGVSILGLADVDvknketQESVPRdGKTmGEIVIKGSSIMKGYLKNPKATSEAF-- 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2558 dpfaaEGGRLyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPS-GKQLAGYVas 2636
Cdd:PLN03102  418 -----KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETPCAFV-- 489
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2637 aVAEQDEDAQAALREALKT-------HLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PLN03102  490 -VLEKGETTKEDRVDKLVTrerdlieYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
2211-2655 6.47e-08

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 59.01  E-value: 6.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2211 TLSYAELDARSNRLARVLRS-HGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS 2289
Cdd:cd17632   67 TITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2290 --------------------------------HAALFEALGELPAGVARWCLEEDGPALDAEDPAPLAALSGPQHQ---A 2334
Cdd:cd17632  147 saehldlaveavleggtpprlvvfdhrpevdaHRAALESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDdplA 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2335 YLIYTSGSTGKPKGvavshgeiAMHCAAVIECFGMRAEDCE---------LHFYSIN-------------------FDAA 2386
Cdd:cd17632  227 LLIYTSGSTGTPKG--------AMYTERLVATFWLKVSSIQdirppasitLNFMPMShiagrislygtlarggtayFAAA 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2387 S---------------ERLLAPLLC-------GARVVLRAQGQWGAEEICELIRAEgvsilgftpsygsqLAQwlESQGR 2444
Cdd:cd17632  299 SdmstlfddlalvrptELFLVPRVCdmlfqryQAELDRRSVAGADAETLAERVKAE--------------LRE--RVLGG 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2445 QLPVRMCitgGEALTGEHLQRIRQAFAPASFFNAYGPTETvvmplaclaperleeGAASVPiGSVVGARVayiLDADLAL 2524
Cdd:cd17632  363 RLLAAVC---GSAPLSAEMKAFMESLLDLDLHDGYGSTEA---------------GAVILD-GVIVRPPV---LDYKLVD 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2525 VPQ---------GATGELYVGGAGLARGYHERPALSAERFVPDPFaaeggrlYRTGDLVRLCDNGQVEYVGRIDHQVKI- 2594
Cdd:cd17632  421 VPElgyfrtdrpHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDVMAELGPDRLVYVDRRNNVLKLs 493
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2595 RGFRIELGEIEARLLEHPQVRE---------ALVLALDSPSGKQLAGyvasavaEQDEDAQAALREALKT 2655
Cdd:cd17632  494 QGEFVTVARLEAVFAASPLVRQifvygnserAYLLAVVVPTQDALAG-------EDTARLRAALAESLQR 556
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3740-4230 7.93e-08

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 58.55  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQA 3819
Cdd:PRK13391   26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3820 CREQALALFDELGCVdRPRLLVwDEIQQGEG----AEHDPQVYSGP---QNL-AYVIYTSGSTGLPKGVmveqagmlnnq 3891
Cdd:PRK13391  106 KLDVARALLKQCPGV-RHRLVL-DGDGELEGfvgyAEAVAGLPATPiadESLgTDMLYSSGTTGRPKGI----------- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3892 lskvpYLELDENDVIAQTASQSFDISVWQFL-------------AAPLFGARVAIVPNAVA-----HDPQGLLAHVGEQG 3953
Cdd:PRK13391  173 -----KRPLPEQPPDTPLPLTAFLQRLWGFRsdmvylspaplyhSAPQRAVMLVIRLGGTVivmehFDAEQYLALIEEYG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3954 ITVLESVPSLIQGML---AEERQALD--GLRWMLPTGEAMPPELARQWLKRYPRIglVNAYgpaecsddvaffrvdLAST 4028
Cdd:PRK13391  248 VTHTQLVPTMFSRMLklpEEVRDKYDlsSLEVAIHAAAPCPPQVKEQMIDWWGPI--IHEY---------------YAAT 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4029 EStylpIGSPTDNNRLYLLGAGA------------DDAFELVPLGAVGELCVAGtGVGRGYVGDPLRTAQAFVPHPfgap 4096
Cdd:PRK13391  311 EG----LGFTACDSEEWLAHPGTvgramfgdlhilDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG---- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4097 geRLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVavqegangkylvgYLVPGE----- 4171
Cdd:PRK13391  382 --TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAV-------------FGVPNEdlgee 446
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620  4172 -----TPRSSADSPAGLMVEQGAWferikqqLRADLPDYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PRK13391  447 vkavvQPVDGVDPGPALAAELIAF-------CRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3727-3995 8.71e-08

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 57.96  E-value: 8.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3727 PQRIAASCLEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHP-TQRLTRI 3805
Cdd:PRK09029   17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPqPLLEELL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3806 VELSRTLVLVCTQACREQALALFDELGCVDRPRLLvWDeiqqgegaehdpqvysgPQNLAYVIYTSGSTGLPKGVmveqA 3885
Cdd:PRK09029   97 PSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVA-WQ-----------------PQRLATMTLTSGSTGLPKAA----V 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3886 GMLNNQL-SKVPYLELdendvIAQTASQS-------FDIS----VWQFLAAplfGARVAIvpnavaHDPQGLLAHVgeQG 3953
Cdd:PRK09029  155 HTAQAHLaSAEGVLSL-----MPFTAQDSwllslplFHVSgqgiVWRWLYA---GATLVV------RDKQPLEQAL--AG 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 15597620  3954 ITVLESVPSLIQGMLAEERQALdGLRWMLPTGEAMPPELARQ 3995
Cdd:PRK09029  219 CTHASLVPTQLWRLLDNRSEPL-SLKAVLLGGAAIPVELTEQ 259
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
2210-2661 9.75e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 58.23  E-value: 9.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2210 QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAG-------GAYVPldpeyplERLQYMIEDS 2282
Cdd:PRK00174   97 RKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGFSA-------EALADRIIDA 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2283 GVRLLLS-------------HAALFEALGELP------------------AGVARWCLEEDGPALDAEDPAPLAAlsgpQ 2331
Cdd:PRK00174  170 GAKLVITadegvrggkpiplKANVDEALANCPsvekvivvrrtggdvdwvEGRDLWWHELVAGASDECEPEPMDA----E 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2332 HQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAED---CEL-------HFYSInfdaaserlLAPLLCGARV 2400
Cdd:PRK00174  246 DPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKyVFDYKDGDvywCTAdvgwvtgHSYIV---------YGPLANGATT 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2401 VL-------RAQGQWGaeeicELIRAEGVSILgftpsYGSQLAqwlesqgrqlpVRMCITGGEALTGEH-LQRIR----- 2467
Cdd:PRK00174  317 LMfegvpnyPDPGRFW-----EVIDKHKVTIF-----YTAPTA-----------IRALMKEGDEHPKKYdLSSLRllgsv 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2468 -QAFAPAS---FFNAYG----P-------TET---VVMPLACLAPerLEEGAASVPIGSVVGArvayILDADLALVPQGA 2529
Cdd:PRK00174  376 gEPINPEAwewYYKVVGgercPivdtwwqTETggiMITPLPGATP--LKPGSATRPLPGIQPA----VVDEEGNPLEGGE 449
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2530 TGELYVGGA--GLARGYHERPalsaERFVPDPFAAEGGRlYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEAR 2607
Cdd:PRK00174  450 GGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 524
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  2608 LLEHPQVREALVL-ALDSPSGKQLAGYVasaVAEQDEDAQAALREALKTHLKQQL 2661
Cdd:PRK00174  525 LVAHPKVAEAAVVgRPDDIKGQGIYAFV---TLKGGEEPSDELRKELRNWVRKEI 576
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
162-234 1.11e-07

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 58.18  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620   162 PQvRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDVIVSWLPLYHDMGLIGGLLQPIFSG 234
Cdd:PRK08043  361 KQ-QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTG 432
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
2198-2627 1.15e-07

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 58.05  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2198 ASPQAPALTFAGQT-----LSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP- 2271
Cdd:cd05943   80 ADADDPAAIYAAEDgerteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGv 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2272 ---LERLQ-----YMIEDSGVRL---LLSHAA-LFEALGELPAGVARWCLEEDGPA--LDAEDPAP-------LAALSGP 2330
Cdd:cd05943  160 pgvLDRFGqiepkVLFAVDAYTYngkRHDVREkVAELVKGLPSLLAVVVVPYTVAAgqPDLSKIAKaltledfLATGAAG 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2331 Q---------HQAYLIYTSGSTGKPKGVAVSHGEIAM-HCAAVIECFGMRAEDcELHFYSI------NFdaaserLLAPL 2394
Cdd:cd05943  240 ElefeplpfdHPLYILYSSGTTGLPKCIVHGAGGTLLqHLKEHILHCDLRPGD-RLFYYTTcgwmmwNW------LVSGL 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2395 LCGARVVL------RAQGQWgaeeICELIRAEGVSILGFTPSYGSQLAQWLESQGRQL---PVRMCITGGEALTGEHLQR 2465
Cdd:cd05943  313 AVGATIVLydgspfYPDTNA----LWDLADEEGITVFGTSAKYLDALEKAGLKPAETHdlsSLRTILSTGSPLKPESFDY 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2466 IRQAFAPASFFNAY-GPTETVvmplACLAperleEGAASVPIGS------VVGARVAYILDADLALVpqGATGELYVGGA 2538
Cdd:cd05943  389 VYDHIKPDVLLASIsGGTDII----SCFV-----GGNPLLPVYRgeiqcrGLGMAVEAFDEEGKPVW--GEKGELVCTKP 457
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2539 GLAR--GYHERPalSAERFVPDPFAAEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVRE 2616
Cdd:cd05943  458 FPSMpvGFWNDP--DGSRYRAAYFAKYPG-VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVED 534
                        490
                 ....*....|.
gi 15597620 2617 ALVLALDSPSG 2627
Cdd:cd05943  535 SLVVGQEWKDG 545
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3836-4233 1.54e-07

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 58.05  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3836 RPRLLVWDEIQqGEGAEHDPQVYSG---PQNLAYVIYTSGSTGLPKGVMVEQAGMLNN--QLSKVpyLELDENDVI--AQ 3908
Cdd:PRK06814  765 RAQIGLADKIK-GLLAGRFPLVYFCnrdPDDPAVILFTSGSEGTPKGVVLSHRNLLANraQVAAR--IDFSPEDKVfnAL 841
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3909 TASQSFDISVWQFLAApLFGARVAIVPNAVAHD--PQgllaHVGEQGITVLESVPSLIQGMlAEERQALD--GLRWMLPT 3984
Cdd:PRK06814  842 PVFHSFGLTGGLVLPL-LSGVKVFLYPSPLHYRiiPE----LIYDTNATILFGTDTFLNGY-ARYAHPYDfrSLRYVFAG 915
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3985 GEAMPPELARQWLKRYpRIGLVNAYGPAECSDDVA-----FFRvdlASTESTYLPigsptdnnrlyllgaGADDAFELVP 4059
Cdd:PRK06814  916 AEKVKEETRQTWMEKF-GIRILEGYGVTETAPVIAlntpmHNK---AGTVGRLLP---------------GIEYRLEPVP 976
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4060 -LGAVGELCVAGTGVGRGYvgdpLRTAQAFVPHPfgaPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIE 4138
Cdd:PRK06814  977 gIDEGGRLFVRGPNVMLGY----LRAENPGVLEP---PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE 1049
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4139 ARLHE-RADVREAAVAVQEGANGKYLVgyLVpgeTPRSSADSPAGLmveqgawferiKQQLRADLPDYMVPLHWLVLDRM 4217
Cdd:PRK06814 1050 ELAAElWPDALHAAVSIPDARKGERII--LL---TTASDATRAAFL-----------AHAKAAGASELMVPAEIITIDEI 1113
                         410
                  ....*....|....*.
gi 15597620  4218 PLNANGKLDRKALPAL 4233
Cdd:PRK06814 1114 PLLGTGKIDYVAVTKL 1129
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
25-227 1.80e-07

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 57.47  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   25 RLALRFLAEDDGegvvLSYRDL--DLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArr 102
Cdd:cd17632   56 RTTLRLLPRFET----ITYAELweRVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASA-- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  103 hhqERLLSIIADAEPRLVLTTA----------------------DLREPLLQMNAQLSAAN---APQLLCVDQLDPAVAE 157
Cdd:cd17632  130 ---AQLAPILAETEPRLLAVSAehldlaveavleggtpprlvvfDHRPEVDAHRAALESARerlAAVGIPVTTLTLIAVR 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  158 AWD-------EPQVRPEHIAFLQYTSGSTALPKGVQVSHgNLVANEVLIRRGFGIG--ADDVIVSWLPLYHDMG---LIG 225
Cdd:cd17632  207 GRDlppaplfRPEPDDDPLALLIYTSGSTGTPKGAMYTE-RLVATFWLKVSSIQDIrpPASITLNFMPMSHIAGrisLYG 285

                 ..
gi 15597620  226 GL 227
Cdd:cd17632  286 TL 287
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
106-567 1.89e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 57.49  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   106 ERLLSIIAD---AEPRLVLTTADLREPLLQMNAQLSAANAPQLLcvdqlDPAVAEaWDEPQVRPEHIAFLQYTSGSTALP 182
Cdd:PRK05620  123 EQLGEILKEcpcVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL-----DGRSTV-YDWPELDETTAAAICYSTGTTGAP 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   183 KGVQVSHGNLVANEVLIRR--GFGIGADDVIVSWLPLYHDMGLiGGLLQPIFSGVPCVL----------------MSPRY 244
Cdd:PRK05620  197 KGVVYSHRSLYLQSLSLRTtdSLAVTHGESFLCCVPIYHVLSW-GVPLAAFMSGTPLVFpgpdlsaptlakiiatAMPRV 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   245 FLERPVRWLEAISQYggtvsggpdfayrlcservAESALQRLDLsgwRVAFSGSEPIRQDSLERFAEKFAASrfdassFF 324
Cdd:PRK05620  276 AHGVPTLWIQLMVHY-------------------LKNPPERMSL---QEIYVGGSAVPPILIKAWEERYGVD------VV 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   325 ACYGLAEATLFVTGGQrgqgiPALAVDGEALARNRIAEGEGSVLMccgrsqpehAVLIVDaaSGEVLG--DDNVGEIWAA 402
Cdd:PRK05620  328 HVWGMTETSPVGTVAR-----PPSGVSGEARWAYRVSQGRFPASL---------EYRIVN--DGQVMEstDRNEGEIQVR 391
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   403 GPSIAHGYWRNP----------------EASAKAFVErDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDI 465
Cdd:PRK05620  392 GNWVTASYYHSPteegggaastfrgedvEDANDRFTA-DG--WLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQL 468
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   466 ER-------TVESEV---PSARKGRvAAFAVTVdgeegigIAAEIGRGVQKsvpAQELIDSIRQAVAEAYqeAPKVVALL 535
Cdd:PRK05620  469 ENyimaapeVVECAVigyPDDKWGE-RPLAVTV-------LAPGIEPTRET---AERLRDQLRDRLPNWM--LPEYWTFV 535
                         490       500       510
                  ....*....|....*....|....*....|..
gi 15597620   536 NpgALPKTSSGKLQRSACRLRLEDGSLDSYAL 567
Cdd:PRK05620  536 D--EIDKTSVGKFDKKDLRQHLADGDFEIIKL 565
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
3856-4230 1.93e-07

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 57.06  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3856 QVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQLSKVPYLELDENDVIaqtasqsfdisvwqFLAAPLFGARVAIVP 3935
Cdd:cd05937   81 FVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRT--------------YTCMPLYHGTAAFLG 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3936 --NAVAHDPQGLLAH----------VGEQGITVLESVPSLIQGMLAEERQALDGL-RWMLPTGEAMPPELARQWLKRY-- 4000
Cdd:cd05937  147 acNCLMSGGTLALSRkfsasqfwkdVRDSGATIIQYVGELCRYLLSTPPSPYDRDhKVRVAWGNGLRPDIWERFRERFnv 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4001 PRIG---------------LVNAYGPAEC-----------SDDVAFFRVDLASTEstylPIGSPTDnnrlyllgagaddA 4054
Cdd:cd05937  227 PEIGefyaategvfaltnhNVGDFGAGAIghhglirrwkfENQVVLVKMDPETDD----PIRDPKT-------------G 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4055 F-ELVPLGAVGELCVAGTGVGR----GYVGDPLRTAQAFVPHPFgAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRG 4129
Cdd:cd05937  290 FcVRAPVGEPGEMLGRVPFKNReafqGYLHNEDATESKLVRDVF-RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKS 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4130 FRIELGEIEARLHERADVREAAVavqegangkylVGYLVPGETPRSSAdspAGLMVEQGAW------FERIKQQLRADLP 4203
Cdd:cd05937  369 ENVSTTEVADVLGAHPDIAEANV-----------YGVKVPGHDGRAGC---AAITLEESSAvpteftKSLLASLARKNLP 434
                        410       420
                 ....*....|....*....|....*..
gi 15597620 4204 DYMVPLHWLVLDRMPLNANGKLDRKAL 4230
Cdd:cd05937  435 SYAVPLFLRLTEEVATTDNHKQQKGVL 461
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
4136-4224 1.93e-07

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 51.01  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   4136 EIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSAdspaglmveqgawfERIKQQLRADLPDYMVPLHWLVL 4214
Cdd:pfam13193    1 EVESALVSHPAVAEAAVvGVPDELKGEAPVAFVVLKPGVELLE--------------EELVAHVREELGPYAVPKEVVFV 66
                           90
                   ....*....|
gi 15597620   4215 DRMPLNANGK 4224
Cdd:pfam13193   67 DELPKTRSGK 76
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
427-658 2.65e-07

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 55.53  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  427 RTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIERTVESEVPSARKGRVAAFAVTVDGEEGIGIAAEIGRGVQk 506
Cdd:COG3433   62 AAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAG- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  507 sVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGSLDSYALFPGLQAVQEAQPPAGD-DE 585
Cdd:COG3433  141 -VGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALEtAL 219
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  586 LLARIGEIWKARLGV--AQVAPRDHFFLLGGNSIGAAQVVAQVRdSLGVALDLRQLFEAPTLQAFSATVARQLAA 658
Cdd:COG3433  220 TEEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDVSFADLAEHPTLAAWWALLAAAQAA 293
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2334-2689 2.84e-07

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 55.95  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2334 AYLIYTSGSTGKPKGVAVSH-GEIAMH-CAAVIECFGMRAE-DCELHFYSINfdAASERLLAPLLCGARVVLRAQGQWGA 2410
Cdd:cd05944    5 AAYFHTGGTTGTPKLAQHTHsNEVYNAwMLALNSLFDPDDVlLCGLPLFHVN--GSVVTLLTPLASGAHVVLAGPAGYRN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2411 E----EICELIRAEGVSILGFTPSYGSQLAQwlesqgrqLPV-------RMCITGGEALTGEHLQRIrQAFAPASFFNAY 2479
Cdd:cd05944   83 PglfdNFWKLVERYRITSLSTVPTVYAALLQ--------VPVnadisslRFAMSGAAPLPVELRARF-EDATGLPVVEGY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2480 GPTETVVMpLACLAPERleegaaSVPIGSVvGARVAY------ILDADLALVPQGA---TGELYVGGAGLARGY----HE 2546
Cdd:cd05944  154 GLTEATCL-VAVNPPDG------PKRPGSV-GLRLPYarvrikVLDGVGRLLRDCApdeVGEICVAGPGVFGGYlyteGN 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2547 RPALSAERFVpdpfaaeggrlyRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVreALVLALDSPS 2626
Cdd:cd05944  226 KNAFVADGWL------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV--AFAGAVGQPD 291
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620 2627 GKqlAGYVASAVAEQDEDAQAAlREALKTHLKQQLPDYM-VPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:cd05944  292 AH--AGELPVAYVQLKPGAVVE-EEELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPAL 352
prpE PRK10524
propionyl-CoA synthetase; Provisional
14-583 2.93e-07

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 56.88  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    14 ALRRRAVQEPERLALRFLAEDDGEGVVLSYRDL-DLRARSIAAALQAHAQLGDRAVLLFPSGPDYVAAFFGCLYAGVI-- 90
Cdd:PRK10524   58 AVDRHLAKRPEQLALIAVSTETDEERTYTFRQLhDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIhs 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    91 ------AVPAyppesarrhhqerLLSIIADAEPRLVLTT-ADLR-------EPLLQMNAQLSAANAPQLLCVD-QLDP-- 153
Cdd:PRK10524  138 vvfggfASHS-------------LAARIDDAKPVLIVSAdAGSRggkvvpyKPLLDEAIALAQHKPRHVLLVDrGLAPma 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   154 ----------AVAEAWDEPQVRPE-----HIAFLQYTSGSTALPKGVQVSHGNL-VANEVLIRRGFGIGADDVIVSwlpl 217
Cdd:PRK10524  205 rvagrdvdyaTLRAQHLGARVPVEwlesnEPSYILYTSGTTGKPKGVQRDTGGYaVALATSMDTIFGGKAGETFFC---- 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   218 YHDMG------------LIGGLLQPIFSGVPCvlmspryfleRPVR--WLEAISQYGGTVSGGPDFAYRLCsERVAESAL 283
Cdd:PRK10524  281 ASDIGwvvghsyivyapLLAGMATIMYEGLPT----------RPDAgiWWRIVEKYKVNRMFSAPTAIRVL-KKQDPALL 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   284 QRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAssffacYGLAEAtlfvtggqrgqGIPALAVdgealarNRIAEG 363
Cdd:PRK10524  350 RKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDN------YWQTET-----------GWPILAI-------ARGVED 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   364 EGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWAAGPsIAHGY----WRNPEASAKAFVERDGRTWLRTGDLGFL- 438
Cdd:PRK10524  406 RPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGP-LPPGCmqtvWGDDDRFVKTYWSLFGRQVYSTFDWGIRd 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   439 RDGELFVTGRLKDMLIVRGHNLYPQDIERTVESE----------VPSARKGRVA-AFAVTVDGEEGIGIAAEigRGVQKS 507
Cdd:PRK10524  485 ADGYYFILGRTDDVINVAGHRLGTREIEESISSHpavaevavvgVKDALKGQVAvAFVVPKDSDSLADREAR--LALEKE 562
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620   508 VpaQELIDSIRQAVAEayqeaPKVVALLNpgALPKTSSGKLQRSAcrlrledgsldsyalfpgLQAVQEAQPPaGD 583
Cdd:PRK10524  563 I--MALVDSQLGAVAR-----PARVWFVS--ALPKTRSGKLLRRA------------------IQAIAEGRDP-GD 610
PRK09192 PRK09192
fatty acyl-AMP ligase;
1154-1295 3.07e-07

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 56.55  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYP-------SERLAYMLADSGV 1226
Cdd:PRK09192   50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQP 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  1227 ELLLTQAHLFE-------RLPGAEGVTPICLDSLkldnwpsQAPGLHL---HGDNLAYVIYTSGSTGQPKGVGNTHAAL 1295
Cdd:PRK09192  130 AAIITPDELLPwvneathGNPLLHVLSHAWFKAL-------PEADVALprpTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
PLN02654 PLN02654
acetate-CoA ligase
2211-2689 3.80e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 56.44  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2211 TLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLS- 2289
Cdd:PLN02654  120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITc 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2290 ----------------HAALFEALGElpaGVA------------------RWCLEED---------GPA------LDAED 2320
Cdd:PLN02654  200 navkrgpktinlkdivDAALDESAKN---GVSvgicltyenqlamkredtKWQEGRDvwwqdvvpnYPTkcevewVDAED 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2321 PAplaalsgpqhqaYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIE-CFGMRAEDcelhFYSINFDAA-----SERLLAPL 2394
Cdd:PLN02654  277 PL------------FLLYTSGSTGKPKGVLHTTGGYMVYTATTFKyAFDYKPTD----VYWCTADCGwitghSYVTYGPM 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2395 LCGARVVL--RAQGQWGAEEICELIRAEGVSILGFTPSYgsqlaqwlesqgrqlpVRMCITGGEALTGEH-------LQR 2465
Cdd:PLN02654  341 LNGATVLVfeGAPNYPDSGRCWDIVDKYKVTIFYTAPTL----------------VRSLMRDGDEYVTRHsrkslrvLGS 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2466 IRQAFAPAS---FFNAYG-----------PTET---VVMPLACLAPERleEGAASVPIGSVVGArvayILDADLALVPQG 2528
Cdd:PLN02654  405 VGEPINPSAwrwFFNVVGdsrcpisdtwwQTETggfMITPLPGAWPQK--PGSATFPFFGVQPV----IVDEKGKEIEGE 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2529 ATGELYVGGA--GLAR---GYHERpalsAERFVPDPFAAeggrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGE 2603
Cdd:PLN02654  479 CSGYLCVKKSwpGAFRtlyGDHER----YETTYFKPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAE 550
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2604 IEARLLEHPQVREALVLALDSPSGKQlaGYVASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGK 2683
Cdd:PLN02654  551 VESALVSHPQCAEAAVVGIEHEVKGQ--GIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGK 628

                  ....*.
gi 15597620  2684 LDRRAL 2689
Cdd:PLN02654  629 IMRRIL 634
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
2214-2637 4.31e-07

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 55.93  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2214 YAELDARS-NRLARVLRSHGVGPevrVGLALERSLEMVVGLLAILKAGGAyVPLDP------------EYPLERLQYMie 2280
Cdd:PRK05851   34 WPEVHGRAeNVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGAA-VSILPgpvrgaddgrwaDATLTRFAGI-- 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2281 dsGVRLLLSHAALFEALGELPAGVArwcLEEDGPALDAEDPAPL--AALSGPqhqAYLIYTSGSTGKPKGVAVSHGEIAM 2358
Cdd:PRK05851  108 --GVRTVLSHGSHLERLRAVDSSVT---VHDLATAAHTNRSASLtpPDSGGP---AVLQGTAGSTGTPRTAILSPGAVLS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2359 HCAAVIECFGM-RAEDCELHFYSINFDAASERLLAPLLCGARVVLRAQG----------QWGAEEICELIRAE--GVSIL 2425
Cdd:PRK05851  180 NLRGLNARVGLdAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTafsaspfrwlSWLSDSRATLTAAPnfAYNLI 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2426 GftpSYGSQLAQWLESQgrqlpVRMCITGGEALTGEHLQRIRQAFAPASF-----FNAYGPTE-----TVVMPLACLAPE 2495
Cdd:PRK05851  260 G---KYARRVSDVDLGA-----LRVALNGGEPVDCDGFERFATAMAPFGFdagaaAPSYGLAEstcavTVPVPGIGLRVD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2496 RLEEGAASVPI------GSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERPALSAerfvpdpfaaegGRLYR 2569
Cdd:PRK05851  332 EVTTDDGSGARrhavlgNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAPIDP------------DDWFP 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2570 TGDLVRLCDNGQVeYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAGYVASA 2637
Cdd:PRK05851  400 TGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAA 466
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
1539-1616 4.44e-07

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 50.24  E-value: 4.44e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620   1539 EIQARLLAQPGVAQAVVV-IREGVAGSQLVGYYTGAVGAEAEAEqnqRLRAALQAELPEYMVPTQLMRLAQMPLGPSGK 1616
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVgVPDELKGEAPVAFVVLKPGVELLEE---ELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK08162 PRK08162
acyl-CoA synthetase; Validated
2192-2666 4.85e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 56.11  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2192 FAARVAAS-PQAPALTFAGQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2270
Cdd:PRK08162   23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2271 PLERLQYMIEDSGVRLLLS----HAALFEALGELPA------GVArwcLEEDGPA-----LDAE------DPAPLAALSG 2329
Cdd:PRK08162  103 DAASIAFMLRHGEAKVLIVdtefAEVAREALALLPGpkplviDVD---DPEYPGGrfigaLDYEaflasgDPDFAWTLPA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2330 PQHQAY-LIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCEL------------HFYSInfdAASerllapllC 2396
Cdd:PRK08162  180 DEWDAIaLNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLwtlpmfhcngwcFPWTV---AAR--------A 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2397 GARVVLRaqgQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLES--QGRQLPVRMcITGGEALTGEHLQRIRQA-Fapa 2473
Cdd:PRK08162  249 GTNVCLR---KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEwrAGIDHPVHA-MVAGAAPPAAVIAKMEEIgF--- 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2474 SFFNAYGPTETVVMPLACLapERLEEGAASVPIGSVVGAR--VAY-------ILDAD-LALVPQ-GAT-GELYVGGAGLA 2541
Cdd:PRK08162  322 DLTHVYGLTETYGPATVCA--WQPEWDALPLDERAQLKARqgVRYplqegvtVLDPDtMQPVPAdGETiGEIMFRGNIVM 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2542 RGYHERPALSAERFvpdpfaaEGGrLYRTGDLVRLCDNGqveYVgridhQVKIR--------GFRIELGEIEARLLEHPQ 2613
Cdd:PRK08162  400 KGYLKNPKATEEAF-------AGG-WFHTGDLAVLHPDG---YI-----KIKDRskdiiisgGENISSIEVEDVLYRHPA 463
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  2614 VREALVLALdsPSGKQlaGYVASAVAEQDEDAQAAlREALKTHLKQQLPDYMV 2666
Cdd:PRK08162  464 VLVAAVVAK--PDPKW--GEVPCAFVELKDGASAT-EEEIIAHCREHLAGFKV 511
PRK07868 PRK07868
acyl-CoA synthetase; Validated
1127-1652 6.46e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 55.88  E-value: 6.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1127 RAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYV 1206
Cdd:PRK07868  446 RISLGRIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAV 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1207 PLDPDypsERLAYMLADSGVELLLTQ-AHLFER-----------------LPGAEGVTPICL-----DSLKLDNWPSQAP 1263
Cdd:PRK07868  526 LMPPD---TDLAAAVRLGGVTEIITDpTNLEAArqlpgrvlvlgggesrdLDLPDDADVIDMekidpDAVELPGWYRPNP 602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1264 GLhlhGDNLAYVIY-TSGSTGQPKGVGNTHAALAerlQWMQATYT-LDGDDVLMQKAP--------VSFDVSVwecfwpl 1333
Cdd:PRK07868  603 GL---ARDLAFIAFsTAGGELVAKQITNYRWALS---AFGTASAAaLDRRDTVYCLTPlhhesgllVSLGGAV------- 669
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1334 VTGCRLVLAapgEHRDPARLVELVRQFGVTTLHFVPPLLQLFIDEPGVAACGSLR-RLFSgGEALPAELRNRVLQRLPAV 1412
Cdd:PRK07868  670 VGGSRIALS---RGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPvRLFI-GSGMPTGLWERVVEAFAPA 745
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1413 ALHNRYGPTETAI---NVTHwqcrAEDGERspiGRPL---GNVVCRVLDAEFNLL---PAGVAGELCIGGLGLargYLGR 1483
Cdd:PRK07868  746 HVVEFFATTDGQAvlaNVSG----AKIGSK---GRPLpgaGRVELAAYDPEHDLIledDRGFVRRAEVNEVGV---LLAR 815
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1484 PalsaeRFVADPFSAAGERLYRTGDR-------ARWNADGVLEYLGRLDQQVK-LRGFrIEPEEIQARLLAQPGVAQAVV 1555
Cdd:PRK07868  816 A-----RGPIDPTASVKRGVFAPADTwisteylFRRDDDGDYWLVDRRGSVIRtARGP-VYTEPVTDALGRIGGVDLAVT 889
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1556 ViREGVAGSQL-VGYYTGAVGAEAEAEQnqrLRAALqAELPEYMVPTQLMRLAQMPLGPS-----GKLDTRALPEP---V 1626
Cdd:PRK07868  890 Y-GVEVGGRQLaVAAVTLRPGAAITAAD---LTEAL-ASLPVGLGPDIVHVVPEIPLSATyrptvSALRAAGIPKPgrqA 964
                         570       580
                  ....*....|....*....|....*..
gi 15597620  1627 WqqreHVEPRTELQRRI-AAIWSEVLG 1652
Cdd:PRK07868  965 W----YFDPETNRYRRLtPAVRAELTG 987
PLN02574 PLN02574
4-coumarate--CoA ligase-like
3740-4153 7.15e-07

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 55.62  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3740 SYAELNRRANRLGHALRAAGvGIDQP--VALLAERGLDLLGMIVGSFKAGAGYLPLDP-GHPTQRLTRIVELSRTLVLVC 3816
Cdd:PLN02574   68 SYSELQPLVKSMAAGLYHVM-GVRQGdvVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPsSSLGEIKKRVVDCSVGLAFTS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3817 TQ-ACREQALALfdelgcvdrPRLLVWDEIQQGEGAEHDPQVYS--------------GPQNLAYVIYTSGSTGLPKGVM 3881
Cdd:PLN02574  147 PEnVEKLSPLGV---------PVIGVPENYDFDSKRIEFPKFYElikedfdfvpkpviKQDDVAAIMYSSGTTGASKGVV 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3882 VEQagmlNNQLSKVPYLELDENDVIAQTASQSFdisvwqFLAA-PLF---------------GARVAIVPNAVAHDpqgL 3945
Cdd:PLN02574  218 LTH----RNLIAMVELFVRFEASQYEYPGSDNV------YLAAlPMFhiyglslfvvgllslGSTIVVMRRFDASD---M 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3946 LAHVGEQGITVLESVPSLIQGMLAEERQA----LDGLRwMLPTGEA-MPPELARQWLKRYPRIGLVNAYGPAEcSDDVAF 4020
Cdd:PLN02574  285 VKVIDRFKVTHFPVVPPILMALTKKAKGVcgevLKSLK-QVSCGAApLSGKFIQDFVQTLPHVDFIQGYGMTE-STAVGT 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4021 fRVDLASTESTYLPIG--SPTDNNRLYLLGAGAddafeLVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPhpfgapgE 4098
Cdd:PLN02574  363 -RGFNTEKLSKYSSVGllAPNMQAKVVDWSTGC-----LLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK-------D 429
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  4099 RLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVA 4153
Cdd:PLN02574  430 GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVT 484
PRK03584 PRK03584
acetoacetate--CoA ligase;
2198-2431 7.48e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 55.57  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2198 ASPQAPALTFAG-----QTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP- 2271
Cdd:PRK03584   96 RRDDRPAIIFRGedgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGv 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2272 ---LERLQyMIE------------------------------DSGVRLLLSHAALFEALGELPAGVARWcleEDgpALDA 2318
Cdd:PRK03584  176 qgvLDRFG-QIEpkvliavdgyryggkafdrrakvaelraalPSLEHVVVVPYLGPAAAAAALPGALLW---ED--FLAP 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2319 EDPAPLAALSGP-QHQAYLIYTSGSTGKPKGVAVSHG--------EIAMHCaaviecfGMRAEDCeLHFYSI------NF 2383
Cdd:PRK03584  250 AEAAELEFEPVPfDHPLWILYSSGTTGLPKCIVHGHGgillehlkELGLHC-------DLGPGDR-FFWYTTcgwmmwNW 321
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  2384 daaserLLAPLLCGARVVL--------RAQGQWgaeeicELIRAEGVSILGFTPSY 2431
Cdd:PRK03584  322 ------LVSGLLVGATLVLydgspfypDPNVLW------DLAAEEGVTVFGTSAKY 365
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
3736-4246 1.09e-06

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 55.01  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRWSYAELNRRANRLGHALRAAGVG------IDQP------VALLA-ERgldlLGMI----VGSF-------------- 3784
Cdd:cd05967   80 ERTYTYAELLDEVSRLAGVLRKLGVVkgdrviIYMPmipeaaIAMLAcAR----IGAIhsvvFGGFaakelasriddakp 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3785 ----KAGAG--------YLPLdpghptqrLTRIVELSRTLVLVCTQACREQAlalfdELGCVDRPRLLVWDEIQQGeGAE 3852
Cdd:cd05967  156 klivTASCGiepgkvvpYKPL--------LDKALELSGHKPHHVLVLNRPQV-----PADLTKPGRDLDWSELLAK-AEP 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3853 HDPQVYSGPQNLaYVIYTSGSTGLPKGVMVEQAG---MLNNQLSKVpyLELDENDVIaQTASqsfDISvW----QFLA-A 3924
Cdd:cd05967  222 VDCVPVAATDPL-YILYTSGTTGKPKGVVRDNGGhavALNWSMRNI--YGIKPGDVW-WAAS---DVG-WvvghSYIVyG 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3925 PLFGARVAIV----PNAVAhDPQGLLAHVGEQGITVLESVPSLIQGMLAEERQA-------LDGLRWMLPTGEAMPPELA 3993
Cdd:cd05967  294 PLLHGATTVLyegkPVGTP-DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGkyikkydLSSLRTLFLAGERLDPPTL 372
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3994 rQWLKRYPRIGLVNAYGPAECSDDVAFFRVDLAStestyLPI--GSPTD---NNRLYLLgagaDDAFELVPLGAVGELCV 4068
Cdd:cd05967  373 -EWAENTLGVPVIDHWWQTETGWPITANPVGLEP-----LPIkaGSPGKpvpGYQVQVL----DEDGEPVGPNELGNIVI 442
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4069 AGT---GVGRGYVGDPLRTAQAFVPHpfgAPGerLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERA 4145
Cdd:cd05967  443 KLPlppGCLLTLWKNDERFKKLYLSK---FPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHP 517
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4146 DVREAAV-AVQEGANGKYLVGYLVPGETPRSSADSpaglmveqgawferIKQQLRADLPDYMVPL----HWLVLDRMPLN 4220
Cdd:cd05967  518 AVAECAVvGVRDELKGQVPLGLVVLKEGVKITAEE--------------LEKELVALVREQIGPVaafrLVIFVKRLPKT 583
                        570       580
                 ....*....|....*....|....*.
gi 15597620 4221 ANGKLDRKALPALdigqMQNQAYQAP 4246
Cdd:cd05967  584 RSGKILRRTLRKI----ADGEDYTIP 605
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
3737-4108 1.18e-06

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 54.88  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3737 QRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP-----GHPTQRLTRIVELSR- 3810
Cdd:PRK08180   68 RRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslvSQDFGKLRHVLELLTp 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3811 TLVLVCTQACREQALALFDELGCV---------DRPRLLVWDEIQQGEGAEHD---PQVysGPQNLAYVIYTSGSTGLPK 3878
Cdd:PRK08180  148 GLVFADDGAAFARALAAVVPADVEvvavrgavpGRAATPFAALLATPPTAAVDaahAAV--GPDTIAKFLFTSGSTGLPK 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3879 GVMVEQAGMLNNQLskvpyleldendVIAQTasqsfdisvWQFLA-APL-----------FGArVAIVPNAVAH------ 3940
Cdd:PRK08180  226 AVINTHRMLCANQQ------------MLAQT---------FPFLAeEPPvlvdwlpwnhtFGG-NHNLGIVLYNggtlyi 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3941 D-----PQGL---LAHVGEQGITVLESVP----SLIQGMLAEE---RQALDGLRWMLPTGEAMPP-------ELARQWLK 3998
Cdd:PRK08180  284 DdgkptPGGFdetLRNLREISPTVYFNVPkgweMLVPALERDAalrRRFFSRLKLLFYAGAALSQdvwdrldRVAEATCG 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3999 RypRIGLVNAYGPAECSDDVAF--FRVDLAStestylPIGSPTdnnrlyllgAGADdaFELVPLGAVGELCVAGTGVGRG 4076
Cdd:PRK08180  364 E--RIRMMTGLGMTETAPSATFttGPLSRAG------NIGLPA---------PGCE--VKLVPVGGKLEVRVKGPNVTPG 424
                         410       420       430
                  ....*....|....*....|....*....|..
gi 15597620  4077 YVGDPLRTAQAFvphpfgaPGERLYRTGDLAR 4108
Cdd:PRK08180  425 YWRAPELTAEAF-------DEEGYYRSGDAVR 449
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2149-2653 1.43e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 54.88  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2149 EALLGDPQRRIAELPLFAAeERKQLLLAGTAGEAGLQDTLHGLFAARVAASPQAPALTFAGQTLSYAELDARSNRLARVL 2228
Cdd:COG3321  850 SALYPGRGRRRVPLPTYPF-QREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA 928
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2229 RSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLLSHAALFEALGELPAGVARWC 2308
Cdd:COG3321  929 LLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2309 LEEDGPALDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELHFYSINFDAASE 2388
Cdd:COG3321 1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAA 1088
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2389 RLLAPLLCGARVVLRAQGQWGAEEICELIRAEGVSILGFTPSYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQ 2468
Cdd:COG3321 1089 ALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALL 1168
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2469 AFAPASFFNAYGPTETVVMPLACLAPERLEEGAASVPIGSVVGARVAYILDADLALVPQGATGELYVGGAGLARGYHERP 2548
Cdd:COG3321 1169 AAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAAL 1248
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2549 ALSAERFVPDPFAAEGGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGK 2628
Cdd:COG3321 1249 AAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAA 1328
                        490       500
                 ....*....|....*....|....*
gi 15597620 2629 QLAGYVASAVAEQDEDAQAALREAL 2653
Cdd:COG3321 1329 ALAALAAAVAAALALAAAAAAAAAA 1353
PRK08308 PRK08308
acyl-CoA synthetase; Validated
2564-2691 1.64e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 53.89  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2564 GGRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVL-ALDSPSGKQlagyVASAVAEQD 2642
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrGKDPVAGER----VKAKVISHE 364
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15597620  2643 EDAQAALREalktHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALPA 2691
Cdd:PRK08308  365 EIDPVQLRE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
2209-2373 1.95e-06

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 53.97  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2209 GQTLSYAELDARSNRLARVLRSHGVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRlll 2288
Cdd:cd05939    1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAK--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2289 shAALFEALGELPAgvarwcleedgpalDAEDPAPLAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFG 2368
Cdd:cd05939   78 --ALIFNLLDPLLT--------------QSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFG 141

                 ....*
gi 15597620 2369 MRAED 2373
Cdd:cd05939  142 MRPED 146
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2813-3080 2.12e-06

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 53.64  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2813 ALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAFRQvDGEWLAQH--RPLREQELLWHVPVQSFDECAELFAKAQRSLDLE 2890
Cdd:cd19546   30 SVALRLRGRLDRDALEAALGDVAARHEILRTTFPG-DGGDVHQRilDADAARPELPVVPATEEELPALLADRAAHLFDLT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2891 QGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVSWRVLLEDLQQVYRQFAEGAEP---ALPAKTSAFRDWAGRLQAYAGS-E 2966
Cdd:cd19546  109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPeraPLPLQFADYALWERELLAGEDDrD 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2967 SL-REELGWWQARLGGQP--VEWPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRTQVNdLLLTALARVLCRWS 3043
Cdd:cd19546  189 SLiGDQIAYWRDALAGAPdeLELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFT-VVQAALAMLLTRLG 267
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15597620 3044 GQPSTLVQLEGHGREalfDDIDLTRSVGWFTSAYPLR 3080
Cdd:cd19546  268 AGTDVTVGTVLPRDD---EEGDLEGMVGPFARPLALR 301
PLN02614 PLN02614
long-chain acyl-CoA synthetase
155-473 3.76e-06

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 53.10  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   155 VAEAWDE------------PQVRPEHIAFLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFG-----IGADDVIVSWLPL 217
Cdd:PLN02614  199 VIYAWDEflklgegkqydlPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPL 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   218 YHDM------------GLIG-------------GLLQP-IFSGVPCVL----------MSPRYFLERPVrWLEAISQYGG 261
Cdd:PLN02614  279 AHIFdrvieecfiqhgAAIGfwrgdvklliedlGELKPtIFCAVPRVLdrvysglqkkLSDGGFLKKFV-FDSAFSYKFG 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   262 TVSGGPDF--AYRLCSERVAESALQRLDlSGWRVAFSGSEPIrQDSLERFAEKFAasrfdASSFFACYGLAE--ATLFVT 337
Cdd:PLN02614  358 NMKKGQSHveASPLCDKLVFNKVKQGLG-GNVRIILSGAAPL-ASHVESFLRVVA-----CCHVLQGYGLTEscAGTFVS 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   338 G-------GQRGQGIPALAVDGEalarnriaegegsvlmccgrSQPEhavLIVDAasgevLGDDNVGEIWAAGPSIAHGY 410
Cdd:PLN02614  431 LpdeldmlGTVGPPVPNVDIRLE--------------------SVPE---MEYDA-----LASTPRGEICIRGKTLFSGY 482
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620   411 WRNPEASAKAFVerDGrtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIErTVESEV 473
Cdd:PLN02614  483 YKREDLTKEVLI--DG--WLHTGDVGeWQPNGSMKIIDRKKNIFkLSQGEYVAVENIE-NIYGEV 542
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
1278-1560 3.85e-06

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 52.63  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1278 TSGSTGQPKGVGNTHAALaERLQWMQAtYTLD-----GDDVLMqkapVSFDVSVWECFWPLVTGC-RL-VLAAPGEHRDP 1350
Cdd:cd05913   86 SSGTTGKPTVVGYTKNDL-DVWAELVA-RCLDaagvtPGDRVQ----NAYGYGLFTGGLGFHYGAeRLgALVIPAGGGNT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1351 ARLVELVRQFGVTTLHFVPPLLQLFIDEpgVAACG------SLRRLFSGGEALPAELRNRVLQRLPAVAlHNRYGPTETA 1424
Cdd:cd05913  160 ERQLQLIKDFGPTVLCCTPSYALYLAEE--AEEEGidprelSLKVGIFGAEPWTEEMRKRIERRLGIKA-YDIYGLTEII 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1425 INVTHWQCRAEDGerspigrpLG----NVVCRVLDAEFN-LLPAGVAGELCIGGlglargyLGRPALSAERfvadpfsaa 1499
Cdd:cd05913  237 GPGVAFECEEKDG--------LHiwedHFIPEIIDPETGePVPPGEVGELVFTT-------LTKEAMPLIR--------- 292
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620 1500 gerlYRTGDRARwNADG----------VLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQA--VVVIREG 1560
Cdd:cd05913  293 ----YRTRDITR-LLPGpcpcgrthrrIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHyqLILTRQE 360
PRK07798 PRK07798
acyl-CoA synthetase; Validated
23-547 3.98e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 52.97  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    23 PERLALRFLAEddgegvVLSYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPA-Yppesa 100
Cdd:PRK07798   17 PDRVALVCGDR------RLTYAELEERANRLAHYLIAQgLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnY----- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   101 rRHHQERLLSIIADAEPRLVLTTADLREPLLQMNAQLS-----------AANAPQLLCVDqLDPAVAEAwDEPQVRPEHI 169
Cdd:PRK07798   86 -RYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPklrtlvvvedgSGNDLLPGAVD-YEDALAAG-SPERDFGERS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   170 A---FLQYTSGSTALPKGVQVSH---------------GNLVANEVLIRRGfgiGADDVIVSWL---PLYHDMGLIGGlL 228
Cdd:PRK07798  163 PddlYLLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKR---AAAGPGMRRFpapPLMHGAGQWAA-F 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   229 QPIFSGVPCVLMSPRYFleRPVRWLEAISQYGGTVSG--GPDFAYRLCSERVAESalqRLDLSGWRVAFSG----SEPIR 302
Cdd:PRK07798  239 AALFSGQTVVLLPDVRF--DADEVWRTIEREKVNVITivGDAMARPLLDALEARG---PYDLSSLFAIASGgalfSPSVK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   303 QDSLERFAEKFAASRFDASSFFACYglaeaTLFVTGGQRGQGIPalavdgealarnriaegegsvlmccgRSQPEHAVLI 382
Cdd:PRK07798  314 EALLELLPNVVLTDSIGSSETGFGG-----SGTVAKGAVHTGGP--------------------------RFTIGPRTVV 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   383 VDAASGEVL-GDDNVGEIwAAGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLR-DGELFVTGRlkDMLIVR--GH 458
Cdd:PRK07798  363 LDEDGNPVEpGSGEIGWI-ARRGHIPLGYYKDPEKTAETFPTIDGVRYAIPGDRARVEaDGTITLLGR--GSVCINtgGE 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   459 NLYPQDIERTVESE----------VPSARKG-RVAAFAVTVDGeegigiaaeigrgvqKSVPAQELIDSIRQAVAeAYQe 527
Cdd:PRK07798  440 KVFPEEVEEALKAHpdvadalvvgVPDERWGqEVVAVVQLREG---------------ARPDLAELRAHCRSSLA-GYK- 502
                         570       580
                  ....*....|....*....|
gi 15597620   528 APKVVALLNpgALPKTSSGK 547
Cdd:PRK07798  503 VPRAIWFVD--EVQRSPAGK 520
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
4247-4316 6.16e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 47.24  E-value: 6.16e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597620    4247 RNELEETLARIWAEVLKVERVGVFD---NFFELGGHSLLATQIASRVQKALQRNVPLRAMFECTTVEELASYI 4316
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PLN03051 PLN03051
acyl-activating enzyme; Provisional
3804-4230 7.05e-06

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 52.13  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3804 RIVELSRTLVLVCTQACREQALALfdelgcvdRPRLLVWDE-------IQQGEGAEHDPqVYSGPQNLAYVIYTSGSTGL 3876
Cdd:PLN03051   63 KVVEAAPAKAIVLPAAGEPVAVPL--------REQDLSWCDflgvaaaQGSVGGNEYSP-VYAPVESVTNILFSSGTTGE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3877 PKGVMVEQAGMLNNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLFGARVAIVPNAvahdP--QGLLAHVGEQGI 3954
Cdd:PLN03051  134 PKAIPWTHLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGA----PlgRGFGKFVQDAGV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3955 TVLESVPSLIQ-----GMLAEERQALDGLRWMLPTGEAMPPElARQWL---KRYPRiGLVNAYGPAECSDDVAFFRVDLA 4026
Cdd:PLN03051  210 TVLGLVPSIVKawrhtGAFAMEGLDWSKLRVFASTGEASAVD-DVLWLssvRGYYK-PVIEYCGGTELASGYISSTLLQP 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4027 STESTYlpiGSPTDNNRLYLLGAGADDAFELVPlgAVGELCVAGTGVG---RGYVGDPLRTAQAFVPHpFGAPGERLYRT 4103
Cdd:PLN03051  288 QAPGAF---STASLGTRFVLLNDNGVPYPDDQP--CVGEVALAPPMLGasdRLLNADHDKVYYKGMPM-YGSKGMPLRRH 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4104 GDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEaRLHERAD---VREAAVAV---QEGANGKYLVGYLVPGETPRSSA 4177
Cdd:PLN03051  362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIE-RACDRAVagiAETAAVGVappDGGPELLVIFLVLGEEKKGFDQA 440
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597620  4178 DSPAGLMVEQGAwferIKQQLRadlPDYMVPlHWLVLDRMPLNANGKLDRKAL 4230
Cdd:PLN03051  441 RPEALQKKFQEA----IQTNLN---PLFKVS-RVKIVPELPRNASNKLLRRVL 485
PRK08308 PRK08308
acyl-CoA synthetase; Validated
4097-4232 8.50e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 51.58  E-value: 8.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4097 GERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAVQEGANGKYLVGYLVPGETPRSS 4176
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP 368
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  4177 ADspaglmveqgawferIKQQLRADLPDYMVPLHWLVLDRMPLNANGKLDRKALPA 4232
Cdd:PRK08308  369 VQ---------------LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
PLN02614 PLN02614
long-chain acyl-CoA synthetase
1156-1530 1.04e-05

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 51.95  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1156 YAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTQ--- 1232
Cdd:PLN02614   82 YQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEekk 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1233 -AHLFERLPGAE----------GVTP-------------------ICLDSLKLDNWPSQAPglhlhgDNLAYVIYTSGST 1282
Cdd:PLN02614  162 iSELFKTCPNSTeymktvvsfgGVSReqkeeaetfglviyawdefLKLGEGKQYDLPIKKK------SDICTIMYTSGTT 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1283 GQPKGVGNTHAALAERLQWM-----QATYTLDGDDVLMQKAPVS--FDVSVWEC---------FW--------------- 1331
Cdd:PLN02614  236 GDPKGVMISNESIVTLIAGVirllkSANAALTVKDVYLSYLPLAhiFDRVIEECfiqhgaaigFWrgdvklliedlgelk 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1332 -------PLV-----TGCRLVLAAPGEHRDPARLVELVRQFGV-----TTLHFVPPLLQLFIDEPGVAACGSLRRLFSGG 1394
Cdd:PLN02614  316 ptifcavPRVldrvySGLQKKLSDGGFLKKFVFDSAFSYKFGNmkkgqSHVEASPLCDKLVFNKVKQGLGGNVRIILSGA 395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1395 EALPAELRNrVLQRLPAVALHNRYGPTETAINvTHWQCRAEDGERSPIGRPLGNVVCR---VLDAEFNLLPAGVAGELCI 1471
Cdd:PLN02614  396 APLASHVES-FLRVVACCHVLQGYGLTESCAG-TFVSLPDELDMLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICI 473
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  1472 GGLGLARGYLGRPALSAERFVadpfsaagERLYRTGDRARWNADGVLEYLGRLDQQVKL 1530
Cdd:PLN02614  474 RGKTLFSGYYKREDLTKEVLI--------DGWLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
1151-1314 1.41e-05

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 51.14  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1151 GGSLGYAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELL 1229
Cdd:cd05938    3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1230 LTQAHLF----ERLPG-----------AEGVTPICLDSL--KLDNWPSQAP----GLHLHGDNLAYVIYTSGSTGQPKGV 1288
Cdd:cd05938   83 VVAPELQeaveEVLPAlradgvsvwylSHTSNTEGVISLldKVDAASDEPVpaslRAHVTIKSPALYIYTSGTTGLPKAA 162
                        170       180
                 ....*....|....*....|....*....
gi 15597620 1289 GNTHaalaERLQWMQATYTLDG---DDVL 1314
Cdd:cd05938  163 RISH----LRVLQCSGFLSLCGvtaDDVI 187
PRK05850 PRK05850
acyl-CoA synthetase; Validated
3739-4154 1.82e-05

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 50.71  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3739 WSyaELNRRANRLGHALRAAGVGIDQpVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRI--VELSRTLVLVC 3816
Cdd:PRK05850   38 WS--QLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERVsaVLRDTSPSVVL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3817 TQACREQALALFDELGCVDR-PRLLVWDEIQQGEGAEHDPQVYSGPqNLAYVIYTSGSTGLPKGVMVEQAGMLNN--QLS 3893
Cdd:PRK05850  115 TTSAVVDDVTEYVAPQPGQSaPPVIEVDLLDLDSPRGSDARPRDLP-STAYLQYTSGSTRTPAGVMVSHRNVIANfeQLM 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3894 KvPYLELDENDVIAQTASQSF-----DISVWQFLAAPLFGARVAIVPNAVAhdpqgllahvgeqgitVLESVPSLIQgML 3968
Cdd:PRK05850  194 S-DYFGDTGGVPPPDTTVVSWlpfyhDMGLVLGVCAPILGGCPAVLTSPVA----------------FLQRPARWMQ-LL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3969 AEERQA-------------------------LDGLRWMLPTGEAMPPELARQWLKRYPRIGLVN-----AYGPAECSDDV 4018
Cdd:PRK05850  256 ASNPHAfsaapnfafelavrktsdddmagldLGGVLGIISGSERVHPATLKRFADRFAPFNLREtairpSYGLAEATVYV 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4019 AFFRVDLAST----ESTYLPIG----SPTDN-NRLYLLGAGADDAFELV--------PLGAVGELCVAGTGVGRGYVGDP 4081
Cdd:PRK05850  336 ATREPGQPPEsvrfDYEKLSAGhakrCETGGgTPLVSYGSPRSPTVRIVdpdtciecPAGTVGEIWVHGDNVAAGYWQKP 415
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  4082 LRTAQAF-----VPHPfGAPGERLYRTGDLArRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVAV 4154
Cdd:PRK05850  416 EETERTFgatlvDPSP-GTPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGGRVAAISV 491
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
3736-3881 2.80e-05

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 50.29  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3736 EQRW-SYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGagyLPldpghptqrltrIVELSRTLvl 3814
Cdd:cd17639    2 EYKYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IP------------IVTVYATL-- 64
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 3815 vctqacREQALAL-FDELGCvdrpRLLVWDeiqqgegaehdpqvySGPQNLAYVIYTSGSTGLPKGVM 3881
Cdd:cd17639   65 ------GEDALIHsLNETEC----SAIFTD---------------GKPDDLACIMYTSGSTGNPKGVM 107
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
64-556 2.93e-05

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 49.87  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   64 GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyppesarrhhqerllsiiadaepRLVLTTADLREPLLQMNAQLSAanap 143
Cdd:cd05974   25 GDRILLMLGNVVELWEAMLAAMKLGAVVIPA-----------------------TTLLTPDDLRDRVDRGGAVYAA---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  144 qllcVDQLDPAvaeawDEPQVrpehiafLQYTSGSTALPKGVQVSHGNLVANEVLIRRGFGIGADDV---IVSWLPLYHD 220
Cdd:cd05974   78 ----VDENTHA-----DDPML-------LYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVhwnISSPGWAKHA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  221 MGligGLLQPIFSGVPCVLMSPRYFleRPVRWLEAISQYGGTVSGGPDFAYRLcservaesaLQRLDLSGWRVAF----S 296
Cdd:cd05974  142 WS---CFFAPWNAGATVFLFNYARF--DAKRVLAALVRYGVTTLCAPPTVWRM---------LIQQDLASFDVKLrevvG 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  297 GSEPIRQDSLERFAEKFAASRFDAssffacYGLAEATLFVtGGQRGQGIPAlavdgealarnriaegeGSVlmccGRSQP 376
Cdd:cd05974  208 AGEPLNPEVIEQVRRAWGLTIRDG------YGQTETTALV-GNSPGQPVKA-----------------GSM----GRPLP 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  377 EHAVLIVDAASGEVLGDDNVGEIWAAGP-SIAHGYWRNPEASAKAFveRDGrtWLRTGDLGFLR-DGELFVTGRLKDMLI 454
Cdd:cd05974  260 GYRVALLDPDGAPATEGEVALDLGDTRPvGLMKGYAGDPDKTAHAM--RGG--YYRTGDIAMRDeDGYLTYVGRADDVFK 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  455 VRGHNLYPQDIERT-VESE-------VPSARKGRVA---AFAVTVDGEEgigiaaeigrgvQKSVPAQELIDSIRQAVAe 523
Cdd:cd05974  336 SSDYRISPFELESVlIEHPavaeaavVPSPDPVRLSvpkAFIVLRAGYE------------PSPETALEIFRFSRERLA- 402
                        490       500       510
                 ....*....|....*....|....*....|...
gi 15597620  524 ayqeAPKVVALLNPGALPKTSSGKLQRSACRLR 556
Cdd:cd05974  403 ----PYKRIRRLEFAELPKTISGKIRRVELRRR 431
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
1108-1296 3.35e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 49.97  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1108 DAEQAAHLAEWGSAPCEPARawLPELLERQLAQSA------ERVALEW----DGGS-------------LGYAELHARAN 1164
Cdd:PTZ00216   55 DEEHERLRNEWYYGPNFLQR--LERICKERGDRRAlayrpvERVEKEVvkdaDGKErtmevthfnetryITYAELWERIV 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1165 RLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAI----VKAGGAYVPLDPDypseRLAYMLADSGVELLLTQAH------ 1234
Cdd:PTZ00216  133 NFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLGED----ALAYALRETECKAIVCNGKnvpnll 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1235 -LFeRLPGAEGVTPICLDSL---------KLDNW----------PSQAPG-LHLHGDNLAYVIYTSGSTGQPKGVGNTHA 1293
Cdd:PTZ00216  209 rLM-KSGGMPNTTIIYLDSLpasvdtegcRLVAWtdvvakghsaGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTHG 287

                  ...
gi 15597620  1294 ALA 1296
Cdd:PTZ00216  288 SLT 290
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
42-219 4.57e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 49.70  E-value: 4.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620    42 SYRDLDLRARSIAAALQAH-AQLGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesarRHHQERLLSIIADAEPRLV 120
Cdd:PRK07008   41 TYRDCERRAKQLAQALAALgVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINP-----RLFPEQIAYIVNHAEDRYV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   121 ---LTTADLREPL------------LQMNAQLSAANAPqLLCVDQLDPAVAEAWDEPQVRPEHIAFLQYTSGSTALPKGV 185
Cdd:PRK07008  116 lfdLTFLPLVDALapqcpnvkgwvaMTDAAHLPAGSTP-LLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGA 194
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 15597620   186 QVSHGNLV--ANEVLIRRGFGIGADDVIVSWLPLYH 219
Cdd:PRK07008  195 LYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFH 230
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
575-656 5.95e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 44.55  E-value: 5.95e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620     575 QEAQPPAGDDELLARIGEIWKARLGVA---QVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFEAPTLQAFSAT 651
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81

                    ....*
gi 15597620     652 VARQL 656
Cdd:smart00823   82 LAAEL 86
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
2568-2712 6.05e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 49.35  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2568 YRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLALDSPSGKQLAgyVASAVAEQDEDAQA 2647
Cdd:PTZ00237  494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVP--IGLLVLKQDQSNQS 571
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597620  2648 A----LREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALpapDPALNRQAYEAPRSVLEQQL 2712
Cdd:PTZ00237  572 IdlnkLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII---SKFLNDSNYQLPDNVNDSEI 637
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
3740-4131 6.36e-05

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 49.27  E-value: 6.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3740 SYAELNRRANRLGHALR-AAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGHPTQRLTRIVELSRTLVLVCTQ 3818
Cdd:cd05905   16 TWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3819 ACREQALALFD---ELGCVDR----PRLLVWDEIQQGEGAEHDPQVYSGPQN---LAYVIYTSGSTGLPKGVMVEQAGML 3888
Cdd:cd05905   96 ACLKGLPKKLLkskTAAEIAKkkgwPKILDFVKIPKSKRSKLKKWGPHPPTRdgdTAYIEYSFSSDGSLSGVAVSHSSLL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3889 NNQLSKVPYLELDENDVIAQTASQSFDISVWQFLAAPLF-GARVAIVP-NAVAHDPQGLL----------AHVGEQGITV 3956
Cdd:cd05905  176 AHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYsGHHTILIPpELMKTNPLLWLqtlsqykvrdAYVKLRTLHW 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3957 LESVPSLIQGMLAEERQALDGLR-WMLPTGEamPPELAR--QWLKRYPRIGL------------------VNAYGPAECS 4015
Cdd:cd05905  256 CLKDLSSTLASLKNRDVNLSSLRmCMVPCEN--RPRISScdSFLKLFQTLGLspravstefgtrvnpficWQGTSGPEPS 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4016 DDVaffrVDLASTESTYLPIGSPTDNNRLYLLGAGaddafeLVPLGA-----------------VGELCVAGTGVGRGY- 4077
Cdd:cd05905  334 RVY----LDMRALRHGVVRLDERDKPNSLPLQDSG------KVLPGAqvaivnpetkglckdgeIGEIWVNSPANASGYf 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620 4078 --VGDPLRTAQAFVPHPFGAP-GERLY-RTGDL----------ARRRADGVLEYVGRIDHQVKIRGFR 4131
Cdd:cd05905  404 llDGETNDTFKVFPSTRLSTGiTNNSYaRTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLR 471
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1634-1707 6.37e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 44.16  E-value: 6.37e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620    1634 EPRTELQRRIAAIWSEVLGLP---RVGLRDDFFELGGHSLLATRIVSRTRQACDVELPLRALFEASELEAFCEQVRA 1707
Cdd:smart00823    8 ERRRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2702-2771 7.98e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 44.16  E-value: 7.98e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597620    2702 EAPRSVLEQQLAGVWREVLNV---ERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQSLAA 2771
Cdd:smart00823    7 AERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPAALAE 80
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
4061-4240 8.27e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 48.45  E-value: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4061 GAVGELCVAGTGVGRGYVgdplrtaqafvPHPFGAPgeRLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEAR 4140
Cdd:PRK07445  299 NQTGNITIQAQSLALGYY-----------PQILDSQ--GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4141 LHERADVREAAV-AVQEGANGKYLVGYLVPGETPRSSadspaglmveqgawfERIKQQLRADLPDYMVPLHWLVLDRMPL 4219
Cdd:PRK07445  366 ILATGLVQDVCVlGLPDPHWGEVVTAIYVPKDPSISL---------------EELKTAIKDQLSPFKQPKHWIPVPQLPR 430
                         170       180
                  ....*....|....*....|.
gi 15597620  4220 NANGKLDRKALPALDIGQMQN 4240
Cdd:PRK07445  431 NPQGKINRQQLQQIAVQRLGL 451
PLN02479 PLN02479
acetate-CoA ligase
2336-2666 8.37e-05

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 48.69  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2336 LIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDC---ELHFYSINFDAASERLLAplLCGARVVLRaqgQWGAEE 2412
Cdd:PLN02479  200 LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVylwTLPMFHCNGWCFTWTLAA--LCGTNICLR---QVTAKA 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2413 ICELIRAEGVSILGFTPSYGSQLAQWLESQgRQLPVRMCI---TGGEALTGEHLQRI-RQAFAPAsffNAYGPTETVVMP 2488
Cdd:PLN02479  275 IYSAIANYGVTHFCAAPVVLNTIVNAPKSE-TILPLPRVVhvmTAGAAPPPSVLFAMsEKGFRVT---HTYGLSETYGPS 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2489 LACL-APErleegAASVPIG--SVVGAR--VAYI----LDA----DLALVP-QGAT-GELYVGGAGLARGYHERPALSAE 2553
Cdd:PLN02479  351 TVCAwKPE-----WDSLPPEeqARLNARqgVRYIglegLDVvdtkTMKPVPaDGKTmGEIVMRGNMVMKGYLKNPKANEE 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2554 RFvpdpfaaEGGrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLA-LDSPSGKQLAG 2632
Cdd:PLN02479  426 AF-------ANG-WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVArPDERWGESPCA 497
                         330       340       350
                  ....*....|....*....|....*....|....
gi 15597620  2633 YVaSAVAEQDEDAQAALREALKTHLKQQLPDYMV 2666
Cdd:PLN02479  498 FV-TLKPGVDKSDEAALAEDIMKFCRERLPAYWV 530
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
396-466 9.25e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 48.45  E-value: 9.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597620   396 VGEIWAAGPSIAHGYWRNPEASAKAFVerdgrtwlrTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIE 466
Cdd:PRK07445  301 TGNITIQAQSLALGYYPQILDSQGIFE---------TDDLGYLdAQGYLHILGRNSQKIITGGENVYPAEVE 363
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
2603-2683 9.78e-05

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 43.30  E-value: 9.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620   2603 EIEARLLEHPQVREALVLAL-DSPSGKQLAGYVasaVAEQDEDAqaaLREALKTHLKQQLPDYMVPAHLLLLASLPLTAN 2681
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVpDELKGEAPVAFV---VLKPGVEL---LEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74

                   ..
gi 15597620   2682 GK 2683
Cdd:pfam13193   75 GK 76
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
3738-4153 1.30e-04

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 48.22  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3738 RWSYAELNRRAN----RLGHALRAAGVGidqpvaLLAERGLDLLGMIVGSFKAGAGyLPLDPGhptqrLTRIVELSR--- 3810
Cdd:PRK05851   31 RHPWPEVHGRAEnvaaRLLDRDRPGAVG------LVGEPTVELVAAIQGAWLAGAA-VSILPG-----PVRGADDGRwad 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3811 TLVLVCTQACREQALA---LFDELGCVDrPRLLVWDEIQQGEGAEHDPQVYSGPQNLAYVIYTSGSTGLPKGVMVEQAGM 3887
Cdd:PRK05851   99 ATLTRFAGIGVRTVLShgsHLERLRAVD-SSVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3888 LNNQLSKVPYLELDE-NDVIAQTASQSFDISVWQFLAAPLFGARVAIVPN-AVAHDPQGLLAHVGEQGITvLESVPSLIQ 3965
Cdd:PRK05851  178 LSNLRGLNARVGLDAaTDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTtAFSASPFRWLSWLSDSRAT-LTAAPNFAY 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3966 GMLAEERQALDG-----LRWMLPTGEAMPPELARQWLKRYPRIGL-----VNAYGPAECSDDVAF------FRVDLASTE 4029
Cdd:PRK05851  257 NLIGKYARRVSDvdlgaLRVALNGGEPVDCDGFERFATAMAPFGFdagaaAPSYGLAESTCAVTVpvpgigLRVDEVTTD 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4030 ST-----YLPIGSPTDNNRLYLlgAGADDAFELVPLGaVGELCVAGTGVGRGYVG-DPLRTAQAFvphpfgapgerlyRT 4103
Cdd:PRK05851  337 DGsgarrHAVLGNPIPGMEVRI--SPGDGAAGVAGRE-IGEIEIRGASMMSGYLGqAPIDPDDWF-------------PT 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597620  4104 GDLArRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAVA 4153
Cdd:PRK05851  401 GDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
171-547 1.50e-04

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 47.38  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  171 FLQYTSGSTALPKGVQVSHGNlvanevlIRRGFGIGAD-----DVIVSWL----------------PLYHDMGLIGGLLQ 229
Cdd:cd05924    7 YILYTGGTTGMPKGVMWRQED-------IFRMLMGGADfgtgeFTPSEDAhkaaaaaagtvmfpapPLMHGTGSWTAFGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  230 PiFSGVPCVLMSPRYfleRPVRWLEAISQYGGTVSG--GPDFAYRLCSERVAESALqrlDLSGWRVAFSG----SEPIRQ 303
Cdd:cd05924   80 L-LGGQTVVLPDDRF---DPEEVWRTIEKHKVTSMTivGDAMARPLIDALRDAGPY---DLSSLFAISSGgallSPEVKQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  304 DSLERFAEKFAASRFDASSffacyglaeatlfvTGGQrgqgipalavdGEALARNRIAEGEGsvlmccgRSQPEHAVLIV 383
Cdd:cd05924  153 GLLELVPNITLVDAFGSSE--------------TGFT-----------GSGHSAGSGPETGP-------FTRANPDTVVL 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  384 DAASGEVL-GDDNVGEIWAAGpSIAHGYWRNPEASAKAFVERDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLY 461
Cdd:cd05924  201 DDDGRVVPpGSGGVGWIARRG-HIPLGYYGDEAKTAETFPEVDGVRYAVPGDRAtVEADGTVTLLGRGSVCINTGGEKVF 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  462 PQDIERTVESE----------VPSARKG-RVAAfavTVDGEEGIGIAAEigrgvqksvpaqELIDSIRQAVAeAYQeAPK 530
Cdd:cd05924  280 PEEVEEALKSHpavydvlvvgRPDERWGqEVVA---VVQLREGAGVDLE------------ELREHCRTRIA-RYK-LPK 342
                        410
                 ....*....|....*..
gi 15597620  531 VVALLnpGALPKTSSGK 547
Cdd:cd05924  343 QVVFV--DEIERSPAGK 357
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
242-756 1.67e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 47.94  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  242 PRYFLERPVRWLEAISQYGGTVSGGPDFAYRLCSERVAESALQRLDLSGWRVAFSGSEPIRQDSLERFAEKFAASRFDAS 321
Cdd:COG3321  864 PTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALL 943
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  322 SFFACYGLAEATLFVTGGQRGQGIPALAVDGEALARNRIAEGEGSVLMCCGRSQPEHAVLIVDAASGEVLGDDNVGEIWA 401
Cdd:COG3321  944 ALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLA 1023
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  402 AGPSIAHGYWRNPEASAKAFVERDGRTWLRTGDLGFLRDGELfvtGRLKDMLIVRGHNLYPQDIERTVESEVPSARKGRV 481
Cdd:COG3321 1024 LAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALAL---AALLLLAALAELALAAAALALAAALAAAALALALA 1100
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  482 AAFAVTVDGEEGIGIAAEIGRGVQKSVPAQELIDSIRQAVAEAYQEAPKVVALLNPGALPKTSSGKLQRSACRLRLEDGS 561
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  562 LDSYALFPGLQAVQEAQPPAGDDELLARIGEIWKARLGVAQVAPRDHFFLLGGNSIGAAQVVAQVRDSLGVALDLRQLFE 641
Cdd:COG3321 1181 LAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  642 APTLQAFSATVARQLAAGLPAEAPMAHLPRGVDLPQSAAQQRLWLTWQIDPQSAAYNIPGGLRLRGELDEAALRASFQRL 721
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 15597620  722 VERHEALRTRFLERDGAALQRIDERGEFAWQFVDL 756
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAA 1375
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
4058-4233 2.31e-04

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 46.96  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4058 VPLGAV------GELCVAGTGVGRGYVGDPlrtaqafVPHPFGAPGerLYRTGDLARRrADGVLEYVGRIDHQVKIRGFR 4131
Cdd:PRK07824  196 VPLDGVrvrvedGRIALGGPTLAKGYRNPV-------DPDPFAEPG--WFRTDDLGAL-DDGVLTVLGRADDAISTGGLT 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4132 IELGEIEARLHERADVREAAV-AVQEGANGKYLVGYLVPGETPrssADSPAGLmveqgawferiKQQLRADLPDYMVPLH 4210
Cdd:PRK07824  266 VLPQVVEAALATHPAVADCAVfGLPDDRLGQRVVAAVVGDGGP---APTLEAL-----------RAHVARTLDRTAAPRE 331
                         170       180
                  ....*....|....*....|...
gi 15597620  4211 WLVLDRMPLNANGKLDRKALPAL 4233
Cdd:PRK07824  332 LHVVDELPRRGIGKVDRRALVRR 354
PRK09192 PRK09192
fatty acyl-AMP ligase;
3735-3889 2.44e-04

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 47.31  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3735 LEQRWSYAELNRRANRLGHALRAAGVGIDQPVALLAERGLDLLGMIVGSFKAGAGYLPLD-PGHPTQRLTRIVELSRTLv 3813
Cdd:PRK09192   46 LEEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIAQLRGML- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3814 lvctQACREQALALFDEL--------GCVDRPRLLVWDEIQQGEGAEHDPQVYSgPQNLAYVIYTSGSTGLPKGVMV-EQ 3884
Cdd:PRK09192  125 ----ASAQPAAIITPDELlpwvneatHGNPLLHVLSHAWFKALPEADVALPRPT-PDDIAYLQYSSGSTRFPRGVIItHR 199

                  ....*
gi 15597620  3885 AGMLN 3889
Cdd:PRK09192  200 ALMAN 204
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
2210-2689 3.05e-04

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 47.08  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2210 QTLSYAELDARSNRLARVLRSH-GVGPEVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLQYMIEDSGVRLLL 2288
Cdd:PRK05620   37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2289 SHAALFEALGELPAGvarwCLEEDGPALDAEDPAPLAALSGPQH--------------------------QAYLIYTSGS 2342
Cdd:PRK05620  117 ADPRLAEQLGEILKE----CPCVRAVVFIGPSDADSAAAHMPEGikvysyealldgrstvydwpeldettAAAICYSTGT 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2343 TGKPKGVAVSHGEIAMHCaaviecFGMRAED-----------CELHFYSInfdaaserL-----LAPLLCGARVVLRAQg 2406
Cdd:PRK05620  193 TGAPKGVVYSHRSLYLQS------LSLRTTDslavthgesflCCVPIYHV--------LswgvpLAAFMSGTPLVFPGP- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2407 QWGAEEICELI------RAEGVSILgftpsYGSQLAQWLESQGRQLPVRMCITGGEALTGEHLQRIRQAFApASFFNAYG 2480
Cdd:PRK05620  258 DLSAPTLAKIIatamprVAHGVPTL-----WIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYG-VDVVHVWG 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2481 PTETVVMplaclaperleeGAASVPIGSVVG-ARVAY--------------ILDADLALVPQGAT-GELYVGGAGLARGY 2544
Cdd:PRK05620  332 MTETSPV------------GTVARPPSGVSGeARWAYrvsqgrfpasleyrIVNDGQVMESTDRNeGEIQVRGNWVTASY 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2545 HERPA----LSAERF-------VPDPFAAEGgrLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQ 2613
Cdd:PRK05620  400 YHSPTeeggGAASTFrgedvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  2614 VREALVLALdsPSGKQLAGYVASAVAEQDEDAQAALREALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRAL 2689
Cdd:PRK05620  478 VVECAVIGY--PDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
431-550 3.94e-04

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 46.46  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  431 RTGDLGFLRDGE----------LFVTGRLKDMLIVRGHNLYPQDIErtvesEVPSARKGRVAAFAVTVDGEEG---IGIA 497
Cdd:cd05913  294 RTRDITRLLPGPcpcgrthrriDRITGRSDDMLIIRGVNVFPSQIE-----DVLLKIPGLGPHYQLILTRQEHldeLTIK 368
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620  498 AEigrgVQKSVPAQELIDSIRQAVAEAYQEAPKV---VALLNPGALPKtSSGKLQR 550
Cdd:cd05913  369 VE----VRPEADDDEKLEALKQRLERHIKSVLGVtveVELVEPGSLPR-SEGKAKR 419
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
3861-3905 4.76e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 46.26  E-value: 4.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 15597620  3861 PQNLAYVIYTSGSTGLPKGVMVEQAGMLNNQ---LSKVPylELDENDV 3905
Cdd:PLN02387  249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVagvMTVVP--KLGKNDV 294
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
2316-2621 5.13e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 46.26  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2316 LDAEDPAPlAALSGPQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECF-GMRAEDCELHFYSIN--FDAASERLLA 2392
Cdd:PLN02387  236 LGKENPVD-PDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAhiLELAAESVMA 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2393 PLLC----------------------GARVVLRAQGQWGAEEICELIR---------AEGVSILGFTPSY--------GS 2433
Cdd:PLN02387  315 AVGAaigygspltltdtsnkikkgtkGDASALKPTLMTAVPAILDRVRdgvrkkvdaKGGLAKKLFDIAYkrrlaaieGS 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2434 QLAQW-LESQ---------------GRqlpVRMCITGGEALTGEhLQRIRQAFAPASFFNAYGPTETvvmplaCLAPERL 2497
Cdd:PLN02387  395 WFGAWgLEKLlwdalvfkkiravlgGR---IRFMLSGGAPLSGD-TQRFINICLGAPIGQGYGLTET------CAGATFS 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2498 EEGAASVpigSVVGARV--AYIldadlALV--PQGA---------TGELYVGGAGLARGYHERPALSAERFVPDpfaAEG 2564
Cdd:PLN02387  465 EWDDTSV---GRVGPPLpcCYV-----KLVswEEGGylisdkpmpRGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERG 533
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597620  2565 GRLYRTGDLVRLCDNGQVEYVGRIDHQVKIR-GFRIELGEIEARLLEHPQVREALVLA 2621
Cdd:PLN02387  534 MRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHA 591
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
2330-2630 7.45e-04

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 45.86  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2330 PQHQAYLIYTSGSTGKPKGVAVSHGEIAMHCAAVIECFGMRAEDCELH----FYSINFDAAserLLAPLLCGARVVL--- 2402
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLyps 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2403 ----RAqgqwgaeeICELIRAEGVSILGFTPSYGSQLAQWLESQ--GRqlpVRMCITGGEALTgEHLQRIRQAFAPASFF 2476
Cdd:PRK08043  441 plhyRI--------VPELVYDRNCTVLFGTSTFLGNYARFANPYdfAR---LRYVVAGAEKLQ-ESTKQLWQDKFGLRIL 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2477 NAYGPTEtvvmplaClAPERleegAASVPIGSVVGArVAYIL---DADLALVP---QGatGELYVGGAGLARGYH--ERP 2548
Cdd:PRK08043  509 EGYGVTE-------C-APVV----SINVPMAAKPGT-VGRILpgmDARLLSVPgieQG--GRLQLKGPNIMNGYLrvEKP 573
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2549 AlsaerfVPDPFAAEGGR------LYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEA-RLLEHPQVREALVLA 2621
Cdd:PRK08043  574 G------VLEVPTAENARgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIK 647

                  ....*....
gi 15597620  2622 LDSPSGKQL 2630
Cdd:PRK08043  648 SDASKGEAL 656
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
2821-3044 7.76e-04

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 45.25  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2821 AIDLGLLRKSLQRLVEQHDALRLAFRQVDGewlAQHRPLREqellwHVPVQSFDECAELFAKAQRSLDLEQGPLLRAVLV 2900
Cdd:cd19537   35 DVDRDRLASAWNTVLARHRILRSRYVPRDG---GLRRSYSS-----SPPRVQRVDTLDVWKEINRPFDLEREDPIRVFIS 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2901 DGpageqRLLLAIHHLVVDGVSWRVLLEDLQQVYRqfaeGAEPALPAKTSAfrDWAGRLQAYAGseslrEELGWWQARLG 2980
Cdd:cd19537  107 PD-----TLLVVMSHIICDLTTLQLLLREVSAAYN----GKLLPPVRREYL--DSTAWSRPASP-----EDLDFWSEYLS 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597620 2981 GQPVewPCDRPQGDNREALAESVSLRLDPQRTRQLLQQAPAAYRT--QvndLLLTALARVLCRWSG 3044
Cdd:cd19537  171 GLPL--LNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITlhQ---LALAAVALALQDLSD 231
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1153-1295 8.46e-04

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 45.42  E-value: 8.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1153 SLGYAELHARANRLAHYLRDK-GVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLT 1231
Cdd:cd05905   14 TLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1232 QAHLFERLPGAEGVTPICLDSLKLDNWPS-----------------QAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA 1294
Cdd:cd05905   94 VEACLKGLPKKLLKSKTAAEIAKKKGWPKildfvkipkskrsklkkWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173

                 .
gi 15597620 1295 L 1295
Cdd:cd05905  174 L 174
PRK03584 PRK03584
acetoacetate--CoA ligase;
1153-1400 9.92e-04

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 45.17  E-value: 9.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1153 SLGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPS----ERLA---------- 1218
Cdd:PRK03584  114 ELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVqgvlDRFGqiepkvliav 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1219 --YMLADSGVELLLTQAHLFERLPGAEGVtpICLDSLKLDNWPSQAPGLHLHGDNLA------------------YVIYT 1278
Cdd:PRK03584  194 dgYRYGGKAFDRRAKVAELRAALPSLEHV--VVVPYLGPAAAAAALPGALLWEDFLApaeaaelefepvpfdhplWILYS 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  1279 SGSTGQPK----GVGNThaaLAERLQWMQATYTLDGDDVL---------MQKAPVSfdvsvwecfwPLVTGCRLVL--AA 1343
Cdd:PRK03584  272 SGTTGLPKcivhGHGGI---LLEHLKELGLHCDLGPGDRFfwyttcgwmMWNWLVS----------GLLVGATLVLydGS 338
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597620  1344 PGeHRDPARLVELVRQFGVTTLHFVPPllqlFID-------EPGVAAC-GSLRRLFSGGEALPAE 1400
Cdd:PRK03584  339 PF-YPDPNVLWDLAAEEGVTVFGTSAK----YLDacekaglVPGETHDlSALRTIGSTGSPLPPE 398
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
2479-2690 1.01e-03

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 44.99  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2479 YGPTETVVMpLACLAPERLEEGAASVpiGSVV-GARVAyildadlalVPQGATGELYVGGAGLARGYHerPALSAERfvp 2557
Cdd:PRK07445  261 YGMTETASQ-IATLKPDDFLAGNNSS--GQVLpHAQIT---------IPANQTGNITIQAQSLALGYY--PQILDSQ--- 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  2558 dpfaaeggRLYRTGDLVRLCDNGQVEYVGRIDHQVKIRGFRIELGEIEARLLEHPQVREALVLAL-DSPSGKQLagyVAS 2636
Cdd:PRK07445  324 --------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLpDPHWGEVV---TAI 392
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597620  2637 AVAEQDEDAQaalrEALKTHLKQQLPDYMVPAHLLLLASLPLTANGKLDRRALP 2690
Cdd:PRK07445  393 YVPKDPSISL----EELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2686-3209 1.22e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 45.25  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2686 RRALPAPDPALNRQAYEAPRSVLEQQLAGVWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQT 2765
Cdd:COG3321  858 RRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAA 937
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2766 VQSLAAVARHSQASQAEQGPVQGDSALTPIQHWFFDLPLARREHWNQALLLQPRQAIDLGLLRKSLQRLVEQHDALRLAF 2845
Cdd:COG3321  938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2846 RQVDGEWLAQHRPLREQELLWHVPVQSFDECAEL---FAKAQRSLDLEQGPLLRAVLVDGPAGEQRLLLAIHHLVVDGVS 2922
Cdd:COG3321 1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALaaaAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 2923 WRVLLEDLQQVYRQFAEGAEPALPAKTSAFRDWAGRLQAYAGSESLREELGWWQARLGGQPVEWPCDR-PQGDNREALAE 3001
Cdd:COG3321 1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAaLLAAAALLLAL 1177
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3002 SVSLRLDPQRTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSTLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRL 3081
Cdd:COG3321 1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLA 1257
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3082 TPAQSPGESIKAIKEQLRAVPHKGLGYGVLRYLADPAVRQAMAALPTAPITFNYLGQFDQSFADALFQPLDQPTGPIHDE 3161
Cdd:COG3321 1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 15597620 3162 QAPLPNELSVDGQVYGGELVLRWTYSRERYDARTVNELAQAYLAELQA 3209
Cdd:COG3321 1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
1154-1635 1.25e-03

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 44.72  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1154 LGYAELHARANRLAHYLRDKGVGPDVRVAICAERSPQLLVGLLAIVKAGGAYVPLDPDYPSERLAYMLADSGVELLLTqa 1233
Cdd:cd05939    4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1234 hlferlpgaEGVTPICLDSLKLdnwPSQAPGLHLHgDNLAYvIYTSGSTGQPKGVGNTHAalaeRLQWMQA----TYTLD 1309
Cdd:cd05939   82 ---------NLLDPLLTQSSTE---PPSQDDVNFR-DKLFY-IYTSGTTGLPKAAVIVHS----RYYRIAAgayyAFGMR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1310 GDDVLMQKAPVSFD----VSVWEC-----------------FWP------------LVTGCRLVLAAPGEHRDPARLVEL 1356
Cdd:cd05939  144 PEDVVYDCLPLYHSaggiMGVGQAllhgstvvirkkfsasnFWDdcvkynctivqyIGEICRYLLAQPPSEEEQKHNVRL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1357 VRQFGVTtlhfvPPLLQLFIDEPGVAACGSLRRLFSGGEALpAELRNRVlqrlPAVALHNRYGPTETAINVThwQCRAED 1436
Cdd:cd05939  224 AVGNGLR-----PQIWEQFVRRFGIPQIGEFYGATEGNSSL-VNIDNHV----GACGFNSRILPSVYPIRLI--KVDEDT 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1437 GErsPIGRPLGNVV-CRvldaefnllpAGVAGELC---IGGLGLAR--GYLGRPAlSAERFVADPFsAAGERLYRTGDRA 1510
Cdd:cd05939  292 GE--LIRDSDGLCIpCQ----------PGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVF-KKGDSAFLSGDVL 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1511 RWNADGVLEYLGRLDQQVKLRGFRIEPEEIQARLLAQPGVAQAVVVireGVAGSQLVGYYTGAVGAEAEAEQN-QRLRAA 1589
Cdd:cd05939  358 VMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVY---GVEVPGVEGRAGMAAIVDPERKVDlDRFSAV 434
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 15597620 1590 LQAELPEYMVPTQLMRLAQMPLGPSGKLDTRALpepvwqQREHVEP 1635
Cdd:cd05939  435 LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL------QKEGYDP 474
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
3838-4152 1.40e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 44.75  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3838 RLLVWDEIQQGEGAEHDPQVYSGPQNLaYVIYTSGSTGLPKGVMVEQAG-MLNNQLSKVPYLELDENDVIAQTAsqsfDI 3916
Cdd:PRK00174  222 RDLWWHELVAGASDECEPEPMDAEDPL-FILYTSGSTGKPKGVLHTTGGyLVYAAMTMKYVFDYKDGDVYWCTA----DV 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3917 --------SVWQFLAAplfGARVAI---VPNAvahdPQ-GLLAHVGEQ-GITVLESVPSLIQGMLAEERQALDG-----L 3978
Cdd:PRK00174  297 gwvtghsyIVYGPLAN---GATTLMfegVPNY----PDpGRFWEVIDKhKVTIFYTAPTAIRALMKEGDEHPKKydlssL 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  3979 RWMLPTGEAMPPElARQWLkrYPRIGlvnaygpaecSDDVAFfrVDLA-STES-----TYLP------IGSPTdnnrLYL 4046
Cdd:PRK00174  370 RLLGSVGEPINPE-AWEWY--YKVVG----------GERCPI--VDTWwQTETggimiTPLPgatplkPGSAT----RPL 430
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4047 LGAGA---DDAFELVPLGAVGELCVAGT--GVGRGYVGDPLRTAQAFVPHPFGapgerLYRTGDLARRRADGVLEYVGRI 4121
Cdd:PRK00174  431 PGIQPavvDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHERFVKTYFSTFKG-----MYFTGDGARRDEDGYYWITGRV 505
                         330       340       350
                  ....*....|....*....|....*....|.
gi 15597620  4122 DHQVKIRGFRIELGEIEARLHERADVREAAV 4152
Cdd:PRK00174  506 DDVLNVSGHRLGTAEIESALVAHPKVAEAAV 536
prpE PRK10524
propionyl-CoA synthetase; Provisional
4088-4233 1.78e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 44.55  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  4088 FVPHPFGAPGERLYRTGDLARRRADGVLEYVGRIDHQVKIRGFRIELGEIEARLHERADVREAAV-AVQEGANGKYLVGY 4166
Cdd:PRK10524  462 FVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVvGVKDALKGQVAVAF 541
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620  4167 LVPGETprSSADSPAGLMVEQGAWFERIKQQLRAdlpdYMVPLHWLVLDRMPLNANGKLDRKALPAL 4233
Cdd:PRK10524  542 VVPKDS--DSLADREARLALEKEIMALVDSQLGA----VARPARVWFVSALPKTRSGKLLRRAIQAI 602
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
3836-4121 2.61e-03

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 43.89  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3836 RPRLLVWDEIQQGEGAEHDPQVYS-----GPQNLAYVIYTSGSTGLPKGVM------------VEQAGMLNN----QLSK 3894
Cdd:cd05933  119 EPNLYSWDEFMELGRSIPDEQLDAiissqKPNQCCTLIYTSGTTGMPKGVMlshdnitwtakaASQHMDLRPatvgQESV 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3895 VPYLELdendviAQTASQSFDISVWQFLAAPLFGARvaivPNAVahdpQGLLAH-VGEQGITVLESVPSL---IQGMLAE 3970
Cdd:cd05933  199 VSYLPL------SHIAAQILDIWLPIKVGGQVYFAQ----PDAL----KGTLVKtLREVRPTAFMGVPRVwekIQEKMKA 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 3971 ERQALDGLRWMLPT---------------GEAMPP---ELARQWLKRYPR--IGL----VNAYGPAECSDDVA--FFRVD 4024
Cdd:cd05933  265 VGAKSGTLKRKIASwakgvgletnlklmgGESPSPlfyRLAKKLVFKKVRkaLGLdrcqKFFTGAAPISRETLefFLSLN 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 4025 LA------STESTYLPIGSPTDNNRLYLLG---AGADDAFELVPLGAVGELCVAGTGVGRGYVGDPLRTAQAFVPHPFga 4095
Cdd:cd05933  345 IPimelygMSETSGPHTISNPQAYRLLSCGkalPGCKTKIHNPDADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGW-- 422
                        330       340
                 ....*....|....*....|....*.
gi 15597620 4096 pgerlYRTGDLARRRADGVLEYVGRI 4121
Cdd:cd05933  423 -----LHSGDLGKLDEDGFLYITGRI 443
COG3903 COG3903
Predicted ATPase [General function prediction only];
865-1197 3.98e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.47  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  865 LAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIRI 944
Cdd:COG3903  558 RGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAA 637
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  945 GVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQLFQVLFNHQQR 1024
Cdd:COG3903  638 AAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAA 717
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1025 DLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGDI 1104
Cdd:COG3903  718 AAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAA 797
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1105 ALVDAEQAAHLAEWGSAPCEPARAWLPELLERQLAQSAERVALEWDGGSLGYAELHARANRLAHYLRDKGVGPDVRVAIC 1184
Cdd:COG3903  798 AAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAA 877
                        330
                 ....*....|...
gi 15597620 1185 AERSPQLLVGLLA 1197
Cdd:COG3903  878 AAAAAALLAAAAA 890
COG3903 COG3903
Predicted ATPase [General function prediction only];
704-1150 6.88e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 42.70  E-value: 6.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  704 RLRGELDEAALRASFQRLVERHEALRTRFLERDGAALQRIDERGEFAWQFVDLAALAEHEraaaaaqrreaeaqqpfdle 783
Cdd:COG3903  508 ELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRW-------------------- 567
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  784 kgpLLRVSLVRLDEQEHQLWVTLHHIVADGWSLNLLLDEFSRLYAEACGGQPADLAPLELHYAEFAAWQRQWLDAGEGAR 863
Cdd:COG3903  568 ---LERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAA 644
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  864 QLAYWRERLGDTAPVLELATDHPRTARQASPAARYSLRVDEALARAIREAALDHEASVFMWLLAAFQALLHRHSGQGEIR 943
Cdd:COG3903  645 AAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAA 724
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620  944 IGVPSANRQRLETQGLVGFFINTLVLRGTPRARQPFAALLGEAREATLGAQANQDLPFDQVLAACGQGGQLFQVLFNHQQ 1023
Cdd:COG3903  725 AALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAA 804
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597620 1024 RDLSALRRLPGLLADELPWHSREAKFDLQLQSEEDARGRLTLNFDYAADLFDEASIRRFAAQYLELLRQVAEDPQRCLGD 1103
Cdd:COG3903  805 AAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAAL 884
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 15597620 1104 IALVDAEQAAHLAEWGSAPCEPARAWLPELLERQLAQSAERVALEWD 1150
Cdd:COG3903  885 LAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
170-224 9.44e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 42.27  E-value: 9.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597620   170 AFLQYTSGSTALPKGVQVSHGNLVA---------NEVlirrgfgIGA---DDVIVSWLPLYHDMGLI 224
Cdd:PTZ00216  267 ALIMYTSGTTGDPKGVMHTHGSLTAgilaledrlNDL-------IGPpeeDETYCSYLPLAHIMEFG 326
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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