|
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
|
|
|