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Conserved domains on  [gi|1246793773|ref|WP_096378477|]
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non-ribosomal peptide synthetase [Lysobacter enzymogenes]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1571163)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12316 super family cl36106
peptide synthase; Provisional
1588-4084 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1465.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1588 REDARAIEHAFPLTPL-QRGVLLESLRGDGAD------------------PYFQQ------------------TVAELDG 1630
Cdd:PRK12316     3 AEDSLKLARRFIELPLeKRRVFLATLRGEGVDfslfpipagvssaerdrlSYAQQrmwflwqlepqsgaynlpSAVRLNG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1631 EIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAP 1710
Cdd:PRK12316    83 PLDRQALERAFASLVQRHETLRTVFPRGA-DDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1711 LARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDLARQ 1783
Cdd:PRK12316   162 LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALP--IQYADyalwqrsWLEAGEQERQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1784 RGWWRERLSGyagtaalpapvaaaHHPVQREECER--------RLSAHD-------SERLRAFCRERGCTLSDLIAMVWG 1848
Cdd:PRK12316   240 LEYWRAQLGE--------------EHPVLELPTDHprpavpsyRGSRYEfsidpalAEALRGTARRQGLTLFMLLLGAFN 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1849 LANARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAEN---------EAV 1919
Cdd:PRK12316   306 VLLHRYSGQTDIRVGVPIANR--NRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHqdlpferlvEAL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1920 GLGEILADSGLDADRLFASLLVVENFPAMAPAQLPFALRVRETRAAnHYALTLRVSERECVRLEALLDAARVDRAAVAAM 1999
Cdd:PRK12316   384 KVERSLSHSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTT-QFDLTLDTYEKGGRLHAALTYATDLFEARTVER 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2000 LDLAVAGLLR-LLQRPDCRVAEL-----------LGGDDAVQAPQPQRASSATaqslLWQMPAQ----AVAVEEGAASWT 2063
Cdd:PRK12316   463 MARHWQNLLRgMVENPQARVDELpmldaeergqlVEGWNATAAEYPLQRGVHR----LFEEQVErtpeAPALAFGEETLD 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2064 YAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAA 2143
Cdd:PRK12316   539 YAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHL 618
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2144 PAWVP--ASVRWLDAESVLDVVSAY-EEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:PRK12316   619 GRKLPlaAGVQVLDLDRPAAWLEGYsEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT 698
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTG 2300
Cdd:PRK12316   699 VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCS 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYL 2380
Cdd:PRK12316   779 GEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE--GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYL 856
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEV 2460
Cdd:PRK12316   857 AGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2461 AAVLALPGAN--GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAdllQQDDADSSAE-A 2537
Cdd:PRK12316   937 AAVLAVDGKQlvGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP---APEASVAQQGyV 1013
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2538 IDETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLsaqVQASSPAPAT 2617
Cdd:PRK12316  1014 APRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSL---ALVAKAGQAT 1090
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2618 IKPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFqRDAAGQWQQTLGD 2697
Cdd:PRK12316  1091 AADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQAYAA 1169
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2698 WQADRFAHREaDAGQREDLLA---QWQAGLSFD-GALLRVLaLPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAE 2773
Cdd:PRK12316  1170 PQAGEVLWQR-QAASEEELLAlceEAQRSLDLEqGPLLRAL-LVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYAD 1247
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2774 RRAgrspALAAEACGFGAWqAALRQLSAATLDGWRSYWRaQAADAEAIALPWQDSD----NRYADTVHLhdRFERDWTER 2849
Cdd:PRK12316  1248 LDA----DLPARTSSYQAW-ARRLHEHAGARAEELDYWQ-AQLEDAPHELPCENPDgaleNRHERKLEL--RLDAERTRQ 1319
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2850 LLTQTARAYGNEPQEVLLTALALAL-RDGGDAATLwVEMEGHGRDDLGAGLDLSRTVGWFTARYPLALHlPAGeDLGAAL 2928
Cdd:PRK12316  1320 LLQEAPAAYRTQVNDLLLTALARVTcRWSGQASVL-VQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLT-PAA-DLGESI 1396
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2929 RSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRaGERDGWALCE---EPDGGGRAGGNRRRHLL 3000
Cdd:PRK12316  1397 KAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFD-RQFDEAALFVpatESAGAAQDPCAPLANWL 1475
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3001 DVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLADLPLAGLDNAPLDALLSQHPQTQD 3079
Cdd:PRK12316  1476 SIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEhCCDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIAD 1555
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGaLDREAFAAAWQQALERHPILRSGFAVQ-GLPSPRQLPHRQVSLPL 3158
Cdd:PRK12316  1556 IYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPF 1634
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSGLEPAQArsRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAAlr 3238
Cdd:PRK12316  1635 AELDWRGREDLGQ--ALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-- 1710
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 esrtpQLPAAP--PFRDYLHWLRGQDEAAARAFWREQLTGL-EPAALPEA---TEPAEGYASSTRRFD---LAAASAWAQ 3309
Cdd:PRK12316  1711 -----QPVAAPggRYRDYIAWLQRQDAAASEAFWKEQLAALeEPTRLAQAartEDGQVGYGDHQQLLDpaqTRALAEFAR 1785
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3310 SHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDL 3389
Cdd:PRK12316  1786 AQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLAL 1865
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3390 RTHGYLPLAQIQRAGAADAVSPFDVLLVFENLP-TESREERS--GMRIEELDHRAHSNYPLMLtAIPDAGGLRIEAALDR 3466
Cdd:PRK12316  1866 REHEHTPLYDIQRWAGQGGEALFDSLLVFENYPvAEALKQGApaGLVFGRVSNHEQTNYPLTL-AVTLGETLSLQYSYDR 1944
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3467 SKLDGWLVEQMLDDLDFVLQQ--VPALQRFDALPLLPSQTRS---AAWTSRERYACTGNLV-SRFAEIARRYPARIAVSA 3540
Cdd:PRK12316  1945 GHFDAAAIERLDRHLLHLLEQmaEDAQAALGELALLDAGERQrilADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVF 2024
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLS 3620
Cdd:PRK12316  2025 GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 VSQRALAVELPGTAlclddpfTRAQLDAVEPGELPEVPTEAP---------AYLIYTSGSTGTPKGVVVTHRNVERLFTA 3691
Cdd:PRK12316  2105 LTQRHLLERLPLPA-------GVARLPLDRDAEWADYPDTAPavqlagenlAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3692 ATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRaVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:PRK12316  2178 AGE--RYELSPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHA 2254
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQ-SPTSRIGSALPDLAVHVLD 3850
Cdd:PRK12316  2255 ERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgAAYVPIGRALGNRRAYILD 2334
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:PRK12316  2335 ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRI 2414
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK12316  2415 ELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLD 2494
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4007 RKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12316  2495 RKALPKPDVSQLRQAYVAPQEglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERP 2574
PRK12316 super family cl36106
peptide synthase; Provisional
87-2812 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1352.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS-----VAAGGGAAVES 161
Cdd:PRK12316    49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqVPLDRPLEVEF 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQDEIDALVE----GFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYR 237
Cdd:PRK12316   129 EDCSGLPEAEQEARLRdeaqRESLQPFDLCEGPLLRVRLLRLGEE-----EHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 VECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:PRK12316   204 AYATGAEPGLPALPIQYADYALWQRSWLEagEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  316 RVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRD 395
Cdd:PRK12316   284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKD 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  396 HQLAALEHQALPLERVIETLQVERSSRHAPLFQLMF---ALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVLVGAGG 472
Cdd:PRK12316   364 TVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYnhqPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGR 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  473 MSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-------DDKREPAPRTVGNVVDAIARA 544
Cdd:PRK12316   444 LHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMlDAEERGQlvegwnaTAAEYPLQRGVHRLFEEQVER 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  545 AdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARR 624
Cdd:PRK12316   524 T---PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL 600
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  625 AEVVAASGCDAVLTDaQGLAGFAPsVAIAVDELKLDGAG-------ENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHA 697
Cdd:PRK12316   601 AYMLEDSGVQLLLSQ-SHLGRKLP-LAAGVQVLDLDRPAawlegysEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHR 678
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  698 ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPAYAN 776
Cdd:PRK12316   679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 758
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  777 ELVRAsvADDWRDLALRCLVVGGDVLPVALAQRWFelGLDRRCALINAYGPTEATIS-SHYHRVQAidASRPVPLGQLLP 855
Cdd:PRK12316   759 AFLQD--EDVASCTSLRRIVCSGEALPADAQEQVF--AKLPQAGLYNLYGPTEAAIDvTHWTCVEE--GGDSVPIGRPIA 832
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:PRK12316   833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGE--RMYRTGDLARYRADGVIEYAGRIDH 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGegaAQRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPA 1015
Cdd:PRK12316   911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GKQLVGYVVLESEGGDWREALKA-------------HLAASLPE 974
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1016 YMVPTQFVALPRLPRNASGKIDRRALPAPPV-LAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSLQ 1093
Cdd:PRK12316   975 YMVPAQWLALERLPLTPNGKLDRKALPAPEAsVAQQGYVAPRNALERTLAAIWQDVLGVErVGLDDNFFELGGDSIVSIQ 1054
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1094 VVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLD 1173
Cdd:PRK12316  1055 VVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLD 1134
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1174 AQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAfarmQEATPLA-GPLV-ALT 1251
Cdd:PRK12316  1135 PDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEA----QRSLDLEqGPLLrALL 1210
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1252 HAHCDDGERLLICAHHLIVDAVSWRLLLGELfdgLAALARGEAWTPsARGASYADYVEALREADDAQRFDAGFWRELAAQ 1331
Cdd:PRK12316  1211 VDMADGSQRLLLVIHHLVVDGVSWRILLEDL---QRAYADLDADLP-ARTSSYQAWARRLHEHAGARAEELDYWQAQLED 1286
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1332 PMQALPQDRPVALADARQSNvgRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-D 1410
Cdd:PRK12316  1287 APHELPCENPDGALENRHER--KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGReD 1364
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1411 VLDGRDWSSVLGWYTAVHPLPLDlGVADGPAQIGALKEQIRALARRGLDYMPLV------ASARIPALPAGQLLFNYHGV 1484
Cdd:PRK12316  1365 LFEDIDLSRTVGWFTSLFPVRLT-PAADLGESIKAIKEQLRAVPDKGIGYGLLRylageeAAARLAALPQPRITFNYLGQ 1443
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1485 VDAGAHPAFEVEPRTLASGNGADN--PPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQP 1562
Cdd:PRK12316  1444 FDRQFDEAALFVPATESAGAAQDPcaPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDE 1523
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1563 GSGALTASDLPQARL---QADEFALlaareDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGeIDAAALAQ 1639
Cdd:PRK12316  1524 RNRGVTPSDFPLAGLsqaQLDALPL-----PAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRA 1597
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1640 AWQQTVRRQPMLRTAIVWE-GLSVPHQIVLADAAAPWQTLDWSALDDAAQDaqLQRWLADDAAQGVDFAHAPLARMSLIG 1718
Cdd:PRK12316  1598 AWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPFAELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVR 1675
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1719 RGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAgaqgatlRLPPAPG--FQAYLDWRERQDLARQRGWWRERLSGYAG 1796
Cdd:PRK12316  1676 TGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-------QPVAAPGgrYRDYIAWLQRQDAAASEAFWKEQLAALEE 1748
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGV 1876
Cdd:PRK12316  1749 PTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGI 1828
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1877 ESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLFASLLVVENFPAM------AP 1950
Cdd:PRK12316  1829 EQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAealkqgAP 1908
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1951 AQLPFA-LRVRETraaNHYALTLRVSERECVRLE-----------ALLDAARVDRAAVAAMLDLAVAGL--LRLLQRPDC 2016
Cdd:PRK12316  1909 AGLVFGrVSNHEQ---TNYPLTLAVTLGETLSLQysydrghfdaaAIERLDRHLLHLLEQMAEDAQAALgeLALLDAGER 1985
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2017 RvaELLGGDDAVQAPQPQRASSATAQSLLWQMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT 2096
Cdd:PRK12316  1986 Q--RILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERS 2063
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2097 FAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWG--AAPAWVPASVRWLDAESVLDVVSAYEEPPRVDV 2174
Cdd:PRK12316  2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRhlLERLPLPAGVARLPLDRDAEWADYPDTAPAVQL 2143
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2175 DADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELa 2254
Cdd:PRK12316  2144 AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL- 2222
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2255 FDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP--RECLVtGGEALTGALVQQVRALAPTLRIVNHYGPTETTV 2332
Cdd:PRK12316  2223 WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPavRVYCF-GGEAVPAASLRLAWEALRPVYLFNGYGPTEAVV 2301
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2333 GILTCTV-PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRL 2410
Cdd:PRK12316  2302 TPLLWKCrPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGER 2381
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2411 LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-----QGSLEG 2485
Cdd:PRK12316  2382 LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVpddaaEDLLAE 2461
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2486 VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQddadssAEAIDETPVNEVLRELWQKLLGREHIG 2561
Cdd:PRK12316  2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALpkpdVSQLRQ------AYVAPQEGLEQRLAAIWQAVLKVEQVG 2535
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2562 AHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSA--QVQASSPAPATIKPATEAEQSFGLTPIQHWFF 2638
Cdd:PRK12316  2536 LDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAAslESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFL 2615
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2639 EQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRF---AHREADAGQRED 2715
Cdd:PRK12316  2616 WQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVledCAGVADAAIRQR 2695
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2716 LLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAA 2795
Cdd:PRK12316  2696 VAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAW 2775
                         2810
                   ....*....|....*...
gi 1246793773 2796 LRQ-LSAATLDGWRSYWR 2812
Cdd:PRK12316  2776 QRAwMDSGEGARQLDYWR 2793
TubC_N super family cl39883
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ...
21-68 7.60e-07

TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.


The actual alignment was detected with superfamily member pfam18563:

Pssm-ID: 436580 [Multi-domain]  Cd Length: 52  Bit Score: 48.67  E-value: 7.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773   21 LERARAAGVALHVEDGRLGYKATRAPLDAQLRADIVAQREALITLLSQ 68
Cdd:pfam18563    5 LAELYALGIKLWLEGGRLRFRAPKGVLTPELREKLKERKAEIIAFLQQ 52
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1588-4084 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1465.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1588 REDARAIEHAFPLTPL-QRGVLLESLRGDGAD------------------PYFQQ------------------TVAELDG 1630
Cdd:PRK12316     3 AEDSLKLARRFIELPLeKRRVFLATLRGEGVDfslfpipagvssaerdrlSYAQQrmwflwqlepqsgaynlpSAVRLNG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1631 EIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAP 1710
Cdd:PRK12316    83 PLDRQALERAFASLVQRHETLRTVFPRGA-DDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1711 LARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDLARQ 1783
Cdd:PRK12316   162 LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALP--IQYADyalwqrsWLEAGEQERQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1784 RGWWRERLSGyagtaalpapvaaaHHPVQREECER--------RLSAHD-------SERLRAFCRERGCTLSDLIAMVWG 1848
Cdd:PRK12316   240 LEYWRAQLGE--------------EHPVLELPTDHprpavpsyRGSRYEfsidpalAEALRGTARRQGLTLFMLLLGAFN 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1849 LANARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAEN---------EAV 1919
Cdd:PRK12316   306 VLLHRYSGQTDIRVGVPIANR--NRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHqdlpferlvEAL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1920 GLGEILADSGLDADRLFASLLVVENFPAMAPAQLPFALRVRETRAAnHYALTLRVSERECVRLEALLDAARVDRAAVAAM 1999
Cdd:PRK12316   384 KVERSLSHSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTT-QFDLTLDTYEKGGRLHAALTYATDLFEARTVER 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2000 LDLAVAGLLR-LLQRPDCRVAEL-----------LGGDDAVQAPQPQRASSATaqslLWQMPAQ----AVAVEEGAASWT 2063
Cdd:PRK12316   463 MARHWQNLLRgMVENPQARVDELpmldaeergqlVEGWNATAAEYPLQRGVHR----LFEEQVErtpeAPALAFGEETLD 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2064 YAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAA 2143
Cdd:PRK12316   539 YAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHL 618
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2144 PAWVP--ASVRWLDAESVLDVVSAY-EEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:PRK12316   619 GRKLPlaAGVQVLDLDRPAAWLEGYsEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT 698
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTG 2300
Cdd:PRK12316   699 VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCS 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYL 2380
Cdd:PRK12316   779 GEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE--GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYL 856
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEV 2460
Cdd:PRK12316   857 AGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2461 AAVLALPGAN--GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAdllQQDDADSSAE-A 2537
Cdd:PRK12316   937 AAVLAVDGKQlvGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP---APEASVAQQGyV 1013
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2538 IDETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLsaqVQASSPAPAT 2617
Cdd:PRK12316  1014 APRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSL---ALVAKAGQAT 1090
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2618 IKPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFqRDAAGQWQQTLGD 2697
Cdd:PRK12316  1091 AADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQAYAA 1169
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2698 WQADRFAHREaDAGQREDLLA---QWQAGLSFD-GALLRVLaLPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAE 2773
Cdd:PRK12316  1170 PQAGEVLWQR-QAASEEELLAlceEAQRSLDLEqGPLLRAL-LVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYAD 1247
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2774 RRAgrspALAAEACGFGAWqAALRQLSAATLDGWRSYWRaQAADAEAIALPWQDSD----NRYADTVHLhdRFERDWTER 2849
Cdd:PRK12316  1248 LDA----DLPARTSSYQAW-ARRLHEHAGARAEELDYWQ-AQLEDAPHELPCENPDgaleNRHERKLEL--RLDAERTRQ 1319
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2850 LLTQTARAYGNEPQEVLLTALALAL-RDGGDAATLwVEMEGHGRDDLGAGLDLSRTVGWFTARYPLALHlPAGeDLGAAL 2928
Cdd:PRK12316  1320 LLQEAPAAYRTQVNDLLLTALARVTcRWSGQASVL-VQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLT-PAA-DLGESI 1396
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2929 RSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRaGERDGWALCE---EPDGGGRAGGNRRRHLL 3000
Cdd:PRK12316  1397 KAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFD-RQFDEAALFVpatESAGAAQDPCAPLANWL 1475
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3001 DVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLADLPLAGLDNAPLDALLSQHPQTQD 3079
Cdd:PRK12316  1476 SIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEhCCDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIAD 1555
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGaLDREAFAAAWQQALERHPILRSGFAVQ-GLPSPRQLPHRQVSLPL 3158
Cdd:PRK12316  1556 IYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPF 1634
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSGLEPAQArsRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAAlr 3238
Cdd:PRK12316  1635 AELDWRGREDLGQ--ALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-- 1710
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 esrtpQLPAAP--PFRDYLHWLRGQDEAAARAFWREQLTGL-EPAALPEA---TEPAEGYASSTRRFD---LAAASAWAQ 3309
Cdd:PRK12316  1711 -----QPVAAPggRYRDYIAWLQRQDAAASEAFWKEQLAALeEPTRLAQAartEDGQVGYGDHQQLLDpaqTRALAEFAR 1785
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3310 SHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDL 3389
Cdd:PRK12316  1786 AQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLAL 1865
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3390 RTHGYLPLAQIQRAGAADAVSPFDVLLVFENLP-TESREERS--GMRIEELDHRAHSNYPLMLtAIPDAGGLRIEAALDR 3466
Cdd:PRK12316  1866 REHEHTPLYDIQRWAGQGGEALFDSLLVFENYPvAEALKQGApaGLVFGRVSNHEQTNYPLTL-AVTLGETLSLQYSYDR 1944
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3467 SKLDGWLVEQMLDDLDFVLQQ--VPALQRFDALPLLPSQTRS---AAWTSRERYACTGNLV-SRFAEIARRYPARIAVSA 3540
Cdd:PRK12316  1945 GHFDAAAIERLDRHLLHLLEQmaEDAQAALGELALLDAGERQrilADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVF 2024
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLS 3620
Cdd:PRK12316  2025 GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 VSQRALAVELPGTAlclddpfTRAQLDAVEPGELPEVPTEAP---------AYLIYTSGSTGTPKGVVVTHRNVERLFTA 3691
Cdd:PRK12316  2105 LTQRHLLERLPLPA-------GVARLPLDRDAEWADYPDTAPavqlagenlAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3692 ATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRaVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:PRK12316  2178 AGE--RYELSPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHA 2254
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQ-SPTSRIGSALPDLAVHVLD 3850
Cdd:PRK12316  2255 ERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgAAYVPIGRALGNRRAYILD 2334
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:PRK12316  2335 ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRI 2414
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK12316  2415 ELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLD 2494
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4007 RKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12316  2495 RKALPKPDVSQLRQAYVAPQEglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERP 2574
PRK12316 PRK12316
peptide synthase; Provisional
87-2812 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1352.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS-----VAAGGGAAVES 161
Cdd:PRK12316    49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqVPLDRPLEVEF 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQDEIDALVE----GFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYR 237
Cdd:PRK12316   129 EDCSGLPEAEQEARLRdeaqRESLQPFDLCEGPLLRVRLLRLGEE-----EHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 VECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:PRK12316   204 AYATGAEPGLPALPIQYADYALWQRSWLEagEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  316 RVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRD 395
Cdd:PRK12316   284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKD 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  396 HQLAALEHQALPLERVIETLQVERSSRHAPLFQLMF---ALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVLVGAGG 472
Cdd:PRK12316   364 TVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYnhqPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGR 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  473 MSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-------DDKREPAPRTVGNVVDAIARA 544
Cdd:PRK12316   444 LHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMlDAEERGQlvegwnaTAAEYPLQRGVHRLFEEQVER 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  545 AdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARR 624
Cdd:PRK12316   524 T---PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL 600
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  625 AEVVAASGCDAVLTDaQGLAGFAPsVAIAVDELKLDGAG-------ENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHA 697
Cdd:PRK12316   601 AYMLEDSGVQLLLSQ-SHLGRKLP-LAAGVQVLDLDRPAawlegysEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHR 678
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  698 ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPAYAN 776
Cdd:PRK12316   679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 758
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  777 ELVRAsvADDWRDLALRCLVVGGDVLPVALAQRWFelGLDRRCALINAYGPTEATIS-SHYHRVQAidASRPVPLGQLLP 855
Cdd:PRK12316   759 AFLQD--EDVASCTSLRRIVCSGEALPADAQEQVF--AKLPQAGLYNLYGPTEAAIDvTHWTCVEE--GGDSVPIGRPIA 832
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:PRK12316   833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGE--RMYRTGDLARYRADGVIEYAGRIDH 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGegaAQRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPA 1015
Cdd:PRK12316   911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GKQLVGYVVLESEGGDWREALKA-------------HLAASLPE 974
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1016 YMVPTQFVALPRLPRNASGKIDRRALPAPPV-LAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSLQ 1093
Cdd:PRK12316   975 YMVPAQWLALERLPLTPNGKLDRKALPAPEAsVAQQGYVAPRNALERTLAAIWQDVLGVErVGLDDNFFELGGDSIVSIQ 1054
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1094 VVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLD 1173
Cdd:PRK12316  1055 VVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLD 1134
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1174 AQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAfarmQEATPLA-GPLV-ALT 1251
Cdd:PRK12316  1135 PDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEA----QRSLDLEqGPLLrALL 1210
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1252 HAHCDDGERLLICAHHLIVDAVSWRLLLGELfdgLAALARGEAWTPsARGASYADYVEALREADDAQRFDAGFWRELAAQ 1331
Cdd:PRK12316  1211 VDMADGSQRLLLVIHHLVVDGVSWRILLEDL---QRAYADLDADLP-ARTSSYQAWARRLHEHAGARAEELDYWQAQLED 1286
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1332 PMQALPQDRPVALADARQSNvgRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-D 1410
Cdd:PRK12316  1287 APHELPCENPDGALENRHER--KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGReD 1364
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1411 VLDGRDWSSVLGWYTAVHPLPLDlGVADGPAQIGALKEQIRALARRGLDYMPLV------ASARIPALPAGQLLFNYHGV 1484
Cdd:PRK12316  1365 LFEDIDLSRTVGWFTSLFPVRLT-PAADLGESIKAIKEQLRAVPDKGIGYGLLRylageeAAARLAALPQPRITFNYLGQ 1443
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1485 VDAGAHPAFEVEPRTLASGNGADN--PPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQP 1562
Cdd:PRK12316  1444 FDRQFDEAALFVPATESAGAAQDPcaPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDE 1523
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1563 GSGALTASDLPQARL---QADEFALlaareDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGeIDAAALAQ 1639
Cdd:PRK12316  1524 RNRGVTPSDFPLAGLsqaQLDALPL-----PAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRA 1597
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1640 AWQQTVRRQPMLRTAIVWE-GLSVPHQIVLADAAAPWQTLDWSALDDAAQDaqLQRWLADDAAQGVDFAHAPLARMSLIG 1718
Cdd:PRK12316  1598 AWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPFAELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVR 1675
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1719 RGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAgaqgatlRLPPAPG--FQAYLDWRERQDLARQRGWWRERLSGYAG 1796
Cdd:PRK12316  1676 TGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-------QPVAAPGgrYRDYIAWLQRQDAAASEAFWKEQLAALEE 1748
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGV 1876
Cdd:PRK12316  1749 PTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGI 1828
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1877 ESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLFASLLVVENFPAM------AP 1950
Cdd:PRK12316  1829 EQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAealkqgAP 1908
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1951 AQLPFA-LRVRETraaNHYALTLRVSERECVRLE-----------ALLDAARVDRAAVAAMLDLAVAGL--LRLLQRPDC 2016
Cdd:PRK12316  1909 AGLVFGrVSNHEQ---TNYPLTLAVTLGETLSLQysydrghfdaaAIERLDRHLLHLLEQMAEDAQAALgeLALLDAGER 1985
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2017 RvaELLGGDDAVQAPQPQRASSATAQSLLWQMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT 2096
Cdd:PRK12316  1986 Q--RILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERS 2063
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2097 FAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWG--AAPAWVPASVRWLDAESVLDVVSAYEEPPRVDV 2174
Cdd:PRK12316  2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRhlLERLPLPAGVARLPLDRDAEWADYPDTAPAVQL 2143
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2175 DADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELa 2254
Cdd:PRK12316  2144 AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL- 2222
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2255 FDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP--RECLVtGGEALTGALVQQVRALAPTLRIVNHYGPTETTV 2332
Cdd:PRK12316  2223 WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPavRVYCF-GGEAVPAASLRLAWEALRPVYLFNGYGPTEAVV 2301
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2333 GILTCTV-PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRL 2410
Cdd:PRK12316  2302 TPLLWKCrPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGER 2381
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2411 LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-----QGSLEG 2485
Cdd:PRK12316  2382 LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVpddaaEDLLAE 2461
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2486 VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQddadssAEAIDETPVNEVLRELWQKLLGREHIG 2561
Cdd:PRK12316  2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALpkpdVSQLRQ------AYVAPQEGLEQRLAAIWQAVLKVEQVG 2535
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2562 AHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSA--QVQASSPAPATIKPATEAEQSFGLTPIQHWFF 2638
Cdd:PRK12316  2536 LDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAAslESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFL 2615
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2639 EQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRF---AHREADAGQRED 2715
Cdd:PRK12316  2616 WQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVledCAGVADAAIRQR 2695
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2716 LLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAA 2795
Cdd:PRK12316  2696 VAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAW 2775
                         2810
                   ....*....|....*...
gi 1246793773 2796 LRQ-LSAATLDGWRSYWR 2812
Cdd:PRK12316  2776 QRAwMDSGEGARQLDYWR 2793
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3065-4084 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: 741.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3065 APLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQgLP 3144
Cdd:COG1020      2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTR-AG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3145 SPRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSA 3224
Cdd:COG1020     81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3225 LLLDEVWRLYAALRESRTPQLPAAPP-----FRDYLHWLRGQDEAAARAFWREQLTGLEPA-ALPE--ATEPAEGYASST 3296
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLlELPTdrPRPAVQSYRGAR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3297 RRFDLAAA-----SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPpeLAGVERMLGVFINSVPLRVTPAG 3371
Cdd:COG1020    241 VSFRLPAEltaalRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3372 EATPAPWLQALQQRNLDLRTHGYLPLAQIQRA---GAADAVSP-FDVLLVFENLPTESREeRSGMRIEELD-HRAHSNYP 3446
Cdd:COG1020    319 DPSFAELLARVRETLLAAYAHQDLPFERLVEElqpERDLSRNPlFQVMFVLQNAPADELE-LPGLTLEPLElDSGTAKFD 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3447 LMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPAL--QRFDALPLLPSQTRS---AAWTSRER-YACTGN 3520
Cdd:COG1020    398 LTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADpdQPLGDLPLLTAAERQqllAEWNATAApYPADAT 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:COG1020    478 LHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVCLSVSQRALAVELPGTA---LCLDDPFTRAQldavePGELPEVPT--EAPAYLIYTSGSTGTP 3675
Cdd:COG1020    558 PAYPAERLAYMLEDAGARLVLTQSALAARLPELGvpvLALDALALAAE-----PATNPPVPVtpDDLAYVIYTSGSTGRP 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVT 3755
Cdd:COG1020    633 KGVMVEHRALVNLLAWMQR--RYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVT 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3756 VLNQTPSAFYALQSQAMRRELALnvRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTS 3835
Cdd:COG1020    711 VLNLTPSLLRALLDAAPEALPSL--RLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSV 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 RIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:COG1020    789 PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVAdpfgFPGARLYRTGDLARWLPDGNLEF 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRL 3990
Cdd:COG1020    869 LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVArEDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAA 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3991 IQLLPALPLTANGKLDRKALPKPETQDRDEGVLESASERR--LAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIR 4068
Cdd:COG1020    949 VVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEeeAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAAR 1028
                         1050
                   ....*....|....*.
gi 1246793773 4069 AEFAIAVPLKSLFEQP 4084
Cdd:COG1020   1029 LLLLLLLLLLLFLAAA 1044
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
75-1374 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: 655.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCI--------- 145
Cdd:COG1020      5 AAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLrtragrpvq 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  146 QGEDSVAAGGGAAVESADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSL 225
Cdd:COG1020     85 VIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLL-----LLLLLLALHHIISDGLSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  226 GLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGA 303
Cdd:COG1020    160 GLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLqgEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  304 KLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDD 383
Cdd:COG1020    240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGD 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  384 PDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELT 463
Cdd:COG1020    320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLT 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  464 LEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-----DDKREPAPRTVGnV 537
Cdd:COG1020    400 LTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLlTAAERQQllaewNATAAPYPADAT-L 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  538 VDAIARAADEFPERAALETAQGRLSYRELLtaadaraaalrrrlgaqARS-----------------VALCLPRGLDWYC 600
Cdd:COG1020    479 HELFEAQAARTPDAVAVVFGDQSLTYAELN-----------------ARAnrlahhlralgvgpgdlVGVCLERSLEMVV 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA--IAVDELKLDGAGENGSGENAAPNQLAY 678
Cdd:COG1020    542 ALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVpvLALDALALAAEPATNPPVPVTPDDLAY 621
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFL 757
Cdd:COG1020    622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALA 701
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  758 AFLSERAITVTDLAPAYANELVRASVADdwrDLALRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYH 837
Cdd:COG1020    702 ELLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLPGAR--LVNLYGPTETTVDSTYY 776
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  838 RVQAIDA-SRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESlRMYRSG 916
Cdd:COG1020    777 EVTPPDAdGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGA-RLYRTG 855
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  917 DRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDgfgqadlnqtd 996
Cdd:COG1020    856 DLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG----------- 924
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  997 sDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVL-AQAERTPPRTAEESALCEVWAEVLQCEV 1075
Cdd:COG1020    925 -AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAaAAAAAAPPAEEEEEEAALALLLLLVVVV 1003
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1076 GIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPI------QRWF 1149
Cdd:COG1020   1004 GDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPplllslLALL 1083
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1150 FDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSR 1229
Cdd:COG1020   1084 LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAA 1163
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1230 VDAAFARMQEATPLAGPLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELfDGLAALARGEAWTPSARGASYADYVE 1309
Cdd:COG1020   1164 AAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL-LLLLLLLLAAAAAALLALALLLALLA 1242
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 1310 ALREADDAQRFDAGFWRELAAQPMQALPQDRPVALADARQSNVGRIVQTLDAGLTADLLERAGEA 1374
Cdd:COG1020   1243 LAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLL 1307
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3533-4010 0e+00

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: 580.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVclsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFtAA 3692
Cdd:cd17643     81 ADSGP----------------SLLLTDP-------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALF-AA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAM 3772
Cdd:cd17643    125 TQRW-FGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RR-ELALNVRAVVFGGEALEPSRLQPWRERY--PQAELVNMYGITETTVHVSFHRLSDEDLQSPT-SRIGSALPDLAVHV 3848
Cdd:cd17643    204 RDgRDPLALRYVIFGGEALEAAMLRPWAGRFglDRPQLVNMYGITETTVHVTFRPLDAADLPAAAaSPIGRPLPGLRVYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd17643    284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVAnpfgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd17643    364 RIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443

                   ....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd17643    444 KLDRAAL 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3547-3946 1.44e-143

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: 454.80  E-value: 1.44e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLI-RQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRA 3625
Cdd:TIGR01733    2 YRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3626 LAVELPGTALC--LDDPFTRAQLDAVEPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFD 3701
Cdd:TIGR01733   82 LASRLAGLVLPviLLDPLELAALDDAPAPPPPDAPSGPddLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR--RYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFL-DLLAEYGVTVLNQTPSAFYALQSQAmrRELALNV 3780
Cdd:TIGR01733  160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAAL--PPALASL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSR-IGSALPDLAVHVLDAAGQPVPLG 3859
Cdd:TIGR01733  238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVpIGRPLANTRLYVLDDDLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVEGDGVAQGYWQRPELTAERFVE-----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPdpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
                          410
                   ....*....|..
gi 1246793773 3935 IASLPQVSDAAV 3946
Cdd:TIGR01733  398 LLRHPGVREAVV 409
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
549-1041 8.79e-128

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: 410.77  E-value: 8.79e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05930     81 EDSGAKLVLTD---------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANELVRAsvADDW 787
Cdd:cd05930    128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVrKDPEALADLLAEEGITVLHLTPSLLRLLLQE--LELA 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RDLALRCLVVGGDVLPVALAQRWFELGldRRCALINAYGPTEATISSHYHRVQA-IDASRPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd05930    206 ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNLYGPTEATVDATYYRVPPdDEEDGRVPIGRPIPNTRVYVLDENL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIEL 946
Cdd:cd05930    284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGE--RMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  947 EEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVAL 1025
Cdd:cd05930    362 GEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDEEELRA-------------HLAERLPDYMVPSAFVVL 428
                          490
                   ....*....|....*.
gi 1246793773 1026 PRLPRNASGKIDRRAL 1041
Cdd:cd05930    429 DALPLTPNGKVDRKAL 444
AMP-binding pfam00501
AMP-binding enzyme;
3525-3922 5.81e-107

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 349.69  E-value: 5.81e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRAL----------AVELPGTALCLDDP--------FTRAQLDAVEPGELPEVPTEAPAYL 3665
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealgKLEVVKLVLVLDRDpvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3666 IYTSGSTGTPKGVVVTHRNVERLFTAA--TQTGRFSFDEHDVWSLFHSHAFDFAV-WELWGAWLYGGRAVLVPEAVCRQP 3742
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYAL-QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVS 3821
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLlEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 FHRLSDEDLQSPTSrIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggQRFYRSGDL 3900
Cdd:pfam00501  320 TPLPLDEDLRSLGS-VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE---DGWYRTGDL 395
                          410       420
                   ....*....|....*....|..
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLR 3922
Cdd:pfam00501  396 GRRDEDGYLEIVGRKKDQIKLG 417
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
588-964 9.53e-102

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: 334.62  E-value: 9.53e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQ--GLAGFAPSVAIAVDELKLDGAGEN 665
Cdd:TIGR01733   28 VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAlaSRLAGLVLPVILLDPLELAALDDA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  666 GSGE----NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA 741
Cdd:TIGR01733  108 PAPPppdaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGA 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  742 C-VVARPDELLEPQRFLAFL-SERAITVTDLAPAYANELVRAsvaDDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRc 819
Cdd:TIGR01733  188 TlVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGAR- 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  820 aLINAYGPTEATISSHYHRVQAIDASR--PVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASER 897
Cdd:TIGR01733  264 -LINLYGPTETTVWSTATLVDPDDAPResPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAE 342
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  898 RFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA 964
Cdd:TIGR01733  343 RFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
88-510 8.76e-69

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: 241.08  E-value: 8.76e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDS-----VAAGGGAAVES 161
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRtVFIRQENGepvqvILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQDE----IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYr 237
Cdd:pfam00668   85 IDISDLSESEeeeaIEAFIQRDLQSPFDLEKGPLFRAGLFRIAEN-----RHHLLLSMHHIIVDGVSLGILLRDLADLY- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 vECGLAAEPAPPLPCQ-YGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:pfam00668  159 -QQLLKGEPLPLPPKTpYKDYAEWLQQYLqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCR 394
Cdd:pfam00668  238 ELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  395 DHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDadlalDLHGVQAHALTL----------PEDVAKHELTL 464
Cdd:pfam00668  318 EDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNY-----LGQDSQEEEFQLseldlsvssvIEEEAKYDLSL 392
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773  465 EVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEP 510
Cdd:pfam00668  393 TASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP 438
TubC_N pfam18563
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ...
21-68 7.60e-07

TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.


Pssm-ID: 436580 [Multi-domain]  Cd Length: 52  Bit Score: 48.67  E-value: 7.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773   21 LERARAAGVALHVEDGRLGYKATRAPLDAQLRADIVAQREALITLLSQ 68
Cdd:pfam18563    5 LAELYALGIKLWLEGGRLRFRAPKGVLTPELREKLKERKAEIIAFLQQ 52
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2545-2610 1.77e-04

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: 43.01  E-value: 1.77e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  2545 EVLRELWQKLLGR---EHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQA 2610
Cdd:smart00823   15 DLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAA 84
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1588-4084 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1465.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1588 REDARAIEHAFPLTPL-QRGVLLESLRGDGAD------------------PYFQQ------------------TVAELDG 1630
Cdd:PRK12316     3 AEDSLKLARRFIELPLeKRRVFLATLRGEGVDfslfpipagvssaerdrlSYAQQrmwflwqlepqsgaynlpSAVRLNG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1631 EIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAP 1710
Cdd:PRK12316    83 PLDRQALERAFASLVQRHETLRTVFPRGA-DDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1711 LARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDLARQ 1783
Cdd:PRK12316   162 LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALP--IQYADyalwqrsWLEAGEQERQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1784 RGWWRERLSGyagtaalpapvaaaHHPVQREECER--------RLSAHD-------SERLRAFCRERGCTLSDLIAMVWG 1848
Cdd:PRK12316   240 LEYWRAQLGE--------------EHPVLELPTDHprpavpsyRGSRYEfsidpalAEALRGTARRQGLTLFMLLLGAFN 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1849 LANARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAEN---------EAV 1919
Cdd:PRK12316   306 VLLHRYSGQTDIRVGVPIANR--NRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHqdlpferlvEAL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1920 GLGEILADSGLDADRLFASLLVVENFPAMAPAQLPFALRVRETRAAnHYALTLRVSERECVRLEALLDAARVDRAAVAAM 1999
Cdd:PRK12316   384 KVERSLSHSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTT-QFDLTLDTYEKGGRLHAALTYATDLFEARTVER 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2000 LDLAVAGLLR-LLQRPDCRVAEL-----------LGGDDAVQAPQPQRASSATaqslLWQMPAQ----AVAVEEGAASWT 2063
Cdd:PRK12316   463 MARHWQNLLRgMVENPQARVDELpmldaeergqlVEGWNATAAEYPLQRGVHR----LFEEQVErtpeAPALAFGEETLD 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2064 YAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAA 2143
Cdd:PRK12316   539 YAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHL 618
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2144 PAWVP--ASVRWLDAESVLDVVSAY-EEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:PRK12316   619 GRKLPlaAGVQVLDLDRPAAWLEGYsEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT 698
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTG 2300
Cdd:PRK12316   699 VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCS 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYL 2380
Cdd:PRK12316   779 GEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE--GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYL 856
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEV 2460
Cdd:PRK12316   857 AGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2461 AAVLALPGAN--GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAdllQQDDADSSAE-A 2537
Cdd:PRK12316   937 AAVLAVDGKQlvGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP---APEASVAQQGyV 1013
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2538 IDETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLsaqVQASSPAPAT 2617
Cdd:PRK12316  1014 APRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSL---ALVAKAGQAT 1090
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2618 IKPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFqRDAAGQWQQTLGD 2697
Cdd:PRK12316  1091 AADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRF-REEDGGWQQAYAA 1169
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2698 WQADRFAHREaDAGQREDLLA---QWQAGLSFD-GALLRVLaLPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAE 2773
Cdd:PRK12316  1170 PQAGEVLWQR-QAASEEELLAlceEAQRSLDLEqGPLLRAL-LVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYAD 1247
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2774 RRAgrspALAAEACGFGAWqAALRQLSAATLDGWRSYWRaQAADAEAIALPWQDSD----NRYADTVHLhdRFERDWTER 2849
Cdd:PRK12316  1248 LDA----DLPARTSSYQAW-ARRLHEHAGARAEELDYWQ-AQLEDAPHELPCENPDgaleNRHERKLEL--RLDAERTRQ 1319
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2850 LLTQTARAYGNEPQEVLLTALALAL-RDGGDAATLwVEMEGHGRDDLGAGLDLSRTVGWFTARYPLALHlPAGeDLGAAL 2928
Cdd:PRK12316  1320 LLQEAPAAYRTQVNDLLLTALARVTcRWSGQASVL-VQLEGHGREDLFEDIDLSRTVGWFTSLFPVRLT-PAA-DLGESI 1396
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2929 RSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRaGERDGWALCE---EPDGGGRAGGNRRRHLL 3000
Cdd:PRK12316  1397 KAIKEQLRAVPDKGIGYGLLRYLAGEeaaarLAALPQPRITFNYLGQFD-RQFDEAALFVpatESAGAAQDPCAPLANWL 1475
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3001 DVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLADLPLAGLDNAPLDALLSQHPQTQD 3079
Cdd:PRK12316  1476 SIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEhCCDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIAD 1555
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGaLDREAFAAAWQQALERHPILRSGFAVQ-GLPSPRQLPHRQVSLPL 3158
Cdd:PRK12316  1556 IYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPF 1634
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSGLEPAQArsRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAAlr 3238
Cdd:PRK12316  1635 AELDWRGREDLGQ--ALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-- 1710
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 esrtpQLPAAP--PFRDYLHWLRGQDEAAARAFWREQLTGL-EPAALPEA---TEPAEGYASSTRRFD---LAAASAWAQ 3309
Cdd:PRK12316  1711 -----QPVAAPggRYRDYIAWLQRQDAAASEAFWKEQLAALeEPTRLAQAartEDGQVGYGDHQQLLDpaqTRALAEFAR 1785
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3310 SHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDL 3389
Cdd:PRK12316  1786 AQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLAL 1865
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3390 RTHGYLPLAQIQRAGAADAVSPFDVLLVFENLP-TESREERS--GMRIEELDHRAHSNYPLMLtAIPDAGGLRIEAALDR 3466
Cdd:PRK12316  1866 REHEHTPLYDIQRWAGQGGEALFDSLLVFENYPvAEALKQGApaGLVFGRVSNHEQTNYPLTL-AVTLGETLSLQYSYDR 1944
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3467 SKLDGWLVEQMLDDLDFVLQQ--VPALQRFDALPLLPSQTRS---AAWTSRERYACTGNLV-SRFAEIARRYPARIAVSA 3540
Cdd:PRK12316  1945 GHFDAAAIERLDRHLLHLLEQmaEDAQAALGELALLDAGERQrilADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVF 2024
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLS 3620
Cdd:PRK12316  2025 GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 VSQRALAVELPGTAlclddpfTRAQLDAVEPGELPEVPTEAP---------AYLIYTSGSTGTPKGVVVTHRNVERLFTA 3691
Cdd:PRK12316  2105 LTQRHLLERLPLPA-------GVARLPLDRDAEWADYPDTAPavqlagenlAYVIYTSGSTGLPKGVAVSHGALVAHCQA 2177
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3692 ATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRaVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:PRK12316  2178 AGE--RYELSPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHA 2254
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQ-SPTSRIGSALPDLAVHVLD 3850
Cdd:PRK12316  2255 ERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCgAAYVPIGRALGNRRAYILD 2334
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:PRK12316  2335 ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRI 2414
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK12316  2415 ELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLD 2494
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4007 RKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12316  2495 RKALPKPDVSQLRQAYVAPQEglEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERP 2574
PRK12467 PRK12467
peptide synthase; Provisional
1628-4084 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1404.91  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1628 LDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIvlaDAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFA 1707
Cdd:PRK12467  1147 LKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVI---HPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLE 1223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1708 HAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDL 1780
Cdd:PRK12467  1224 QGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALP--IQYADyavwqrqWMDAGER 1301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1781 ARQRGWWRERLSGyagtaalpapvaaaHHPVQREECERRLSAHDSER---------------LRAFCRERGCTLSDLIAM 1845
Cdd:PRK12467  1302 ARQLAYWKAQLGG--------------EQPVLELPTDRPRPAVQSHRgarlafelppalaegLRALARREGVTLFMLLLA 1367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1846 VWGLANARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLgEIL 1925
Cdd:PRK12467  1368 SFQTLLHRYSGQDDIRVGVPIANR--NRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPF-EQL 1444
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1926 ADSgLDADR------LFASLLVVENFPAMAPAQLPfALRVR----ETRAAnHYALTLRVSEREcvrlEALLDAARVDRAA 1995
Cdd:PRK12467  1445 VEA-LQPERslshspLFQVMFNHQRDDHQAQAQLP-GLSVEslswESQTA-QFDLTLDTYESS----EGLQASLTYATDL 1517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1996 VAAMLDLAVAG-LLRLLQ----RPDCRVAE--LLGGDDAVQAPQPQRASSA--TAQSLLWQMPA-------QAVAVEEGA 2059
Cdd:PRK12467  1518 FEASTIERLAGhWLNLLQglvaDPERRLGEldLLDEAERRQILEGWNATHTgyPLARLVHQLIEdqaaatpEAVALVFGE 1597
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2060 ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIG 2139
Cdd:PRK12467  1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 WGAAPAWVPA--SVRWLDAESVLDVVSAY-EEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG 2216
Cdd:PRK12467  1678 QSHLQARLPLpdGLRSLVLDQEDDWLEGYsDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLS 1757
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2217 EDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAG-LLAAAGGTAVLPRE 2295
Cdd:PRK12467  1758 AADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQlLQMDEQVEHPLSLR 1837
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQG-VPVGHPLAGNEAWVLDRFGLPAPVGV 2374
Cdd:PRK12467  1838 RVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDsVPIGQPIANLSTYILDASLNPVPIGV 1917
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2375 AGELYLGGGNLSLGYWQRAEQTAERFVAHPLA-PDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLA 2453
Cdd:PRK12467  1918 AGELYLGGVGLARGYLNRPALTAERFVADPFGtVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLR 1997
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2454 QLPGVEVAAVLALPGANG-------------VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQ 2520
Cdd:PRK12467  1998 EQGGVREAVVIAQDGANGkqlvayvvptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRK 2077
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2521 AL----ADLLQQDDADSSAEAidetpvNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLY 2596
Cdd:PRK12467  2078 ALpapdASELQQAYVAPQSEL------EQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLF 2151
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2597 DHPTLAGLSAQVQASSPAPATIKPATEAEQSfgLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAH 2676
Cdd:PRK12467  2152 QHQTVQSLAAVAQEGDGTVSIDQGPVTGDLP--LLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHH 2229
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2677 PMLRARFqRDAAGQWQQTLGDWQADR----FAHREADAGQREDLLAQWQAGLSF-DGALLRVLALPDPqDGDTRVLFAAH 2751
Cdd:PRK12467  2230 DALRLGF-VQEDGGWSAMHRAPEQERrpllWQVVVADKEELEALCEQAQRSLDLeEGPLLRAVLATLP-DGSQRLLLVIH 2307
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2752 HLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSA-ATLDGWRSYWRAQAADAEAIaLPWQDSD- 2829
Cdd:PRK12467  2308 HLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAAsAALADELGYWQAQLQGASTE-LPCDHPQg 2386
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2830 ---NRYADTVHLHdrFERDWTERLLTQTARAYGNEPQEVLLTALALA-LRDGGDAATLwVEMEGHGRDDLGAGLDLSRTV 2905
Cdd:PRK12467  2387 glqRRHAASVTTH--LDSEWTRRLLQEAPAAYRTQVNDLLLTALARViARWTGQASTL-IQLEGHGREDLFDEIDLTRTV 2463
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2906 GWFTARYPLALHLPAgeDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRAG-ERDGW 2979
Cdd:PRK12467  2464 GWFTSLYPVKLSPTA--SLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEaarqtLQALPVPRITFNYLGQFDGSfDAEKQ 2541
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2980 AL---CEEPDGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLA 3055
Cdd:PRK12467  2542 ALfvpSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEhCCSNDQRGVTPS 2621
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3056 DLPLAGLDNAPLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGaLDREAFAAAWQQALERHPILR 3135
Cdd:PRK12467  2622 DFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILR 2700
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3136 SGFAVQG-LPSPRQLPHRQVSLPLAEQDWSglEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRH 3214
Cdd:PRK12467  2701 SGFLWDGeLEEPLQVVYKQARLPFSRLDWR--DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNH 2778
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3215 HLIVDGWSSALLLDEVWRLYAAlresrtpQLPAAPP--FRDYLHWLRGQDEAAARAFWREQL------TGLEPAALPEAT 3286
Cdd:PRK12467  2779 HILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQDAEASEAFWKEQLaaleepTRLARALYPAPA 2851
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3287 EPAEGYASSTRRFD---LAAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSV 3363
Cdd:PRK12467  2852 EAVAGHGAHYLHLDatqTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTL 2931
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3364 PLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSPFDVLLVFENLPTESREER---SGMRIEELDHR 3440
Cdd:PRK12467  2932 PVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQgapSGLRFGAVSSR 3011
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3441 AHSNYPLMLtAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQ--VPALQRFDALPLL----PSQTRSAAWTSRER 3514
Cdd:PRK12467  3012 EQTNYPLTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAmlNNPAARLGELPTLaaheRRQVLHAWNATAAA 3090
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3515 YACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGA 3594
Cdd:PRK12467  3091 YPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGG 3170
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3595 AYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELP----GTALCLDDpftraqldAVEPGELPEVPT-----EAPAYL 3665
Cdd:PRK12467  3171 AYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPapagDTALTLDR--------LDLNGYSENNPStrvmgENLAYV 3242
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3666 IYTSGSTGTPKGVVVTHRNVERLFTAATQTgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcRQPDAF 3745
Cdd:PRK12467  3243 IYTSGSTGKPKGVGVRHGALANHLCWIAEA--YELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEEL 3319
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTPSAFYALQSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVSFHRL 3825
Cdd:PRK12467  3320 WQAIHAHRISIACFPPAYLQQFAEDAGGADCA-SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVV-TVTLWK 3397
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3826 SDEDLQ--SPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGD 3899
Cdd:PRK12467  3398 CGGDAVceAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVadpfSGSGGRLYRTGD 3477
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALR 3979
Cdd:PRK12467  3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLA 3557
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEGVL-ESASERRLAELWRQLLGGELPGRGAHFFARGGHSL 4058
Cdd:PRK12467  3558 ASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVApRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSL 3637
                         2570      2580
                   ....*....|....*....|....*.
gi 1246793773 4059 LVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12467  3638 LALQVLSRIRQSLGLKLSLRDLMSAP 3663
PRK12316 PRK12316
peptide synthase; Provisional
1573-4084 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1387.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1573 PQARLQADEFALLAAREDARAIEHAFPLTPLQRGVLLESLRGD-----------GADPYFQQTVAELDGEIDAAALAQAW 1641
Cdd:PRK12316  2567 LRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQqrqwflwqlepESAAYHLPSALHLRGVLDQAALEQAF 2646
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1642 QQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAqlqrwLADDAAQGVDFAHAPLARMSLIGRGG 1721
Cdd:PRK12316  2647 DALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQR-----VAEEIQRPFDLARGPLLRVRLLALDG 2721
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1722 GRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPGFQA-----YLDWRERQDLARQRGWWRERLSGYAG 1796
Cdd:PRK12316  2722 QEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYAdyaawQRAWMDSGEGARQLDYWRERLGGEQP 2801
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQREECER-RLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRppELAG 1875
Cdd:PRK12316  2802 VLELPLDRPRPALQSHRGARLDvALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAE 2879
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1876 VESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILA----DSGLDADRLFASLLVVENFPAMAPA 1951
Cdd:PRK12316  2880 TERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEalqpERSLSHSPLFQVMYNHQSGERAAAQ 2959
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1952 Q-LPFALRVRETRAANHYALTLRVSERECVRLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVAELLGGDDAVQA 2030
Cdd:PRK12316  2960 LpGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEER 3039
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2031 PQPQRASSATA----------QSLLWQMPAQ--AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFA 2098
Cdd:PRK12316  3040 GQLLEAWNATAaeyplergvhRLFEEQVERTpdAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLE 3119
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2099 QLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVPASVRWLDAESVLDvvSAYEEPPRVDVDADT 2178
Cdd:PRK12316  3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDE--NYAEANPAIRTMPEN 3197
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQ 2258
Cdd:PRK12316  3198 LAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPA 3277
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLrivNHYGPTETTVGILTCT 2338
Cdd:PRK12316  3278 LLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLY---NLYGPTEATITVTHWQ 3354
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEEWPVEqgVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLA 2418
Cdd:PRK12316  3355 CVEEGKDA--VPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLA 3432
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS--LEGVAEALAQRLPE 2496
Cdd:PRK12316  3433 RYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGdlREALKAHLKASLPE 3512
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2497 YLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQDDAdssaeaideTPVNEVLREL---WQKLLGREHIGAHDNFFAL 2569
Cdd:PRK12316  3513 YMVPAHLLFLERMPLTPNGKLDRKALprpdAALLQQDYV---------APVNELERRLaaiWADVLKLEQVGLTDNFFEL 3583
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2570 GGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLSAQVQASSPAPATIKPATEAEQsfgLTPIQHWFFEQALDQPAHWN 2649
Cdd:PRK12316  3584 GGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETL---LLPIQQQFFEEPVPERHHWN 3660
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2650 MSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLG-------DWQADRfahreADAGQREDLLAQWQA 2722
Cdd:PRK12316  3661 QSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPvelggalLWRAEL-----DDAEELERLGEEAQR 3735
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2723 GLSF-DGALLRVLaLPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQ-LS 2800
Cdd:PRK12316  3736 SLDLaDGPLLRAL-LATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEhAR 3814
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2801 AATLDGWRSYWRAQ---AADAEAIALPWQDSDNRYADTVHlhDRFERDWTERLLTQTARAYGNEPQEVLLTALALAL-RD 2876
Cdd:PRK12316  3815 GEALKAELAYWQEQlqgVSSELPCDHPQGALQNRHAASVQ--TRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVcRW 3892
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2877 GGDAATLwVEMEGHGRDDLGAGLDLSRTVGWFTARYPLalHLPAGEDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE-- 2954
Cdd:PRK12316  3893 TGEASAL-VQLEGHGREDLFADIDLSRTVGWFTSLFPV--RLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEes 3969
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2955 ---LAELPVPQVCFNYLGQLRAGERDGWAL---CEEPDGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQ 3028
Cdd:PRK12316  3970 rrtLAGLPVPRITFNYLGQFDGSFDEEMALfvpAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQ 4049
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3029 ALSRRYLAVLRELIA-CVQTAEPRPTLADLPLAGLDNAPLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQT 3107
Cdd:PRK12316  4050 RLADDYAAELTALVEhCCDAERHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQM 4129
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3108 TVALHGaLDREAFAAAWQQALERHPILRSGFAVQG-LPSPRQLPHRQVSLPLAEQDWSGLEPAQARsrLSELQAQQCEAG 3186
Cdd:PRK12316  4130 RVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGeLGRPLQVVHKQVSLPFAELDWRGRADLQAA--LDALAAAERERG 4206
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3187 FDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAAlresRTPQLPAAPpFRDYLHWLRGQDEAAA 3266
Cdd:PRK12316  4207 FDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSG----RPPAQPGGR-YRDYIAWLQRQDAAAS 4281
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3267 RAFWREQLTGL-EPAALPEATE-----PAEGYASSTRRFD---LAAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFA 3337
Cdd:PRK12316  4282 EAFWREQLAALdEPTRLAQAIAradlrSANGYGEHVRELDataTARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVA 4361
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3338 LGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSPFDVLLV 3417
Cdd:PRK12316  4362 FGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLV 4441
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3418 FENLPTESREER---SGMRIEELDHRAHSNYPLMLtAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPA--LQ 3492
Cdd:PRK12316  4442 FENYPVSEALQQgapGGLRFGEVTNHEQTNYPLTL-AVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEdpQR 4520
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3493 RFDALPLLPSQTRSAA---WTSRE-RYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGP 3568
Cdd:PRK12316  4521 RLGELQLLEKAEQQRIvalWNRTDaGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGP 4600
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3569 GQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPGTA----LCLDdpftRA 3644
Cdd:PRK12316  4601 EVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDglasLALD----RD 4676
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3645 QLDAVEPGELPEVPTEAP--AYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELW 3722
Cdd:PRK12316  4677 EDWEGFPAHDPAVRLHPDnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGE--RYELTPDDRVLQFMSFSFDGSHEGLY 4754
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3723 GAWLYGGRaVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERY 3802
Cdd:PRK12316  4755 HPLINGAS-VVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRAL 4833
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3803 PQAELVNMYGITETTVHVSFHRLSDEDLQSPTS-RIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPEL 3881
Cdd:PRK12316  4834 KPVYLFNGYGPTETTVTVLLWKARDGDACGAAYmPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPAL 4913
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3882 TAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWL 3957
Cdd:PRK12316  4914 TAERFVpdpfGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQL 4993
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3958 MAYAVAADGAEPDP--------QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPET--QDRDEGVLESAS 4027
Cdd:PRK12316  4994 VGYVVPQDPALADAdeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDAslLQQAYVAPRSEL 5073
                         2570      2580      2590      2600      2610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 4028 ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:PRK12316  5074 EQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTP 5130
PRK12316 PRK12316
peptide synthase; Provisional
87-2812 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1352.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS-----VAAGGGAAVES 161
Cdd:PRK12316    49 RDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqVPLDRPLEVEF 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQDEIDALVE----GFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYR 237
Cdd:PRK12316   129 EDCSGLPEAEQEARLRdeaqRESLQPFDLCEGPLLRVRLLRLGEE-----EHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 VECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:PRK12316   204 AYATGAEPGLPALPIQYADYALWQRSWLEagEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAE 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  316 RVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRD 395
Cdd:PRK12316   284 ALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKD 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  396 HQLAALEHQALPLERVIETLQVERSSRHAPLFQLMF---ALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVLVGAGG 472
Cdd:PRK12316   364 TVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYnhqPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGR 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  473 MSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-------DDKREPAPRTVGNVVDAIARA 544
Cdd:PRK12316   444 LHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMlDAEERGQlvegwnaTAAEYPLQRGVHRLFEEQVER 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  545 AdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARR 624
Cdd:PRK12316   524 T---PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERL 600
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  625 AEVVAASGCDAVLTDaQGLAGFAPsVAIAVDELKLDGAG-------ENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHA 697
Cdd:PRK12316   601 AYMLEDSGVQLLLSQ-SHLGRKLP-LAAGVQVLDLDRPAawlegysEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHR 678
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  698 ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPAYAN 776
Cdd:PRK12316   679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 758
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  777 ELVRAsvADDWRDLALRCLVVGGDVLPVALAQRWFelGLDRRCALINAYGPTEATIS-SHYHRVQAidASRPVPLGQLLP 855
Cdd:PRK12316   759 AFLQD--EDVASCTSLRRIVCSGEALPADAQEQVF--AKLPQAGLYNLYGPTEAAIDvTHWTCVEE--GGDSVPIGRPIA 832
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:PRK12316   833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGE--RMYRTGDLARYRADGVIEYAGRIDH 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGegaAQRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPA 1015
Cdd:PRK12316   911 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GKQLVGYVVLESEGGDWREALKA-------------HLAASLPE 974
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1016 YMVPTQFVALPRLPRNASGKIDRRALPAPPV-LAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSLQ 1093
Cdd:PRK12316   975 YMVPAQWLALERLPLTPNGKLDRKALPAPEAsVAQQGYVAPRNALERTLAAIWQDVLGVErVGLDDNFFELGGDSIVSIQ 1054
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1094 VVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLD 1173
Cdd:PRK12316  1055 VVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLD 1134
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1174 AQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAfarmQEATPLA-GPLV-ALT 1251
Cdd:PRK12316  1135 PDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEA----QRSLDLEqGPLLrALL 1210
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1252 HAHCDDGERLLICAHHLIVDAVSWRLLLGELfdgLAALARGEAWTPsARGASYADYVEALREADDAQRFDAGFWRELAAQ 1331
Cdd:PRK12316  1211 VDMADGSQRLLLVIHHLVVDGVSWRILLEDL---QRAYADLDADLP-ARTSSYQAWARRLHEHAGARAEELDYWQAQLED 1286
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1332 PMQALPQDRPVALADARQSNvgRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-D 1410
Cdd:PRK12316  1287 APHELPCENPDGALENRHER--KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGReD 1364
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1411 VLDGRDWSSVLGWYTAVHPLPLDlGVADGPAQIGALKEQIRALARRGLDYMPLV------ASARIPALPAGQLLFNYHGV 1484
Cdd:PRK12316  1365 LFEDIDLSRTVGWFTSLFPVRLT-PAADLGESIKAIKEQLRAVPDKGIGYGLLRylageeAAARLAALPQPRITFNYLGQ 1443
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1485 VDAGAHPAFEVEPRTLASGNGADN--PPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQP 1562
Cdd:PRK12316  1444 FDRQFDEAALFVPATESAGAAQDPcaPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDE 1523
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1563 GSGALTASDLPQARL---QADEFALlaareDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGeIDAAALAQ 1639
Cdd:PRK12316  1524 RNRGVTPSDFPLAGLsqaQLDALPL-----PAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRA 1597
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1640 AWQQTVRRQPMLRTAIVWE-GLSVPHQIVLADAAAPWQTLDWSALDDAAQDaqLQRWLADDAAQGVDFAHAPLARMSLIG 1718
Cdd:PRK12316  1598 AWQATVDRHEILRSGFLWQdGLEQPLQVIHKQVELPFAELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVR 1675
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1719 RGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAgaqgatlRLPPAPG--FQAYLDWRERQDLARQRGWWRERLSGYAG 1796
Cdd:PRK12316  1676 TGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-------QPVAAPGgrYRDYIAWLQRQDAAASEAFWKEQLAALEE 1748
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGV 1876
Cdd:PRK12316  1749 PTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGI 1828
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1877 ESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLFASLLVVENFPAM------AP 1950
Cdd:PRK12316  1829 EQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAealkqgAP 1908
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1951 AQLPFA-LRVRETraaNHYALTLRVSERECVRLE-----------ALLDAARVDRAAVAAMLDLAVAGL--LRLLQRPDC 2016
Cdd:PRK12316  1909 AGLVFGrVSNHEQ---TNYPLTLAVTLGETLSLQysydrghfdaaAIERLDRHLLHLLEQMAEDAQAALgeLALLDAGER 1985
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2017 RvaELLGGDDAVQAPQPQRASSATAQSLLWQMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT 2096
Cdd:PRK12316  1986 Q--RILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERS 2063
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2097 FAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWG--AAPAWVPASVRWLDAESVLDVVSAYEEPPRVDV 2174
Cdd:PRK12316  2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRhlLERLPLPAGVARLPLDRDAEWADYPDTAPAVQL 2143
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2175 DADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELa 2254
Cdd:PRK12316  2144 AGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL- 2222
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2255 FDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP--RECLVtGGEALTGALVQQVRALAPTLRIVNHYGPTETTV 2332
Cdd:PRK12316  2223 WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPavRVYCF-GGEAVPAASLRLAWEALRPVYLFNGYGPTEAVV 2301
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2333 GILTCTV-PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRL 2410
Cdd:PRK12316  2302 TPLLWKCrPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGER 2381
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2411 LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-----QGSLEG 2485
Cdd:PRK12316  2382 LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVpddaaEDLLAE 2461
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2486 VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQddadssAEAIDETPVNEVLRELWQKLLGREHIG 2561
Cdd:PRK12316  2462 LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALpkpdVSQLRQ------AYVAPQEGLEQRLAAIWQAVLKVEQVG 2535
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2562 AHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSA--QVQASSPAPATIKPATEAEQSFGLTPIQHWFF 2638
Cdd:PRK12316  2536 LDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAAslESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFL 2615
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2639 EQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRF---AHREADAGQRED 2715
Cdd:PRK12316  2616 WQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVledCAGVADAAIRQR 2695
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2716 LLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAA 2795
Cdd:PRK12316  2696 VAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAW 2775
                         2810
                   ....*....|....*...
gi 1246793773 2796 LRQ-LSAATLDGWRSYWR 2812
Cdd:PRK12316  2776 QRAwMDSGEGARQLDYWR 2793
PRK12467 PRK12467
peptide synthase; Provisional
69-2628 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1339.04  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   69 TQDADWRAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGE 148
Cdd:PRK12467  1098 AAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQE 1177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  149 DS-----VAAGGGAAVESADLRGRGQDE--IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACD 221
Cdd:PRK12467  1178 DGrtrqvIHPVGSLTLEEPLLLAADKDEaqLKVYVEAEARQPFDLEQGPLLRVGLLRLAAD-----EHVLVLTLHHIVSD 1252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  222 GVSLGLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLG 299
Cdd:PRK12467  1253 GWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDagERARQLAYWKAQLGGEQPVLELPTDRPRPAVQS 1332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  300 QSGAKLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQ 379
Cdd:PRK12467  1333 HRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAE 1412
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  380 LHDDPDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLAL-DLHGVQAHALTLPEDVA 458
Cdd:PRK12467  1413 VDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTA 1492
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  459 KHELTLEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEP--ALSWPWPADELAL------DDKREPA 530
Cdd:PRK12467  1493 QFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRlgELDLLDEAERRQIlegwnaTHTGYPL 1572
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  531 PRTVGNVvdaIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGL 610
Cdd:PRK12467  1573 ARLVHQL---IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG 1649
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  611 SVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFA-----PSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGS 685
Cdd:PRK12467  1650 AYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPlpdglRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGS 1729
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  686 TGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERA 764
Cdd:PRK12467  1730 TGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGArLVIAPPGAHRDPEQLIQLIERQQ 1809
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  765 ITVTDLAPAYANELVRAsVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRrcALINAYGPTEATISSHYHRVQAID- 843
Cdd:PRK12467  1810 VTTLHFVPSMLQQLLQM-DEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDT--GLFNLYGPTETAVDVTHWTCRRKDl 1886
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  844 -ASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESlRMYRSGDRVRLL 922
Cdd:PRK12467  1887 eGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVGS-RLYRTGDLARYR 1965
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  923 DDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGfgqadLNQTDSDQTES 1002
Cdd:PRK12467  1966 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGL-----VDDDEAQVALR 2040
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1003 ERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAP-PVLAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDS 1080
Cdd:PRK12467  2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPdASELQQAYVAPQSELEQRLAAIWQDVLGLEqVGLHDN 2120
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1081 FFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLV-GEVGLSPIQRWFFDSAPAQPDR 1159
Cdd:PRK12467  2121 FFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQGPVtGDLPLLPIQQMFFADDIPERHH 2200
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1160 YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaiQAQDWRGAADLDSRVDAAFARMQE 1239
Cdd:PRK12467  2201 WNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQER--RPLLWQVVVADKEELEALCEQAQR 2278
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1240 ATPLA-GPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALRE--AD 1315
Cdd:PRK12467  2279 SLDLEeGPLLRAVLATLPDGSqRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTyaAS 2358
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1316 DAQRFDAGFWRelaAQpMQALPQDRPVALADARQSN--VGRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALAT 1393
Cdd:PRK12467  2359 AALADELGYWQ---AQ-LQGASTELPCDHPQGGLQRrhAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIAR 2434
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1394 RTGRNRLWLDRERHGR-DVLDGRDWSSVLGWYTAVHPLPLDlGVADGPAQIGALKEQIRALARRGLDYMPL------VAS 1466
Cdd:PRK12467  2435 WTGQASTLIQLEGHGReDLFDEIDLTRTVGWFTSLYPVKLS-PTASLATSIKTIKEQLRAVPNKGLGFGVLrylgseAAR 2513
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1467 ARIPALPAGQLLFNYHGVVD----AGAHPAFEVEPRTLASGNGADNPPGALVEINARVQAGRLGLVWNYAGEAYDAATIE 1542
Cdd:PRK12467  2514 QTLQALPVPRITFNYLGQFDgsfdAEKQALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQ 2593
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1543 AWSQAFAAELAALVAHCLQPGSGALTASDLPQARL-QADEFALLAAREDaraIEHAFPLTPLQRGVLLESLRGDGADPYF 1621
Cdd:PRK12467  2594 RLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLsQEQLDRLPVAVGD---IEDIYPLSPMQQGMLFHTLYEGGAGDYI 2670
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1622 QQTVAELDGeIDAAALAQAWQQTVRRQPMLRTAIVWEG-LSVPHQIVLADAAAPWQTLDWSALDDAAQDaqLQRWLADDA 1700
Cdd:PRK12467  2671 NQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQA--LDALAAADR 2747
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1701 AQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAgaqgatlRLPPAPG--FQAYLDWRERQ 1778
Cdd:PRK12467  2748 QQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFG-------QPPPAREgrYRDYIAWLQAQ 2820
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1779 DLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREECERRL--SAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGN 1856
Cdd:PRK12467  2821 DAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLhlDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTG 2900
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1857 HDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLF 1936
Cdd:PRK12467  2901 QDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALF 2980
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1937 ASLLVVENFPA------MAPAQLPF-ALRVRETraaNHYALTLRVSERECVRLEaLLDAARVDRAAVAAMLDLAVAGLLR 2009
Cdd:PRK12467  2981 DSILVFENYPIsealkqGAPSGLRFgAVSSREQ---TNYPLTLAVGLGDTLELE-FSYDRQHFDAAAIERLAESFDRLLQ 3056
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2010 -LLQRPDCRVAEL--LGGDDAVQAPQPQRASSAT--AQSLLWQM-------PAQAVAVEEGAASWTYAQLRAAAGRIAGA 2077
Cdd:PRK12467  3057 aMLNNPAARLGELptLAAHERRQVLHAWNATAAAypSERLVHQLieaqvarTPEAPALVFGDQQLSYAELNRRANRLAHR 3136
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVP--ASVRWLD 2155
Cdd:PRK12467  3137 LIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPapAGDTALT 3216
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2156 AESvLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTA 2235
Cdd:PRK12467  3217 LDR-LDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER 3295
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2236 LFGALLSGRRVRLLPAELaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRAL 2315
Cdd:PRK12467  3296 FLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRK 3374
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVGILTCTVP-EEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAE 2394
Cdd:PRK12467  3375 LKPRGLTNGYGPTEAVVTVTLWKCGgDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPS 3454
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2395 QTAERFVAHPL--APDRlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANG- 2471
Cdd:PRK12467  3455 LTAERFVADPFsgSGGR-LYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGk 3533
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2472 ----VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLlqqdDADSSAEAIdeTPVNEVL 2547
Cdd:PRK12467  3534 qlvaYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP----DAKGSREYV--APRSEVE 3607
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2548 REL---WQKLLGREHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQASSPAPATIKPATE 2623
Cdd:PRK12467  3608 QQLaaiWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAGYSPLGDVPVNLLLDLNR 3687

                   ....*
gi 1246793773 2624 AEQSF 2628
Cdd:PRK12467  3688 LETGF 3692
PRK12316 PRK12316
peptide synthase; Provisional
75-2617 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1237.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS---- 150
Cdd:PRK12316  2590 RAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEqtrq 2669
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  151 -VAAGGGAAVESADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLT 229
Cdd:PRK12316  2670 vILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQ-----EHVLVITQHHIVSDGWSMQVMV 2744
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  230 QDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRL 307
Cdd:PRK12316  2745 DELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDsgEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDV 2824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  308 AFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFA 387
Cdd:PRK12316  2825 ALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFR 2904
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  388 SLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVL 467
Cdd:PRK12316  2905 DLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTW 2984
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  468 VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW---PADELALDD-----KREPAPRTVGNVVD 539
Cdd:PRK12316  2985 ESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMldaEERGQLLEAwnataAEYPLERGVHRLFE 3064
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  540 AIARAAdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEW 619
Cdd:PRK12316  3065 EQVERT---PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  620 PQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAAL 699
Cdd:PRK12316  3142 PEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL 3221
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  700 AAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERaiTVTDLAPAYANELV 779
Cdd:PRK12316  3222 SNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINS--EGVDVLHAYPSMLQ 3299
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  780 RASVADDWRDL-ALRCLVVGGDVLPVALAQRWFELGldrrcALINAYGPTEATISSHYHRVQAIDASRPvPLGQLLPGRI 858
Cdd:PRK12316  3300 AFLEEEDAHRCtSLKRIVCGGEALPADLQQQVFAGL-----PLYNLYGPTEATITVTHWQCVEEGKDAV-PIGRPIANRA 3373
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  859 AAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVK 938
Cdd:PRK12316  3374 CYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGE--RLYRTGDLARYRADGVIEYIGRVDHQVK 3451
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  939 LRGYRIELEEIEHCLGQLPQVRAAaagVVGEGAAQRLVAWVEcagedgfgqadlnQTDSDQTESERWHRALCERLPAYMV 1018
Cdd:PRK12316  3452 IRGFRIELGEIEARLLEHPWVREA---VVLAVDGRQLVAYVV-------------PEDEAGDLREALKAHLKASLPEYMV 3515
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRRALPAPPV-LAQAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSLQVVA 1096
Cdd:PRK12316  3516 PAHLLFLERMPLTPNGKLDRKALPRPDAaLLQQDYVAPVNELERRLAAIWADVLKLEqVGLTDNFFELGGDSIISLQVVS 3595
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1097 RLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQH 1176
Cdd:PRK12316  3596 RARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREALDAAA 3675
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1177 LAQVWDALWRRHDLLRASFERADGQWRqqvAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLA-GPLV-ALTHAH 1254
Cdd:PRK12316  3676 LEAALQALVEHHDALRLRFVEDAGGWT---AEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLAdGPLLrALLATL 3752
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1255 CDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALRE--ADDAQRFDAGFWRELAAQP 1332
Cdd:PRK12316  3753 ADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEhaRGEALKAELAYWQEQLQGV 3832
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1333 MQALPQDRPvalADARQSNVGRIVQT-LDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-D 1410
Cdd:PRK12316  3833 SSELPCDHP---QGALQNRHAASVQTrLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGReD 3909
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1411 VLDGRDWSSVLGWYTAVHPLPLDLGVADGpAQIGALKEQIRALARRGLDYMPL------VASARIPALPAGQLLFNYHGV 1484
Cdd:PRK12316  3910 LFADIDLSRTVGWFTSLFPVRLSPVEDLG-ASIKAIKEQLRAIPNKGIGFGLLrylgdeESRRTLAGLPVPRITFNYLGQ 3988
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1485 VDAgahpAFEVEPRTL---ASGNGADNPPGALVE----INARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVA 1557
Cdd:PRK12316  3989 FDG----SFDEEMALFvpaGESAGAEQSPDAPLDnwlsLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVE 4064
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1558 HCLQPGSGALTASDLPQARLqaDEFALLAAREDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGeIDAAAL 1637
Cdd:PRK12316  4065 HCCDAERHGVTPSDFPLAGL--DQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERF 4141
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1638 AQAWQQTVRRQPMLRTAIVWEG-LSVPHQIVLADAAAPWQTLDWSALDDaaQDAQLQRWLADDAAQGVDFAHAPLARMSL 1716
Cdd:PRK12316  4142 RAAWQAALDRHDVLRSGFVWQGeLGRPLQVVHKQVSLPFAELDWRGRAD--LQAALDALAAAERERGFDLQRAPLLRLVL 4219
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1717 IGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGatlrlPPAPGFQAYLDWRERQDLARQRGWWRERLSGY-A 1795
Cdd:PRK12316  4220 VRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPA-----QPGGRYRDYIAWLQRQDAAASEAFWREQLAALdE 4294
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1796 GTAALPAPVAAAHHPVQ-REECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELA 1874
Cdd:PRK12316  4295 PTRLAQAIARADLRSANgYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELP 4374
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1875 GVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADRLFASLLVVENFPAMAPAQLP 1954
Cdd:PRK12316  4375 GIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQG 4454
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1955 FALRVRETRAANH----YALTLRVSERECVRLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVAEL--LGGDDAV 2028
Cdd:PRK12316  4455 APGGLRFGEVTNHeqtnYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELqlLEKAEQQ 4534
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2029 QAPQPQRASSA--TAQSLLWQ-------MPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQ 2099
Cdd:PRK12316  4535 RIVALWNRTDAgyPATRCVHQlvaerarMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEM 4614
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2100 LAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVI--GWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVDAD 2177
Cdd:PRK12316  4615 MVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLtqSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPD 4694
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELaFDA 2257
Cdd:PRK12316  4695 NLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL-WDP 4773
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILT 2336
Cdd:PRK12316  4774 ERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSlRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLL 4853
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2337 CTVPE-EWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRS 2414
Cdd:PRK12316  4854 WKARDgDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRT 4933
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVlQLGACIQGSLEGVAE------ 2488
Cdd:PRK12316  4934 GDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGK-QLVGYVVPQDPALADadeaqa 5012
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2489 --------ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL----ADLLQQddadssAEAIDETPVNEVLRELWQKLLG 2556
Cdd:PRK12316  5013 elrdelkaALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALpqpdASLLQQ------AYVAPRSELEQQVAAIWAEVLQ 5086
                         2570      2580      2590      2600      2610      2620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2557 REHIGAHDNFFALGGDSILSLQLVARAR-QAGLALMPRQLYDHPTLAGLSAQVQASSPAPAT 2617
Cdd:PRK12316  5087 LERVGLDDNFFELGGHSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
PRK05691 PRK05691
peptide synthase; Validated
1625-4082 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1207.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1625 VAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGV 1704
Cdd:PRK05691  1756 MARLSGVLDVDRFEAALQALILRHETLRTTFPSVD-GVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPF 1834
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1705 DFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRER 1777
Cdd:PRK05691  1835 DLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLP--VQYLDysvwqrqWLES 1912
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1778 QDLARQRGWWRERLsgyaGTA--ALPAPVAAAHHPVQ--REECER-RLSAHDSERLRAFCRERGCTLSDLIAMVWGLANA 1852
Cdd:PRK05691  1913 GERQRQLDYWKAQL----GNEhpLLELPADRPRPPVQshRGELYRfDLSPELAARVRAFNAQRGLTLFMTMTATLAALLY 1988
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1853 RYGNHDDVVLGATRSGR-PPElagVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILadSGLD 1931
Cdd:PRK05691  1989 RYSGQRDLRIGAPVANRiRPE---SEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLV--EALQ 2063
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1932 ADR------LFASLLVVENFPAMAPAQLP---FALRVRETRAANhYALTLRVSERE-----CVRLEALLDAARVDRAAVA 1997
Cdd:PRK05691  2064 PPRsaaynpLFQVMCNVQRWEFQQSRQLAgmtVEYLVNDARATK-FDLNLEVTDLDgrlgcCLTYSRDLFDEPRIARMAE 2142
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1998 AMLDLAVAgllrLLQRPDCRVAELLGGDDAVQ-------APQP-QRASSATAQSLLWQMPA---QAVAVEEGAASWTYAQ 2066
Cdd:PRK05691  2143 HWQNLLEA----LLGDPQQRLAELPLLAAAEQqqlldslAGEAgEARLDQTLHGLFAAQAArtpQAPALTFAGQTLSYAE 2218
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2067 LRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGA---A 2143
Cdd:PRK05691  2219 LDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRAlfeA 2298
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2144 PAWVPASV-RWL--DAESVLDVVSAyEEPPRVDVdADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:PRK05691  2299 LGELPAGVaRWCleDDAAALAAYSD-APLPFLSL-PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDC 2376
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVrLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLA-AAGGTAVLPRECLVT 2299
Cdd:PRK05691  2377 ELHFYSINFDAASERLLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQwLAGQGEQLPVRMCIT 2455
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2300 GGEALTGALVQQVR-ALAPTLrIVNHYGPTETTVGILTCTVPEEWPVEQG-VPVGHPLAGNEAWVLDRFGLPAPVGVAGE 2377
Cdd:PRK05691  2456 GGEALTGEHLQRIRqAFAPQL-FFNAYGPTETVVMPLACLAPEQLEEGAAsVPIGRVVGARVAYILDADLALVPQGATGE 2534
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2378 LYLGGGNLSLGYWQRAEQTAERFVAHPLAPDR-LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLP 2456
Cdd:PRK05691  2535 LYVGGAGLAQGYHDRPGLTAERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP 2614
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2457 GVEVAAVLALPGANG----------VLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL-AD 2524
Cdd:PRK05691  2615 AVREAVVLALDTPSGkqlagylvsaVAGQDDEAQAALrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALpAP 2694
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2525 LLQQDDADSSAeaidetPVNEVLREL---WQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTL 2601
Cdd:PRK05691  2695 DPELNRQAYQA------PRSELEQQLaqiWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTV 2768
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2602 AGLSAQVQASSPAPATIKPATEAEqsfGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRA 2681
Cdd:PRK05691  2769 QTLAAVATHSEAAQAEQGPLQGAS---GLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRL 2845
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2682 RFqRDAAGQWQ---QTLGD----WQAdrfahREADAGQREDLLAQWQAGLSF-DGALLRVLALPDPQdGDTRVLFAAHHL 2753
Cdd:PRK05691  2846 RF-SQADGRWQaeyRAVTAqellWQV-----TVADFAECAALFADAQRSLDLqQGPLLRALLVDGPQ-GQQRLLLAIHHL 2918
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2754 LVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSAA-TLDGWRSYWRAQAADAEAI---ALPWQDSD 2829
Cdd:PRK05691  2919 VVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSeSLREELGWWQAQLGGPRAElpcDRPQGGNL 2998
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2830 NRYADTVHLhdRFERDWTERLLTQTARAYGNEPQEVLLTALALAL-RDGGDAATLwVEMEGHGRDDLGAGLDLSRTVGWF 2908
Cdd:PRK05691  2999 NRHAQTVSV--RLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLcRWSGQPSVL-VQLEGHGREALFDDIDLTRSVGWF 3075
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2909 TARYPLAL--HLPAGEDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE-----LAELPVPQVCFNYLGQLRAG-ERDG-W 2979
Cdd:PRK05691  3076 TSAYPLRLtpAPGDDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAavreaMAALPQAPITFNYLGQFDQSfASDAlF 3155
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2980 ALCEEPDGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA-CVQTAEPRPTLADLP 3058
Cdd:PRK05691  3156 RPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAhCLADGAGGLTPSDFP 3235
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3059 LAGLDNAPLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF 3138
Cdd:PRK05691  3236 LAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASF 3315
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3139 AVQGLPSPRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIV 3218
Cdd:PRK05691  3316 SWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILI 3395
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3219 DGWSSALLLDEVWRLYAALRESRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLE-PAALP-------EATEPAE 3290
Cdd:PRK05691  3396 DAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFErPTPIPsdrpflrEHAGDSG 3475
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3291 GYASSTRRFDLAAASA-----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPL 3365
Cdd:PRK05691  3476 GMVVGDCYTRLDAADGarlreLAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIAL 3555
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3366 RV---TPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSP-FDVLLVFENLPTESR--EERSGMRIEELDH 3439
Cdd:PRK05691  3556 RVqlpAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPlFDSLFVFENAPVEVSvlDRAQSLNASSDSG 3635
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3440 RAHSNYPLMLTAIP-DAGGLRIeaALDRSKLDGWLVEQMLDDLDFVLqqVPALQRFD----ALPLLPSQTRS----AAWT 3510
Cdd:PRK05691  3636 RTHTNFPLTAVCYPgDDLGLHL--SYDQRYFDAPTVERLLGEFKRLL--LALVQGFHgdlsELPLLGEQERDflldGCNR 3711
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3511 SRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAIL 3590
Cdd:PRK05691  3712 SERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSF 3791
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3591 KTGAAYVPVDPHAPAARRGFILEDSG----VClSVSQRALAVELPGTALCLDDPftraQLDAVEPGELPEVPTEAP---- 3662
Cdd:PRK05691  3792 KAGAGYLPLDPGLPAQRLQRIIELSRtpvlVC-SAACREQARALLDELGCANRP----RLLVWEEVQAGEVASHNPgiys 3866
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 -----AYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEA 3737
Cdd:PRK05691  3867 gpdnlAYVIYTSGSTGLPKGVMVEQRGM--LNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNA 3944
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 VCRQPDAFLDLLAEYGVTVLNQTPSafyALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITET 3816
Cdd:PRK05691  3945 IAHDPQGLLAHVQAQGITVLESVPS---LIQGMLAEDRQALDgLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAEC 4021
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER----GGQ 3892
Cdd:PRK05691  4022 SDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHpfgaPGE 4101
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3893 RFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQ 3972
Cdd:PRK05691  4102 RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGA 4181
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3973 SL---REALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPE---TQDRDEGVLESASERRLAELWRQLLGGELPGR 4046
Cdd:PRK05691  4182 LLeriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDigqLQSQAYLAPRNELEQTLATIWADVLKVERVGV 4261
                         2570      2580      2590
                   ....*....|....*....|....*....|....*.
gi 1246793773 4047 GAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFE 4082
Cdd:PRK05691  4262 HDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFE 4297
PRK05691 PRK05691
peptide synthase; Validated
75-2609 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1082.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS---- 150
Cdd:PRK05691  1716 SQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGvpvq 1795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  151 -VAAGGGAAVE----SADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSL 225
Cdd:PRK05691  1796 qVAEDSGLRMDwqdfSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAER-----EHYFVLTLHHIVTEGWAM 1870
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  226 GLLTQDLSRAYrvECGLAAEPAP--PLPCQYGDYARWQRDTLDRLDAS--LRHHVEALSGAPHLHELPLDHERPAVLGQS 301
Cdd:PRK05691  1871 DIFARELGALY--EAFLDDRESPlePLPVQYLDYSVWQRQWLESGERQrqLDYWKAQLGNEHPLLELPADRPRPPVQSHR 1948
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  302 GAKLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLH 381
Cdd:PRK05691  1949 GELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLD 2028
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  382 DDPDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFAL-RHDADLALDLHGVQAHALTLPEDVAKH 460
Cdd:PRK05691  2029 GQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVqRWEFQQSRQLAGMTVEYLVNDARATKF 2108
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  461 ELTLEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW--PADELALDDKREPAP---RTVG 535
Cdd:PRK05691  2109 DLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLlaAAEQQQLLDSLAGEAgeaRLDQ 2188
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  536 NVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPL 615
Cdd:PRK05691  2189 TLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPL 2268
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  616 DTEWPQARRAEVVAASGCDAVLTDA---QGLAGFAPSVA---IAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIP 689
Cdd:PRK05691  2269 DPEYPLERLHYMIEDSGIGLLLSDRalfEALGELPAGVArwcLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKP 2348
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  690 KGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERAITVTD 769
Cdd:PRK05691  2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILG 2428
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  770 LAPAYANELVRAsVADDWRDLALRCLVVGGDVLPVALAQRWfelgldRRC----ALINAYGPTEATI----SSHYHRVQA 841
Cdd:PRK05691  2429 FTPSYGSQLAQW-LAGQGEQLPVRMCITGGEALTGEHLQRI------RQAfapqLFFNAYGPTETVVmplaCLAPEQLEE 2501
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  842 IDASrpVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLpSGESLRMYRSGDRVRL 921
Cdd:PRK05691  2502 GAAS--VPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPF-AADGGRLYRTGDLVRL 2578
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  922 LDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVEC--AGEDGFGQADLNqtdsdq 999
Cdd:PRK05691  2579 RADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSavAGQDDEAQAALR------ 2652
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1000 tesERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAP-PVLAQAERTPPRTAEESALCEVWAEVLQCE-VGI 1077
Cdd:PRK05691  2653 ---EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPdPELNRQAYQAPRSELEQQLAQIWREVLNVErVGL 2729
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1078 HDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQP 1157
Cdd:PRK05691  2730 GDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQP 2809
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1158 DRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPA-IQAQdwrgAADLDSRvDAAFAR 1236
Cdd:PRK05691  2810 QHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELlWQVT----VADFAEC-AALFAD 2884
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1237 MQEATPLA-GPLV-ALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALRE- 1313
Cdd:PRK05691  2885 AQRSLDLQqGPLLrALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAy 2964
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1314 -ADDAQRFDAGFWRELAAQPMQALPQDRPVALADARQSNVGRIvqTLDAGLTADLLERAGEAYRCRTDEVLLIALARALA 1392
Cdd:PRK05691  2965 aGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSV--RLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLC 3042
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1393 TRTGRNRLWLDRERHGRDVL-DGRDWSSVLGWYTAVHPL---PLDLGVADGPAQIGALKEQIRALARRGLDYMPL----- 1463
Cdd:PRK05691  3043 RWSGQPSVLVQLEGHGREALfDDIDLTRSVGWFTSAYPLrltPAPGDDAARGESIKAIKEQLRAVPHKGLGYGVLrylad 3122
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1464 -VASARIPALPAGQLLFNYHGVVDAGAHPAFEVEPRTLASGnGADNPPGAL---VEINARVQAGRLGLVWNYAGEAYDAA 1539
Cdd:PRK05691  3123 aAVREAMAALPQAPITFNYLGQFDQSFASDALFRPLDEPAG-PAHDPDAPLpneLSVDGQVYGGELVLRWTYSAERYDEQ 3201
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1540 TIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQARLQADEFALLAAreDARAIEHAFPLTPLQRGVLLESLRGDGADP 1619
Cdd:PRK05691  3202 TIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPV--PAAEIEDVYPLTPMQEGLLLHTLLEPGTGL 3279
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1620 YFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADD 1699
Cdd:PRK05691  3280 YYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQE 3359
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1700 AAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPGFQAYLDWRERQD 1779
Cdd:PRK05691  3360 REAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPPRYRDYIGWLQRQD 3439
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1780 LARQRGWWRERLSGYAGTaalpaPVAAAHHPVQRE-----------ECERRLSAHDSERLRAFCRERGCTLSDLIAMVWG 1848
Cdd:PRK05691  3440 LAQARQWWQDNLRGFERP-----TPIPSDRPFLREhagdsggmvvgDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWA 3514
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1849 LANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRI-DAGQPAL--DLLSALRSQSLEVAENEAVGLGEIL 1925
Cdd:PRK05691  3515 LVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQLpAAGQRCSvrQWLQGLLDSNMELREYEYLPLVAIQ 3594
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1926 ADSGL-DADRLFASLLVVENfpamAPAQLPFALRVRETRAAN-------HYALTLRVSERECVRLEALLDAARVDRAAVA 1997
Cdd:PRK05691  3595 ECSELpKGQPLFDSLFVFEN----APVEVSVLDRAQSLNASSdsgrthtNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVE 3670
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1998 AMLDLAVAGLLRLLQRPDCRVAE--LLGGDDA---VQAPQPQRASSATAQSLLWQMPAQAVAVEEGAA------SWTYAQ 2066
Cdd:PRK05691  3671 RLLGEFKRLLLALVQGFHGDLSElpLLGEQERdflLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAascldqQWSYAE 3750
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2067 LRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAW 2146
Cdd:PRK05691  3751 LNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQ 3830
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2147 VPASVRWLDAES-----VLDVVSAYEEP---PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGED 2218
Cdd:PRK05691  3831 ARALLDELGCANrprllVWEEVQAGEVAshnPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEA 3910
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2219 ASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLV 2298
Cdd:PRK05691  3911 DVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLP 3990
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2299 TgGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGEL 2378
Cdd:PRK05691  3991 T-GEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGEL 4069
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2379 YLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPG 2457
Cdd:PRK05691  4070 CVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAE 4149
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2458 VEVAAVLALPGANGVLQLGACIQGS--------LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA--DLLQ 2527
Cdd:PRK05691  4150 VREAAVAVQEGVNGKHLVGYLVPHQtvlaqgalLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPalDIGQ 4229
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2528 QDDADSSAEaidETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMP-RQLYDHPTLAGLSA 2606
Cdd:PRK05691  4230 LQSQAYLAP---RNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPlRAMFECSTVEELAE 4306

                   ...
gi 1246793773 2607 QVQ 2609
Cdd:PRK05691  4307 YIE 4309
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3065-4084 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: 741.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3065 APLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQgLP 3144
Cdd:COG1020      2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTR-AG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3145 SPRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSA 3224
Cdd:COG1020     81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3225 LLLDEVWRLYAALRESRTPQLPAAPP-----FRDYLHWLRGQDEAAARAFWREQLTGLEPA-ALPE--ATEPAEGYASST 3296
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLlELPTdrPRPAVQSYRGAR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3297 RRFDLAAA-----SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPpeLAGVERMLGVFINSVPLRVTPAG 3371
Cdd:COG1020    241 VSFRLPAEltaalRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3372 EATPAPWLQALQQRNLDLRTHGYLPLAQIQRA---GAADAVSP-FDVLLVFENLPTESREeRSGMRIEELD-HRAHSNYP 3446
Cdd:COG1020    319 DPSFAELLARVRETLLAAYAHQDLPFERLVEElqpERDLSRNPlFQVMFVLQNAPADELE-LPGLTLEPLElDSGTAKFD 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3447 LMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPAL--QRFDALPLLPSQTRS---AAWTSRER-YACTGN 3520
Cdd:COG1020    398 LTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADpdQPLGDLPLLTAAERQqllAEWNATAApYPADAT 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:COG1020    478 LHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVCLSVSQRALAVELPGTA---LCLDDPFTRAQldavePGELPEVPT--EAPAYLIYTSGSTGTP 3675
Cdd:COG1020    558 PAYPAERLAYMLEDAGARLVLTQSALAARLPELGvpvLALDALALAAE-----PATNPPVPVtpDDLAYVIYTSGSTGRP 632
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVT 3755
Cdd:COG1020    633 KGVMVEHRALVNLLAWMQR--RYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVT 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3756 VLNQTPSAFYALQSQAMRRELALnvRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTS 3835
Cdd:COG1020    711 VLNLTPSLLRALLDAAPEALPSL--RLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSV 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 RIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:COG1020    789 PIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVAdpfgFPGARLYRTGDLARWLPDGNLEF 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRL 3990
Cdd:COG1020    869 LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVArEDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAA 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3991 IQLLPALPLTANGKLDRKALPKPETQDRDEGVLESASERR--LAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIR 4068
Cdd:COG1020    949 VVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEeeAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAAR 1028
                         1050
                   ....*....|....*.
gi 1246793773 4069 AEFAIAVPLKSLFEQP 4084
Cdd:COG1020   1029 LLLLLLLLLLLFLAAA 1044
PRK12467 PRK12467
peptide synthase; Provisional
3075-4085 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 676.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3075 PQTQDVY---PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGlPSPRQLPH 3151
Cdd:PRK12467    41 PQVRSAFeriPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDE-EGFRQVID 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3152 RQVSLPLAEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVW 3231
Cdd:PRK12467   120 ASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELV 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3232 RLYAALRESRTPQLPAAP-PFRDYLHWLRGQDEAAARA----FWREQLTGLEPA-ALP-EATEPA-EGYASSTRRFDL-- 3301
Cdd:PRK12467   200 QLYSAYSQGREPSLPALPiQYADYAIWQRSWLEAGERErqlaYWQEQLGGEHTVlELPtDRPRPAvPSYRGARLRVDLpq 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3302 ---AAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPElaGVERMLGVFINSVPLRVTPAGEATPAPW 3378
Cdd:PRK12467   280 alsAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLEL 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3379 LQALQQRNLDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLPTESRE----ERSGMRIEELDHRAHS-N 3444
Cdd:PRK12467   358 LQQVKRTALGAQAHQDLPFEQL-----VEALQPerslshsplFQVMFNHQNTATGGRDregaQLPGLTVEELSWARHTaQ 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3445 YPLMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPA--LQRFDALPLLPSQTRSA---AWTSRERYACTG 3519
Cdd:PRK12467   433 FDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAepRRRLGELPLLDAEERARelvRWNAPATEYAPD 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK12467   513 CVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGVCLSVSQRALAVELPG----TALCLDDPftrAQLDAVEPGELPEVPTEAP--AYLIYTSGSTG 3673
Cdd:PRK12467   593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVpaglRSLCLDEP---ADLLCGYSGHNPEVALDPDnlAYVIYTSGSTG 669
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYG 3753
Cdd:PRK12467   670 QPKGVAISHGALANYVCVIAE--RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQG 747
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3754 VTVLNQTPSAFYALQsQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSP 3833
Cdd:PRK12467   748 VTVLKIVPSHLQALL-QASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG 826
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3834 TSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSL 3909
Cdd:PRK12467   827 NVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPdpfgADGGRLYRTGDLARYRADGVI 906
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3910 EYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQS-----LREALRALLPD 3984
Cdd:PRK12467   907 EYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHQatrdeLKAQLRQVLPD 986
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3985 YMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVR 4062
Cdd:PRK12467   987 YMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTelEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQ 1066
                         1050      1060
                   ....*....|....*....|...
gi 1246793773 4063 LAEAIRAEFAIAVPLKSLFEQPR 4085
Cdd:PRK12467  1067 VISRVRQRLGIQVPLRTLFEHQT 1089
PRK12467 PRK12467
peptide synthase; Provisional
84-1371 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 664.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   84 AGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVL--------DRCIQGEDSVAAGG 155
Cdd:PRK12467    46 AFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLrtrfvqdeEGFRQVIDASLSLT 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  156 GAAVESADLRGRGQDE-IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSR 234
Cdd:PRK12467   126 IPLDDLANEQGRARESqIEAYINEEVARPFDLANGPLLRVRLLRLADD-----EHVLVVTLHHIISDGWSMRVLVEELVQ 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  235 AYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPG 312
Cdd:PRK12467   201 LYSAYSQGREPSLPALPIQYADYAIWQRSWLEagERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQA 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  313 LSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:PRK12467   281 LSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQ 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  393 CRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDA-----DLALDLHGVQAHALTLPEDVAKHELTLEVL 467
Cdd:PRK12467   361 VKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTAtggrdREGAQLPGLTVEELSWARHTAQFDLALDTY 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  468 VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWP-WPADELALDDKREPAPRTV---GNVVDAIAR 543
Cdd:PRK12467   441 ESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPlLDAEERARELVRWNAPATEyapDCVHQLIEA 520
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  544 AADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQAR 623
Cdd:PRK12467   521 QARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR 600
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  624 RAEVVAASGCDAVLTDAQGLAGFA-----PSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:PRK12467   601 LAYMLDDSGVRLLLTQSHLLAQLPvpaglRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARP-DELLEPQRFLAFLSERAITVTDLAPAYANE 777
Cdd:PRK12467   681 LANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPpDCARDAEAFAALMADQGVTVLKIVPSHLQA 760
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  778 LVRASVADDwrDLALRCLVVGGDVLPVALAQRWFELGLDrrCALINAYGPTEATISSHYHRVQAIDA-SRPVPLGQLLPG 856
Cdd:PRK12467   761 LLQASRVAL--PRPQRALVCGGEALQVDLLARVRALGPG--ARLINHYGPTETTVGVSTYELSDEERdFGNVPIGQPLAN 836
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  857 RIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrLPSG-ESLRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:PRK12467   837 LGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVP--DPFGaDGGRLYRTGDLARYRADGVIEYLGRMDH 914
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAW-VECAGEDGFGQADLNQTdsdqteserWHRALCERLP 1014
Cdd:PRK12467   915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYlVPAAVADGAEHQATRDE---------LKAQLRQVLP 985
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1015 AYMVPTQFVALPRLPRNASGKIDRRALPAPPVLA-QAERTPPRTAEESALCEVWAEVLQCE-VGIHDSFFRLGGDSIRSL 1092
Cdd:PRK12467   986 DYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAvQATFVAPQTELEKRLAAIWADVLKVErVGLTDNFFELGGHSLLAT 1065
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1093 QVVARLRER-GYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGE---VGLSPIQ--RWFFDSAPAQPDRYHQYVAL 1166
Cdd:PRK12467  1066 QVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRdqpLPLSYAQerQWFLWQLEPGSAAYHIPQAL 1145
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1167 RLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAAD---LDSRVDAAFARMQEATpl 1243
Cdd:PRK12467  1146 RLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDeaqLKVYVEAEARQPFDLE-- 1223
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1244 AGPLVALTHAHCDDGERLLICA-HHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALReaddaQRFDA 1322
Cdd:PRK12467  1224 QGPLLRVGLLRLAADEHVLVLTlHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQR-----QWMDA 1298
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 1323 G-------FWREL--AAQPMQALPQDRPvalADARQSNVG-RIVQTLDAGLTADLLERA 1371
Cdd:PRK12467  1299 GerarqlaYWKAQlgGEQPVLELPTDRP---RPAVQSHRGaRLAFELPPALAEGLRALA 1354
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
75-1374 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: 655.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   75 RAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCI--------- 145
Cdd:COG1020      5 AAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLrtragrpvq 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  146 QGEDSVAAGGGAAVESADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSL 225
Cdd:COG1020     85 VIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLL-----LLLLLLALHHIISDGLSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  226 GLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGA 303
Cdd:COG1020    160 GLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLqgEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  304 KLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDD 383
Cdd:COG1020    240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGD 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  384 PDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELT 463
Cdd:COG1020    320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLT 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  464 LEVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEPALSWPW-PADELAL-----DDKREPAPRTVGnV 537
Cdd:COG1020    400 LTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLlTAAERQQllaewNATAAPYPADAT-L 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  538 VDAIARAADEFPERAALETAQGRLSYRELLtaadaraaalrrrlgaqARS-----------------VALCLPRGLDWYC 600
Cdd:COG1020    479 HELFEAQAARTPDAVAVVFGDQSLTYAELN-----------------ARAnrlahhlralgvgpgdlVGVCLERSLEMVV 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA--IAVDELKLDGAGENGSGENAAPNQLAY 678
Cdd:COG1020    542 ALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVpvLALDALALAAEPATNPPVPVTPDDLAY 621
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFL 757
Cdd:COG1020    622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALA 701
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  758 AFLSERAITVTDLAPAYANELVRASVADdwrDLALRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYH 837
Cdd:COG1020    702 ELLARHRVTVLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLPGAR--LVNLYGPTETTVDSTYY 776
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  838 RVQAIDA-SRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESlRMYRSG 916
Cdd:COG1020    777 EVTPPDAdGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGA-RLYRTG 855
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  917 DRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDgfgqadlnqtd 996
Cdd:COG1020    856 DLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG----------- 924
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  997 sDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVL-AQAERTPPRTAEESALCEVWAEVLQCEV 1075
Cdd:COG1020    925 -AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAaAAAAAAPPAEEEEEEAALALLLLLVVVV 1003
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1076 GIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPI------QRWF 1149
Cdd:COG1020   1004 GDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPplllslLALL 1083
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1150 FDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSR 1229
Cdd:COG1020   1084 LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAA 1163
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1230 VDAAFARMQEATPLAGPLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELfDGLAALARGEAWTPSARGASYADYVE 1309
Cdd:COG1020   1164 AAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL-LLLLLLLLAAAAAALLALALLLALLA 1242
                         1290      1300      1310      1320      1330      1340
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 1310 ALREADDAQRFDAGFWRELAAQPMQALPQDRPVALADARQSNVGRIVQTLDAGLTADLLERAGEA 1374
Cdd:COG1020   1243 LAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLL 1307
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3533-4010 0e+00

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: 580.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVclsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFtAA 3692
Cdd:cd17643     81 ADSGP----------------SLLLTDP-------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALF-AA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAM 3772
Cdd:cd17643    125 TQRW-FGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RR-ELALNVRAVVFGGEALEPSRLQPWRERY--PQAELVNMYGITETTVHVSFHRLSDEDLQSPT-SRIGSALPDLAVHV 3848
Cdd:cd17643    204 RDgRDPLALRYVIFGGEALEAAMLRPWAGRFglDRPQLVNMYGITETTVHVTFRPLDAADLPAAAaSPIGRPLPGLRVYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd17643    284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVAnpfgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd17643    364 RIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443

                   ....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd17643    444 KLDRAAL 450
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1583-2887 1.22e-178

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: 590.68  E-value: 1.22e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1583 ALLAAREDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSV 1662
Cdd:COG1020      4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1663 PHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQgvDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPL 1742
Cdd:COG1020     84 QVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPF--DLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1743 LVGEMLQRYTAGAQGATLRLPPAPG-----FQAYLDWRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQR-EEC 1816
Cdd:COG1020    162 LLAELLRLYLAAYAGAPLPLPPLPIqyadyALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgARV 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1817 ERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPpeLAGVESMVGVFINTLPLRLRIDAG 1896
Cdd:COG1020    242 SFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGD 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1897 QPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADR----LFASLLVVENFPaMAPAQLPfALRVRETRAAN---HYA 1969
Cdd:COG1020    320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLsrnpLFQVMFVLQNAP-ADELELP-GLTLEPLELDSgtaKFD 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1970 LTLRVSER-ECVRLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVAEL--LGGDDAVQ------APQPQRASSAT 2040
Cdd:COG1020    398 LTLTVVETgDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLplLTAAERQQllaewnATAAPYPADAT 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2041 AQSLLWQMPAQ---AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLD 2117
Cdd:COG1020    478 LHELFEAQAARtpdAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2118 PQHPDARQIAVLDDSGARIVIGWGAAPAWVPA-SVRWLDAESvLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVV 2196
Cdd:COG1020    558 PAYPAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALDA-LALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2197 VSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVP 2276
Cdd:COG1020    637 VEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTP 716
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 SHLAGLLAAAGGtAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLA 2356
Cdd:COG1020    717 SLLRALLDAAPE-ALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIA 795
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQ 2435
Cdd:COG1020    796 NTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQ 875
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2436 VKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAE------ALAQRLPEYLCPSRWRAVESM 2509
Cdd:COG1020    876 VKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaallrlALALLLPPYMVPAAVVLLLPL 955
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2510 PRLGNGKIDRQALADLlqqDDADSSAEAIDETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLA 2589
Cdd:COG1020    956 PLTGNGKLDRLALPAP---AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2590 LMPRQLYDHPTLAGLSAQVQASSPAPATIkPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAAL 2669
Cdd:COG1020   1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAA-PLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLAL 1111
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2670 ADVAAAHPMLRARFQRDAAGQWQQtlgDWQADRFAHREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFA 2749
Cdd:COG1020   1112 LLLLALLLALLAALRARRAVRQEG---PRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLL 1188
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2750 AHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSAATLDGWRSYWRAQAADAEAIALPWQDSD 2829
Cdd:COG1020   1189 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLA 1268
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2830 NRYADTVHLHDRFERDWTERLLTQTARAYGNEPQEVLLTALALALRDGGDAATLWVEM 2887
Cdd:COG1020   1269 LALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLL 1326
PRK12467 PRK12467
peptide synthase; Provisional
3082-4081 4.39e-176

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 614.48  E-value: 4.39e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPLAEQ 3161
Cdd:PRK12467  1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQVIHPVGSLTLEEP 1196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3162 --DWSGLEPAQARSRLsELQAQQCeagFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:PRK12467  1197 llLAADKDEAQLKVYV-EAEARQP---FDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQ 1272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAP-PFRDYLHWLRGQDEAAAR----AFWREQLTGLEPA-ALP-EATEPAEG-YASSTRRFDLAAA-----SA 3306
Cdd:PRK12467  1273 GQSLQLPALPiQYADYAVWQRQWMDAGERarqlAYWKAQLGGEQPVlELPtDRPRPAVQsHRGARLAFELPPAlaeglRA 1352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRppELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRN 3386
Cdd:PRK12467  1353 LARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANR--NRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAA 1430
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3387 LDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLPTESREERSGMRIEEL--DHRaHSNYPLMLTAIPDA 3455
Cdd:PRK12467  1431 LEAQAHQDLPFEQL-----VEALQPerslshsplFQVMFNHQRDDHQAQAQLPGLSVESLswESQ-TAQFDLTLDTYESS 1504
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3456 GGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPA--LQRFDALPLLPSQTRSA---AWTSRERYACTGNLV-SRFAEIA 3529
Cdd:PRK12467  1505 EGLQASLTYATDLFEASTIERLAGHWLNLLQGLVAdpERRLGELDLLDEAERRQileGWNATHTGYPLARLVhQLIEDQA 1584
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3530 RRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRG 3609
Cdd:PRK12467  1585 AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3610 FILEDSGVCLSVSQRALAVELPGT----ALCLDdpftraQLDAVEPGELPEVPTEAP-----AYLIYTSGSTGTPKGVVV 3680
Cdd:PRK12467  1665 YMIEDSGIELLLTQSHLQARLPLPdglrSLVLD------QEDDWLEGYSDSNPAVNLapqnlAYVIYTSGSTGRPKGAGN 1738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQT 3760
Cdd:PRK12467  1739 RHGALVNRLCATQE--AYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFV 1816
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3761 PSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQ-SPTSRIGS 3839
Cdd:PRK12467  1817 PSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEgRDSVPIGQ 1896
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 ALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRG 3915
Cdd:PRK12467  1897 PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVadpfGTVGSRLYRTGDLARYRADGVIEYLGRI 1976
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3916 DDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDP--------QSLREALRALLPDYML 3987
Cdd:PRK12467  1977 DHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLPEYMV 2056
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3988 PRLIQLLPALPLTANGKLDRKALPKPETQDRDEGVLESAS--ERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAE 4065
Cdd:PRK12467  2057 PAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSelEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS 2136
                         1050
                   ....*....|....*.
gi 1246793773 4066 AIRAEfAIAVPLKSLF 4081
Cdd:PRK12467  2137 RARQA-GIRFTPKDLF 2151
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3533-4010 7.44e-173

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: 540.19  E-value: 7.44e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVclsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd05930     81 EDSGA----------------KLVLTDP-------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALqSQAM 3772
Cdd:cd05930    126 QE--AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL-LQEL 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAA 3852
Cdd:cd05930    203 ELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDEN 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3853 GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPG 3929
Cdd:cd05930    283 LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPnpfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3930 EIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRK 4008
Cdd:cd05930    363 EIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442

                   ..
gi 1246793773 4009 AL 4010
Cdd:cd05930    443 AL 444
PRK12467 PRK12467
peptide synthase; Provisional
1582-2812 4.73e-164

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 574.80  E-value: 4.73e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1582 FALLAAREDARAIEhAFPLTPLQ-RGVLLESLRGDGAdPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGL 1660
Cdd:PRK12467    35 FANLPIPQVRSAFE-RIPLSYAQeRQWFLWQLDPDSA-AYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1661 SVpHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWST 1740
Cdd:PRK12467   113 GF-RQVIDASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSM 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1741 PLLVGEMLQRYTAGAQGATLRLPPAPgfQAYLD-------WRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQR 1813
Cdd:PRK12467   192 RVLVEELVQLYSAYSQGREPSLPALP--IQYADyaiwqrsWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYR 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1814 -EECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPElaGVESMVGVFINTLPLRLR 1892
Cdd:PRK12467   270 gARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--ETERLIGFFVNTQVLKAE 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1893 IDAGQPALDLLSALRSQSLEVAEN---------EAVGLGEILADSGL-------------DADRLFASL--LVVENFP-A 1947
Cdd:PRK12467   348 VDPQASFLELLQQVKRTALGAQAHqdlpfeqlvEALQPERSLSHSPLfqvmfnhqntatgGRDREGAQLpgLTVEELSwA 427
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1948 MAPAQLPFALRVRETRAANHYALTLRVSERECVRLEALldaarvdraavaamldlaVAGLLRLLQR----PDCRVAELLG 2023
Cdd:PRK12467   428 RHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERL------------------ATHWRNLLEAivaePRRRLGELPL 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2024 GDDAVQAPQPQR----ASSATAQSL--LWQMPAQ----AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCL 2093
Cdd:PRK12467   490 LDAEERARELVRwnapATEYAPDCVhqLIEAQARqhpeRPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAV 569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2094 PRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGW--GAAPAWVPASVRWLDAESVLDVVSAY-EEPP 2170
Cdd:PRK12467   570 ERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQshLLAQLPVPAGLRSLCLDEPADLLCGYsGHNP 649
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2171 RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLP 2250
Cdd:PRK12467   650 EVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLP 729
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2251 AELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTET 2330
Cdd:PRK12467   730 PDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTET 809
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2331 TVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPD-R 2409
Cdd:PRK12467   810 TVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADgG 889
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---------- 2479
Cdd:PRK12467   890 RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaavadgaeh 969
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2480 QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAdllqQDDADSSAEAID--ETPVNEVLRELWQKLLGR 2557
Cdd:PRK12467   970 QATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALP----KPDASAVQATFVapQTELEKRLAAIWADVLKV 1045
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2558 EHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQASSPAPATIKPATEAEQSFGLTPIQ-- 2634
Cdd:PRK12467  1046 ERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQer 1125
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2635 HWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFqRDAAGQWQQTLGDWQADRFAHREADAG--- 2711
Cdd:PRK12467  1126 QWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTF-VQEDGRTRQVIHPVGSLTLEEPLLLAAdkd 1204
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2712 -QREDLLAQWQAGLSFD---GALLRVLALPDPQDGDTRVLfAAHHLLVDAVSWGIIVDDLQHAYAERRAGRS---PALAA 2784
Cdd:PRK12467  1205 eAQLKVYVEAEARQPFDleqGPLLRVGLLRLAADEHVLVL-TLHHIVSDGWSMQVLVDELVALYAAYSQGQSlqlPALPI 1283
                         1290      1300
                   ....*....|....*....|....*....
gi 1246793773 2785 EACGFGAWQaalRQ-LSAATLDGWRSYWR 2812
Cdd:PRK12467  1284 QYADYAVWQ---RQwMDAGERARQLAYWK 1309
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3082-4085 9.66e-154

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 516.13  E-value: 9.66e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPLAE- 3160
Cdd:PRK10252     9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRF-TEDNGEVWQWVDPALTFPLPEi 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSGlEPAQARSRLSELQAqqceagfDLAAP-------PLMRLALLRrSADEHWLVWTR-HHLIVDGWSSALLLDEVWR 3232
Cdd:PRK10252    88 IDLRT-QPDPHAAAQALMQA-------DLQQDlrvdsgkPLVFHQLIQ-LGDNRWYWYQRyHHLLVDGFSFPAITRRIAA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3233 LYAALRESRTPQLPAAPPFRD----YLHWLRGQDEAAARAFWREQLTGL-EPAALpeATEPAEGYASSTR------RFDL 3301
Cdd:PRK10252   159 IYCAWLRGEPTPASPFTPFADvveeYQRYRASEAWQRDAAFWAEQRRQLpPPASL--SPAPLPGRSASADilrlklEFTD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3302 AAASAW-AQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGveRMLGVFINSVPLRVTPAGEATPAPWLQ 3380
Cdd:PRK10252   237 GAFRQLaAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAAL--TATGPVLNVLPLRVHIAAQETLPELAT 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3381 ALQQRNLDLRTHGYLPLAQIQR-----AGAADAVSPFDVLLVFENLPtesreersgmRIEELDHRAH--SNYP---LMLT 3450
Cdd:PRK10252   315 RLAAQLKKMRRHQRYDAEQIVRdsgraAGDEPLFGPVLNIKVFDYQL----------DFPGVQAQTHtlATGPvndLELA 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3451 AIPD-AGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQ---VPALQRFDALPLLPSQTRSAAWTSRERYAC-TGNLVSRF 3525
Cdd:PRK10252   385 LFPDeHGGLSIEILANPQRYDEATLIAHAERLKALIAQfaaDPALLCGDVDILLPGEYAQLAQVNATAVEIpETTLSALV 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3526 AEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPA 3605
Cdd:PRK10252   465 AQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPD 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3606 ARRGFILEDSGVCLSVSQRALAVELPG----TALCLDDPFTRAQldaVEPGELPEvpTEAPAYLIYTSGSTGTPKGVVVT 3681
Cdd:PRK10252   545 DRLKMMLEDARPSLLITTADQLPRFADvpdlTSLCYNAPLAPQG---AAPLQLSQ--PHHTAYIIFTSGSTGRPKGVMVG 619
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3682 HRN-VERLFTAATQTGrfsFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQT 3760
Cdd:PRK10252   620 QTAiVNRLLWMQNHYP---LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFV 696
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3761 PS---AFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSR- 3836
Cdd:PRK10252   697 PSmlaAFVASLTPEGARQSCASLRQVFCSGEALPADLCREW-QQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSs 775
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 --IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:PRK10252   776 vpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAdpfAPGERMYRTGDVARWLDDGAVEY 855
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-------TVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPD 3984
Cdd:PRK10252   856 LGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPP 935
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3985 YMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEG-VLESASERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRL 4063
Cdd:PRK10252   936 HMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGrAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKL 1015
                         1050      1060
                   ....*....|....*....|..
gi 1246793773 4064 AEAIRAEFAIAVPLKSLFEQPR 4085
Cdd:PRK10252  1016 AAQLSRQFARQVTPGQVMVAST 1037
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3524-4010 1.07e-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: 475.54  E-value: 1.07e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:cd12117      2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRALAVELPGTALCLDdpfTRAQLDAVEPGELPEVPT-EAPAYLIYTSGSTGTPKGVVVTH 3682
Cdd:cd12117     82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVV---IDEALDAGPAGNPAVPVSpDDLAYVMYTSGSTGRPKGVAVTH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 RNVERLftaATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPS 3762
Cdd:cd12117    159 RGVVRL---VKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 AFYAL---QSQAMRrelalNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGS 3839
Cdd:cd12117    236 LFNQLadeDPECFA-----GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 ALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd12117    311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVAdpfGPGERLYRTGDLARWLPDGRLEFLGRID 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAAdgAEPDPQSLREALRALLPDYMLPRLIQLLP 3995
Cdd:cd12117    391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGdKRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAAFVVLD 468
                          490
                   ....*....|....*
gi 1246793773 3996 ALPLTANGKLDRKAL 4010
Cdd:cd12117    469 ELPLTANGKVDRRAL 483
PRK05691 PRK05691
peptide synthase; Validated
3082-4082 1.16e-146

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 517.80  E-value: 1.16e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQ-GLPSPRQLPhrQVSLPLAE 3160
Cdd:PRK05691   677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERdGVALQRIDA--QGEFALQR 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRES 3240
Cdd:PRK05691   755 IDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQG 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3241 RTPQLPAAP-PFRDYLHWLR---GQDEAAA-RAFWREQLtGLEPAALPEATE-PAEGY-ASSTRRFDL-------AAASA 3306
Cdd:PRK05691   835 QTAELAPLPlGYADYGAWQRqwlAQGEAARqLAYWKAQL-GDEQPVLELATDhPRSARqAHSAARYSLrvdaslsEALRG 913
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRP-PELAGverMLGVFINSVPLRVTPAGEATPAPWLQALQQR 3385
Cdd:PRK05691   914 LAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPrLETQG---LVGFFINTQVLRAQLDGRLPFTALLAQVRQA 990
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3386 NLDLRTHGYLPLAQIQRA-GAADAVSPFDVLLVFENLPTESREERSGMRIEELD-HRAHSNYPLMLTAIPDAGGlRIEAA 3463
Cdd:PRK05691   991 TLGAQAHQDLPFEQLVEAlPQAREQGLFQVMFNHQQRDLSALRRLPGLLAEELPwHSREAKFDLQLHSEEDRNG-RLTLS 1069
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3464 LDRSK--LDGWLVEQMLDDLDFVLQQV---PALQRFDaLPLL--PSQTRSAAWTSRERYACTGNLVSRFAEIARRYPARI 3536
Cdd:PRK05691  1070 FDYAAelFDAATIERLAEHFLALLEQVcedPQRALGD-VQLLdaAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERI 1148
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3537 AVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG 3616
Cdd:PRK05691  1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 VCLSVSQRALAVELPG----TALCLDdpftraQLdavepgELPEVPTEAP---------AYLIYTSGSTGTPKGVVVTHR 3683
Cdd:PRK05691  1229 VELLLTQSHLLERLPQaegvSAIALD------SL------HLDSWPSQAPglhlhgdnlAYVIYTSGSTGQPKGVGNTHA 1296
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 N-VERL-FTAATqtgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTP 3761
Cdd:PRK05691  1297 AlAERLqWMQAT----YALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVP 1372
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SafyaLQSQAMRRELALN---VRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDED-LQSPtsrI 3837
Cdd:PRK05691  1373 P----LLQLFIDEPLAAActsLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDgERSP---I 1445
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3838 GSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRG 3913
Cdd:PRK05691  1446 GRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPdplgEDGARLYRTGDRARWNADGALEYLG 1525
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3914 RGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQL 3993
Cdd:PRK05691  1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIR 1605
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3994 LPALPLTANGKLDRKALPKPETQDRDEGVLESASERRLAELWRQLLGgeLPGRGAH--FFARGGHSLLVVRLAEAIRAEF 4071
Cdd:PRK05691  1606 LDQMPLGPSGKLDRRALPEPVWQQREHVEPRTELQQQIAAIWREVLG--LPRVGLRddFFALGGHSLLATQIVSRTRQAC 1683
                         1050
                   ....*....|.
gi 1246793773 4072 AIAVPLKSLFE 4082
Cdd:PRK05691  1684 DVELPLRALFE 1694
PRK05691 PRK05691
peptide synthase; Validated
68-1341 1.36e-143

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 507.78  E-value: 1.36e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   68 QTQDADWRAQSIERAPAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQG 147
Cdd:PRK05691   656 QLAGGGAAQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYE 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  148 EDSVA-----AGGGAAVESADLRGRGQDEIDALVEGFR----LRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHI 218
Cdd:PRK05691   736 RDGVAlqridAQGEFALQRIDLSDLPEAEREARAAQIReeeaRQPFDLEKGPLLRVTLVRLDDE-----EHQLLVTLHHI 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  219 ACDGVSLGLLTQDLSRAYRVECGLAAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHLHELPLDHERPA 296
Cdd:PRK05691   811 VADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAqgEAARQLAYWKAQLGDEQPVLELATDHPRSA 890
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  297 VLGQSGAKLRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVL 376
Cdd:PRK05691   891 RQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVL 970
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  377 RTQLHDDPDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSrhaPLFQLMFALRH-DADLALDLHGVQAHALTLPE 455
Cdd:PRK05691   971 RAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQ---GLFQVMFNHQQrDLSALRRLPGLLAEELPWHS 1047
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  456 DVAKHELTLEVLVGAGG-MSAVWEYNTALWNPATVARWAERYFVALAAMLENPhEPALSwpwpadELALDDKRE------ 528
Cdd:PRK05691  1048 REAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDP-QRALG------DVQLLDAAEraqlaq 1120
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  529 ----PAPRTVGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLG 604
Cdd:PRK05691  1121 wgqaPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLA 1200
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  605 AWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFaPSV----AIAVDELKLDGAGENGSGENAAPNQLAYIL 680
Cdd:PRK05691  1201 ILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERL-PQAegvsAIALDSLHLDSWPSQAPGLHLHGDNLAYVI 1279
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  681 YTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAF 759
Cdd:PRK05691  1280 YTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCrLVLAGPGEHRDPQRIAEL 1359
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  760 LSERAITVTDLAPAYANELVRASVADDWRdlALRCLVVGGDVLPVALAQRwfELGLDRRCALINAYGPTEATISSHYHRV 839
Cdd:PRK05691  1360 VQQYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNR--VLQRLPQVQLHNRYGPTETAINVTHWQC 1435
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  840 QAIDASRpVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrLPSGES-LRMYRSGDR 918
Cdd:PRK05691  1436 QAEDGER-SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP--DPLGEDgARLYRTGDR 1512
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  919 VRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWvecagedgfgqadLNQTDSD 998
Cdd:PRK05691  1513 ARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGY-------------YTGEAGQ 1579
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  999 QTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPApPVLAQAERTPPRTAEESALCEVWAEVL-QCEVGI 1077
Cdd:PRK05691  1580 EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE-PVWQQREHVEPRTELQQQIAAIWREVLgLPRVGL 1658
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1078 HDSFFRLGGDSIRSLQVVARLRERGYAVTP-KLMYQYQSAAELAPQLIALQAAPAEAAPLVGE-------VGLSPIQR-- 1147
Cdd:PRK05691  1659 RDDFFALGGHSLLATQIVSRTRQACDVELPlRALFEASELGAFAEQVARIQAAGERNSQGAIArvdrsqpVPLSYSQQrm 1738
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1148 WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGpAPAIQAQDWRG-AADL 1226
Cdd:PRK05691  1739 WFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS-GLRMDWQDFSAlPADA 1817
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1227 DSRVDAAFARMQEATPL---AGPLVALTHAHCDDGERLLICAHHLIVDAvSWRL-----LLGELFDGLAAlARGEAWTPS 1298
Cdd:PRK05691  1818 RQQRLQQLADSEAHQPFdleRGPLLRACLVKAAEREHYFVLTLHHIVTE-GWAMdifarELGALYEAFLD-DRESPLEPL 1895
                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773 1299 ArgASYADYVEALR---EADDAQRfDAGFWRELAA--QPMQALPQDRP 1341
Cdd:PRK05691  1896 P--VQYLDYSVWQRqwlESGERQR-QLDYWKAQLGneHPLLELPADRP 1940
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3547-3946 1.44e-143

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: 454.80  E-value: 1.44e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLI-RQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRA 3625
Cdd:TIGR01733    2 YRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3626 LAVELPGTALC--LDDPFTRAQLDAVEPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFD 3701
Cdd:TIGR01733   82 LASRLAGLVLPviLLDPLELAALDDAPAPPPPDAPSGPddLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR--RYGLD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFL-DLLAEYGVTVLNQTPSAFYALQSQAmrRELALNV 3780
Cdd:TIGR01733  160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAAL--PPALASL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSR-IGSALPDLAVHVLDAAGQPVPLG 3859
Cdd:TIGR01733  238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVpIGRPLANTRLYVLDDDLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVEGDGVAQGYWQRPELTAERFVE-----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPdpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
                          410
                   ....*....|..
gi 1246793773 3935 IASLPQVSDAAV 3946
Cdd:TIGR01733  398 LLRHPGVREAVV 409
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3525-4010 2.27e-138

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: 443.26  E-value: 2.27e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17646      4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRALAVELPGTAlclDDPFTRAQLDAVEPGELPEVPTE--APAYLIYTSGSTGTPKGVVVTH 3682
Cdd:cd17646     84 ADRLAYMLADAGPAVVLTTADLAARLPAGG---DVALLGDEALAAPPATPPLVPPRpdNLAYVIYTSGSTGRPKGVMVTH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 RN-VERLftaATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTP 3761
Cdd:cd17646    161 AGiVNRL---LWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALqSQAMRRELALNVRAVVFGGEALEPSRLQPWRERyPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSrIGSAL 3841
Cdd:cd17646    238 SMLRVF-LAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAETPSVP-IGRPV 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd17646    315 PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPdpfGPGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGA-WLMAYAVAADGAE-PDPQSLREALRALLPDYMLPRLIQLLPA 3996
Cdd:cd17646    395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDA 474
                          490
                   ....*....|....
gi 1246793773 3997 LPLTANGKLDRKAL 4010
Cdd:cd17646    475 LPLTANGKLDRAAL 488
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
2050-2522 9.91e-138

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: 439.27  E-value: 9.91e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05930     81 EDSGAKLVL-----------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGT 2289
Cdd:cd05930    126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 AVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd05930    206 ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRP 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd05930    286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGANGVLQLGACIQG------SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05930    366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPdeggelDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
3080-3488 9.93e-137

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: 435.48  E-value: 9.93e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19543      1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19543     81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLE-PAALPEAT--EPAEGYASSTRRFDLAAA-----SAWAQSH 3311
Cdd:cd19543    161 GQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEePTPLPKELpaDADGSYEPGEVSFELSAEltarlQELARQH 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 GLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRT 3391
Cdd:cd19543    241 GVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELRE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3392 HGYLPLAQIQRAgAADAVSPFDVLLVFENLPT----ESREERSGMRIEELDHRAHSNYPLMLTAIPDaGGLRIEAALDRS 3467
Cdd:cd19543    321 HEYVPLYEIQAW-SEGKQALFDHLLVFENYPVdeslEEEQDEDGLRITDVSAEEQTNYPLTVVAIPG-EELTIKLSYDAE 398
                          410       420
                   ....*....|....*....|.
gi 1246793773 3468 KLDGWLVEQMLDDLDFVLQQV 3488
Cdd:cd19543    399 VFDEATIERLLGHLRRVLEQV 419
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3533-4010 1.15e-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: 431.72  E-value: 1.15e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGelPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPR--TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPsAFYALQSQAM 3772
Cdd:cd12116    159 RE--RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATP-ATWRMLLDAG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 RRELAlNVRAVVfGGEALEPSRLQPWRERypQAELVNMYGITETTVHVSFHRLSDEDLQSPtsrIGSALPDLAVHVLDAA 3852
Cdd:cd12116    236 WQGRA-GLTALC-GGEALPPDLAARLLSR--VGSLWNLYGPTETTIWSTAARVTAAAGPIP---IGRPLANTQVYVLDAA 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3853 GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:cd12116    309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPdpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRK 4008
Cdd:cd12116    389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468

                   ..
gi 1246793773 4009 AL 4010
Cdd:cd12116    469 AL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3533-4011 3.41e-134

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: 428.98  E-value: 3.41e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQralavelpgtalclddpftraqldavepgelpevpTEAPAYLIYTSGSTGTPKGVVVTHRNVERLftAA 3692
Cdd:cd17652     81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL--AA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAM 3772
Cdd:cd17652    124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 rrelaLNVRAVVFGGEALEPSRLQPWReryPQAELVNMYGITETTVHVSFHRLsDEDLQSPTsrIGSALPDLAVHVLDAA 3852
Cdd:cd17652    204 -----PDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCATMAGP-LPGGGVPP--IGRPVPGTRVYVLDAR 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3853 GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:cd17652    273 LRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVAdpfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIEL 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17652    353 GEVEAALTEHPGVAEAVVVVRDDRPGdKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432

                   ....
gi 1246793773 4008 KALP 4011
Cdd:cd17652    433 RALP 436
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3525-4011 7.11e-134

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: 430.23  E-value: 7.11e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRALAVELPGTA---LCLDDPFTRAQLDAVepgelPEVPTEA--PAYLIYTSGSTGTPKGVV 3679
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELvavTLLDQPGAAAGADAE-----PDPALDAddLAYVIYTSGSTGRPKGVV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3680 VTHRNVERLftAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQ 3759
Cdd:cd17651    156 MPHRSLANL--VAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3760 TPSAFYALQSQAMRRELAL-NVRAVVFGGEALEP-SRLQPWRERYPQAELVNMYGITETTVhVSFHRLSDEDLQSP-TSR 3836
Cdd:cd17651    234 PTVALRALAEHGRPLGVRLaALRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPaPPP 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRG 3913
Cdd:cd17651    313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPdpfVPGARMYRTGDLARWLPDGELEFLG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3914 RGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQ 3992
Cdd:cd17651    393 RADDQVKIRGFRIELGEIEAALARHPGVREAVVLArEDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFV 472
                          490
                   ....*....|....*....
gi 1246793773 3993 LLPALPLTANGKLDRKALP 4011
Cdd:cd17651    473 LLDALPLTPNGKLDRRALP 491
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
549-1041 8.79e-128

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: 410.77  E-value: 8.79e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05930     81 EDSGAKLVLTD---------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANELVRAsvADDW 787
Cdd:cd05930    128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVrKDPEALADLLAEEGITVLHLTPSLLRLLLQE--LELA 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RDLALRCLVVGGDVLPVALAQRWFELGldRRCALINAYGPTEATISSHYHRVQA-IDASRPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd05930    206 ALPSLRLVLVGGEALPPDLVRRWRELL--PGARLVNLYGPTEATVDATYYRVPPdDEEDGRVPIGRPIPNTRVYVLDENL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIEL 946
Cdd:cd05930    284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGE--RMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  947 EEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVAL 1025
Cdd:cd05930    362 GEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDEEELRA-------------HLAERLPDYMVPSAFVVL 428
                          490
                   ....*....|....*.
gi 1246793773 1026 PRLPRNASGKIDRRAL 1041
Cdd:cd05930    429 DALPLTPNGKVDRKAL 444
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
87-507 6.40e-127

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: 407.51  E-value: 6.40e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGED-----SVAAGGGAAVES 161
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDgepvqVILPPLPLPLPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRG----QDEIDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYR 237
Cdd:cd19531     81 VDLSGLPeaerEAEAQRLAREEARRPFDLARGPLLRATLLRL-----GEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 VECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:cd19531    156 AFLAGRPSPLPPLPIQYADYAVWQREWLqgEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  316 RVAAYAQASRAT-------AFHVLQAafaallaRCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFAS 388
Cdd:cd19531    236 ALRALARREGATlfmtllaAFQVLLH-------RYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  389 LVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEVLV 468
Cdd:cd19531    309 LLARVRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTE 388
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1246793773  469 GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19531    389 TDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3525-4010 1.29e-126

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: 407.47  E-value: 1.29e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd12115      5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRAlavelpgtalclddpftraqldavepgelpevpteAPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd12115     85 PERLRFILEDAQARLVLTDPD-----------------------------------DLAYVIYTSGSTGRPKGVAIEHRN 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 -VERLFTAATQtgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcrqpdAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd12115    130 aAAFLQWAAAA---FSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVL-----ALPDLPAAAEVTLINTVPSA 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQamrRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTsrIGSALPD 3843
Cdd:cd12115    202 AAELLRH---DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVS--IGRPLAN 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV---ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:cd12115    277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLpdpFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVK 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGA-WLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPL 3999
Cdd:cd12115    357 VRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPL 436
                          490
                   ....*....|.
gi 1246793773 4000 TANGKLDRKAL 4010
Cdd:cd12115    437 TPNGKIDRSAL 447
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3524-4014 3.17e-124

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: 402.48  E-value: 3.17e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:cd17655      2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEApAYLIYTSGSTGTPKGVVVTHR 3683
Cdd:cd17655     82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDL-AYVIYTSGSTGKPKGVMIEHR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 NVERLFTAATQtgRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd17655    161 GVVNLVEWANK--VIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALqsQAMRRELALNVRAVVFGGEALEPSRLQPWRERY-PQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALP 3842
Cdd:cd17655    239 LKLL--DAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd17655    317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDdpfVPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADgaEPDPQSLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:cd17655    397 KIRGYRIELGEIEARLLQHPDIKEAVVIArKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
                          490
                   ....*....|....*.
gi 1246793773 3999 LTANGKLDRKALPKPE 4014
Cdd:cd17655    475 LTPNGKVDRKALPEPD 490
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3533-4011 3.18e-119

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: 386.34  E-value: 3.18e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRAlavelpgtalclddpftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd17649     81 EDSGAGLLLTHHP----------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TqtGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFY--ALQSQ 3770
Cdd:cd17649    127 A--ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQqlAEEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3771 AMRRELALNVRAVVFGGEALEPSRLQPWReryPQAE-LVNMYGITETTVHVS-FHRLSDEDLQSPTSRIGSALPDLAVHV 3848
Cdd:cd17649    205 RTGDGRPPSLRLYIFGGEALSPELLRRWL---KAPVrLFNAYGPTEATVTPLvWKCEAGAARAGASMPIGRPLGGRSAYI 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER----GGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfgaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEP--DPQSLREALRALLPDYMLPRLIQLLPALPLTAN 4002
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441

                   ....*....
gi 1246793773 4003 GKLDRKALP 4011
Cdd:cd17649    442 GKLDRKALP 450
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3533-4010 1.99e-118

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: 385.09  E-value: 1.99e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELPGTalclDDPFTRAQLDAVEPGELPEVPTE--APAYLIYTSGSTGTPKGVVVTHRNVerLFT 3690
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAV----FDVLILDLDALAAPAPPPPVDVApdDLAYVIFTSGSTGTPKGVMISHRAA--LNT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAF-----Y 3765
Cdd:cd12114    155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLemlldV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3766 ALQSQAMRRELalnvRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLA 3845
Cdd:cd12114    235 LEAAQALLPSL----RLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3846 VHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERG-GQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd12114    311 YRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPdGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVA-ADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd12114    391 RIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANG 470

                   ....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd12114    471 KVDRAAL 477
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
2051-2522 2.77e-116

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: 379.24  E-value: 2.77e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd12117     12 DAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAyeEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVl 2210
Cdd:cd12117     92 DAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPA--GNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIvpshlagllaaaggTA 2290
Cdd:cd12117    169 NYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL--------------TA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPRE-------------CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAG 2357
Cdd:cd12117    235 ALFNQladedpecfaglrELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIAN 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2358 NEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVK 2437
Cdd:cd12117    315 TRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVK 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2438 IRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI----QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:cd12117    395 IRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVvaegALDAAELRAFLRERLPAYMVPAAFVVLDELPLTA 474

                   ....*....
gi 1246793773 2514 NGKIDRQAL 2522
Cdd:cd12117    475 NGKVDRRAL 483
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3529-4010 5.19e-116

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: 376.97  E-value: 5.19e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARr 3608
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 gfiledsgvclsvsqralavelpgtalclddpfTRAQLDAVEPGELPEVPTEaPAYLIYTSGSTGTPKGVVVTHRNVErL 3688
Cdd:cd05945     80 ---------------------------------IREILDAAKPALLIADGDD-NAYIIFTSGSTGRPKGVQISHDNLV-S 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATqTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPS-AFYAL 3767
Cdd:cd05945    125 FTNWM-LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSfAAMCL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3768 QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDL-QSPTSRIGSALPDLAV 3846
Cdd:cd05945    204 LSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLdGYDRLPIGYAKPGAKL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3847 HVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:cd05945    284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGA-WLMAYAVAADGAE-PDPQSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:cd05945    364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVtELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443

                   ....*.
gi 1246793773 4005 LDRKAL 4010
Cdd:cd05945    444 IDRKAL 449
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3525-4011 8.09e-115

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: 374.46  E-value: 8.09e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17644      6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQralavelpgtalclddpftraqldavePGELpevpteapAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd17644     86 QERLTYILEDAQISVLLTQ---------------------------PENL--------AYVIYTSGSTGKPKGVMIEHQS 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VERLFTAATQTgrFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAF 3764
Cdd:cd17644    131 LVNLSHGLIKE--YGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYW 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3765 YALQSQAMRRELAL--NVRAVVFGGEALEPSRLQPWRE-RYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTS-RIGSA 3840
Cdd:cd17644    209 HLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKnVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSvPIGRP 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV-----ERGGQRFYRSGDLGRYRADGSLEYRGRG 3915
Cdd:cd17644    289 IANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIshpfnSSESERLYKTGDLARYLPDGNIEYLGRI 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3916 DDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLL 3994
Cdd:cd17644    369 DNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVrEDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVL 448
                          490
                   ....*....|....*..
gi 1246793773 3995 PALPLTANGKLDRKALP 4011
Cdd:cd17644    449 EELPLTPNGKIDRRALP 465
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3525-4010 3.22e-114

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: 373.42  E-value: 3.22e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd05918      5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSqralavelpgtalclDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd05918     85 LQRLQEILQDTGAKVVLT---------------SSP-------------------SDAAYVIFTSGSTGKPKGVVIEHRA 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VerlFTAATQTGR-FSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRqpDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd05918    131 L---STSALAHGRaLGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRL--NDLAGFINRLRVTWAFLTPSV 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 fyalqSQAMRRELALNVRAVVFGGEALEPSRLQPWRERypqAELVNMYGITETTVHVSFHRLSDEdlqSPTSRIGSALPd 3843
Cdd:cd05918    206 -----ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADR---VRLINAYGPAECTIAATVSPVVPS---TDPRNIGRPLG- 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAA--GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----------RGGQRFYRSGDLGRYRADGSLEY 3911
Cdd:cd05918    274 ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqegsGRGRRLYRTGDLVRYNPDGSLEY 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3912 RGRGDDQVKLRGYRIEPGEIAAKI-ASLPQVSDAAVTV---EGQGEGAWLMAyAVAADGAEPD----------------- 3970
Cdd:cd05918    354 VGRKDTQVKIRGQRVELGEIEHHLrQSLPGAKEVVVEVvkpKDGSSSPQLVA-FVVLDGSSSGsgdgdslflepsdefra 432
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 3971 -PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05918    433 lVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3521-4021 3.33e-114

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: 372.22  E-value: 3.33e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVclsvsqRALAVelpgtalclddpftraqldavepgelpevpteapAYLIYTSGSTGTPKGVVV 3680
Cdd:COG0318     81 PRLTAEELAYILEDSGA------RALVT----------------------------------ALILYTSGTTGRPKGVML 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFdfaVWELWGAWLYGGRAVLVPEavcRQPDAFLDLLAEYGVTV 3756
Cdd:COG0318    121 THRNL--LANAAAIAAALGLTPGDVVlvalPLFHVFGL---TVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTV 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3757 LNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFhRLSDEDLQSPTS 3835
Cdd:COG0318    193 LFGVPTMLARLLRHPEFARYDLsSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTV-NPEDPGERRPGS 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 rIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRG 3915
Cdd:COG0318    271 -VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--RDG--WLRTGDLGRLDEDGYLYIVGRK 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3916 DDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLL 3994
Cdd:COG0318    346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFV 425
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 3995 PALPLTANGKLDRKALPKPETQDRDEG 4021
Cdd:COG0318    426 DELPRTASGKIDRRALRERYAAGALEA 452
PRK05691 PRK05691
peptide synthase; Validated
1628-2793 4.52e-112

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 403.78  E-value: 4.52e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1628 LDGEIDAAALAQAWQQTVRRQPMLRTAIvWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFA 1707
Cdd:PRK05691   706 LRGELDEAALRASFQRLVERHESLRTRF-YERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLE 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1708 HAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAP-GFQAYLDWrERQDLA----- 1781
Cdd:PRK05691   785 KGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPlGYADYGAW-QRQWLAqgeaa 863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1782 RQRGWWRERLSGYAGTAALPAPVAAAHHpvQREECER---RLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHD 1858
Cdd:PRK05691   864 RQLAYWKAQLGDEQPVLELATDHPRSAR--QAHSAARyslRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQG 941
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1859 DVVLGATRSGRP-PELAGvesMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADSGLDADR-LF 1936
Cdd:PRK05691   942 DIRIGVPNANRPrLETQG---LVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQgLF 1018
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1937 A--------SLLVVENFPAMAPAQLPFalRVRETRaanhYALTLRVSERECVRLEalLDAARVDRAAVAAMLDLAVAGLL 2008
Cdd:PRK05691  1019 QvmfnhqqrDLSALRRLPGLLAEELPW--HSREAK----FDLQLHSEEDRNGRLT--LSFDYAAELFDAATIERLAEHFL 1090
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2009 RLLQ----RPDCRVAE--LLGGDDAVQAPQPQRASSATAQSLLWQM-------PAQAVAVEEGAASWTYAQLRAAAGRIA 2075
Cdd:PRK05691  1091 ALLEqvceDPQRALGDvqLLDAAERAQLAQWGQAPCAPAQAWLPELlneqarqTPERIALVWDGGSLDYAELHAQANRLA 1170
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2076 GALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVPAS--VRW 2153
Cdd:PRK05691  1171 HYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAegVSA 1250
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2154 LDAESvLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGF 2233
Cdd:PRK05691  1251 IALDS-LHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSV 1329
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2234 TALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVR 2313
Cdd:PRK05691  1330 WECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVL 1409
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2314 ALAPTLRIVNHYGPTETTVGIltctvpEEW--PVEQG--VPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGY 2389
Cdd:PRK05691  1410 QRLPQVQLHNRYGPTETAINV------THWqcQAEDGerSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGY 1483
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2390 WQRAEQTAERFVAHPLAPD-RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG 2468
Cdd:PRK05691  1484 LGRPALTAERFVPDPLGEDgARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREG 1563
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2469 ANGVLQLG-----ACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQddadsSAEAID-ETP 2542
Cdd:PRK05691  1564 AAGAQLVGyytgeAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ-----QREHVEpRTE 1638
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2543 VNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARARQAGLALMP-RQLYDHPTLAGLSAQVQASSPAPAT-IKP 2620
Cdd:PRK05691  1639 LQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPlRALFEASELGAFAEQVARIQAAGERnSQG 1718
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2621 ATEA---EQSFGLTPIQH--WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTL 2695
Cdd:PRK05691  1719 AIARvdrSQPVPLSYSQQrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVA 1798
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2696 GD------WQadRFAHREADA-GQREDLLAQWQAGLSFD---GALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVD 2765
Cdd:PRK05691  1799 EDsglrmdWQ--DFSALPADArQQRLQQLADSEAHQPFDlerGPLLRA-CLVKAAEREHYFVLTLHHIVTEGWAMDIFAR 1875
                         1210      1220      1230
                   ....*....|....*....|....*....|.
gi 1246793773 2766 DLQHAYAERRAGR-SP--ALAAEACGFGAWQ 2793
Cdd:PRK05691  1876 ELGALYEAFLDDReSPlePLPVQYLDYSVWQ 1906
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
87-507 1.24e-109

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: 358.27  E-value: 1.24e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLdRCIQGED------SVAAGGGAAVE 160
Cdd:cd19540      1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESL-RTVFPEDdggpyqVVLPAAEARPD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  161 sADLRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVEC 240
Cdd:cd19540     80 -LTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRL-----GPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  241 GlAAEPA-PPLPCQYGDYARWQRDTLD-------RLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPG 312
Cdd:cd19540    154 A-GRAPDwAPLPVQYADYALWQRELLGdeddpdsLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  313 LSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:cd19540    233 LHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLAR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  393 CRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEV------ 466
Cdd:cd19540    313 VRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLterrda 392
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1246793773  467 LVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19540    393 DGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
2063-2463 2.45e-109

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: 356.19  E-value: 2.45e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVI--- 2138
Cdd:TIGR01733    1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLtds 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 GWGAAPAWVPASVR-WLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE 2217
Cdd:TIGR01733   81 ALASRLAGLVLPVIlLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2218 DASLATLSTVAADLGFTALFGALLSGRRVRLLP-AELAFDAQALAAHLQAHPVDCLKIVPSHLAG-LLAAAGGTAVLPRe 2295
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPeDEERDDAALLAALIAEHPVTVLNLTPSLLALlAAALPPALASLRL- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 cLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVG--ILTCTVPEEwPVEQGVPVGHPLAGNEAWVLDRFGLPAPVG 2373
Cdd:TIGR01733  240 -VILGGEALTPALVDRWRARGPGARLINLYGPTETTVWstATLVDPDDA-PRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2374 VAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPD--RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQV 2451
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdgARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
                          410
                   ....*....|..
gi 1246793773 2452 LAQLPGVEVAAV 2463
Cdd:TIGR01733  398 LLRHPGVREAVV 409
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
82-1120 3.55e-107

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 377.08  E-value: 3.55e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   82 APAGTPAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDSV-----AAGG 155
Cdd:PRK10252     2 EPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRmRFTEDNGEVwqwvdPALT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  156 GAAVESADLRgrgqDEID------ALVEGFRLRPFELQRQRPL-RMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLL 228
Cdd:PRK10252    82 FPLPEIIDLR----TQPDphaaaqALMQADLQQDLRVDSGKPLvFHQLIQL-----GDNRWYWYQRYHHLLVDGFSFPAI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  229 TQDLSRAYRVECGLAAEPAPPLPCQYG---DYARWQRDTLDRLDASLRHhvEALSGAPHLHELPldhERPAVLGQSGAK- 304
Cdd:PRK10252   153 TRRIAAIYCAWLRGEPTPASPFTPFADvveEYQRYRASEAWQRDAAFWA--EQRRQLPPPASLS---PAPLPGRSASADi 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  305 LRLAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDP 384
Cdd:PRK10252   228 LRLKLEFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQE 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  385 DFASLVARCRDHQLAALEHQALPLERVIETLQVERSSR--HAPLFQL-MFalrhdaDLALDLHGVQAHALTL---PEDva 458
Cdd:PRK10252   308 TLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEplFGPVLNIkVF------DYQLDFPGVQAQTHTLatgPVN-- 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  459 khELTLEVLV-GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPH----EPALSWPWPADELA-LDDKREPAPR 532
Cdd:PRK10252   380 --DLELALFPdEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPAllcgDVDILLPGEYAQLAqVNATAVEIPE 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  533 TvgNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSV 612
Cdd:PRK10252   458 T--TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  613 IPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFA--PSVAIA-VDELKLDGAGEngSGENAAPNQLAYILYTSGSTGIP 689
Cdd:PRK10252   536 LPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFAdvPDLTSLcYNAPLAPQGAA--PLQLSQPHHTAYIIFTSGSTGRP 613
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  690 KGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVT 768
Cdd:PRK10252   614 KGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKlVMAEPEAHRDPLAMQQFFAEYGVTTT 693
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  769 DLAPAYANELVRASVADDWRD--LALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEATISSHYHRVQAID--- 843
Cdd:PRK10252   694 HFVPSMLAAFVASLTPEGARQscASLRQVFCSGEALPADLCREWQQL---TGAPLHNLYGPTEAAVDVSWYPAFGEElaa 770
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  844 -ASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLL 922
Cdd:PRK10252   771 vRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGE--RMYRTGDVARWL 848
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  923 DDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-------GVVGEGAAQRLVAWVECAGEDGFGQADLnqt 995
Cdd:PRK10252   849 DDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTSAL--- 925
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  996 dsdqteserwHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVLAQAERTPPRTAEESALCEVWAEVLQCEV 1075
Cdd:PRK10252   926 ----------QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDV 995
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*..
gi 1246793773 1076 -GIHDSFFRLGGDSIRSLQVVARL-RERGYAVTPKLMYQYQSAAELA 1120
Cdd:PRK10252   996 vDADADFFALGGHSLLAMKLAAQLsRQFARQVTPGQVMVASTVAKLA 1042
AMP-binding pfam00501
AMP-binding enzyme;
3525-3922 5.81e-107

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 349.69  E-value: 5.81e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRAL----------AVELPGTALCLDDP--------FTRAQLDAVEPGELPEVPTEAPAYL 3665
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealgKLEVVKLVLVLDRDpvlkeeplPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3666 IYTSGSTGTPKGVVVTHRNVERLFTAA--TQTGRFSFDEHDVWSLFHSHAFDFAV-WELWGAWLYGGRAVLVPEAVCRQP 3742
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYAL-QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVS 3821
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLlEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 FHRLSDEDLQSPTSrIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggQRFYRSGDL 3900
Cdd:pfam00501  320 TPLPLDEDLRSLGS-VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE---DGWYRTGDL 395
                          410       420
                   ....*....|....*....|..
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLR 3922
Cdd:pfam00501  396 GRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3533-4010 2.72e-106

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: 349.07  E-value: 2.72e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQralavelpgtalclddpftraqldavepgelpevPTEaPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA 3692
Cdd:cd17650     81 EDSGAKLLLTQ----------------------------------PED-LAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQtgRFSFDEHDVWSL-FHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:cd17650    126 RR--EYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALN-VRAVVFGGEALEPSRLQPWRERYPQA-ELVNMYGITETTVHVSFHRLSDEDL-QSPTSRIGSALPDLAVHV 3848
Cdd:cd17650    204 YRNGLDLSaMRLLIVGSDGCKAQDFKTLAARFGQGmRIINSYGVTEATIDSTYYEEGRDPLgDSANVPIGRPLPNTAMYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER---GGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYR 3925
Cdd:cd17650    284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENpfaPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3926 IEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVAAdgAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:cd17650    364 IELGEIESQLARHPAIDEAVVAVrEDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441

                   ....*.
gi 1246793773 4005 LDRKAL 4010
Cdd:cd17650    442 VDRRAL 447
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1599-1978 6.97e-106

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: 346.88  E-value: 6.97e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWREL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 DWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGA 1758
Cdd:cd19543     83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1759 TLRLPPAPGFQAYLDWRERQDLARQRGWWRERLSGY-AGTAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRERGC 1837
Cdd:cd19543    163 PPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFeEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1838 TLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENE 1917
Cdd:cd19543    243 TLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHE 322
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 1918 AVGLGEILADSGLDaDRLFASLLVVENFP---AMAPAQLPFALRVRETRAA--NHYALTLRVSERE 1978
Cdd:cd19543    323 YVPLYEIQAWSEGK-QALFDHLLVFENYPvdeSLEEEQDEDGLRITDVSAEeqTNYPLTVVAIPGE 387
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3525-4010 5.01e-105

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: 345.06  E-value: 5.01e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17653      3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLsvsqralavelpgtALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd17653     83 SARIQAILRTSGATL--------------LLTTDSP-------------------DDLAYIIFTSGSTGIPKGVMVPHRG 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VerlfTAATQTGRFSFD--EHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLvpeavcRQPDA-FLDLLAEygVTVLNQTP 3761
Cdd:cd17653    130 V----LNYVSQPPARLDvgPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDpFAHVART--VDALMSTP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALQSQAMRrelalNVRAVVFGGEALEPSRLQPWRERypqAELVNMYGITETTVHVSFHRLSDEDlqsPTSrIGSAL 3841
Cdd:cd17653    198 SILSTLSPQDFP-----NLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTMTELLPGQ---PVT-IGKPI 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd17653    266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPdpfWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASL-PQVSDAAVTVEGQGegawLMAYAVAADgaePDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:cd17653    346 VKVRGFRINLEEIEEVVLQSqPEVTQAAAIVVNGR----LVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALDSF 418
                          490
                   ....*....|...
gi 1246793773 3998 PLTANGKLDRKAL 4010
Cdd:cd17653    419 PLTANGKVDRKAL 431
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
542-1041 4.37e-104

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: 344.18  E-value: 4.37e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  542 ARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQ 621
Cdd:cd12117      4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  622 ARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAA 701
Cdd:cd12117     84 ERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  702 HIDAAAEALALSaDDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVR 780
Cdd:cd12117    164 LVKNTNYVTLGP-DDRVLQTSPLAFDASTFEIWGALLNGArLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLAD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  781 ASVADdwrdLA-LRCLVVGGDVLPVALAQRWFelgldRRCA---LINAYGPTEATISSHYHRVQAIDAS-RPVPLGQLLP 855
Cdd:cd12117    243 EDPEC----FAgLRELLTGGEVVSPPHVRRVL-----AACPglrLVNGYGPTENTTFTTSHVVTELDEVaGSIPIGRPIA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:cd12117    314 NTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGE--RLYRTGDLARWLPDGRLEFLGRIDD 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV-GEGAAQRLVAWVecAGEDGFGQADLnqtdsdqteserwhRALC-ERL 1013
Cdd:cd12117    392 QVKIRGFRIELGEIEAALRAHPGVREAVVVVReDAGGDKRLVAYV--VAEGALDAAEL--------------RAFLrERL 455
                          490       500
                   ....*....|....*....|....*...
gi 1246793773 1014 PAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd12117    456 PAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
2052-2522 1.63e-103

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: 341.96  E-value: 1.63e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd12116      3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILED 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAyeEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd12116     83 AEPALVLTDDALPDRLPAGLPVLLLALAAAAAAP--AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPShlagLLAAAGGTAV 2291
Cdd:cd12116    161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPA----TWRMLLDAGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2292 LPRECL--VTGGEALTGALVQQVraLAPTLRIVNHYGPTETTVGILTCTVPEEWPveqGVPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd12116    237 QGRAGLtaLCGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAG---PIPIGRPLANTQVYVLDAALRP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDR-LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEV 2448
Cdd:cd12116    312 VPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGsRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEI 391
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2449 EQVLAQLPGVEVAAVLALPGAN-----GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd12116    392 EAALAAHPGVAQAAVVVREDGGdrrlvAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
549-1041 1.81e-103

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: 341.96  E-value: 1.81e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDAQGLAGF-APSVAIAVDELKLDGAGENgSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAA 707
Cdd:cd12116     81 EDAEPALVLTDDALPDRLpAGLPVLLLALAAAAAAPAA-PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  708 EALALSADDRVLHVAGLAVD-TTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAyaneLVRASVADD 786
Cdd:cd12116    160 ERLGLGPGDRLLAVTTYAFDiSLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPA----TWRMLLDAG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  787 WRDLALRCLVVGGDVLPVALAQRWfelgLDRRCALINAYGPTEATISSHYHRVQaiDASRPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd12116    236 WQGRAGLTALCGGEALPPDLAARL----LSRVGSLWNLYGPTETTIWSTAARVT--AAAGPIPIGRPLANTQVYVLDAAL 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrLPSGES-LRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:cd12116    310 RPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVP--DPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  946 LEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGFGQAdlnqtdsdqteseRWHRALCERLPAYMVPTQFVAL 1025
Cdd:cd12116    388 LGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAA-------------ALRAHLRATLPAYMVPSAFVRL 454
                          490
                   ....*....|....*.
gi 1246793773 1026 PRLPRNASGKIDRRAL 1041
Cdd:cd12116    455 DALPLTANGKLDRKAL 470
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
538-1041 2.03e-102

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: 339.64  E-value: 2.03e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  538 VDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDT 617
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  618 EWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIA-VDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVAlLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  697 AALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVTDLAPAYA 775
Cdd:cd17646    161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHFVPSML 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  776 NELVRASVADDWRdlALRCLVVGGDVLPVALAQRWFELGldrRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLLP 855
Cdd:cd17646    241 RVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALP---GAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVP 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  856 GRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlPSGESLRMYRSGDRVRLLDDGELQFLGRADF 935
Cdd:cd17646    316 NTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPD--PFGPGSRMYRTGDLARWRPDGALEFLGRSDD 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  936 QVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGA-AQRLVAWVECAGedgfGQADLNQtdsdqtesERWHRALCERLP 1014
Cdd:cd17646    394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAgAARLVGYVVPAA----GAAGPDT--------AALRAHLAERLP 461
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 1015 AYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17646    462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
588-964 9.53e-102

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: 334.62  E-value: 9.53e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQ--GLAGFAPSVAIAVDELKLDGAGEN 665
Cdd:TIGR01733   28 VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAlaSRLAGLVLPVILLDPLELAALDDA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  666 GSGE----NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA 741
Cdd:TIGR01733  108 PAPPppdaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGA 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  742 C-VVARPDELLEPQRFLAFL-SERAITVTDLAPAYANELVRAsvaDDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRc 819
Cdd:TIGR01733  188 TlVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRARGPGAR- 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  820 aLINAYGPTEATISSHYHRVQAIDASR--PVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASER 897
Cdd:TIGR01733  264 -LINLYGPTETTVWSTATLVDPDDAPResPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAE 342
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  898 RFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA 964
Cdd:TIGR01733  343 RFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
2051-2522 2.11e-100

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: 333.86  E-value: 2.11e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17646     13 DAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASvrwLDAESVLDVVSAYEE--PPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd17646     93 DAGPAVVLTTADLAARLPAG---GDVALLGDEALAAPPatPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLW 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGG 2288
Cdd:cd17646    170 MQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAA 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALTGALVQQVRALaPTLRIVNHYGPTETTVGILTCTVPEEWPvEQGVPVGHPLAGNEAWVLDRFGL 2368
Cdd:cd17646    250 GSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAE-TPSVPIGRPVPNTRLYVLDDALR 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2369 PAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEV 2448
Cdd:cd17646    328 PVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEI 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2449 EQVLAQLPGVEVAAVLALPGANGVLQL-------GACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQA 2521
Cdd:cd17646    408 EAALAAHPAVTHAVVVARAAPAGAARLvgyvvpaAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAA 487

                   .
gi 1246793773 2522 L 2522
Cdd:cd17646    488 L 488
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3533-4011 5.77e-100

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: 332.13  E-value: 5.77e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELP--GTALCLDDPFTRAQLDAvepgELP-EVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLF 3689
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSfnKSTILLEDPSISQEDTS----NIDyINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3690 T-AATQTGRFSFDehDVWSlFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNqTPSAFyaLQ 3768
Cdd:cd17656    158 HfEREKTNINFSD--KVLQ-FATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF-LPVAF--LK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3769 SQAMRRE----LALNVRAVVFGGEALEPSrlQPWRE--RYPQAELVNMYGITETTVhVSFHRLSDEDLQSPTSRIGSALP 3842
Cdd:cd17656    232 FIFSEREfinrFPTCVKHIITAGEQLVIT--NEFKEmlHEHNVHLHNHYGPSETHV-VTTYTINPEAEIPELPPIGKPIS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd17656    309 NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPdpfDPNERMYRTGDLARYLPDGNIEFLGRADHQV 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADgAEPDPQsLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:cd17656    389 KIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGeKYLCAYFVMEQ-ELNISQ-LREYLAKQLPEYMIPSFFVPLDQLP 466
                          490
                   ....*....|...
gi 1246793773 3999 LTANGKLDRKALP 4011
Cdd:cd17656    467 LTPNGKVDRKALP 479
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
2051-2522 1.42e-99

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: 331.62  E-value: 1.42e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17651     10 DAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17651     90 DAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVD--CLKIVPSHLAGLLAAAGG 2288
Cdd:cd17651    170 RASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISrvFLPTVALRALAEHGRPLG 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALT-GALVQQVRALAPTLRIVNHYGPTETTVgiLTCTV----PEEWPveQGVPVGHPLAGNEAWVL 2363
Cdd:cd17651    250 VRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHV--VTALSlpgdPAAWP--APPPIGRPIDNTRVYVL 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd17651    326 DAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRI 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQG------SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd17651    406 ELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGdpeapvDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485

                   ....*
gi 1246793773 2518 DRQAL 2522
Cdd:cd17651    486 DRRAL 490
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
549-1042 3.15e-99

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: 328.94  E-value: 3.15e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTdaqglagfapsvaiavdelkldgagengsgenAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17649     81 EDSGAGLLLT--------------------------------HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSER-AITVTDLAPAYANELVRASVADDW 787
Cdd:cd17649    129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRElGVTVLDLPPAYLQQLAEEADRTGD 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RD-LALRCLVVGGDVLPVALAQRWFELGldrrCALINAYGPTEATISSHYHRVQAIDASRP--VPLGQLLPGRIAAVLDA 864
Cdd:cd17649    209 GRpPSLRLYIFGGEALSPELLRRWLKAP----VRLFNAYGPTEATVTPLVWKCEAGAARAGasMPIGRPLGGRSAYILDA 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  865 HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:cd17649    285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVP-DPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  945 ELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVEcAGEDGFGQADLnqtdsdqtesERWHRALCERLPAYMVPTQFVA 1024
Cdd:cd17649    364 ELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVV-LRAAAAQPELR----------AQLRTALRASLPDYMVPAHLVF 432
                          490
                   ....*....|....*...
gi 1246793773 1025 LPRLPRNASGKIDRRALP 1042
Cdd:cd17649    433 LARLPLTPNGKLDRKALP 450
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
2052-2522 7.31e-99

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: 329.29  E-value: 7.31e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17655     13 HTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILED 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGAapawVPASVRWLDAESVLDVVSAYEEPP---RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd17655     93 SGADILLTQSH----LQPPIAFIGLIDLLDEDTIYHEESenlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEW 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGG 2288
Cdd:cd17655    169 ANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDS 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPREcLVTGGEALTGALVQQVRALAPT-LRIVNHYGPTETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFG 2367
Cdd:cd17655    249 EGLSLKH-LIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYG 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2368 LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGE 2447
Cdd:cd17655    328 RPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGE 407
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2448 VEQVLAQLPGVEVAAVLALPGANGVLQLGACIQG----SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17655    408 IEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSekelPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
2050-2522 1.28e-98

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: 326.97  E-value: 1.28e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd12115     13 PDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFIL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV--- 2206
Cdd:cd12115     93 EDAQARLVL-----------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLqwa 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2207 AGVLPVLDLGedASLATLStVAADLGFTALFGALLSGRRVRLLPAELAFdaqalAAHLQAHPVDCLKIVPShlagllaaa 2286
Cdd:cd12115    138 AAAFSAEELA--GVLASTS-ICFDLSVFELFGPLATGGKVVLADNVLAL-----PDLPAAAEVTLINTVPS--------- 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2287 GGTAVLPRECLVTG-------GEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNE 2359
Cdd:cd12115    201 AAAELLRHDALPASvrvvnlaGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPG--ASGEVSIGRPLANTQ 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2360 AWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIR 2439
Cdd:cd12115    279 AYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVR 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2440 GYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:cd12115    359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIvaepgaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438

                   ....*....
gi 1246793773 2514 NGKIDRQAL 2522
Cdd:cd12115    439 NGKIDRSAL 447
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1597-2625 4.36e-98

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 349.34  E-value: 4.36e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1597 AFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVwEGLSVPHQIVLADAAAP-W 1675
Cdd:PRK10252     7 HLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFT-EDNGEVWQWVDPALTFPlP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1676 QTLDWSALDDAAQDAQlqRWLADDAAQGVDFAHA-PLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAG 1754
Cdd:PRK10252    86 EIIDLRTQPDPHAAAQ--ALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1755 AQGATLRLPPAPGFQA----YLDWRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREeCERRLSAHDSERLRA 1830
Cdd:PRK10252   164 LRGEPTPASPFTPFADvveeYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADI-LRLKLEFTDGAFRQL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1831 FCRERGCTLSDLIAMVWGLANARYGNHDDVVLG---ATRSGRPPelAGVESMVgvfINTLPLRLRIDAGQPALDLLSALR 1907
Cdd:PRK10252   243 AAQASGVQRPDLALALVALWLGRLCGRMDYAAGfifMRRLGSAA--LTATGPV---LNVLPLRVHIAAQETLPELATRLA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1908 SQSLEVAENEAVGLGEILADSGL--DADRLFASLLVVENFPAmapaQLPFA-----LRVRETRAANHYALTLRVSERECV 1980
Cdd:PRK10252   318 AQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGPVLNIKVFDY----QLDFPgvqaqTHTLATGPVNDLELALFPDEHGGL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1981 RLEALLDAARVDRAAVAAMLDLAVAGLLRLLQRPDCRVA--ELLGGDDAVQ--------APQPQRASSATAQSLLWQMPa 2050
Cdd:PRK10252   394 SIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGdvDILLPGEYAQlaqvnataVEIPETTLSALVAQQAAKTP- 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:PRK10252   473 DAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGA-APAWVPASVRWLDAESVLDVVSAYEepPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:PRK10252   553 DARPSLLITTADqLPRFADVPDLTSLCYNAPLAPQGAA--PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPS----HLAGLLAA 2285
Cdd:PRK10252   631 QNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSmlaaFVASLTPE 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 AGGTAVLPRECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTVGIltctvpEEWPVE---------QGVPVGHPLA 2356
Cdd:PRK10252   711 GARQSCASLRQVFCSGEALPADLCREWQQLTGA-PLHNLYGPTEAAVDV------SWYPAFgeelaavrgSSVPIGYPVW 783
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQV 2436
Cdd:PRK10252   784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2437 KIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQ------------GSLEGVAEALAQRLPEYLCPSRWR 2504
Cdd:PRK10252   864 KIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGGDARQlvgylvsqsglpLDTSALQAQLRERLPPHMVPVVLL 943
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2505 AVESMPRLGNGKIDRQALAdlLQQDDADSSAEAIdETPVNEVLRELWQKLLGREHIGAHDNFFALGGDSILSLQLVARAR 2584
Cdd:PRK10252   944 QLDQLPLSANGKLDRKALP--LPELKAQVPGRAP-KTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLS 1020
                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|....*..
gi 1246793773 2585 QA-GLALMPRQLYDHPTLAGLSAQVQASSP-----APATIKPATEAE 2625
Cdd:PRK10252  1021 RQfARQVTPGQVMVASTVAKLATLLDAEEDesrrlGFGTILPLREGD 1067
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3533-4011 7.19e-98

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: 325.12  E-value: 7.19e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAG-PGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFI 3611
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGvclsvsqralavelpgtalclddpftrAQLDAVEPGELpevpteapAYLIYTSGSTGTPKGVVVTHRNVERLFTA 3691
Cdd:cd17648     81 LEDTG---------------------------ARVVITNSTDL--------AYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3692 ATqtGRFSFDEHD--VWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAfyaLQS 3769
Cdd:cd17648    126 LS--ERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSV---LQQ 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3770 QAMRRELALnvRAVVFGGEALEPSRLQPWRERYPqAELVNMYGITETTV--HVSFHRLSDEDLQSptsrIGSALPDLAVH 3847
Cdd:cd17648    201 YDLARLPHL--KRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVtnHKRFFPGDQRFDKS----LGRPVRNTKCY 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE----------RG-GQRFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd17648    274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqteqeraRGrNARLYKTGDLVRWLPSGELEYLGRND 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAV------TVEGQGEGAWLMAYAVAADGAEPDpQSLREALRALLPDYMLPRL 3990
Cdd:cd17648    354 FQVKIRGQRIEPGEVEAALASYPGVRECAVvakedaSQAQSRIQKYLVGYYLPEPGHVPE-SDLLSFLRAKLPRYMVPAR 432
                          490       500
                   ....*....|....*....|.
gi 1246793773 3991 IQLLPALPLTANGKLDRKALP 4011
Cdd:cd17648    433 LVRLEGIPVTINGKLDVRALP 453
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
541-1042 2.35e-97

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: 325.07  E-value: 2.35e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  541 IARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWP 620
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  621 QARRAEVVAASGCDAVLT--DAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:cd17651     81 AERLAFMLADAGPVLVLThpALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANE 777
Cdd:cd17651    161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVrTDPPALAAWLDEQRISRVFLPTVALRA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  778 LVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdRRCALINAYGPTEATI-SSHYHRVQAIDASRPVPLGQLLPG 856
Cdd:cd17651    241 LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGL-PGLRLHNHYGPTETHVvTALSLPGDPAAWPAPPPIGRPIDN 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  857 RIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQ 936
Cdd:cd17651    320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPD--PFVPGARMYRTGDLARWLPDGELEFLGRADDQ 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  937 VKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAgedgfgqadlnQTDSDQTESerWHRALCERLPA 1015
Cdd:cd17651    398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYVVGD-----------PEAPVDAAE--LRAALATHLPE 464
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 1016 YMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd17651    465 YMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
2051-2522 2.49e-95

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: 317.71  E-value: 2.49e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17643      2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGwgaapawvpasvrwldaesvldvvsayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17643     82 DSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPS--HLAGLLAAAGG 2288
Cdd:cd17643    127 RWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSafYQLVEAADRDG 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALTGALVQQ--VRALAPTLRIVNHYGPTETTV----GILTctvPEEWPVEQGVPVGHPLAGNEAWV 2362
Cdd:cd17643    207 RDPLALRYVIFGGEALEAAMLRPwaGRFGLDRPQLVNMYGITETTVhvtfRPLD---AADLPAAAASPIGRPLPGLRVYV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2363 LDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHP--LAPDRLlYRSGDLARLDGEGRIVYLGRGDHQVKIRG 2440
Cdd:cd17643    284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPfgGPGSRM-YRTGDLARRLPDGELEYLGRADEQVKIRG 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2441 YRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI--QGSLEGVAEAL----AQRLPEYLCPSRWRAVESMPRLGN 2514
Cdd:cd17643    363 FRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVvaDDGAAADIAELrallKELLPDYMVPARYVPLDALPLTVN 442

                   ....*...
gi 1246793773 2515 GKIDRQAL 2522
Cdd:cd17643    443 GKLDRAAL 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
2051-2522 1.11e-94

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: 315.35  E-value: 1.11e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17652      2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17652     82 DARPALLL-----------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPShlagLLAAAGGTA 2290
Cdd:cd17652    127 AAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA----ALAALPPDD 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPRECLVTGGEALTGALVQQvraLAPTLRIVNHYGPTETTVGiltCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPA 2370
Cdd:cd17652    203 LPDLRTLVVAGEACPAELVDR---WAPGRRMINAYGPTETTVC---ATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2371 PVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd17652    277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGANGVLQLGACIQGS------LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17652    357 AALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApgaaptAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3525-4011 1.28e-94

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: 315.26  E-value: 1.28e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:cd17645      4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQralavelpgtalclddpftraqldavePGELpevpteapAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd17645     84 GERIAYMLADSSAKILLTN---------------------------PDDL--------AYVIYTSGSTGLPKGVMIEHHN 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VERLftAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTV-LNQTPSA 3763
Cdd:cd17645    129 LVNL--CEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFLPTGAA 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 --FYALQSQAMRrelalnvrAVVFGGEALEPSRLQPWRerypqaeLVNMYGITETTVHVSFHRLSDEDLQSPtsrIGSAL 3841
Cdd:cd17645    207 eqFMQLDNQSLR--------VLLTGGDKLKKIERKGYK-------LVNNYGPTENTVVATSFEIDKPYANIP---IGKPI 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFV---ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd17645    269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIvhpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADgaEPDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:cd17645    349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGrKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKAL 426
                          490
                   ....*....|....
gi 1246793773 3998 PLTANGKLDRKALP 4011
Cdd:cd17645    427 PLTANGKVDRKALP 440
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
549-1041 3.45e-94

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: 315.36  E-value: 3.45e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVV-ARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDW 787
Cdd:cd12114    161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVlPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RDLALRCLVVGGDVLPVALAQRWFELGLDrrCALINAYGPTEATISSHYHRVQAIDAS-RPVPLGQLLPGRIAAVLDAHG 866
Cdd:cd12114    241 LLPSLRLVLLSGDWIPLDLPARLRALAPD--ARLISLGGATEASIWSIYHPIDEVPPDwRSIPYGRPLANQRYRVLDPRG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  867 RIVPRGVCGELALGGIGLAEGYRGDAAASERRFapLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIEL 946
Cdd:cd12114    319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARF--VTHPDGE--RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  947 EEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECagedgfgqadlnQTDSDQTESERWHRALCERLPAYMVPTQFVALP 1026
Cdd:cd12114    395 GEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVP------------DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALE 462
                          490
                   ....*....|....*
gi 1246793773 1027 RLPRNASGKIDRRAL 1041
Cdd:cd12114    463 ALPLTANGKVDRAAL 477
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
549-1041 1.37e-92

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: 309.56  E-value: 1.37e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd05945      5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05945     85 DAAKPALLIAD---------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLS 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLE-PQRFLAFLSERAITVTDLAPAYAnELVRASVADDW 787
Cdd:cd05945    132 DFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATAdPKQLFRFLAEHGITVWVSTPSFA-AMCLLSPTFTP 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RDLA-LRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYHRVQA--IDASRPVPLGQLLPGRIAAVLDA 864
Cdd:cd05945    211 ESLPsLRHFLFCGEVLPHKTARALQQRFPDAR--IYNTYGPTEATVAVTYIEVTPevLDGYDRLPIGYAKPGAKLVILDE 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  865 HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:cd05945    289 DGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFP-----DEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  945 ELEEIEHCLGQLPQVRAAAAGVVGEG-AAQRLVAWVEcaGEDGFGQADLNqtdsdqteseRWHRALCERLPAYMVPTQFV 1023
Cdd:cd05945    364 ELEEIEAALRQVPGVKEAVVVPKYKGeKVTELIAFVV--PKPGAEAGLTK----------AIKAELAERLPPYMIPRRFV 431
                          490
                   ....*....|....*...
gi 1246793773 1024 ALPRLPRNASGKIDRRAL 1041
Cdd:cd05945    432 YLDELPLNANGKIDRKAL 449
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
2051-2522 6.97e-92

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: 307.76  E-value: 6.97e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17649      2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGwgaapawvpasvrwldaesvldvvsayEEPprvdvdaDTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17649     82 DSGAGLLLT---------------------------HHP-------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTA 2290
Cdd:cd17649    128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 ---VLPRECLVTGGEALTGALVQqvRALAPTLRIVNHYGPTETTVGILTCTVPEE----WPVeqgVPVGHPLAGNEAWVL 2363
Cdd:cd17649    208 dgrPPSLRLYIFGGEALSPELLR--RWLKAPVRLFNAYGPTEATVTPLVWKCEAGaaraGAS---MPIGRPLGGRSAYIL 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL-APDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYR 2442
Cdd:cd17649    283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFR 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2443 VELGEVEQVLAQLPGVEVAAVLALPGANG-------VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNG 2515
Cdd:cd17649    363 IELGEIEAALLEHPGVREAAVVALDGAGGkqlvayvVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNG 442

                   ....*..
gi 1246793773 2516 KIDRQAL 2522
Cdd:cd17649    443 KLDRKAL 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
2050-2522 1.04e-91

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: 307.25  E-value: 1.04e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05945      5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05945     85 DAAKPALLI-----------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGT 2289
Cdd:cd05945    130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFT 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 -AVLPRecLVT---GGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwPVEQG--VPVGHPLAGNEAWVL 2363
Cdd:cd05945    210 pESLPS--LRHflfCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPE-VLDGYdrLPIGYAKPGAKLVIL 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlapDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd05945    287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS-------LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05945    364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKpgaeaglTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443

                   ....*.
gi 1246793773 2517 IDRQAL 2522
Cdd:cd05945    444 IDRKAL 449
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2628-3043 3.30e-91

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: 304.95  E-value: 3.30e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2628 FGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAaGQWQQTLGDWQADRFAHR- 2706
Cdd:cd19534      2 VPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRRED-GGWQQRIRGDVEELFRLEv 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2707 -----EADAGQREDLLAQWQAGLS-FDGALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSP 2780
Cdd:cd19534     81 vdlssLAQAAAIEALAAEAQSSLDlEEGPLLAA-ALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2781 ALAAEAcGFGAWQAALRQLSA-ATLDGWRSYWRAQAADAEAIaLPwQDSDNRYADTVHLHDRFERDWTERLLTQTARAYG 2859
Cdd:cd19534    160 PLPSKT-SFQTWAELLAEYAQsPALLEELAYWRELPAADYWG-LP-KDPEQTYGDARTVSFTLDEEETEALLQEANAAYR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2860 NEPQEVLLTALALALRDGGDAATLWVEMEGHGRDDLGAGLDLSRTVGWFTARYPLALHLPAGEDLGAALRSTKDRMRAVP 2939
Cdd:cd19534    237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKEQLRRIP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2940 DRGLGFGVLRYLHGE----LAELPVPQVCFNYLGQLRAGERDGWALCEEPDGGGRAGGNRR--RHLLDVNAMLVDGELRL 3013
Cdd:cd19534    317 NKGIGYGILRYLTPEgtkrLAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTprFALLDINAVVEGGQLVI 396
                          410       420       430
                   ....*....|....*....|....*....|
gi 1246793773 3014 DWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:cd19534    397 TVSYSRNMYHEETIQQLADSYKEALEALIE 426
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
549-1042 1.29e-90

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: 303.41  E-value: 1.29e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17652     81 ADARPALLLTT---------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVaddw 787
Cdd:cd17652    128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATlVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDL---- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 rdLALRCLVVGGDVLPVALAQRWfelGLDRRcaLINAYGPTEATISSHYHRVQAidASRPVPLGQLLPGRIAAVLDAHGR 867
Cdd:cd17652    204 --PDLRTLVVAGEACPAELVDRW---APGRR--MINAYGPTETTVCATMAGPLP--GGGVPPIGRPVPGTRVYVLDARLR 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  868 IVPRGVCGELALGGIGLAEGYRGDAAASERRFA--PLRLPSGeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:cd17652    275 PVPPGVPGELYIAGAGLARGYLNRPGLTAERFVadPFGAPGS---RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIE 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  946 LEEIEHCLGQLPQVRAAAAGVVGEGAA-QRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVA 1024
Cdd:cd17652    352 LGEVEAALTEHPGVAEAVVVVRDDRPGdKRLVAYVVPAPGAAPTAAELRA-------------HLAERLPGYMVPAAFVV 418
                          490
                   ....*....|....*...
gi 1246793773 1025 LPRLPRNASGKIDRRALP 1042
Cdd:cd17652    419 LDALPLTPNGKLDRRALP 436
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
549-1041 1.86e-90

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: 303.46  E-value: 1.86e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17643     81 ADSGPSLLLTD---------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAYANELVRASVADDW 787
Cdd:cd17643    128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVaRSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGR 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RDLALRCLVVGGDVLPVALAQRWFELGLDRRCALINAYGPTEATISSHYHRVQAIDASRP--VPLGQLLPGRIAAVLDAH 865
Cdd:cd17643    208 DPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAaaSPIGRPLPGLRVYVLDAD 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  866 GRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:cd17643    288 GRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANP-FGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIE 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  946 LEEIEHCLGQLPQVRAAAAGV-VGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwHRALCERLPAYMVPTQFVA 1024
Cdd:cd17643    367 LGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDGAAADIAEL-------------RALLKELLPDYMVPARYVP 433
                          490
                   ....*....|....*..
gi 1246793773 1025 LPRLPRNASGKIDRRAL 1041
Cdd:cd17643    434 LDALPLTVNGKLDRAAL 450
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
88-507 1.61e-89

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: 299.95  E-value: 1.61e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDSVAAGGGAAVESADLR-- 165
Cdd:cd19538      2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKle 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  166 ------GRGQDEIDALVEgfrlRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVE 239
Cdd:cd19538     82 ikevdeEELESEINEAVR----YPFDLSEEPPFRATLFEL-----GENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRAR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  240 CGLAAEPAPPLPCQYGDYARWQRDTL-------DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPG 312
Cdd:cd19538    153 CKGEAPELAPLPVQYADYALWQQELLgdesdpdSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSE 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  313 LSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:cd19538    233 LHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLER 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  393 CRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLPEDVAKHELTLEV-----L 467
Cdd:cd19538    313 VKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELreqynD 392
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1246793773  468 VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19538    393 GTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
549-1044 1.33e-87

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: 296.93  E-value: 1.33e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17655     11 PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDAQGLAGFAPSVAIAVDElklDGAGENGSGENAAP----NQLAYILYTSGSTGIPKGVEVGHAALAAHID 704
Cdd:cd17655     91 EDSGADILLTQSHLQPPIAFIGLIDLLD---EDTIYHEESENLEPvsksDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVE 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  705 AAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGAC-VVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRAsv 783
Cdd:cd17655    168 WANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAA-- 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  784 aDDWRDLALRCLVVGGDVLPVALAQRWFELGLDRrCALINAYGPTEATISSHYHRVQAIDASRP-VPLGQLLPGRIAAVL 862
Cdd:cd17655    246 -DDSEGLSLKHLIVGGEALSTELAKKIIELFGTN-PTITNAYGPTETTVDASIYQYEPETDQQVsVPIGKPLGNTRIYIL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  863 DAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGY 942
Cdd:cd17655    324 DQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGE--RMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  943 RIELEEIEHCLGQLPQVRAAAAGVV-GEGAAQRLVAWVecAGEDGFGQADLNQTdsdqteserwhraLCERLPAYMVPTQ 1021
Cdd:cd17655    402 RIELGEIEARLLQHPDIKEAVVIARkDEQGQNYLCAYI--VSEKELPVAQLREF-------------LARELPDYMIPSY 466
                          490       500
                   ....*....|....*....|...
gi 1246793773 1022 FVALPRLPRNASGKIDRRALPAP 1044
Cdd:cd17655    467 FIKLDEIPLTPNGKVDRKALPEP 489
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
537-1041 8.14e-87

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: 294.06  E-value: 8.14e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  617 TEWPQARRAEVVAASGCDAVLTDAqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSS--------------------------------PSDAAYVIFTSGSTGKPKGVVIEH 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  697 AALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELLePQRFLAFLSERAITVTDLAPAYAN 776
Cdd:cd05918    129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDR-LNDLAGFINRLRVTWAFLTPSVAR 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  777 ELVRASVADdwrdlaLRCLVVGGDVLPVALAQRWFElgldrRCALINAYGPTEATISSHYHRVqaIDASRPVPLGQLLPG 856
Cdd:cd05918    208 LLDPEDVPS------LRTLVLGGEALTQSDVDTWAD-----RVRLINAYGPAECTIAATVSPV--VPSTDPRNIGRPLGA 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  857 RiAAVLDA--HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF-----APLRLPSGESLRMYRSGDRVRLLDDGELQF 929
Cdd:cd05918    275 T-CWVVDPdnHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpaWLKQEGSGRGRRLYRTGDLVRYNPDGSLEY 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  930 LGRADFQVKLRGYRIELEEIEHCLGQ-LPQVRAAAAGVV---GEGAAQRLVAWVECAGEDGFGQAD----LNQTDSDQTE 1001
Cdd:cd05918    354 VGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVkpkDGSSSPQLVAFVVLDGSSSGSGDGdslfLEPSDEFRAL 433
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1246793773 1002 SERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05918    434 VAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
2051-2522 1.59e-83

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: 284.55  E-value: 1.59e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd12114      2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAyeEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd12114     82 DAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPA--PPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDIN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTA 2290
Cdd:cd12114    160 RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPR--ECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTC---TVPEEWPVeqgVPVGHPLAGNEAWVLDR 2365
Cdd:cd12114    240 ALLPslRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHpidEVPPDWRS---IPYGRPLANQRYRVLDP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2366 FGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlaPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd12114    317 RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2446 GEVEQVLAQLPGVEVAAVLALPGANG------VLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd12114    395 GEIEAALQAHPGVARAVVVVLGDPGGkrlaafVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474

                   ...
gi 1246793773 2520 QAL 2522
Cdd:cd12114    475 AAL 477
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
539-1041 6.96e-83

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: 281.51  E-value: 6.96e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTE 618
Cdd:cd12115      3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  619 WPQARRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:cd12115     83 YPPERLRFILEDAQARLVLTD---------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRN 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVarpdeLLEPQRFLAFLSERA-ITVTDLAPAYANE 777
Cdd:cd12115    130 AAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVV-----LADNVLALPDLPAAAeVTLINTVPSAAAE 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  778 LVRASVADDwrdlALRCLVVGGDVLPVALAQRWFELGLDRRcaLINAYGPTEATISSHYHRVQAiDASRPVPLGQLLPGR 857
Cdd:cd12115    205 LLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVER--VVNLYGPSEDTTYSTVAPVPP-GASGEVSIGRPLANT 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  858 IAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQV 937
Cdd:cd12115    278 QAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGA--RLYRTGDLVRWRPDGLLEFLGRADNQV 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  938 KLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQR-LVAWVECAGEDGFGQADLNQTdsdqteserwhraLCERLPAY 1016
Cdd:cd12115    356 KVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERrLVAYIVAEPGAAGLVEDLRRH-------------LGTRLPAY 422
                          490       500
                   ....*....|....*....|....*
gi 1246793773 1017 MVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd12115    423 MVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
539-1041 6.38e-82

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: 278.04  E-value: 6.38e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTE 618
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  619 WPQARRAEVVAASGCDAVLTdaqglagfapsvaiavdelkldgagengsgeNAAPNQLAYILYTSGSTGIPKGVEVGHAA 698
Cdd:cd17653     81 LPSARIQAILRTSGATLLLT-------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRG 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  699 LAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVarpdeLLEPQRFLAFLSeRAITVTDLAPAYANEL 778
Cdd:cd17653    130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLV-----LADPSDPFAHVA-RTVDALMSTPSILSTL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  779 VRASVADdwrdlaLRCLVVGGDVLPVALAQRWFElgldRRCaLINAYGPTEATISSHYHRVQAIDasrPVPLGQLLPGRI 858
Cdd:cd17653    204 SPQDFPN------LKTIFLGGEAVPPSLLDRWSP----GRR-LYNAYGPTECTISSTMTELLPGQ---PVTIGKPIPNST 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  859 AAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVK 938
Cdd:cd17653    270 CYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGS--RMYRTGDYGRWTEDGGLEFLGREDNQVK 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  939 LRGYRIELEEIEHCLGQL-PQVRAAAAGVVGegaaQRLVAWVECAGEDGfgqadlnqtdsDQTESErwhraLCERLPAYM 1017
Cdd:cd17653    348 VRGFRINLEEIEEVVLQSqPEVTQAAAIVVN----GRLVAFVTPETVDV-----------DGLRSE-----LAKHLPSYA 407
                          490       500
                   ....*....|....*....|....
gi 1246793773 1018 VPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17653    408 VPDRIIALDSFPLTANGKVDRKAL 431
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
88-507 1.24e-80

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: 274.26  E-value: 1.24e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVES 161
Cdd:cd19539      2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGgvprqeILPPGPAPLEV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQD---EIDALVEGFRLRPFELQRQRPLRMQLLRldgqgDGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRV 238
Cdd:cd19539     82 RDLSDPDSDrerRLEELLRERESRGFDLDEEPPIRAVLGR-----FDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  239 ECGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHeLPLDHERPAVLGQSGAKLRLAFPPGLSER 316
Cdd:cd19539    157 RRKGPAAPLPELRQQYKEYAAWQREALaaPRAAELLDFWRRRLRGAEPTA-LPTDRPRPAGFPYPGADLRFELDAELVAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  317 VAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRDH 396
Cdd:cd19539    236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  397 QLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALDLHG-VQAHALTLPEDVAKHELTLEVLVGAGGMSA 475
Cdd:cd19539    316 LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGgLSYTEGSDIPDGAKFDLNLTVTEEGTGLRG 395
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1246793773  476 VWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19539    396 SLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
2052-2524 1.39e-80

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: 274.19  E-value: 1.39e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17653     13 AVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawVPASvrwldaesvldvvsayeepprvdvdADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd17653     93 SGATLLL--------TTDS-------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPA 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASLATLSTVAADLGFTALFGALLSGrrvrllpAELAFDAQALAAHLQAHPVDCLKIVPShlagllaaagGTAV 2291
Cdd:cd17653    140 RLDVGPGSRVAQVLSIAFDACIGEIFSTLCNG-------GTLVLADPSDPFAHVARTVDALMSTPS----------ILST 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2292 LPR------ECLVTGGEALTGALVqqvRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQgVPVGHPLAGNEAWVLDR 2365
Cdd:cd17653    203 LSPqdfpnlKTIFLGGEAVPPSLL---DRWSPGRRLYNAYGPTECTI---SSTMTELLPGQP-VTIGKPIPNSTCYILDA 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2366 FGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd17653    276 DLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINL 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2446 GEVEQVLAQL-PGVEVAAVLAlpgANGVLQLGACIQGS-LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:cd17653    356 EEIEEVVLQSqPEVTQAAAIV---VNGRLVAFVTPETVdVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432

                   .
gi 1246793773 2524 D 2524
Cdd:cd17653    433 E 433
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
537-1043 3.02e-80

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: 273.99  E-value: 3.02e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  617 TEWPQARRAEVVAASGCDAVLTdaqglagfapsvaiavdelkldgagengsgenaapnqlAYILYTSGSTGIPKGVEVGH 696
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  697 AALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGACVVARPDelLEPQRFLAFLSERAITVTDL 770
Cdd:COG0318    123 RNLLANAAAIAAALGLTPGDVVLvalplfHVFGLTV-----GLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFG 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  771 APAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE-LGldrrCALINAYGPTEATISSHYHRVQAIDAsRPVP 849
Cdd:COG0318    196 VPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEErFG----VRIVEGYGLTETSPVVTVNPEDPGER-RPGS 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  850 LGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLDDGELQF 929
Cdd:COG0318    271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD---------GWLRTGDLGRLDEDGYLYI 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  930 LGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwHRA 1008
Cdd:COG0318    342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAeAAVVGVPDEKWGERVVAFVVLRPGAELDAEEL-------------RAF 408
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 1009 LCERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:COG0318    409 LRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3078-3481 3.24e-80

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: 274.21  E-value: 3.24e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3078 QDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQ--LPHRQVS 3155
Cdd:pfam00668    2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQviLEERPFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3156 LPLAE-QDWSGLEPAQARSRLSELQAQQceaGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLY 3234
Cdd:pfam00668   82 LEIIDiSDLSESEEEEAIEAFIQRDLQS---PFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3235 AALRESRTPQLPAAPPFRDYLHWLR----GQDEAAARAFWREQLTGLEP-AALPE-ATEPAEG-YASSTRRFDLAAASA- 3306
Cdd:pfam00668  159 QQLLKGEPLPLPPKTPYKDYAEWLQqylqSEDYQKDAAYWLEQLEGELPvLQLPKdYARPADRsFKGDRLSFTLDEDTEe 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 ----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPpeLAGVERMLGVFINSVPLRVTPAGEATPAPWLQAL 3382
Cdd:pfam00668  239 llrkLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3383 QQRNLDLRTHGYLPLAQIQR----AGAADAVSPFDVLLVFENLP------TESREERSGMRIEELDHRAhSNYPLMLTAI 3452
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNdlrlPRDLSRHPLFDPMFSFQNYLgqdsqeEEFQLSELDLSVSSVIEEE-AKYDLSLTAS 395
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1246793773 3453 PDAGGLRIE-----AALDRSKLDGWL--VEQMLDDL 3481
Cdd:pfam00668  396 ERGGGLTIKidyntSLFDEETIERFAehFKELLEQA 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
2050-2533 5.95e-80

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: 273.22  E-value: 5.95e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:COG0318     13 PDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYIL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGwgaapawvpasvrwldaesvldvvsayeepprvdvdadtpAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:COG0318     93 EDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAI 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTA-LFGALLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGG 2288
Cdd:COG0318    133 AAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPTMLARLLRHPEF 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAV-LPR-ECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTVgiLTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRF 2366
Cdd:COG0318    210 ARYdLSSlRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTETSP--VVTVNPEDPGERRPGSVGRPLPGVEVRIVDED 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:COG0318    287 GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPA 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQ------GSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQ 2520
Cdd:COG0318    360 EVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVlrpgaeLDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRR 439
                          490
                   ....*....|...
gi 1246793773 2521 ALADLLQQDDADS 2533
Cdd:COG0318    440 ALRERYAAGALEA 452
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
2051-2522 7.02e-80

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: 273.54  E-value: 7.02e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:cd17644     15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVL 2210
Cdd:cd17644     95 DAQISVLL-----------------------------------TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLI 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2211 PVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPS--HLAGLLAAAGG 2288
Cdd:cd17644    140 KEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAywHLLVLELLLST 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVL--PRECLVtGGEALTGALVQQ-VRALAPTLRIVNHYGPTETTVGILTC--TVPEEWPVEQgVPVGHPLAGNEAWVL 2363
Cdd:cd17644    220 IDLPssLRLVIV-GGEAVQPELVRQwQKNVGNFIQLINVYGPTEATIAATVCrlTQLTERNITS-VPIGRPIANTQVYIL 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLA--PDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:cd17644    298 DENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGF 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNG 2515
Cdd:cd17644    378 RIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIvphyeeSPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNG 457

                   ....*..
gi 1246793773 2516 KIDRQAL 2522
Cdd:cd17644    458 KIDRRAL 464
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
549-1042 1.10e-79

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: 272.77  E-value: 1.10e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARraevv 628
Cdd:cd17644     14 PDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER----- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 aasgCDAVLTDAQglagfapsVAIAVDElkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd17644     89 ----LTYILEDAQ--------ISVLLTQ----------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIK 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDELL-EPQRFLAFLSERAITVTDLAPAYANELVRASVADDW 787
Cdd:cd17644    141 EYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTI 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 R-DLALRCLVVGGDVLPVALAQRWFELgLDRRCALINAYGPTEATISSHYHRVQAI--DASRPVPLGQLLPGRIAAVLDA 864
Cdd:cd17644    221 DlPSSLRLVIVGGEAVQPELVRQWQKN-VGNFIQLINVYGPTEATIAATVCRLTQLteRNITSVPIGRPIANTQVYILDE 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  865 HGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:cd17644    300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRI 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  945 ELEEIEHCLGQLPQVRAAAAgVVGEGAA--QRLVAWVecagedgfgQADLNQTDSdqteSERWHRALCERLPAYMVPTQF 1022
Cdd:cd17644    380 ELGEIEAVLSQHNDVKTAVV-IVREDQPgnKRLVAYI---------VPHYEESPS----TVELRQFLKAKLPDYMIPSAF 445
                          490       500
                   ....*....|....*....|
gi 1246793773 1023 VALPRLPRNASGKIDRRALP 1042
Cdd:cd17644    446 VVLEELPLTPNGKIDRRALP 465
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
2052-2522 1.79e-79

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: 272.81  E-value: 1.79e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17656      4 AVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaAPAWVPASVRWLDAESVLDVVSAYEEPP---RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd17656     84 SGVRVVL----TQRHLKSKLSFNKSTILLEDPSISQEDTsniDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLkIVPSHLAGLLAAAGG 2288
Cdd:cd17656    160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSERE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECL---VTGGEAL--TGALVQQVRALAPTLRivNHYGPTETTVgILTCTVPEEWPVEQGVPVGHPLAGNEAWVL 2363
Cdd:cd17656    239 FINRFPTCVkhiITAGEQLviTNEFKEMLHEHNVHLH--NHYGPSETHV-VTTYTINPEAEIPELPPIGKPISNTWIYIL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd17656    316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGA--CIQGSL--EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17656    396 ELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyfVMEQELniSQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475

                   ...
gi 1246793773 2520 QAL 2522
Cdd:cd17656    476 KAL 478
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
2052-2528 1.79e-78

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: 269.80  E-value: 1.79e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd05918     15 APAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvldvVSayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd05918     95 TGAKVVL------------------------TS----------SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASLATLSTVAADLGFTALFGALLSG----------RRVRLLPAELAFDaqalaahlqahpVDCLKIVPShlag 2281
Cdd:cd05918    141 ALGLTSESRVLQFASYTFDVSILEIFTTLAAGgclcipseedRLNDLAGFINRLR------------VTWAFLTPS---- 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2282 llaaaggTAVL--PREC-----LVTGGEALTGALVQQvraLAPTLRIVNHYGPTETTVGiltCTVPEEWPVEQGVPVGHP 2354
Cdd:cd05918    205 -------VARLldPEDVpslrtLVLGGEALTQSDVDT---WADRVRLINAYGPAECTIA---ATVSPVVPSTDPRNIGRP 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2355 LAGNeAWVLDRF--GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHP-------LAPDRLLYRSGDLARLDGEGR 2425
Cdd:cd05918    272 LGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGS 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2426 IVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVE---VAAVLALPGANGVLQLGACIQGS-------------------- 2482
Cdd:cd05918    351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAkevVVEVVKPKDGSSSPQLVAFVVLDgsssgsgdgdslflepsdef 430
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773 2483 ---LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:cd05918    431 ralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3520-4010 2.29e-78

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 270.61  E-value: 2.29e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRV---GLCLPrgcDLLVALLAILKTGAAY 3596
Cdd:PRK04813     3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIivfGHMSP---EMLATFLGAVKAGHAY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPVDPHAPAARRGFILEdsgvclsVSQRAL--AVElpgtalclDDPFTRAQLDAVEPGELPEVPTEAPA----------- 3663
Cdd:PRK04813    80 IPVDVSSPAERIEMIIE-------VAKPSLiiATE--------ELPLEILGIPVITLDELKDIFATGNPydfdhavkgdd 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 --YLIYTSGSTGTPKGVVVTHRNVERlFTAaTQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQ 3741
Cdd:PRK04813   145 nyYIIFTSGTTGKPKGVQISHDNLVS-FTN-WMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTAN 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3742 PDAFLDLLAEYGVTVLNQTPS-AFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHV 3820
Cdd:PRK04813   223 FKQLFETLPQLPINVWVSTPSfADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAV 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDL-QSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGD 3899
Cdd:PRK04813   303 TSIEITDEMLdQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGD 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA-AVTVEGQGEGAWLMAYAVAADGA-EPDPQ---SL 3974
Cdd:PRK04813   383 AG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAvVVPYNKDHKVQYLIAYVVPKEEDfEREFEltkAI 461
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1246793773 3975 REALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK04813   462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
3662-4006 4.66e-78

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: 263.38  E-value: 4.66e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEavcRQ 3741
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNL--LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3742 PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERyPQAELVNMYGITETTVHV 3820
Cdd:cd04433     77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLsSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDLQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDL 3900
Cdd:cd04433    156 ATGPPDDDARKPGS--VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--EDG--WYRTGDL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALR 3979
Cdd:cd04433    230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
                          330       340
                   ....*....|....*....|....*..
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:cd04433    310 ERLAPYKVPRRVVFVDALPRTASGKID 336
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
3081-3471 4.38e-76

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: 260.84  E-value: 4.38e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3081 YPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLAE 3160
Cdd:cd19536      2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSGLEpaQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHW-LVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19536     82 LDLTPLE--EQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLRGQ-DEAAARAFWREQLTGLEPAALP--EATEPAEGYASSTRRFDLAAAS---AWAQSHGL 3313
Cdd:cd19536    160 YKPLSLPPAQPYRDFVAHERASiQQAASERYWREYLAGATLATLPalSEAVGGGPEQDSELLVSVPLPVrsrSLAKRSGI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3314 TASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATpAPWLQALQQRNLDLRTHG 3393
Cdd:cd19536    240 PLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETV-EDLLKRAQEQELESLSHE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3394 YLPLAQIQRagAADAVSPFDVLLVFENLP----TESREERSGMRIEELDHRAHSNYPLMLTAIPDAGGLRIEAALDRSKL 3469
Cdd:cd19536    319 QVPLADIQR--CSEGEPLFDSIVNFRHFDldfgLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLELKLAYNSQVL 396

                   ..
gi 1246793773 3470 DG 3471
Cdd:cd19536    397 DE 398
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1139-1559 1.09e-74

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: 257.18  E-value: 1.09e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1139 EVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAP-AIQA 1217
Cdd:cd19534      1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELfRLEV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRgAADLDSRVDAAFARMQEATPLA-GPLVALTHAH-CDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGE-- 1293
Cdd:cd19534     81 VDLS-SLAQAAAIEALAAEAQSSLDLEeGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEpi 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1294 AWTPSargASYADYVEALREA--DDAQRFDAGFWRELAAQPMQALPQDRPVALADARqsnvgRIVQTLDAGLTADLLERA 1371
Cdd:cd19534    160 PLPSK---TSFQTWAELLAEYaqSPALLEELAYWRELPAADYWGLPKDPEQTYGDAR-----TVSFTLDEEETEALLQEA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1372 GEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGR-DVLDGRDWSSVLGWYTAVHPLPLDLGVADGPAQ-IGALKEQ 1449
Cdd:cd19534    232 NAAYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGReEIDPGLDLSRTVGWFTSMYPVVLDLEASEDLGDtLKRVKEQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1450 IRALARRGLDYMPL-----VASARIPALPAGQLLFNYHGVVDAG--AHPAFEVEPRTLASGNGADNPPGALVEINARVQA 1522
Cdd:cd19534    312 LRRIPNKGIGYGILryltpEGTKRLAFHPQPEISFNYLGQFDQGerDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEG 391
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1246793773 1523 GRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHC 1559
Cdd:cd19534    392 GQLVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3529-4007 1.17e-74

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: 257.15  E-value: 1.17e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:cd17631      5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSgvclsvsqralavelpGTALCLDDpftraqldavepgelpevpteaPAYLIYTSGSTGTPKGVVVTHRNVerL 3688
Cdd:cd17631     85 AYILADS----------------GAKVLFDD----------------------LALLMYTSGTTGRPKGAMLTHRNL--L 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATQTGRFSFDEHDVW----SLFHSHAFD-FAVWELWgawlYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd17631    125 WNAVNALAALDLGPDDVLlvvaPLFHIGGLGvFTLPTLL----RGGTVVILRKF---DPETVLDLIERHRVTSFFLVPTM 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPqaELVNMYGITETTVHVSFhrLSDEDLQsptSRIGSA-- 3840
Cdd:cd17631    198 IQALLQHPRFATTDLsSLRAVIYGGAPMPERLLRALQARGV--KFVQGYGMTETSPGVTF--LSPEDHR---RKLGSAgr 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 -LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd17631    271 pVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--RDG--WFHTGDLGRLDEDGYLYIVDRKKDMI 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPA 3996
Cdd:cd17631    347 ISGGENVYPAEVEDVLYEHPAVAEVAVI--GVPDEKWgeaVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDA 424
                          490
                   ....*....|.
gi 1246793773 3997 LPLTANGKLDR 4007
Cdd:cd17631    425 LPRNATGKILK 435
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3521-4010 2.77e-74

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: 257.49  E-value: 2.77e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSGVclsvsqralavelpgTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVV 3680
Cdd:cd05936     81 PLYTPRELEHILNDSGA---------------KALIVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THRNverLFTAATQTGRFSFDEHD-------VWSLFHSHAFDFAvweLWGAWLYGGRAVLVPEAVcrqPDAFLDLLAEYG 3753
Cdd:cd05936    146 THRN---LVANALQIKAWLEDLLEgddvvlaALPLFHVFGLTVA---LLLPLALGATIVLIPRFR---PIGVLKEIRKHR 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3754 VTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDEdlQS 3832
Cdd:cd05936    217 VTIFPGVPTMYIALLNAPEFKKRDFsSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPLDGP--RK 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3833 PTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYR 3912
Cdd:cd05936    294 PGS-IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF--VDG--WLRTGDIGYMDEDGYFFIV 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLI 3991
Cdd:cd05936    369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQV 448
                          490
                   ....*....|....*....
gi 1246793773 3992 QLLPALPLTANGKLDRKAL 4010
Cdd:cd05936    449 EFRDELPKSAVGKILRREL 467
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
2052-2522 7.86e-74

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: 255.47  E-value: 7.86e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17650      3 AIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLED 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd17650     83 SGAKLLL-----------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDL-GEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTA 2290
Cdd:cd17650    128 EYELdSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNG 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2291 VLPR--ECLVTGGEALTGA-LVQQVRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQG----VPVGHPLAGNEAWVL 2363
Cdd:cd17650    208 LDLSamRLLIVGSDGCKAQdFKTLAARFGQGMRIINSYGVTEATI---DSTYYEEGRDPLGdsanVPIGRPLPNTAMYVL 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2364 DRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRV 2443
Cdd:cd17650    285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS----LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17650    365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAatlnTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444

                   ...
gi 1246793773 2520 QAL 2522
Cdd:cd17650    445 RAL 447
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
3080-3453 3.14e-73

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: 252.62  E-value: 3.14e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19547      1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19547     81 LLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLR---GQDEAAARaFWREQLTGLEPAALPEATEPAEGYASS-----TRRFDLAAASAwAQSH 3311
Cdd:cd19547    161 GREPQLSPCRPYRDYVRWIRartAQSEESER-FWREYLRDLTPSPFSTAPADREGEFDTvvhefPEQLTRLVNEA-ARGY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 GLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRT 3391
Cdd:cd19547    239 GVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAA 318
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3392 HGYLPLAQIQRAGAADAVSP---FDVLLVFENLPTES-REERSGMRIEELDHRAHSNYPLMLTAIP 3453
Cdd:cd19547    319 HGHVPLAQIKSWASGERLSGgrvFDNLVAFENYPEDNlPGDDLSIQIIDLHAQEKTEYPIGLIVLP 384
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
549-1041 7.73e-73

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: 252.39  E-value: 7.73e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDA-AA 707
Cdd:cd17650     81 EDSGAKLLLTQ---------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAwRR 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  708 EALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL-LEPQRFLAFLSERAITVTDLAPAyaneLVRASVAD- 785
Cdd:cd17650    128 EYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVkLDPAALYDLILKSRITLMESTPA----LIRPVMAYv 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  786 DWRDL---ALRCLVVGGDVLPValaqRWFELGLDR---RCALINAYGPTEATISSHYHRVQA--IDASRPVPLGQLLPGR 857
Cdd:cd17650    204 YRNGLdlsAMRLLIVGSDGCKA----QDFKTLAARfgqGMRIINSYGVTEATIDSTYYEEGRdpLGDSANVPIGRPLPNT 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  858 IAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQV 937
Cdd:cd17650    280 AMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGE--RMYRTGDLARWRADGNVELLGRVDHQV 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  938 KLRGYRIELEEIEHCLGQLPQVRAAAAGVVGE-GAAQRLVAWVecagedgfgqadlnqTDSDQTESERWHRALCERLPAY 1016
Cdd:cd17650    358 KIRGFRIELGEIESQLARHPAIDEAVVAVREDkGGEARLCAYV---------------VAAATLNTAELRAFLAKELPSY 422
                          490       500
                   ....*....|....*....|....*
gi 1246793773 1017 MVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17650    423 MIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
2047-2522 4.28e-72

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: 250.16  E-value: 4.28e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQI 2126
Cdd:cd17645      9 ERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2127 AVLDDSGARIVIGwgaapawvpasvrwldaesvldvvsayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV 2206
Cdd:cd17645     89 YMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2207 AGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVdCLKIVPSHLAGLLAAA 2286
Cdd:cd17645    134 EWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPTGAAEQFMQL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2287 GGTAVlprECLVTGGEALTgalvqqvRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRF 2366
Cdd:cd17645    213 DNQSL---RVLLTGGDKLK-------KIERKGYKLVNNYGPTENTV---VATSFEIDKPYANIPIGKPIDNTRVYILDEA 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:cd17645    280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPG 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPGANGVLQLGACI----QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17645    360 EIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVtapeEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3520-4010 2.94e-70

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 248.87  E-value: 2.94e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSaEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:COG0365     13 NCLDRHAEGRGDKVALIWEG-EDGEertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPVD----PHAPAARrgfiLEDSGV----------------------------------CLSVSQRALAVELPGtALCLD 3638
Cdd:COG0365     92 SPVFpgfgAEALADR----IEDAEAkvlitadgglrggkvidlkekvdealeelpslehVIVVGRTGADVPMEG-DLDWD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3639 DpftraqLDAVEPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVerlFTAATQTGRFSFD--EHDV--------W 3706
Cdd:COG0365    167 E------LLAAASAEFEPEPTDAddPLFILYTSGTTGKPKGVVHTHGGY---LVHAATTAKYVLDlkPGDVfwctadigW 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SLFHShafdfavWELWGAWLYGGRAVLVPEAVC-RQPDAFLDLLAEYGVTVLNQTPSAFYAL--QSQAMRRELAL-NVRA 3782
Cdd:COG0365    238 ATGHS-------YIVYGPLLNGATVVLYEGRPDfPDPGRLWELIEKYGVTVFFTAPTAIRALmkAGDEPLKKYDLsSLRL 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDEdlQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:COG0365    311 LGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTETGGIFISNLPGLP--VKPGS-MGKPVPGYDVAVVDEDGNPVPPGEEG 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGD--GVAQGYWQRPELTAERFVERGgQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQ 3940
Cdd:COG0365    387 ELVIKGPwpGMFRGYWNDPERYRETYFGRF-PGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3941 VSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:COG0365    466 VAEAAVVgVPDEIRGQVVKAFVVLKPGVEPSDelaKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
88-510 8.76e-69

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: 241.08  E-value: 8.76e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDS-----VAAGGGAAVES 161
Cdd:pfam00668    5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRtVFIRQENGepvqvILEERPFELEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQDE----IDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYr 237
Cdd:pfam00668   85 IDISDLSESEeeeaIEAFIQRDLQSPFDLEKGPLFRAGLFRIAEN-----RHHLLLSMHHIIVDGVSLGILLRDLADLY- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 vECGLAAEPAPPLPCQ-YGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:pfam00668  159 -QQLLKGEPLPLPPKTpYKDYAEWLQQYLqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCR 394
Cdd:pfam00668  238 ELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  395 DHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDadlalDLHGVQAHALTL----------PEDVAKHELTL 464
Cdd:pfam00668  318 EDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNY-----LGQDSQEEEFQLseldlsvssvIEEEAKYDLSL 392
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773  465 EVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENPHEP 510
Cdd:pfam00668  393 TASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP 438
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
3080-3487 1.88e-68

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: 237.97  E-value: 1.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEAdpYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVqgLPSPRQLphrQVSLPLA 3159
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGA--YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQ--SDSGGLL---QVVVKES 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGlepaqaRSRLSELQAQQCEAGFDLAAPpLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYaalre 3239
Cdd:cd19545     74 PISWTE------STSLDEYLEEDRAAPMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY----- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 sRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLEPAALPEAtePAEGY-ASSTRRFDLAAASAWAQSHGLTASSL 3318
Cdd:cd19545    142 -QGEPVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPL--PSSRYqPRPDATLEHSISLPSSASSGVTLATV 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3319 LQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLA 3398
Cdd:cd19545    219 LRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQ 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3399 QIQRAGAADAVSP-FDVLLVFE-NLPTESREERSGMRIEEL-DHRAHSNYPLMLTAIPDAGGLRIEAALDRSKLDGWLVE 3475
Cdd:cd19545    299 NIRRLGPDARAACnFQTLLVVQpALPSSTSESLELGIEEESeDLEDFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVE 378
                          410
                   ....*....|..
gi 1246793773 3476 QMLDDLDFVLQQ 3487
Cdd:cd19545    379 RLLDQFEHVLQQ 390
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
2051-2522 2.97e-67

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: 236.53  E-value: 2.97e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVG-VQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd17648      2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpASVRWLdaesvldvvsayeepprvdvdadtpAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd17648     82 EDTGARVVI----------TNSTDL-------------------------AYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLG--EDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPShlaglLAAAG 2287
Cdd:cd17648    127 SERYFGRdnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS-----VLQQY 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2288 GTAVLPR-ECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTVGILTCTVPEEWPVEQGVpvGHPLAGNEAWVLDRF 2366
Cdd:cd17648    202 DLARLPHlKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYVLNDA 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPDR--------LLYRSGDLARLDGEGRIVYLGRGDHQVKI 2438
Cdd:cd17648    279 MKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKI 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2439 RGYRVELGEVEQVLAQLPGVEVAAVLALPGANG-------------VLQLGACIQGSLEgvaEALAQRLPEYLCPSRWRA 2505
Cdd:cd17648    359 RGQRIEPGEVEAALASYPGVRECAVVAKEDASQaqsriqkylvgyyLPEPGHVPESDLL---SFLRAKLPRYMVPARLVR 435
                          490
                   ....*....|....*..
gi 1246793773 2506 VESMPRLGNGKIDRQAL 2522
Cdd:cd17648    436 LEGIPVTINGKLDVRAL 452
AMP-binding pfam00501
AMP-binding enzyme;
2052-2439 3.47e-67

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 234.90  E-value: 3.47e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGA-ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:pfam00501   11 KTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGAAPA----------WVPASVRWLDAESVLDVVSAYEE--------PPRVDVDADTPAYLIYTSGSTGTP 2192
Cdd:pfam00501   91 DSGAKVLITDDALKLeellealgklEVVKLVLVLDRDPVLKEEPLPEEakpadvppPPPPPPDPDDLAYIIYTSGTTGKP 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2193 KGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGF-----TALFGALLSGRRVRLLPAELAFDAQALAAHLQAH 2267
Cdd:pfam00501  171 KGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHdfglsLGLLGPLLAGATVVLPPGFPALDPAALLELIERY 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 PVDCLKIVPSHLAG-LLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTvGILTCTVPEEWPV 2345
Cdd:pfam00501  251 KVTVLYGVPTLLNMlLEAGAPKRALLSSlRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETT-GVVTTPLPLDEDL 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2346 EQGVPVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRlLYRSGDLARLDGEG 2424
Cdd:pfam00501  329 RSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-----DG-WYRTGDLGRRDEDG 402
                          410
                   ....*....|....*
gi 1246793773 2425 RIVYLGRGDHQVKIR 2439
Cdd:pfam00501  403 YLEIVGRKKDQIKLG 417
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
3529-4012 6.79e-67

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: 237.37  E-value: 6.79e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:TIGR03098   10 AARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALAVEL-PGTALCLD------------DPFTRAQLDAVEPGELPEVPTEAP---------AYLI 3666
Cdd:TIGR03098   90 AHILADCNVRLLVTSSERLDLLhPALPGCHDlrtliivgdpahASEGHPGEEPASWPKLLALGDADPphpvidsdmAAIL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcrqPDAFL 3746
Cdd:TIGR03098  170 YTSGSTGRPKGVVLSHRNL--VAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLL---PRDVL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3747 DLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITEttvhvSFHR-- 3824
Cdd:TIGR03098  245 KALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-----AFRSty 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3825 LSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERF---------VERGGQRFY 3895
Cdd:TIGR03098  320 LPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrplppfpgeLHLPELAVW 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3896 rSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSL 3974
Cdd:TIGR03098  400 -SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAIVLVVTPPGGEELDRAAL 478
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 3975 REALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:TIGR03098  479 LAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
AMP-binding pfam00501
AMP-binding enzyme;
541-940 2.88e-66

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 232.20  E-value: 2.88e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  541 IARAADEFPERAALETAQG-RLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEW 619
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  620 PQARRAEVVAASGCDAVLTD----AQGLAGFAPSVAIAVDELKLDGAGENGSG----------------ENAAPNQLAYI 679
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDdalkLEELLEALGKLEVVKLVLVLDRDPVLKEEplpeeakpadvpppppPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  680 LYTSGSTGIPKGVEVGHA----ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLE-QILAAWSRGACVV-ARPDELLEP 753
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRnlvaNVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVlPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  754 QRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGldrRCALINAYGPTEATIS 833
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELF---GGALVNGYGLTETTGV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  834 SHYHRVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRM 912
Cdd:pfam00501  318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF--------DEDGW 389
                          410       420
                   ....*....|....*....|....*...
gi 1246793773  913 YRSGDRVRLLDDGELQFLGRADFQVKLR 940
Cdd:pfam00501  390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1594-1978 3.17e-65

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: 230.68  E-value: 3.17e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1594 IEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAA 1673
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1674 PWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTA 1753
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1754 GAQGATLRLPPAPGFQAYLDWRER----QDLARQRGWWRERLSGYAGTAALPAPVAAAhhPVQREECER---RLSAHDSE 1826
Cdd:pfam00668  161 LLKGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARP--ADRSFKGDRlsfTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1827 RLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPpeLAGVESMVGVFINTLPLRLRIDAGQPALDLLSAL 1906
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1907 RSQSLEVAENEAVGLGEILADSGLDAD----RLFASLLVVENFP-------AMAPAQLPFALRVRETRAANhYALTLRVS 1975
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLPRDlsrhPLFDPMFSFQNYLgqdsqeeEFQLSELDLSVSSVIEEEAK-YDLSLTAS 395

                   ...
gi 1246793773 1976 ERE 1978
Cdd:pfam00668  396 ERG 398
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3547-4011 3.66e-64

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: 226.40  E-value: 3.66e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSqral 3626
Cdd:cd05934      6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 avelpgtalclddpftraqldavepgelpevpteAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW 3706
Cdd:cd05934     82 ----------------------------------DPASILYTSGTTGPPKGVVITHANL--TFAGYYSARRFGLGEDDVY 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 ----SLFHSHAfdfAVWELWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRA 3782
Cdd:cd05934    126 ltvlPLFHINA---QAVSVLAALSVGATLVLLPRF---SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALePSRLQPWRERYpQAELVNMYGITETTVHVsfhrLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:cd05934    200 AAYGAPNP-PELHEEFEERF-GVRLLEGYGMTETIVGV----IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPG 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVV---EGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLP 3939
Cdd:cd05934    274 ELVIrglRGWGFFKGYYNMPEATAEAM--RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHP 349
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3940 QVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALP 4011
Cdd:cd05934    350 AVREAAVvAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3529-4010 1.88e-62

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 224.68  E-value: 1.88e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK06187    16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALAVELPGTalclddpftRAQLDAV------EPGELPEVPTEAPAY------------------ 3664
Cdd:PRK06187    96 AYILNDAEDRVVLVDSEFVPLLAAI---------LPQLPTVrtviveGDGPAAPLAPEVGEYeellaaasdtfdfpdide 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 -----LIYTSGSTGTPKGVVVTHRNverLFT-AATQTGRFSFDEHDVwSL-----FHSHAfdfavwelWG----AWLYGG 3729
Cdd:PRK06187   167 ndaaaMLYTSGTTGHPKGVVLSHRN---LFLhSLAVCAWLKLSRDDV-YLvivpmFHVHA--------WGlpylALMAGA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 RAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRERYpQAELV 3808
Cdd:PRK06187   235 KQVIPRRF---DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREFKEKF-GIDLV 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3809 NMYGITETTVHVSFHRLSDEDLQSPTSRI--GSALPDLAVHVLDAAGQPVP--LGVVGELVVEGDGVAQGYWQRPELTAE 3884
Cdd:PRK06187   311 QGYGMTETSPVVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3885 RFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYA 3961
Cdd:PRK06187   391 TI--DGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI--GVPDEKWgerPVAVV 464
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773 3962 VAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06187   465 VLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
549-1042 2.44e-62

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: 222.28  E-value: 2.44e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARS-VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEV 627
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  628 VAASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAA 707
Cdd:cd17648     81 LEDTGARVVITN---------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  708 EA--LALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDE-LLEPQRFLAFLSERAITVTDLAPAYAN--ELVRAS 782
Cdd:cd17648    128 ERyfGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQqyDLARLP 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  783 vaddwrdlALRCLVVGGDVLPvalAQRWFELGLDRRCALINAYGPTEATISSHYHR---VQAIDASrpvpLGQLLPGRIA 859
Cdd:cd17648    208 --------HLKRVDAAGEEFT---APVFEKLRSRFAGLIINAYGPTETTVTNHKRFfpgDQRFDKS----LGRPVRNTKC 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  860 AVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF------APLRLPSGESLRMYRSGDRVRLLDDGELQFLGRA 933
Cdd:cd17648    273 YVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqTEQERARGRNARLYKTGDLVRWLPSGELEYLGRN 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  934 DFQVKLRGYRIELEEIEHCLGQLPQVRAAA------AGVVGEGAAQRLVAWVECAgEDGFGQADLnqtdsdqtesERWHR 1007
Cdd:cd17648    353 DFQVKIRGQRIEPGEVEAALASYPGVRECAvvakedASQAQSRIQKYLVGYYLPE-PGHVPESDL----------LSFLR 421
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 1008 AlceRLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd17648    422 A---KLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
549-1042 1.01e-61

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: 221.19  E-value: 1.01e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDAQ--GLAGFAPSVAIAVDELKLDGAGENGSGENAApNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAA 706
Cdd:cd17656     82 LDSGVRVVLTQRHlkSKLSFNKSTILLEDPSISQEDTSNIDYINNS-DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  707 AEALALSADDRVLHVAGLAVDTTLEQILAAW-SRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELvrASVAD 785
Cdd:cd17656    161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLlSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI--FSERE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  786 DWRDLA--LRCLVVGGDVLPVAlaQRWFELGLDRRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLD 863
Cdd:cd17656    239 FINRFPtcVKHIITAGEQLVIT--NEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  864 AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYR 943
Cdd:cd17656    317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPD--PFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  944 IELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVawveCAgedgFGQADLNQTDSDQTESerwhraLCERLPAYMVPTQFV 1023
Cdd:cd17656    395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYL----CA----YFVMEQELNISQLREY------LAKQLPEYMIPSFFV 460
                          490
                   ....*....|....*....
gi 1246793773 1024 ALPRLPRNASGKIDRRALP 1042
Cdd:cd17656    461 PLDQLPLTPNGKVDRKALP 479
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
3080-3488 1.51e-60

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: 215.25  E-value: 1.51e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLfHSLLNAEADpYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSP-RQLPHRQVSLPL 3158
Cdd:cd19542      1 IYPCTPMQEGML-LSQLRSPGL-YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKSLDPPI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AE-QDWSGLEPAQARSrlsELQAQqceagfDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYaal 3237
Cdd:cd19542     79 EEvETDEDSLDALTRD---LLDDP------TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY--- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3238 resRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLEPAALPEAT--EPAEGYASSTRRfDLAAASAWAQSHGLTA 3315
Cdd:cd19542    147 ---NGQLLPPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSpkRPAERSLSSTRR-SLAKLEAFCASLGVTL 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3316 SSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYL 3395
Cdd:cd19542    223 ASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHL 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3396 PLAQIQRA-GAADAVSPFDVLLVFENLPTESREERSGMRIEELDH-RAHSNYPLMLTAIPDAGGLRIEAALDRSKLDGWL 3473
Cdd:cd19542    303 SLREIQRAlGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAaEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQ 382
                          410
                   ....*....|....*
gi 1246793773 3474 VEQMLDDLDFVLQQV 3488
Cdd:cd19542    383 AEELLEQFDDILEAL 397
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3520-4010 1.49e-59

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 215.92  E-value: 1.49e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK07656     6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGVCL------------SVSQRALAVEL-----PGTALCLDDPFTRAQlDAVEPGEL----PEVP 3658
Cdd:PRK07656    86 NTRYTADEAAYILARGDAKAlfvlglflgvdySATTRLPALEHvviceTEEDDPHTEKMKTFT-DFLAAGDPaeraPEVD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3659 TEAPAYLIYTSGSTGTPKGVVVTHRNverLFTAATQTG-RFSFDEHD----VWSLFhsHAFDFAVweLWGAWLYGGrAVL 3733
Cdd:PRK07656   165 PDDVADILFTSGTTGRPKGAMLTHRQ---LLSNAADWAeYLGLTEGDrylaANPFF--HVFGYKA--GVNAPLMRG-ATI 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPEAVCrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYG 3812
Cdd:PRK07656   237 LPLPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLsSLRLAVTGAASMPVALLERFESELGVDIVLTGYG 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVHVSFHRLSDEDLQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgq 3892
Cdd:PRK07656   316 LSEASGVTTFNRLDDDRKTVAGT-IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADG-- 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3893 rFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP 3971
Cdd:PRK07656   393 -WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgVPDERLGEVGKAYVVLKPGAELTE 471
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1246793773 3972 QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07656   472 EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3080-3461 1.93e-59

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: 212.99  E-value: 1.93e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF-AVQGlpSPRQLPHRQVSLPL 3158
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFvEVDG--EPVQVILPPLPLPL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALR 3238
Cdd:cd19531     79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 ESRTPQLPAAPP-FRDYLHWLRG--QDEAAAR--AFWREQLTGLEPA-ALPeaTE---PAE-GYASSTRRFDLAAA---- 3304
Cdd:cd19531    159 AGRPSPLPPLPIqYADYAVWQREwlQGEVLERqlAYWREQLAGAPPVlELP--TDrprPAVqSFRGARVRFTLPAEltaa 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3305 -SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRP-PELagvERMLGVFINSVPLRVTPAGEATPAPWLQAL 3382
Cdd:cd19531    237 lRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNrAEL---EGLIGFFVNTLVLRTDLSGDPTFRELLARV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3383 QQRNLDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLPtESREERSGMRIEELD-HRAHSNYPLMLTAI 3452
Cdd:cd19531    314 RETALEAYAHQDLPFEKL-----VEALQPerdlsrsplFQVMFVLQNAP-AAALELPGLTVEPLEvDSGTAKFDLTLSLT 387

                   ....*....
gi 1246793773 3453 PDAGGLRIE 3461
Cdd:cd19531    388 ETDGGLRGS 396
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3552-4010 2.30e-59

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: 213.46  E-value: 2.30e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAA----YVPVDPHAPAARRGFILEDSGVCLSVSQRALA 3627
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3628 VELPGTALCLDDPFTRAQLDAVEPGELP----EVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEH 3703
Cdd:cd05922     81 DRLRDALPASPDPGTVLDADGIRAARASapahEVSHEDLALLLYTSGSTGSPKLVRLSHQNL--LANARSIAEYLGITAD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3704 DVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCrqPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAV 3783
Cdd:cd05922    159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSF---HRLsdedLQSPTSrIGSALPDLAVHVLDAAGQPVPLGV 3860
Cdd:cd05922    237 TQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYlppERI----LEKPGS-IGLAIPGGEFEILDDDGTPTPPGE 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 VGELVVEGDGVAQGYWQRPeltAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQ 3940
Cdd:cd05922    312 PGEIVHRGPNVMKGYWNDP---PYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3941 VSDAAVTVEGQGEGAWLMAYAVAADGAEPDPqsLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05922    389 IIEAAAVGLPDPLGEKLALFVTAPDKIDPKD--VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
3525-4084 6.51e-59

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: 226.48  E-value: 6.51e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAV----SAEDG-----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAA 3595
Cdd:TIGR03443  242 FADNAEKHPDRTCVvetpSFLDPssktrSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGAT 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3596 YVPVDPHAPAAR----------RGFI-LEDSGVcLSVSQR-------ALAVELPGTALCLDDPFTRAQLDAVEPG----- 3652
Cdd:TIGR03443  322 FSVIDPAYPPARqtiylsvakpRALIvIEKAGT-LDQLVRdyidkelELRTEIPALALQDDGSLVGGSLEGGETDvlapy 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3653 -ELPEVPT------EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDEHDVWSLFHSHAFD------FAVw 3719
Cdd:TIGR03443  401 qALKDTPTgvvvgpDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK--RFGLSENDKFTMLSGIAHDpiqrdmFTP- 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3720 elwgawLYGGRAVLVPEAVCRQ-PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALnvRAVVFGGEAL---EPSRL 3795
Cdd:TIGR03443  478 ------LFLGAQLLVPTADDIGtPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSL--HHAFFVGDILtkrDCLRL 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3796 QPWRErypQAELVNMYGITETTVHVSFH----RLSDED-LQSPTSRI--GSALPD---LAVHVLDAAgQPVPLGVVGELV 3865
Cdd:TIGR03443  550 QTLAE---NVCIVNMYGTTETQRAVSYFeipsRSSDSTfLKNLKDVMpaGKGMKNvqlLVVNRNDRT-QTCGVGEVGEIY 625
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3866 VEGDGVAQGYWQRPELTAERFV-----------------ERGGQ--------RFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:TIGR03443  626 VRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkenNKPERefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVK 705
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDaAVT----------------VEGQGEGAWLMAYAVAADGAEPDP------------Q 3972
Cdd:TIGR03443  706 IRGFRIELGEIDTHLSQHPLVRE-NVTlvrrdkdeeptlvsyiVPQDKSDELEEFKSEVDDEESSDPvvkglikyrkliK 784
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3973 SLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPET--------QDRDEGVLESAS--ERRLAELWRQLlgge 4042
Cdd:TIGR03443  785 DIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTaqlaavakNRSASAADEEFTetEREIRDLWLEL---- 860
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773 4043 LPGRGAH------FFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:TIGR03443  861 LPNRPATispddsFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSP 908
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1598-1946 1.34e-58

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: 210.25  E-value: 1.34e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQT 1677
Cdd:cd19547      2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1678 LDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG 1757
Cdd:cd19547     82 LDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLRLPPAPGFQAYLDW---RERQDLARQRgWWRERLSGYAGTAALPApvaaahhPVQREECERRLSAHDSERLRAF--- 1831
Cdd:cd19547    162 REPQLSPCRPYRDYVRWiraRTAQSEESER-FWREYLRDLTPSPFSTA-------PADREGEFDTVVHEFPEQLTRLvne 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1832 -CRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQS 1910
Cdd:cd19547    234 aARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1246793773 1911 LEVAENEAVGLGEILADSG---LDADRLFASLLVVENFP 1946
Cdd:cd19547    314 ATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYP 352
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3535-4010 1.91e-58

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: 210.61  E-value: 1.91e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGA-GPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILE 3613
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3614 DSGVCLSVsqralavelpgtalclddpftraqldavepgelpevpteAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAAT 3693
Cdd:cd05941     82 DSEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALV 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3694 QTGRFSFDEH--DVWSLFHSHAFDFAvweLWGAWLYGGRAVLVPEavcrqPDAFLDLLAEY--GVTVLNQTPsAFY---- 3765
Cdd:cd05941    123 DAWRWTEDDVllHVLPLHHVHGLVNA---LLCPLFAGASVEFLPK-----FDPKEVAISRLmpSITVFMGVP-TIYtrll 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3766 ------ALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVSfHRLSDEdlQSPTSrIGS 3839
Cdd:cd05941    194 qyyeahFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMALS-NPLDGE--RRPGT-VGM 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 ALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRG-DD 3917
Cdd:cd05941    269 PLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDG---WFKTGDLGVVDEDGYYWILGRSsVD 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3918 QVKLRGYRIEPGEIAAKIASLPQVSDAAVT---VEGQGEGAwlMAYAVAADGAEP-DPQSLREALRALLPDYMLPRLIQL 3993
Cdd:cd05941    346 IIKSGGYKVSALEIERVLLAHPGVSECAVIgvpDPDWGERV--VAVVVLRAGAAAlSLEELKEWAKQRLAPYKRPRRLIL 423
                          490
                   ....*....|....*..
gi 1246793773 3994 LPALPLTANGKLDRKAL 4010
Cdd:cd05941    424 VDELPRNAMGKVNKKEL 440
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1597-1946 2.51e-58

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: 209.23  E-value: 2.51e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1597 AFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQ 1676
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 TLDWSALDDaaQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGG-GRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGA 1755
Cdd:cd19536     81 ELDLTPLEE--QLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDErERFLLVISDHHSILDGWSLYLLVKEILAVYNQLL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1756 QGATLRLPPAPGFQAYLDWRER--QDLARQRgWWRERLSGYAGTAALPAPVAAAHHPVQREecERRLSAHDSERLRAFCR 1833
Cdd:cd19536    159 EYKPLSLPPAQPYRDFVAHERAsiQQAASER-YWREYLAGATLATLPALSEAVGGGPEQDS--ELLVSVPLPVRSRSLAK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1834 ERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIdAGQPALDLLSALRSQSLEV 1913
Cdd:cd19536    236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELES 314
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1246793773 1914 AENEAVGLGEILADSglDADRLFASLLVVENFP 1946
Cdd:cd19536    315 LSHEQVPLADIQRCS--EGEPLFDSIVNFRHFD 345
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
588-1042 1.42e-56

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: 205.10  E-value: 1.42e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengs 667
Cdd:cd17645     51 VGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTN---------------------------- 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 genaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARP 747
Cdd:cd17645    103 -----PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVP 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  748 DEL-LEPQRFLAFLSERAITVTDLAPAYANELVRASvaddwrDLALRCLVVGGDVLPVALAQRWfelgldrrcALINAYG 826
Cdd:cd17645    178 SERrLDLDALNDYFNQEGITISFLPTGAAEQFMQLD------NQSLRVLLTGGDKLKKIERKGY---------KLVNNYG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  827 PTEATISSHYHRVQAIDASrpVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPS 906
Cdd:cd17645    243 PTENTVVATSFEIDKPYAN--IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  907 GEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQR-LVAWVecaged 985
Cdd:cd17645    321 GE--RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYV------ 392
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  986 gfgqadlnqTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd17645    393 ---------TAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3529-4010 1.74e-56

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: 206.84  E-value: 1.74e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:cd05959     14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALA----------------VELPGTALCLDDPFTRAQLDAVEPGELPEVPTEA--PAYLIYTSG 3670
Cdd:cd05959     94 AYYLEDSRARVVVVSGELApvlaaaltksehtlvvLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHAddPAFWLYSSG 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3671 STGTPKGVVVTHRN---VERLFtaATQTGRFSfdEHDVW----SLFHSHAFD----FAVWelwgawlYGGRAVLVPEAVc 3739
Cdd:cd05959    174 STGRPKGVVHLHADiywTAELY--ARNVLGIR--EDDVCfsaaKLFFAYGLGnsltFPLS-------VGATTVLMPERP- 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 rQPDAFLDLLAEYGVTVLNQTPsAFYA--LQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITEtT 3817
Cdd:cd05959    242 -TPAAVFKRIRRYRPTVFFGVP-TLYAamLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTE-M 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSfhrLSD--EDLQSPTSriGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVerGGqrFY 3895
Cdd:cd05959    318 LHIF---LSNrpGRVRYGTT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ--GE--WT 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3896 RSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGawLM---AYAVAADGAEP--- 3969
Cdd:cd05959    389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG--LTkpkAFVVLRPGYEDsea 466
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 3970 DPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05959    467 LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
3081-3488 2.11e-56

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: 204.18  E-value: 2.11e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3081 YPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAvQGLPSPRQLPHRQVSLP-LA 3159
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVVLDKTVRFrIE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLepAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19066     81 IIDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAPPFRDYLHWLRGQ--DEAAAR--AFWREQLTGL-EPAALPEATEPAEGYASSTRRFDLAAASAW------- 3307
Cdd:cd19066    159 QKPTLPPPVGSYADYAAWLEKQleSEAAQAdlAYWTSYLHGLpPPLPLPKAKRPSQVASYEVLTLEFFLRSEEtkrlrev 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3308 AQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPElaGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNL 3387
Cdd:cd19066    239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3388 DLRTHGYLPLAQIQRA-----GAADAVSpFDVLLVFENLPTESREERSGMRIEEL-DHRAHSNYPLMLTAIPDA-GGLRI 3460
Cdd:cd19066    317 EAIEHQRVPFIELVRHlgvvpEAPKHPL-FEPVFTFKNNQQQLGKTGGFIFTTPVyTSSEGTVFDLDLEASEDPdGDLLL 395
                          410       420
                   ....*....|....*....|....*...
gi 1246793773 3461 EAALDRSKLDGWLVEQMLDDLDFVLQQV 3488
Cdd:cd19066    396 RLEYSRGVYDERTIDRFAERYMTALRQL 423
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
2178-2518 3.97e-56

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: 200.20  E-value: 3.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLStVAADLGFTALFGALLSGRRVRLLPAelaFD 2256
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEgDVFLSTLP-LFHIGGLFGLLGALLAGGTVVLLPK---FD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2257 AQALAAHLQAHPVDCLKIVPS-HLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETTVGI 2334
Cdd:cd04433     77 PEAALELIEREKVTILLGVPTlLARLLKAPESAGYDLSSlRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEWpvEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplapDRLLYRS 2414
Cdd:cd04433    156 ATGPPDDDA--RKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRT 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQ------GSLEGVAE 2488
Cdd:cd04433    227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVlrpgadLDAEELRA 306
                          330       340       350
                   ....*....|....*....|....*....|
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:cd04433    307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
3080-3467 6.47e-56

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: 202.28  E-value: 6.47e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3080 VYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19544      1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EqdwsgLEPAQARSRLSELQAqQCEAG---FDLAAPPLMRLALLR-RSADEHWLVWTRHHLIVDGWSSALLLDEVwrlyA 3235
Cdd:cd19544     81 E-----LTLDPGDDALAQLRA-RFDPRryrLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----Q 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3236 ALRESRTPQLPAAPPFRDYL-HWLRGQDEAAARAFWREQLTGLEpaalpEATEP-------AEGYASSTRRFDLAAASA- 3306
Cdd:cd19544    151 AILAGRAAALPPPVPYRNFVaQARLGASQAEHEAFFREMLGDVD-----EPTAPfglldvqGDGSDITEARLALDAELAq 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 ----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPwLQAL 3382
Cdd:cd19544    226 rlraQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVREA-VRQT 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3383 QQRNLDLRTHGYLPLAQIQRAGAADAVSP-FDVLLVF--ENLPTESREERSGMRIEELDHRAHSNYPLMLtAIPDAG-GL 3458
Cdd:cd19544    305 HARLAELLRHEHASLALAQRCSGVPAPTPlFSALLNYrhSAAAAAAAALAAWEGIELLGGEERTNYPLTL-SVDDLGdGF 383

                   ....*....
gi 1246793773 3459 RIEAALDRS 3467
Cdd:cd19544    384 SLTAQVVAP 392
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
675-1037 2.07e-55

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: 197.89  E-value: 2.07e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEllEPQ 754
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF--DPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  755 RFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEATISS 834
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEA---PGIKLVNGYGLTETGGTV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  835 HYHRVqAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYR 914
Cdd:cd04433    156 ATGPP-DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED---------GWYR 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  915 SGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLN 993
Cdd:cd04433    226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAeAAVVGVPDPEWGERVVAVVVLRPGADLDAEELR 305
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1246793773  994 QtdsdqteserwhrALCERLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:cd04433    306 A-------------HVRERLAPYKVPRRVVFVDALPRTASGKID 336
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3550-4010 4.13e-54

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: 197.65  E-value: 4.13e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3550 LDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP-HAPAARRgFILEDSGVclsvsqRALAV 3628
Cdd:cd05971     12 LKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFAlFGPEALE-YRLSNSGA------SALVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3629 ELPgtalclDDPftraqldavepgelpevpteapAYLIYTSGSTGTPKGVVVTHR-------NVERLFTAATQTGRFSFD 3701
Cdd:cd05971     85 DGS------DDP----------------------ALIIYTSGTTGPPKGALHAHRvllghlpGVQFPFNLFPRDGDLYWT 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHDvWslfhshAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELA-LNV 3780
Cdd:cd05971    137 PAD-W------AWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAqVKL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSfhrlSDEDLQSP-TSRIGSALPDLAVHVLDAAGQPVPLG 3859
Cdd:cd05971    210 RAIATGGESLGEELLG-WAREQFGVEVNEFYGQTECNLVIG----NCSALFPIkPGSMGKPIPGHRVAIVDDNGTPLPPG 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVE-GDGVAQ-GYWQRPELTAERFVerGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIAS 3937
Cdd:cd05971    285 EVGEIAVElPDPVAFlGYWNNPSATEKKMA--GD--WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLK 360
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3938 LPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05971    361 HPAVLMAAVVgIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
89-507 1.67e-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: 195.71  E-value: 1.67e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVL-DRCIQGEDSVA-----AGGGAAVESA 162
Cdd:cd19066      3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLrTRFCEEAGRYEqvvldKTVRFRIEII 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  163 DLR------GRGQDEIDALVEgfrlRPFELQRQRPLRMQLLRLDGQGDgpvrHWLqVVVHHIACDGVSLGLLTQDLSRAY 236
Cdd:cd19066     83 DLRnladpeARLLELIDQIQQ----TIYDLERGPLVRVALFRLADERD----VLV-VAIHHIIVDGGSFQILFEDISSVY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  237 RVECGLAAEPAPPLPcQYGDYARWQRDTLDR--LDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:cd19066    154 DAAERQKPTLPPPVG-SYADYAAWLEKQLESeaAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEET 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCR 394
Cdd:cd19066    233 KRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  395 DHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALrHDADLALDLHGVQAHALTL--PEDVAKHELTLEVLVGA-G 471
Cdd:cd19066    313 EQSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTF-KNNQQQLGKTGGFIFTTPVytSSEGTVFDLDLEASEDPdG 391
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1246793773  472 GMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19066    392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3547-4010 2.23e-53

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: 195.77  E-value: 2.23e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsQRAL 3626
Cdd:cd17654     19 YADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV-----SYLL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 AVELPGTALCLDDPFTRaQLDAVEPGELpevpteapAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTgrFSFDEHDVW 3706
Cdd:cd17654     94 QNKELDNAPLSFTPEHR-HFNIRTDECL--------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSL--FNITSEDIL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAE-YGVTVLNQTPSAFYALQSQAMRREL---ALNVRA 3782
Cdd:cd17654    163 FLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVlsaTSSLRV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALePSR--LQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPtsrIGSALPDLAVHVLDAAGQPVPlgv 3860
Cdd:cd17654    243 LALGGEPF-PSLviLSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQ---LGSPLLGTVIEVRDQNGSEGT--- 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 vGELVVEGD---GVAQGYWQRPELTaerfverggqrFYRSGDLGRyRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIAS 3937
Cdd:cd17654    316 -GQVFLGGLnrvCILDDEVTVPKGT-----------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3938 LPQVSDAAVTVEGQGEgawLMAYAVAADGAEPDPQSLREAL--RALLPDYMLprliqLLPALPLTANGKLDRKAL 4010
Cdd:cd17654    383 CLGVESCAVTLSDQQR---LIAFIVGESSSSRIHKELQLTLlsSHAIPDTFV-----QIDKLPLTSHGKVDKSEL 449
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
3535-4010 4.41e-52

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: 191.91  E-value: 4.41e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILED 3614
Cdd:cd05919      1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SgvclsvsqRALAVELPGTALClddpftraqldavepgelpevpteapaYLIYTSGSTGTPKGVVVTHRNVeRLFTAATQ 3694
Cdd:cd05919     81 C--------EARLVVTSADDIA---------------------------YLLYSSGTTGPPKGVMHAHRDP-LLFADAMA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3695 TGRFSFDEHDV----------WSLFHShafdfavweLWGAWLYGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPsAF 3764
Cdd:cd05919    125 REALGLTPGDRvfssakmffgYGLGNS---------LWFPLAVGASAVLNPGW--PTAERVLATLARFRPTVLYGVP-TF 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3765 YA--LQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETtVHVSFHRLSDEdlqsptSRIGSA-- 3840
Cdd:cd05919    193 YAnlLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEV-GHIFLSNRPGA------WRLGSTgr 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 -LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd05919    265 pVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--NGG--WYRTGDKFCRDADGWYTHAGRADDML 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPD---PQSLREALRALLPDYMLPRLIQLLP 3995
Cdd:cd05919    341 KVGGQWVSPVEVESLIIQHPAVAEAAVVaVPESTGLSRLTAFVVLKSPAAPQeslARDIHRHLLERLSAHKVPRRIAFVD 420
                          490
                   ....*....|....*
gi 1246793773 3996 ALPLTANGKLDRKAL 4010
Cdd:cd05919    421 ELPRTATGKLQRFKL 435
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1597-1974 1.04e-51

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: 189.43  E-value: 1.04e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1597 AFPLTPLQRGVLLESLRGDGAdpYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQ 1676
Cdd:cd19545      1 IYPCTPLQEGLMALTARQPGA--YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 tldwsalddaaQDAQLQRWLADDAAQGVDFaHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTagaQ 1756
Cdd:cd19545     79 -----------ESTSLDEYLEEDRAAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ---G 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1757 GATLRLPPAPGFQAYLDwreRQDLARQRGWWRERLSGyAGTAALPAPVAAAHHPVQREECERRLSAhdserlrAFCRERG 1836
Cdd:cd19545    144 EPVPQPPPFSRFVKYLR---QLDDEAAAEFWRSYLAG-LDPAVFPPLPSSRYQPRPDATLEHSISL-------PSSASSG 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1837 CTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAEN 1916
Cdd:cd19545    213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 1917 EAVGLGEILADS-GLDADRLFASLLVVE-NFPAMAPAQLPFALRVRETRAANH--YALTLRV 1974
Cdd:cd19545    293 EHTGLQNIRRLGpDARAACNFQTLLVVQpALPSSTSESLELGIEEESEDLEDFssYGLTLEC 354
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3529-4010 1.76e-51

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 193.72  E-value: 1.76e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALA--VE--LPGTAL----------------------CLDDP---------FTRAQLDAVEPGE 3653
Cdd:PRK06178   123 SYELNDAGAEVLLALDQLApvVEqvRAETSLrhvivtsladvlpaeptlplpdSLRAPrlaaagaidLLPALRACTAPVP 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3654 LPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTG-RFSFDEHDVWSLFhshafdfaVWELWGA-----WLY 3727
Cdd:PRK06178   203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDM--VYTAAAAYAvAVVGGEDSVFLSF--------LPEFWIAgenfgLLF 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 ----GGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYAL--QSQAMRRELAL--NVRAVVFGgEALEPSRLQPWR 3799
Cdd:PRK06178   273 plfsGATLVLLARW---DAVAFMAAVERYRVTRTVMLVDNAVELmdHPRFAEYDLSSlrQVRVVSFV-KKLNPDYRQRWR 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3800 ERYPQAELVNMYGITETTVHVSFHR---LSDEDLQSPTSRIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGY 3875
Cdd:PRK06178   349 ALTGSVLAEAAWGMTETHTCDTFTAgfqDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGY 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3876 WQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV---TVEGQG 3952
Cdd:PRK06178   429 WNKPEATAEAL--RDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVvgrPDPDKG 504
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3953 EGAwlMAYAVAADGAEPDPQSLREALRALLPDYMLPRlIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06178   505 QVP--VAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
88-431 2.52e-51

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: 188.82  E-value: 2.52e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQgedsVAAGGGAAV-----ESA 162
Cdd:cd19532      2 EPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFF----TDPEDGEPMqgvlaSSP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  163 D----LRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19532     78 LrlehVQISDEAEVEEEFERLKNHVYDLESGETMRIVLLSL-----SPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  239 ecglaAEPAPPLPCQYGDYARWQRDTLD--RLDASLRHHVEALSGAPHlhELPL-----DHERPAVL--GQSGAKLRLaf 309
Cdd:cd19532    152 -----GQPLLPPPLQYLDFAARQRQDYEsgALDEDLAYWKSEFSTLPE--PLPLlpfakVKSRPPLTryDTHTAERRL-- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  310 PPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASL 389
Cdd:cd19532    223 DAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADV 302
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1246793773  390 VARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMF 431
Cdd:cd19532    303 LKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFI 344
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3526-4010 2.65e-51

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: 190.62  E-value: 2.65e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3526 AEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAayVPVdpHA-P 3604
Cdd:cd05920     22 ARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV--LAlP 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRgfiLEDSGVCLSVSQRALAVelPGTALCLDDPFTRAQLDAvepgELPEvpteaPAYLIYTSGSTGTPKGVVVTHRN 3684
Cdd:cd05920     98 SHRR---SELSAFCAHAEAVAYIV--PDRHAGFDHRALARELAE----SIPE-----VALFLLSGGTTGTPKLIPRTHND 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3685 VERLFTAATQTGRfsFDEHDVW--SLFHSHAFDFAVWELWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPS 3762
Cdd:cd05920    164 YAYNVRASAEVCG--LDQDTVYlaVLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREGVTVTALVPA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 -AFYALQSQAMRRELALNVRAVVFGGEALEPSRLQpwreRYPQA---ELVNMYGITETTvhVSFHRLSDEDLQSPTSRIG 3838
Cdd:cd05920    239 lVSLWLDAAASRRADLSSLRLLQVGGARLSPALAR----RVPPVlgcTLQQVFGMAEGL--LNYTRLDDPDEVIIHTQGR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3839 SALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:cd05920    313 PMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDG---FYRTGDLVRRTPDGYLVVEGRIKDQ 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAA-VTVEGQGEGAWLMAYAVAADgAEPDPQSLREALRAL-LPDYMLPRLIQLLPA 3996
Cdd:cd05920    390 INRGGEKIAAEEVENLLLRHPAVHDAAvVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRERgLAAYKLPDRIEFVDS 468
                          490
                   ....*....|....
gi 1246793773 3997 LPLTANGKLDRKAL 4010
Cdd:cd05920    469 LPLTAVGKIDKKAL 482
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
3547-4010 7.52e-50

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: 184.85  E-value: 7.52e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsqRAL 3626
Cdd:cd05972      3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------KAI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 AVELpgtalclddpftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRnverLFTAATQTGRFSFDEHD-- 3704
Cdd:cd05972     77 VTDA-----------------------------EDPALIYFTSGTTGLPKGVLHTHS----YPLGHIPTAAYWLGLRPdd 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 -VWSLfHSHAFDFAVW-ELWGAWLYGGrAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRA 3782
Cdd:cd05972    124 iHWNI-ADPGWAKGAWsSFFGPWLLGA-TVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRlsDEDLQsPTSrIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:cd05972    202 VVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFP--DMPVK-PGS-MGRPTPGYDVAIIDDDGRELPPGEEG 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGD--GVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQ 3940
Cdd:cd05972    277 DIAIKLPppGLFLGYVGDPEKTEASI--RGD--YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3941 VSDAAVT-----VEGQgegaWLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05972    353 VAEAAVVgspdpVRGE----VVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3541-4009 2.33e-49

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: 186.68  E-value: 2.33e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV-DPHAP--AARRGFILEDSG- 3616
Cdd:cd05931     21 REETLTYAELDRRARAIAARL-QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpPPTPGrhAERLAAILADAGp 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 -VCLSVSQRALAVELPGTALCLDDPFTRAQLDAVE-----PGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerLFT 3690
Cdd:cd05931    100 rVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPdtsaaDWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNL--LAN 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATQTGRFSFDEHDV---W-SLFHshafDFAVWELWGA-WLYGGRAVLV-PEAVCRQPDAFLDLLAEYGVTVlNQTPSAF 3764
Cdd:cd05931    178 VRQIRRAYGLDPGDVvvsWlPLYH----DMGLIGGLLTpLYSGGPSVLMsPAAFLRRPLRWLRLISRYRATI-SAAPNFA 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3765 YALQSQAMRRE----LAL-NVRAVVFGGEALEPSRLQPWRERY------PQAeLVNMYGITETTVHVSF---------HR 3824
Cdd:cd05931    253 YDLCVRRVRDEdlegLDLsSWRVALNGAEPVRPATLRRFAEAFapfgfrPEA-FRPSYGLAEATLFVSGgppgtgpvvLR 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3825 LSDEDLQSPTSRI-------------GSALPDLAVHVLDAAG-QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERG 3890
Cdd:cd05931    332 VDRDALAGRAVAVaaddpaarelvscGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 GQ---RFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD----AAVTVEGQGEGAWLMAYAVA 3963
Cdd:cd05931    412 ATdegGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcvAAFSVPDDGEERLVVVAEVE 490
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3964 ADGAEPDPQSLREALRALLPDY--MLPRLIQLLP--ALPLTANGKLDRKA 4009
Cdd:cd05931    491 RGADPADLAAIAAAIRAAVAREhgVAPADVVLVRpgSIPRTSSGKIQRRA 540
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
3083-3314 2.73e-49

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 176.77  E-value: 2.73e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3083 LAPLQEGLLFhslLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPLAEQD 3162
Cdd:COG4908      1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRF-VEEDGEPVQRIDPDADLPLEVVD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3163 WSGLEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESRT 3242
Cdd:COG4908     77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3243 PQLPAAP-PFRDYLHWLR----GQDEAAARAFWREQLTGLEPA-ALP-EATEPAEG-YASSTRRFDLAAA-----SAWAQ 3309
Cdd:COG4908    157 PPLPELPiQYADYAAWQRawlqSEALEKQLEYWRQQLAGAPPVlELPtDRPRPAVQtFRGATLSFTLPAEltealKALAK 236

                   ....*
gi 1246793773 3310 SHGLT 3314
Cdd:COG4908    237 AHGAT 241
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3525-4010 4.61e-49

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: 185.35  E-value: 4.61e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAayVPVdpHAP 3604
Cdd:COG1021     31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV--FAL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRgfILEDSGVClSVSQ---------------RALAVEL------PGTALCLDDPFTRAQLDAV----EPGELPEVPT 3659
Cdd:COG1021    107 PAHR--RAEISHFA-EQSEavayiipdrhrgfdyRALARELqaevpsLRHVLVVGDAGEFTSLDALlaapADLSEPRPDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRnvERLFTAATQTGRFSFDEHDVW--SLFHSHAFDFAVWELWGAWLYGGRAVLVPEA 3737
Cdd:COG1021    184 DDVAFFQLSGGTTGLPKLIPRTHD--DYLYSVRASAEICGLDADTVYlaALPAAHNFPLSSPGVLGVLYAGGTVVLAPDP 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVTVLNQTPSAFYA-LQSQAMRRELALNVRAVVFGGEALEPSRlqpwRERYPQA---ELVNMYGI 3813
Cdd:COG1021    262 ---SPDTAFPLIERERVTVTALVPPLALLwLDAAERSRYDLSSLRVLQVGGAKLSPEL----ARRVRPAlgcTLQQVFGM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETTVhvSFHRLSD-EDLQSPTsrIGSAL-PDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGg 3891
Cdd:COG1021    335 AEGLV--NYTRLDDpEEVILTT--QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDG- 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3892 qrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQGEGAwlMAYAVaADGAE 3968
Cdd:COG1021    410 --FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAmpdEYLGERS--CAFVV-PRGEP 484
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 3969 PDPQSLREALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:COG1021    485 LTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3544-4013 7.93e-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: 184.64  E-value: 7.93e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGfiledsgVCLSVSQ 3623
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQN-------IYLGVAK 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 -RALAVelpgtalclddpfTRAQLDAVEPGELPEvpteapayLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDE 3702
Cdd:cd17647     93 pRGLIV-------------IRAAGVVVGPDSNPT--------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAK--RFNLSE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3703 HDVWSLFHSHAFDFAVWELWGAwLYGGRAVLVPEAV-CRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNvR 3781
Cdd:cd17647    150 NDKFTMLSGIAHDPIQRDMFTP-LFLGAQLLVPTQDdIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLH-H 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3782 AVvFGGEAL---EPSRLQPWRERYpqaELVNMYGITETTVHVSFH----RLSDED-LQSPTSRI--GSALPDLAVHVLDA 3851
Cdd:cd17647    228 AF-FVGDILtkrDCLRLQTLAENV---RIVNMYGTTETQRAVSYFevpsRSSDPTfLKNLKDVMpaGRGMLNVQLLVVNR 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 --AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER--------GGQ-----------------RFYRSGDLGRYR 3904
Cdd:cd17647    304 ndRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwNYLdkdnnepwrqfwlgprdRLYRTGDLGRYL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3905 ADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-EGQGEGAWLMAYAVA----------ADGAEPDPQS 3973
Cdd:cd17647    384 PNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVrRDKDEEPTLVSYIVPrfdkpddesfAQEDVPKEVS 463
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3974 -----------------LREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKP 4013
Cdd:cd17647    464 tdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3536-4005 1.73e-48

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: 182.80  E-value: 1.73e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3536 IAVSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILED 3614
Cdd:cd05911      1 AQIDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SG------------VCLSVSQRA--------LAVELPG-TALCLDDPFTRAQLDAVEPGELPEVPTEaPAYLIYTSGSTG 3673
Cdd:cd05911     81 SKpkviftdpdgleKVKEAAKELgpkdkiivLDDKPDGvLSIEDLLSPTLGEEDEDLPPPLKDGKDD-TAAILYSSGTTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNverlFTAATQTGRFSFDEHDVWS--------LFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAF 3745
Cdd:cd05911    160 LPKGVCLSHRN----LIANLSQVQTFLYGNDGSNdvilgflpLYHIYGLFTTLASL----LNGATVIIMPKF---DSELF 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGG-----EALEpsRLQPwreRYPQAELVNMYGITETTVH 3819
Cdd:cd05911    229 LDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLsSLRVILSGGaplskELQE--LLAK---RFPNATIKQGYGMTETGGI 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3820 VSFHRLSDEDLQSptsrIGSALPDLAVHVLDAAG-QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSG 3898
Cdd:cd05911    304 LTVNPDGDDKPGS----VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDG---WLHTG 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3899 DLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV---TVEGQGEGAwlMAYAVAADGAEPDPQSLR 3975
Cdd:cd05911    377 DIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigiPDEVSGELP--RAYVVRKPGEKLTEKEVK 454
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1246793773 3976 EALRALLPDYMlpRL---IQLLPALPLTANGKL 4005
Cdd:cd05911    455 DYVAKKVASYK--QLrggVVFVDEIPKSASGKI 485
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3544-4010 2.45e-48

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: 180.75  E-value: 2.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVsq 3623
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 ralavelpgtalclddpfTRAQLDAVepgelpevpteapAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEH 3703
Cdd:cd05935     79 ------------------VGSELDDL-------------ALIPYTSGTTGLPKGCMHTHFSA--AANALQSAVWTGLTPS 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3704 DVW----SLFHSHAFDFAVwelwGAWLYGGRAVLVPEAVCRqpDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN 3779
Cdd:cd05935    126 DVIlaclPLFHVTGFVGSL----NTAVYVGGTYVLMARWDR--ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLS 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3780 -VRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETT--VHVS-FHRLSDEDLQSPTSRIGSALPDLAvhvldaAGQP 3855
Cdd:cd05935    200 sLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMsqTHTNpPLRPKLQCLGIP*FGVDARVIDIE------TGRE 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3856 VPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKI 3935
Cdd:cd05935    273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3936 ASLPQVSDAAV-TVEGQGEGAWLMAYAVAADG--AEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05935    353 YKHPAI*EVCViSVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
90-327 2.48e-48

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 174.07  E-value: 2.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   90 LSLGQERLWFLEqfePGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLdRC----IQGE--DSVAAGGGAAVESAD 163
Cdd:COG4908      1 LSPAQKRFLFLE---PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPAL-RTrfveEDGEpvQRIDPDADLPLEVVD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  164 LRG----RGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVE 239
Cdd:COG4908     77 LSAlpepEREAELEELVAEEASRPFDLARGPLLRAALIRLGED-----EHVLLLTIHHIISDGWSLGILLRELAALYAAL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  240 CGLAAEPAPPLPCQYGDYARWQRDTL--DRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSERV 317
Cdd:COG4908    152 LEGEPPPLPELPIQYADYAAWQRAWLqsEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEAL 231
                          250
                   ....*....|
gi 1246793773  318 AAYAQASRAT 327
Cdd:COG4908    232 KALAKAHGAT 241
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3535-4010 5.63e-48

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: 181.36  E-value: 5.63e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILED 3614
Cdd:cd05926      5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SGVCLSV--------SQRALAVELPGTA-LCLDDPFTRAQLDAVEPGELPEVPTEA----------PAYLIYTSGSTGTP 3675
Cdd:cd05926     85 LGSKLVLtpkgelgpASRAASKLGLAILeLALDVGVLIRAPSAESLSNLLADKKNAksegvplpddLALILHTSGTTGRP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVERLFTAATQTgrFSFDEHD----VWSLFHSHAFDFAVWelwgAWLYGGRAVLVPEAVcrQPDAFLDLLAE 3751
Cdd:cd05926    165 KGVPLTHRNLAASATNITNT--YKLTPDDrtlvVMPLFHVHGLVASLL----STLAAGGSVVLPPRF--SASTFWPDVRD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAFYALQSQAM---RRELALnVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTvhvsfHRLSDE 3828
Cdd:cd05926    237 YNATWYTAVPTIHQILLNRPEpnpESPPPK-LRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAA-----HQMTSN 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3829 DLQSPTSRIGSA-LPDLA-VHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRAD 3906
Cdd:cd05926    310 PLPPGPRKPGSVgKPVGVeVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG---WFRTGDLGYLDAD 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3907 GSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQGEGAWlmAYAVAADGAEPDPQSLREALRALLP 3983
Cdd:cd05926    387 GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAvafGVPDEKYGEEVA--AAVVLREGASVTEEELRAFCRKHLA 464
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05926    465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
2052-2523 6.89e-48

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: 181.52  E-value: 6.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIA-VLD 2130
Cdd:TIGR03098   16 ATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL-KAEQVAhILA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGA-------APAWVP---------------------ASVRWLDAESVLDVVSAyeePPRVDVDadtPAYL 2182
Cdd:TIGR03098   95 DCNVRLLVTSSErldllhpALPGCHdlrtliivgdpahaseghpgeEPASWPKLLALGDADPP---HPVIDSD---MAAI 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2183 IYTSGSTGTPKGVVVSQGNLanyVAGVLPV---LDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELafdaqa 2259
Cdd:TIGR03098  169 LYTSGSTGRPKGVVLSHRNL---VAGAQSVatyLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLL------ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2260 laahlqahPVDCLKIVPSHlagllAAAGGTAVLP------------------RECLVTGGeALTGALVQQVRALAPTLRI 2321
Cdd:TIGR03098  240 --------PRDVLKALEKH-----GITGLAAVPPlwaqlaqldwpesaapslRYLTNSGG-AMPRATLSRLRSFLPNARL 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2322 VNHYGPTEttvGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFV 2401
Cdd:TIGR03098  306 FLMYGLTE---AFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2402 AHPLAPDRLLYR-----SGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGV 2472
Cdd:TIGR03098  383 PLPPFPGELHLPelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIV 462
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2473 LQLGACIQGSL--EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:TIGR03098  463 LVVTPPGGEELdrAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALA 515
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3530-4022 2.63e-47

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 180.18  E-value: 2.63e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3530 RRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRG 3609
Cdd:PRK06188    23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3610 FILEDSGVCLSVS------QRALAV--ELPGTA--LCLDD-PFTR---AQLDAVEPGEL--PEVPTEaPAYLIYTSGSTG 3673
Cdd:PRK06188   103 YVLEDAGISTLIVdpapfvERALALlaRVPSLKhvLTLGPvPDGVdllAAAAKFGPAPLvaAALPPD-IAGLAYTGGTTG 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVERLftAATQTGRFSFDEHD----VWSLFHSHAFDFAVwelwgAWLYGGRAVLVPEAvcrQPDAFLDLL 3749
Cdd:PRK06188   182 KPKGVMGTHRSIATM--AQIQLAEWEWPADPrflmCTPLSHAGGAFFLP-----TLLRGGTVIVLAKF---DPAEVLRAI 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3750 AEYGVTVLNQTPSAFYAL--QSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVSFHRLSD 3827
Cdd:PRK06188   252 EEQRITATFLVPTMIYALldHPDLRTRDLS-SLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEAPMVITYLRKRD 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3828 EDLQSPtSRIGSA---LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYR 3904
Cdd:PRK06188   330 HDPDDP-KRLTSCgrpTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--RDG--WLHTGDVARED 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3905 ADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLP 3983
Cdd:PRK06188   405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKG 484
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEGV 4022
Cdd:PRK06188   485 SVHAPKQVDFVDSLPLTALGKPDKKALRARYWEGRGRAV 523
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
2050-2522 5.44e-47

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: 177.76  E-value: 5.44e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05936     13 PDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHIL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwlDAESVLDVVSAYE-EPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL---ANY 2205
Cdd:cd05936     93 NDSGAKALI----------------VAVSFTDLLAAGApLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLvanALQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 VAGVLPVLDLGEDASLATLSTVAAdLGFT-ALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPSHLAGLLA 2284
Cdd:cd05936    157 IKAWLEDLLEGDDVVLAALPLFHV-FGLTvALLLPLALGATIVLIP---RFRPIGVLKEIRKHRVTIFPGVPTMYIALLN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2285 AAGGTAVLPRE--CLVTGGEALTGALVQQVRALAPTlRIVNHYGPTETtvGILTCTVPEEWPVEQGvPVGHPLAGNEAWV 2362
Cdd:cd05936    233 APEFKKRDFSSlrLCISGGAPLPVEVAERFEELTGV-PIVEGYGLTET--SPVVAVNPLDGPRKPG-SIGIPLPGTEVKI 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2363 LDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYR 2442
Cdd:cd05936    309 VDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DGWL-RTGDIGYMDEDGYFFIVDRKKDMIIVGGFN 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2443 VELGEVEQVLAQLPGVEVAAVLALPGANG--------VLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGN 2514
Cdd:cd05936    382 VYPREVEEVLYEHPAVAEAAVVGVPDPYSgeavkafvVLKEGASL--TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAV 459

                   ....*...
gi 1246793773 2515 GKIDRQAL 2522
Cdd:cd05936    460 GKILRREL 467
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1598-1974 9.96e-47

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: 174.80  E-value: 9.96e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLLESLRGDGAdpYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVP-HQIVLADAAAPWQ 1676
Cdd:cd19542      2 YPCTPMQEGMLLSQLRSPGL--YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKSLDPPIE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 TLDwSALDDAAQdaqlqrwLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYtagaQ 1756
Cdd:cd19542     80 EVE-TDEDSLDA-------LTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----N 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1757 GATLrlPPAPGFQAYLDWRERQDLARQRGWWRERLSGYAGTaalpapvaaaHHP--VQREECERRLSAHDS--ERLRAFC 1832
Cdd:cd19542    148 GQLL--PPAPPFSDYISYLQSQSQEESLQYWRKYLQGASPC----------AFPslSPKRPAERSLSSTRRslAKLEAFC 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1833 RERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLE 1912
Cdd:cd19542    216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 1913 VAENEAVGLGEILADSGLDADR-LFASLLVVENFPAmAPAQLPFALRVRETRA---ANHYALTLRV 1974
Cdd:cd19542    296 SLPHQHLSLREIQRALGLWPSGtLFNTLVSYQNFEA-SPESELSGSSVFELSAaedPTEYPVAVEV 360
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3529-3947 2.16e-46

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: 177.04  E-value: 2.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIA-VSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:cd05904     15 ASAHPSRPAlIDAATGrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQRALAVELPGTAL---CLDDPFTRAQ-----LDAVEPGELP--EVPTEAPAYLIYTSGSTGTPK 3676
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELAEKLASLALpvvLLDSAEFDSLsfsdlLFEADEAEPPvvVIKQDDVAALLYSSGTTGRSK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3677 GVVVTHRNverlFTAATQTGRFSFDEHD--------VWSLFHSHAFdfaVWELWGAWLYGGRAVLVPEAVCRqpdAFLDL 3748
Cdd:cd05904    175 GVMLTHRN----LIAMVAQFVAGEGSNSdsedvflcVLPMFHIYGL---SSFALGLLRLGATVVVMPRFDLE---ELLAA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3749 LAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHrLSD 3827
Cdd:cd05904    245 IERYKVTHLPVVPPIVLALVKSPIVDKYDLsSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC-FAP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3828 EDLQSPTSRIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRAD 3906
Cdd:cd05904    324 EKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEG---WLHTGDLCYIDED 400
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 3907 GSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT 3947
Cdd:cd05904    401 GYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVI 441
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2078-2523 2.22e-46

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: 175.71  E-value: 2.22e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAW----LPLDPQHPDARQIAVLDDSGARIVI-GWGAAPAWVPASVR 2152
Cdd:cd05922     10 LLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLglvfVPLNPTLKESVLRYLVADAGGRIVLaDAGAADRLRDALPA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2153 WLDAESVLDV---VSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAA 2229
Cdd:cd05922     90 SPDPGTVLDAdgiRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2230 DLGFTALFGALLSGRRVRL-----LPAELAFDAQALAahlqahpVDCLKIVPSHLAGLLAAAGGTAVLPRECLVT-GGEA 2303
Cdd:cd05922    170 DYGLSVLNTHLLRGATLVLtndgvLDDAFWEDLREHG-------ATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTqAGGR 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2304 LTGALVQQVRALAPTLRIVNHYGPTETTVGIltCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGG 2383
Cdd:cd05922    243 LPQETIARLRELLPGAQVYVMYGQTEATRRM--TYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2384 NLSLGYWQRAeqtaerfvAHPLAPDR--LLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVA 2461
Cdd:cd05922    321 NVMKGYWNDP--------PYRRKEGRggGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2462 AVLALPGANGVlQLGACIQGSLEG----VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:cd05922    393 AAVGLPDPLGE-KLALFVTAPDKIdpkdVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
87-507 2.66e-46

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: 174.98  E-value: 2.66e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDrciqgedSVAAGGGAAVESADL-- 164
Cdd:cd19546      4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILR-------TTFPGDGGDVHQRILda 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  165 -RGR--------GQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRA 235
Cdd:cd19546     77 dAARpelpvvpaTEEELPALLADRAAHLFDLTRETPWRCTLFALSDT-----EHVLLLVVHRIAADDESLDVLVRDLAAA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  236 Y--RVEcGLAAEPAPpLPCQYGDYARWQRDTLDRLDA-------SLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLR 306
Cdd:cd19546    152 YgaRRE-GRAPERAP-LPLQFADYALWERELLAGEDDrdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  307 LAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRV-RPELDSLVGLFVNTVVLRTQLHDDPD 385
Cdd:cd19546    230 LRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPT 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  386 FASLVARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRHDADLALD---LHGVQAHALTLPEDVAKHEL 462
Cdd:cd19546    310 FRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDapeLPGLRTSPVPLGTEAMELDL 389
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  463 TLEVLV------GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19546    390 SLALTErrnddgDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2050-2523 3.59e-46

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 176.24  E-value: 3.59e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK04813    16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGAAPAWVpASVRWLDAESVLDVVSAYEEPPRVD-VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:PRK04813    96 EVAKPSLIIATEELPLEI-LGIPVITLDELKDIFATGNPYDFDHaVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNW 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDASL---ATLSTvaaDLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAA 2285
Cdd:PRK04813   175 MLEDFALPEGPQFlnqAPYSF---DLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSFADMCLLD 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 AGGTAV-LPRecLVT---GGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWpVEQG--VPVGHPLAGNE 2359
Cdd:PRK04813   252 PSFNEEhLPN--LTHflfCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEM-LDQYkrLPIGYAKPDSP 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2360 AWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPdrlLYRSGDLARLDgEGRIVYLGRGDHQVKIR 2439
Cdd:PRK04813   329 LLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQP---AYHTGDAGYLE-DGLLFYQGRIDFQIKLN 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2440 GYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---QGSLEG-------VAEALAQRLPEYLCPSRWRAVESM 2509
Cdd:PRK04813   405 GYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVvpkEEDFERefeltkaIKKELKERLMEYMIPRKFIYRDSL 484
                          490
                   ....*....|....
gi 1246793773 2510 PRLGNGKIDRQALA 2523
Cdd:PRK04813   485 PLTPNGKIDRKALI 498
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
3529-4010 1.63e-45

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 174.28  E-value: 1.63e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLI-RQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAAR 3607
Cdd:PRK06839    12 AYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3608 RGFILEDSG---VCLSVSQRALAVELPGTA-----LCLDDP---FTRAQLDAVEPGElpevptEAPAYLIYTSGSTGTPK 3676
Cdd:PRK06839    92 LIFQLKDSGttvLFVEKTFQNMALSMQKVSyvqrvISITSLkeiEDRKIDNFVEKNE------SASFIICYTSGTTGKPK 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3677 GVVVTHRNVerLFTAATQTGRFSFDEHDV----WSLFHSHAFD-FAvwelWGAWLYGGRaVLVPEAVcrQPDAFLDLLAE 3751
Cdd:PRK06839   166 GAVLTQENM--FWNALNNTFAIDLTMHDRsivlLPLFHIGGIGlFA----FPTLFAGGV-IIVPRKF--EPTKALSMIEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRER-YPQAElvnMYGITETTVHVSFhrLSDED 3829
Cdd:PRK06839   237 HKVTVVMGVPTIHQALINCSKFETTNLQsVRWFYNGGAPCPEELMREFIDRgFLFGQ---GFGMTETSPTVFM--LSEED 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSL 3909
Cdd:PRK06839   312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--QDG--WLCTGDLARVDEDGFV 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3910 EYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLP 3988
Cdd:PRK06839   388 YIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVgRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIP 467
                          490       500
                   ....*....|....*....|..
gi 1246793773 3989 RLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06839   468 KEIVFLKELPKNATGKIQKAQL 489
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
536-1041 2.24e-45

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: 173.79  E-value: 2.24e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  536 NVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALClpRGLDWYCL--LLGAWRAGLSVI 613
Cdd:TIGR01734    1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVY--GHMEPHMLvaFLGSIKSGHAYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  614 PLDTEWPQARRAEVVAASGCDAVLTdAQGLAGFAPSVAI----AVDELKLDGAgeNGSGENA-APNQLAYILYTSGSTGI 688
Cdd:TIGR01734   79 PVDTSIPSERIEMIIEAAGPELVIH-TAELSIDAVGTQIitlsALEQAETSGG--PVSFDHAvKGDDNYYIIYTSGSTGN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  689 PKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARP-DELLEPQRFLAFLSERAITV 767
Cdd:TIGR01734  156 PKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDkDITNNFKLLFEELPKTGLNV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  768 TDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQrwfELgLDR--RCALINAYGPTEAT--ISSHYHRVQAID 843
Cdd:TIGR01734  236 WVSTPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAK---AL-LERfpKATIYNTYGPTEATvaVTSVKITQEILD 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  844 ASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpSGESLRMYRSGDRVRLlD 923
Cdd:TIGR01734  312 QYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF-----SHEGQPAYRTGDAGTI-T 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  924 DGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA--GVVGEGAAQRLVAWVECAGEDgfgqadlnqTDSDQTE 1001
Cdd:TIGR01734  386 DGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVvpKYNKDHKVEYLIAAIVPETED---------FEKEFQL 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1246793773 1002 SERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:TIGR01734  457 TKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
89-507 2.88e-45

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: 171.73  E-value: 2.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGED-----SVAAGGGAAVESAD 163
Cdd:cd20484      3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDgvpfqKIEPSKPLSFQEED 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  164 LRGRGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYR-VECGL 242
Cdd:cd20484     83 ISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQ-----EHFVLITIHHIIFDGSSSLTLIHSLLDAYQaLLQGK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  243 AAEPAPPLPcQYGDYARWQRDTLDRLD--ASLRHHVEALSGA-PHLhELPLDHERPAVLGQSGAKLRLAFPPGLSERVAA 319
Cdd:cd20484    158 QPTLASSPA-SYYDFVAWEQDMLAGAEgeEHRAYWKQQLSGTlPIL-ELPADRPRSSAPSFEGQTYTRRLPSELSNQIKS 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  320 YAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASLVarcRDHQLA 399
Cdd:cd20484    236 FARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFI---RKLQLT 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  400 ---ALEHQALPLERVIETLQVERSSRHAPLFQLMFA----LRHDadlalDLHGVQAH-----ALTLPEDVAK---HELTL 464
Cdd:cd20484    313 vldGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFyqnfLQST-----SLQQFLAEyqdvlSIEFVEGIHQegeYELVL 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1246793773  465 EVLVGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd20484    388 EVYEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
2052-2519 3.74e-45

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: 171.25  E-value: 3.74e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:cd17631     11 RTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILAD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdvdaDTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP 2211
Cdd:cd17631     91 SGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALA 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2212 VLDLGEDASL---ATLSTVAADLGFTalFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPS-HLAGLLAAAG 2287
Cdd:cd17631    133 ALDLGPDDVLlvvAPLFHIGGLGVFT--LPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTmIQALLQHPRF 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2288 GTAVLPR-ECLVTGGEALTGALVQQVRALAPtlRIVNHYGPTETTVGIltCTVPEEWPVEQGVPVGHPLAGNEAWVLDRF 2366
Cdd:cd17631    208 ATTDLSSlRAVIYGGAPMPERLLRALQARGV--KFVQGYGMTETSPGV--TFLSPEDHRRKLGSAGRPVFFVEVRIVDPD 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:cd17631    284 GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-------WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPA 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGAciQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:cd17631    357 EVEDVLYEHPAVAEVAVIGVPDekwgeavvAVVVPRPGA--ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434

                   .
gi 1246793773 2519 R 2519
Cdd:cd17631    435 K 435
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
87-496 1.85e-44

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: 169.36  E-value: 1.85e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQ-----GEDSVAAGGGAAVES 161
Cdd:cd20483      1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFegddfGEQQVLDDPSFHLIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRGRGQDE--IDALVEGFRLRPFELQRQRPLRMQLLRLdgqgdgPVRHW-LQVVVHHIACD-GVSLGLLTQ--DLSRA 235
Cdd:cd20483     81 IDLSEAADPEaaLDQLVRNLRRQELDIEEGEVIRGWLVKL------PDEEFaLVLASHHIAWDrGSSKSIFEQftALYDA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  236 YRVECGLAAEPAPPLpcQYGDYARWQRDTLDrlDASLRHHV----EALSGAPHLHE-LPLDH-ERPAVLGQSGAKLRLAF 309
Cdd:cd20483    155 LRAGRDLATVPPPPV--QYIDFTLWHNALLQ--SPLVQPLLdfwkEKLEGIPDASKlLPFAKaERPPVKDYERSTVEATL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  310 PPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDDPDFASL 389
Cdd:cd20483    231 DKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDL 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  390 VARCRDHQLAALEHQALPLERVIETLQVERSSRHAPLFQLMFALRhdadlaldLHGVQAHALTLPEDVAKH--------- 460
Cdd:cd20483    311 LESTKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ--------VHGKFPEYDTGDFKFTDYdhydiptac 382
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1246793773  461 ELTLEVL-VGAGGMSAVWEYNTALWNPATVARWAERY 496
Cdd:cd20483    383 DIALEAEeDPDGGLDLRLEFSTTLYDSADMERFLDNF 419
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
3547-4010 2.83e-43

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: 166.14  E-value: 2.83e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAARrgfiLEDSGVCLSVS 3622
Cdd:cd05969      3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDR----LENSEAKVLIT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 QRALAvelpgtalclddpftraqlDAVEPgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTGRFSFDE 3702
Cdd:cd05969     79 TEELY-------------------ERTDP--------EDPTLLHYTSGTTGTPKGVLHVHDAM----IFYYFTGKYVLDL 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3703 HD---VWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQ--AMRRELA 3777
Cdd:cd05969    128 HPddiYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIRMLMKEgdELARKYD 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LN-VRAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSFHRLSDEdlQSPTSrIGSALPDLAVHVLDAAGQPV 3856
Cdd:cd05969    206 LSsLRFIHSVGEPLNPEAIR-WGMEVFGVPIHDTWWQTETGSIMIANYPCMP--IKPGS-MGKPLPGVKAAVVDENGNEL 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PLGVVGELVVEGD--GVAQGYWQRPELTAERFVerGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:cd05969    282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFI--DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3935 IASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDpQSLREAL----RALLPDYMLPRLIQLLPALPLTANGKLDRKA 4009
Cdd:cd05969    358 LMEHPAVAEAGVIgKPDPLRGEIIKAFISLKEGFEPS-DELKEEIinfvRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436

                   .
gi 1246793773 4010 L 4010
Cdd:cd05969    437 L 437
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1600-1839 4.69e-43

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 159.05  E-value: 4.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1600 LTPLQRGVLLEslrGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLD 1679
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1680 WSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGAT 1759
Cdd:COG4908     77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1760 LRLPPAPG-FQAYLDW----RERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQR-EECERRLSAHDSERLRAFCR 1833
Cdd:COG4908    157 PPLPELPIqYADYAAWqrawLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRgATLSFTLPAELTEALKALAK 236

                   ....*.
gi 1246793773 1834 ERGCTL 1839
Cdd:COG4908    237 AHGATV 242
PRK07514 PRK07514
malonyl-CoA synthase; Validated
3518-4010 6.10e-43

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 166.59  E-value: 6.10e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3518 TGNLVSRFAEIARRyPARIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:PRK07514     2 NNNLFDALRAAFAD-RDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPVDPHAPAARRGFILEDSG----VCLSVSQRALA--VELPGTA--LCLDDPFT--RAQLDAVEPGELPEVPTEA--PAY 3664
Cdd:PRK07514    81 LPLNTAYTLAELDYFIGDAEpalvVCDPANFAWLSkiAAAAGAPhvETLDADGTgsLLEAAAAAPDDFETVPRGAddLAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFDFAvweLWGAWLYGGRAVLVPEAvcr 3740
Cdd:PRK07514   161 ILYTSGTTGRSKGAMLSHGNL--LSNALTLVDYWRFTPDDVLihalPIFHTHGLFVA---TNVALLAGASMIFLPKF--- 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 QPDAFLDLLAEygVTVLNQTPSaFYA--LQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELvNMYGITETTV 3818
Cdd:PRK07514   233 DPDAVLALMPR--ATVMMGVPT-FYTrlLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL-ERYGMTETNM 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3819 HVSfHRLSDEdlqsptsRI----GSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PRK07514   309 NTS-NPYDGE-------RRagtvGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG--- 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQ-----GEGAwlMAYAVAADGAE 3968
Cdd:PRK07514   378 FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI--GVphpdfGEGV--TAVVVPKPGAA 453
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1246793773 3969 PDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07514   454 LDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
3082-3491 6.58e-43

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: 164.47  E-value: 6.58e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQ--LPHRQVSLPLA 3159
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQeiLPPGPAPLEVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 EQDWSGLEPAQARSRLSELQAQQceaGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRE 3239
Cdd:cd19539     83 DLSDPDSDRERRLEELLRERESR---GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3240 SRTPQLPAAP-PFRDYLHWLRGQDE----AAARAFWREQLTGLEPAALPEA-TEPAE-GYASSTRRFDL-----AAASAW 3307
Cdd:cd19539    160 GPAAPLPELRqQYKEYAAWQREALAapraAELLDFWRRRLRGAEPTALPTDrPRPAGfPYPGADLRFELdaelvAALREL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3308 AQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAgvERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNL 3387
Cdd:cd19539    240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRF--ESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3388 DLRTHGYLPLAQIQrAGAADAVSP-----FDVLLVFENLPTESREERSGMRIEEL-DHRAHSNYPLMLTAIPDAGGLRIE 3461
Cdd:cd19539    318 DAQRHQELPFQQLV-AELPVDRDAgrhplVQIVFQVTNAPAGELELAGGLSYTEGsDIPDGAKFDLNLTVTEEGTGLRGS 396
                          410       420       430
                   ....*....|....*....|....*....|
gi 1246793773 3462 AALDRSKLDGWLVEQMLDDLDFVLQQVPAL 3491
Cdd:cd19539    397 LGYATSLFDEETIQGFLADYLQVLRQLLAN 426
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3529-4005 9.40e-43

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 166.65  E-value: 9.40e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLcLPRGCDLLVAL-LAILKTGAAYVPVDPHAPAAR 3607
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSDAYALLwLACARAGAVHVPVNFMLTGEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3608 RGFILEDSGVCLSVSQRALA--VELPGTALCLDDPFTRAQLDAVEPGE-----------------LPEVPTEAPAYLIYT 3668
Cdd:PRK08316   100 LAYILDHSGARAFLVDPALAptAEAALALLPVDTLILSLVLGGREAPGgwldfadwaeagsvaepDVELADDDLAQILYT 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3669 SGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWS--LFHS---HAFdfavwelWGAWLY-GGRAVLVPEAvcrQP 3742
Cdd:PRK08316   180 SGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHAlpLYHCaqlDVF-------LGPYLYvGATNVILDAP---DP 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYALQSQAM--RRELAlNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITE----T 3816
Cdd:PRK08316   250 ELILRTIEAERITSFFAPPTVWISLLRHPDfdTRDLS-SLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEiaplA 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVhvsfhrLSDEDLQsptSRIGSA-LPDLAVH--VLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqr 3893
Cdd:PRK08316   329 TV------LGPEEHL---RRPGSAgRPVLNVEtrVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF--RGG-- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWLMAYA---VAADGAEPD 3970
Cdd:PRK08316   396 WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI--GLPDPKWIEAVTavvVPKAGATVT 473
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 3971 PQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK08316   474 EDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1645-1978 1.14e-42

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: 163.68  E-value: 1.14e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1645 VRRQPMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRY 1724
Cdd:cd19531     49 VARHEALRTTFVEVD-GEPVQVILPPLPLPLPVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEH 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1725 WLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgFQaYLD-------WRERQDLARQRGWWRERLSG---- 1793
Cdd:cd19531    128 VLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPPLP-IQ-YADyavwqreWLQGEVLERQLAYWREQLAGappv 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1794 --------------YAGtaalpapvaaahhpvqrEECERRLSAHDSERLRAFCRERGCTLSdliaMV----WGLANARYG 1855
Cdd:cd19531    206 lelptdrprpavqsFRG-----------------ARVRFTLPAELTAALRALARREGATLF----MTllaaFQVLLHRYS 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1856 NHDDVVLGATRSGRP-PELagvESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILADsgLDADR 1934
Cdd:cd19531    265 GQDDIVVGTPVAGRNrAEL---EGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLVEA--LQPER 339
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 1935 ------LFASLLVVENFPaMAPAQLPfALRVRETRAANHYA---LTLRVSERE 1978
Cdd:cd19531    340 dlsrspLFQVMFVLQNAP-AAALELP-GLTVEPLEVDSGTAkfdLTLSLTETD 390
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
89-507 1.14e-42

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: 163.91  E-value: 1.14e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVESA 162
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLgeplqvVLKDRKLPWREL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  163 DLRGRGQDEIDALVEGF----RLRPFELQRQRPLRMQLLRLdgqgdGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYR- 237
Cdd:cd19543     83 DLSHLSEAEQEAELEALaeedRERGFDLARAPLMRLTLIRL-----GDDRYRLVWSFHHILLDGWSLPILLKELFAIYAa 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  238 VECGLAAEPAPPLPcqYGDYARW--QRDtldrLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSE 315
Cdd:cd19543    158 LGEGQPPSLPPVRP--YRDYIAWlqRQD----KEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  316 RVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRvRPELD---SLVGLFVNTVVLRTQLHDDPDFASLVAR 392
Cdd:cd19543    232 RLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELPgieTMVGLFINTLPVRVRLDPDQTVLELLKD 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  393 CRDHQLAALEHQALPLERVietlQvERSSRHAPLFQLMFALRHDADLALDLHGVQAHALTLpEDVAKHE-----LTLEVL 467
Cdd:cd19543    311 LQAQQLELREHEYVPLYEI----Q-AWSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRI-TDVSAEEqtnypLTVVAI 384
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1246793773  468 VGaGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19543    385 PG-EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
3518-4010 6.21e-42

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: 163.45  E-value: 6.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3518 TGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYV 3597
Cdd:cd05923      2 TVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 PVDPHAPAARRGFILEDSGVCLSVSQRALAV--ELPGTALCL----DDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGS 3671
Cdd:cd05923     82 LINPRLKAAELAELIERGEMTAAVIAVDAQVmdAIFQSGVRVlalsDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3672 TGTPKGVVVTHRNVE-RLFTAATQTGrFSFDEHDV----WSLFHSHAFdFAVweLWGAWLYGGRAVLVPEAvcrQPDAFL 3746
Cdd:cd05923    162 TGLPKGAVIPQRAAEsRVLFMSTQAG-LRHGRHNVvlglMPLYHVIGF-FAV--LVAALALDGTYVVVEEF---DPADAL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3747 DLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTvhvsfhrl 3825
Cdd:cd05923    235 KLIEQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLERV-NQHLPGEKVNIYGTTEAM-------- 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3826 sdEDLQSPTSRIGSAL-PDL-----AVHVLDAAGQPVPLGVVGELVV--EGDGVAQGYWQRPELTAERFVErggqRFYRS 3897
Cdd:cd05923    306 --NSLYMRDARTGTEMrPGFfsevrIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD----GWYRT 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3898 GDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAePDPQSLRE 3976
Cdd:cd05923    380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACVVPREGT-LSADELDQ 458
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 3977 ALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05923    459 FCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
539-1043 6.81e-42

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: 163.80  E-value: 6.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTE 618
Cdd:TIGR03098    4 HLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  619 WPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA--------IAVDEL----------------KLDGAGENGSGENAAPN 674
Cdd:TIGR03098   84 LKAEQVAHILADCNVRLLVTSSERLDLLHPALPgchdlrtlIIVGDPahaseghpgeepaswpKLLALGDADPPHPVIDS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVarPDELLEPQ 754
Cdd:TIGR03098  164 DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV--LHDYLLPR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  755 RFLAFLSERAIT-VTDLAPAYAnELVRasvaDDWRDLA---LRCLVVGGDVLPVALAQRWFELGLDRRCALInaYGPTEA 830
Cdd:TIGR03098  242 DVLKALEKHGITgLAAVPPLWA-QLAQ----LDWPESAapsLRYLTNSGGAMPRATLSRLRSFLPNARLFLM--YGLTEA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  831 tISSHYHRVQAIDaSRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPL-RLPSGES 909
Cdd:TIGR03098  315 -FRSTYLPPEEVD-RRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLpPFPGELH 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  910 LR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECAGEDG 986
Cdd:TIGR03098  393 LPelAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVaEAVAFGVPDPTLGQAIVLVVTPPGGEE 472
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  987 FGQADLnqtdsdqteserwHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:TIGR03098  473 LDRAAL-------------LAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
2061-2540 5.75e-41

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 162.20  E-value: 5.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLdpqHPD--ARQIAV-LDDSGARIV 2137
Cdd:COG0365     39 TLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV---FPGfgAEALADrIEDAEAKVL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2138 I----GW------------GAAPAWVPaSVR----------------WLDAESVLDVVSAYEEPprVDVDADTPAYLIYT 2185
Cdd:COG0365    116 ItadgGLrggkvidlkekvDEALEELP-SLEhvivvgrtgadvpmegDLDWDELLAAASAEFEP--EPTDADDPLFILYT 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2186 SGSTGTPKGVVVSQGNLANYVAGVLP-VLDLGEDASLATlstvAADLGFT-----ALFGALLSGRRVRLLPAELAF-DAQ 2258
Cdd:COG0365    193 SGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWC----TADIGWAtghsyIVYGPLLNGATVVLYEGRPDFpDPG 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVP-------SHLAGLLAAAGGTAVlprECLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETT 2331
Cdd:COG0365    269 RLWELIEKYGVTVFFTAPtairalmKAGDEPLKKYDLSSL---RLLGSAGEPLNPEVWEWWYE-AVGVPIVDGWGQTETG 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2332 VGILTCtvPEEWPVEQGVPvGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLS--LGYWQRAEQTAERFVAHPlaPDr 2409
Cdd:COG0365    345 GIFISN--LPGLPVKPGSM-GKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGRF--PG- 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 lLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANG--------VLQLGAciQG 2481
Cdd:COG0365    419 -WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRgqvvkafvVLKPGV--EP 495
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2482 SLEGVAE---ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDA-DSSA----EAIDE 2540
Cdd:COG0365    496 SDELAKElqaHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLgDTSTledpEALDE 562
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3525-4006 7.46e-41

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 161.21  E-value: 7.46e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP 3604
Cdd:PRK07798     9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3605 AARRGFILEDSGVCLSVSQRALA-------VELPG--TALCLDDPFTRAQL-------DAVEPGElPEVPTEAPA----Y 3664
Cdd:PRK07798    89 EDELRYLLDDSDAVALVYEREFAprvaevlPRLPKlrTLVVVEDGSGNDLLpgavdyeDALAAGS-PERDFGERSpddlY 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVER-LFTAAT-QTGRFSFDEHDVWS---------------LFHSHAFdfavWELWGAWLY 3727
Cdd:PRK07798   168 LLYTGGTTGMPKGVMWRQEDIFRvLLGGRDfATGEPIEDEEELAKraaagpgmrrfpappLMHGAGQ----WAAFAALFS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 GGRAVLVPEAVCRqPDAFLDLLAEYGVTVLNQTPSAFYA--LQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQ 3804
Cdd:PRK07798   244 GQTVVLLPDVRFD-ADEVWRTIEREKVNVITIVGDAMARplLDALEARGPYDLsSLFAIASGGALFSPSVKEALLELLPN 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 AELVNMYGITETTVHvSFHRLSDEDLQSPTSRIGsalPDLAVHVLDAAGQPVPLG--VVGELVVEGDgVAQGYWQRPELT 3882
Cdd:PRK07798   323 VVLTDSIGSSETGFG-GSGTVAKGAVHTGGPRFT---IGPRTVVLDEDGNPVEPGsgEIGWIARRGH-IPLGYYKDPEKT 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3883 AERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWlmAYAV 3962
Cdd:PRK07798   398 AETFPTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV--GVPDERW--GQEV 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773 3963 AA-----DGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK07798   474 VAvvqlrEGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3535-4010 1.45e-40

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: 158.03  E-value: 1.45e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGELDYATLDRRSSQLATLLIRQGAG-PGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILE 3613
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3614 DSGvclsvsqralavelPGTALCLDdpftraQLDAVEPgelpevpteaPAYLIYTSGSTGTPKGVVVTHRNVERLF-TAA 3692
Cdd:cd05958     81 KAR--------------ITVALCAH------ALTASDD----------ICILAFTSGTTGAPKATMHFHRDPLASAdRYA 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3693 TQTGRFSFDEHDVWS--LFHSHAFDFAVWELWGAwlyGGRAVLVPEAVcrqPDAFLDLLAEYGVTVLNQTPSAFYA-LQS 3769
Cdd:cd05958    131 VNVLRLREDDRFVGSppLAFTFGLGGVLLFPFGV---GASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAmLAH 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3770 QAMRRELALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITEttvhvSFHRL--SDEDLQSPtSRIGSALPDLAVH 3847
Cdd:cd05958    205 PDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTE-----MFHIFisARPGDARP-GATGKPVPGYEAK 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VLDAAGQPVPLGVVGELVVEGDgvaQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIE 3927
Cdd:cd05958    278 VVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGG---WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3928 PGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:cd05958    352 PPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431

                   ....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd05958    432 KLQRFAL 438
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3525-4007 1.64e-40

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 160.71  E-value: 1.64e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPAR--IAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPH 3602
Cdd:PRK12583    24 FDATVARFPDReaLVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 APAARRGFILEDSGV----CL----SVSQRALAVEL--------PGTALCLDDPFTR--AQLDAVEPGEL---PEVPTEA 3661
Cdd:PRK12583   104 YRASELEYALGQSGVrwviCAdafkTSDYHAMLQELlpglaegqPGALACERLPELRgvVSLAPAPPPGFlawHELQARG 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 -------------------PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFDFAV 3718
Cdd:PRK12583   184 etvsrealaerqasldrddPINIQYTSGTTGFPKGATLSHHNI--LNNGYFVAESLGLTEHDRLcvpvPLYHCFGMVLAN 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3719 WelwgAWLYGGRAVLVPeAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQP 3797
Cdd:PRK12583   262 L----GCMTVGACLVYP-NEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSsLRTGIMAGAPCPIEVMRR 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WRERYPQAELVNMYGITETTvHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQ 3877
Cdd:PRK12583   337 VMDEMHMAEVQIAYGMTETS-PVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWN 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAW 3956
Cdd:PRK12583   416 NPEATAESIDEDG---WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFgVPDEKYGEE 492
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3957 LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:PRK12583   493 IVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
2051-2524 2.22e-40

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: 157.45  E-value: 2.22e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVG-VQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIgwgaapawvpasvrwldaesvldvvsayeepprvdvdadTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG- 2208
Cdd:cd05941     81 TDSEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAl 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 -----------VLPVLDLGEDASLatlstvaadlgFTALFGALLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVP- 2276
Cdd:cd05941    122 vdawrwteddvLLHVLPLHHVHGL-----------VNALLCPLFAGASVEFLPK---FDPKEVAISRLMPSITVFMGVPt 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 -------SHLAGLLAAAGGTAVLPREC--LVTGGEALTGALVQQVRALApTLRIVNHYGPTETtvGILTcTVPEEWPVEQ 2347
Cdd:cd05941    188 iytrllqYYEAHFTDPQFARAAAAERLrlMVSGSAALPVPTLEEWEAIT-GHTLLERYGMTEI--GMAL-SNPLDGERRP 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVpVGHPLAGNEAWVLDRF-GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLlYRSGDLARLDGEGRI 2426
Cdd:cd05941    264 GT-VGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD-----DGW-FKTGDLGVVDEDGYY 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2427 VYLGRG-DHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN-G-------VLQLGACiQGSLEGVAEALAQRLPEY 2497
Cdd:cd05941    337 WILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGervvavvVLRAGAA-ALSLEELKEWAKQRLAPY 415
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 2498 LCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05941    416 KRPRRLILVDELPRNAMGKVNKKELRK 442
PRK09088 PRK09088
acyl-CoA synthetase; Validated
3529-4010 7.77e-40

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 157.28  E-value: 7.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVS--AEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK09088     5 ARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQRALAVelpGTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNve 3686
Cdd:PRK09088    85 ELDALLQDAEPRLLLGDDAVAA---GRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN-- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3687 rLFTAATQTGRFSFDEHDvwSLFHSHAFDFAVWELWGAW---LYGGRAVLVPEAVcrQPDAFLDLLAE--YGVTVLNQTP 3761
Cdd:PRK09088   160 -LQQTAHNFGVLGRVDAH--SSFLCDAPMFHIIGLITSVrpvLAVGGSILVSNGF--EPKRTLGRLGDpaLGITHYFCVP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALQSQAMRRELALNVRAVVFGGEALEPSR-LQPWRERypQAELVNMYGITET-TVhvsFHRLSDEDLQSptSRIGS 3839
Cdd:PRK09088   235 QMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEdILGWLDD--GIPMVDGFGMSEAgTV---FGMSVDCDVIR--AKAGA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3840 A---LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:PRK09088   308 AgipTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDG---WFRTGDIARRDADGFFWVVDRKK 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQL 3993
Cdd:PRK09088   385 DMFISGGENVYPAEIEAVLADHPGIRECAVV--GMADAQWgevGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRL 462
                          490
                   ....*....|....*..
gi 1246793773 3994 LPALPLTANGKLDRKAL 4010
Cdd:PRK09088   463 VDALPRTASGKLQKARL 479
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3510-3946 9.28e-40

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 159.11  E-value: 9.28e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3510 TSRERYACTGNLVSRFAEIARRYPARIAVSAEDG----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVA 3585
Cdd:COG1022      2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3586 LLAILKTGAAYVPVDPHAPAARRGFILEDSGV-CLSVS-----QRALAV--ELPG--TALCLDDPFTRAQLDAV------ 3649
Cdd:COG1022     82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAkVLFVEdqeqlDKLLEVrdELPSlrHIVVLDPRGLRDDPRLLsldell 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3650 -------EPGELPEVPTEA----PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVWSLF--HSHAFDF 3716
Cdd:COG1022    162 algrevaDPAELEARRAAVkpddLATIIYTSGTTGRPKGVMLTHRNL--LSNARALLERLPLGPGDRTLSFlpLAHVFER 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3717 aVWELwgAWLYGGRAVlvpeAVCRQPDAFLDLLAEYGVTVL--------------------------------------- 3757
Cdd:COG1022    240 -TVSY--YALAAGATV----AFAESPDTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkrklfrwalavgrry 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3758 ------NQTPSAFYALQSQ--------AMRRELALNVRAVVFGGEALEPsRLQpwreRYPQA---ELVNMYGITETTVHV 3820
Cdd:COG1022    313 ararlaGKSPSLLLRLKHAladklvfsKLREALGGRLRFAVSGGAALGP-ELA----RFFRAlgiPVLEGYGLTETSPVI 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDedlqsptSRIGSalpdlavhvldaAGQPVP-----LGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFY 3895
Cdd:COG1022    388 TVNRPGD-------NRIGT------------VGPPLPgvevkIAEDGEILVRGPNVMKGYYKNPEATAEAFDADG---WL 445
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3896 RSGDLGRYRADGSLEYRGRGDDQVKLR-GYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:COG1022    446 HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
282-1101 1.00e-39

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: 163.70  E-value: 1.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  282 APHLHELPLDHERPAVLGQSGAKLRLAFPPglservAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRP 361
Cdd:TIGR03443    8 NPTLSVLPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  362 eldslvglfvntVVLRTQLHDDPDFASLVARCRDHQLAALEHQALPLERVIETLQVE-RSSRHAPLFQLMFalrhdadla 440
Cdd:TIGR03443   82 ------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAkKLERTPPLFRLAF--------- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  441 LDLHGVQAhaltlpEDVAKHELT-LEVLVGAGGMSAVWE--YNTALWNPATVARWAERYFVALAAMLENPHEPALSWPwp 517
Cdd:TIGR03443  141 QDAPDNQQ------TTYSTGSTTdLTVFLTPSSPELELSiyYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVS-- 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  518 adeLALDDKRE--PAPRT-------VGNVVDAIARAADEFPER-------AALETAQGR--LSYRELLTAADARAAALRR 579
Cdd:TIGR03443  213 ---LITPSQKSllPDPTKdldwsgfRGAIHDIFADNAEKHPDRtcvvetpSFLDPSSKTrsFTYKQINEASNILAHYLLK 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  580 RLGAQARSVALCLPRGLDWYCLLLGAWRAG--LSVIplDTEWPQAR----------RAEVVAASgcdavltdaqglAG-F 646
Cdd:TIGR03443  290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGatFSVI--DPAYPPARqtiylsvakpRALIVIEK------------AGtL 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  647 APSVAIAVD-ELKL-----------DGAGENGSGENAAPNQLAYIL--------------------YTSGSTGIPKGVEV 694
Cdd:TIGR03443  356 DQLVRDYIDkELELrteipalalqdDGSLVGGSLEGGETDVLAPYQalkdtptgvvvgpdsnptlsFTSGSEGIPKGVLG 435
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  695 GHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELLEPQRFLAFLSERAITVTDLAPA 773
Cdd:TIGR03443  436 RHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAqLLVPTADDIGTPGRLAEWMAKYGATVTHLTPA 515
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  774 YANELVRASVAddwRDLALRCLVVGGDVLP-------VALAQrwfelgldrRCALINAYGPTEATISSHYHRVQAIDASR 846
Cdd:TIGR03443  516 MGQLLSAQATT---PIPSLHHAFFVGDILTkrdclrlQTLAE---------NVCIVNMYGTTETQRAVSYFEIPSRSSDS 583
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  847 P--------VPLG------QLLpgriaaVLDAHGRIVPRGV--CGELALGGIGLAEGYRGDAAASERRFA------PLRL 904
Cdd:TIGR03443  584 TflknlkdvMPAGkgmknvQLL------VVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdPSHW 657
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  905 PS--------------GESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEG 970
Cdd:TIGR03443  658 IDldkennkperefwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDK 737
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  971 AAQR-LVAWVecagEDGFGQADLNQ--TDSDQTESE-------RWHRALCE--------RLPAYMVPTQFVALPRLPRNA 1032
Cdd:TIGR03443  738 DEEPtLVSYI----VPQDKSDELEEfkSEVDDEESSdpvvkglIKYRKLIKdireylkkKLPSYAIPTVIVPLKKLPLNP 813
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1033 SGKIDRRALPAPPV--LAQAERTPPRTAEESALCE-------VWAEVL---QCEVGIHDSFFRLGGDSIRSLQVVARLRE 1100
Cdd:TIGR03443  814 NGKVDKPALPFPDTaqLAAVAKNRSASAADEEFTEtereirdLWLELLpnrPATISPDDSFFDLGGHSILATRMIFELRK 893

                   .
gi 1246793773 1101 R 1101
Cdd:TIGR03443  894 K 894
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
3529-4019 9.49e-39

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: 154.96  E-value: 9.49e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAV-----SAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVdPHA 3603
Cdd:cd05970     27 AKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA-THQ 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAAR-----------RGFILEDSGVCLSVSQRALA--VELPGTALCLDD------PFTRAQLDAVEPGELPEVPTEA--- 3661
Cdd:cd05970    106 LTAKdivyriesadiKMIVAIAEDNIPEEIEKAAPecPSKPKLVWVGDPvpegwiDFRKLIKNASPDFERPTANSYPcge 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 -PAYLIYTSGSTGTPKgvVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVW-ELWGAWLyGGRAVLVPEAVC 3739
Cdd:cd05970    186 dILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWI-AGAAVFVYDYDK 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 RQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRErYPQAELVNMYGITETTVH 3819
Cdd:cd05970    263 FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTETTLT 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3820 V-SFHRLSDEdlqsPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD-----GVAQGYWQRPELTAERFVERggqr 3893
Cdd:cd05970    342 IaTFPWMEPK----PGS-MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG---- 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDpq 3972
Cdd:cd05970    413 YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTgVPDPIRGQVVKATIVLAKGYEPS-- 490
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3973 slrEALRALLPD--------YMLPRLIQLLPALPLTANGKLDRKalpkpETQDRD 4019
Cdd:cd05970    491 ---EELKKELQDhvkkvtapYKYPRIVEFVDELPKTISGKIRRV-----EIRERD 537
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
537-1041 9.57e-39

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: 153.49  E-value: 9.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  617 tewPQARRAEVvaasgcDAVLTDAQglagfaPSVAIAVDELKLDGAGENGSGENAA--PNQLAYILYTSGSTGIPKGVEV 694
Cdd:cd05936     81 ---PLYTPREL------EHILNDSG------AKALIVAVSFTDLLAAGAPLGERVAltPEDVAVLQYTSGTTGVPKGAML 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  695 GHA--ALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGACVVARPDelLEPQRFLAFLSERAIT 766
Cdd:cd05936    146 THRnlVANALQIKAWLEDLLEGDDVVLaalplfHVFGLTV-----ALLLPLALGATIVLIPR--FRPIGVLKEIRKHRVT 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  767 VTDLAPAYANELVRAsVADDWRDL-ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEATISSHYHRVQaiDAS 845
Cdd:cd05936    219 IFPGVPTMYIALLNA-PEFKKRDFsSLRLCISGGAPLPVEVAERFEEL---TGVPIVEGYGLTETSPVVAVNPLD--GPR 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  846 RPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLpsgeslrmyRSGDRVRLLDDG 925
Cdd:cd05936    293 KPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL---------RTGDIGYMDEDG 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  926 ELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteser 1004
Cdd:cd05936    364 YFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVvGVPDPYSGEAVKAFVVLKEGASLTEEEI------------ 431
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 1005 whRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05936    432 --IAFCrEQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3547-4005 1.04e-38

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: 155.81  E-value: 1.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAAR------RGFILEDSG 3616
Cdd:cd17634     87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfggfAPEAVAGRiidsssRLLITADGG 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 V-------CLSVSQRALAVELPG--TALCLD------------DPFTRAQLDAVEPGELPE-VPTEAPAYLIYTSGSTGT 3674
Cdd:cd17634    167 VragrsvpLKKNVDDALNPNVTSveHVIVLKrtgsdidwqegrDLWWRDLIAKASPEHQPEaMNAEDPLFILYTSGTTGK 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3675 PKGVVVTHRNverLFTAATQTGRFSFDEH--DVWSLFHSHAfdfavWELWGAWL-YG----GRAVLVPEAVCRQPDA--F 3745
Cdd:cd17634    247 PKGVLHTTGG---YLVYAATTMKYVFDYGpgDIYWCTADVG-----WVTGHSYLlYGplacGATTLLYEGVPNWPTParM 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTPSAFYALQ---SQAMRRELALNVRAVVFGGEALEPsrlQPWR--------ERYPqaeLVNMYGIT 3814
Cdd:cd17634    319 WQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINP---EAYEwywkkigkEKCP---VVDTWWQT 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTVHVSFHRLSDEDLQSPTSRIgsALPDLAVHVLDAAGQPVPLGVVGELVVEGD--GVAQGYWQRPELTAERFVERGgQ 3892
Cdd:cd17634    393 ETGGFMITPLPGAIELKAGSATR--PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFSTF-K 469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3893 RFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP 3971
Cdd:cd17634    470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgIPHAIKGQAPYAYVVLNHGVEPSP 549
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 3972 qSLREALRALLPDYM----LPRLIQLLPALPLTANGKL 4005
Cdd:cd17634    550 -ELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3545-4005 3.00e-38

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: 150.99  E-value: 3.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSgvclsvSQR 3624
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRA------KAK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3625 ALavelpgtalclddpFTRAQLDAVEPGELPEvpteAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAatQTGRFSFDEHD 3704
Cdd:cd05903     76 VF--------------VVPERFRQFDPAAMPD----AVALLLFTSGTTGEPKGVMHSHNTLSASIRQ--YAERLGLGPGD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VW----SLFHSHAFDFAVWElwgAWLYGGRAVLvpeavCR--QPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL 3778
Cdd:cd05903    136 VFlvasPMAHQTGFVYGFTL---PLLLGAPVVL-----QDiwDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPL 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 -NVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDEDLQSPTSriGSALPDLAVHVLDAAGQPVP 3857
Cdd:cd05903    208 sRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD--GRPLPGVEIKVVDDTGATLA 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 LGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIAS 3937
Cdd:cd05903    285 PGVEGELLSRGPSVFLGYLDRPDLTADAAPE----GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3938 LPQVSDAAVTV---EGQGEGAwlMAYAVAADGAEPDPQSLREAL-RALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:cd05903    361 HPGVIEAAVVAlpdERLGERA--CAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3501-4005 4.68e-38

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 153.01  E-value: 4.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3501 PSQTRSAAWTsreryactgNLVSRFAEIArryPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGC 3580
Cdd:PRK07786    11 PYLARRQNWV---------NQLARHALMQ---PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3581 DLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALA---------VELPGTALCLDDPFTRAQLD---- 3647
Cdd:PRK07786    79 EFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALApvatavrdiVPLLSTVVVAGGSSDDSVLGyedl 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3648 ---AVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTGRFSFD---EHDVW----SLFHSHAFDFA 3717
Cdd:PRK07786   159 laeAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANL----TGQAMTCLRTNGadiNSDVGfvgvPLFHIAGIGSM 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3718 VWELwgawLYGGRAVLVPEAVCrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQP 3797
Cdd:PRK07786   235 LPGL----LLGAPTVIYPLGAF-DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQ 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WRERYPQAELVNMYGITETTvHVSFHRLSDEDLQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQ 3877
Cdd:PRK07786   310 MAATFPEAQILAAFGQTEMS-PVTCMLLGEDAIRKLGS-VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWN 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW- 3956
Cdd:PRK07786   388 NPEATAEAF--AGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI--GRADEKWg 461
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3957 ---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK07786   462 evpVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
603-1041 9.78e-38

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 151.20  E-value: 9.78e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  603 LGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAGENGSGENAA--PNQLAYIL 680
Cdd:PRK04813    70 LGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAvkGDDNYYII 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  681 YTSGSTGIPKGVEVGHaalaahidaaaealalsaddrvlhvaglavDTTLEqiLAAWsrgacvvARPD-ELLEPQRFLA- 758
Cdd:PRK04813   150 FTSGTTGKPKGVQISH------------------------------DNLVS--FTNW-------MLEDfALPEGPQFLNq 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  759 ----F-LSeraitVTDLAPAYA-----NELVRAsVADDWRDL--ALRCLVVG---------------------------- 798
Cdd:PRK04813   191 apysFdLS-----VMDLYPTLAsggtlVALPKD-MTANFKQLfeTLPQLPINvwvstpsfadmclldpsfneehlpnlth 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  799 ----GDVLPVALAQRWFELGLDRRcaLINAYGPTEAT--ISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRG 872
Cdd:PRK04813   265 flfcGEELPHKTAKKLLERFPSAT--IYNTYGPTEATvaVTSIEITDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDG 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  873 VCGELALGGIGLAEGYRGDAAASERRFAPLrlpsgESLRMYRSGDRVRLlDDGELQFLGRADFQVKLRGYRIELEEIEHC 952
Cdd:PRK04813   343 EQGEIVISGPSVSKGYLNNPEKTAEAFFTF-----DGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQN 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  953 LGQLPQVRAA-AAGVVGEGAAQRLVAWVECAGEDGFGQADLNQtdsdQTESErwhraLCERLPAYMVPTQFVALPRLPRN 1031
Cdd:PRK04813   417 LRQSSYVESAvVVPYNKDHKVQYLIAYVVPKEEDFEREFELTK----AIKKE-----LKERLMEYMIPRKFIYRDSLPLT 487
                          490
                   ....*....|
gi 1246793773 1032 ASGKIDRRAL 1041
Cdd:PRK04813   488 PNGKIDRKAL 497
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3545-4010 1.02e-37

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: 150.05  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsqR 3624
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA------K 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3625 ALAVELPgtalclDDPFTraqldavepgelpevpteapayLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDEHD 3704
Cdd:cd05907     80 ALFVEDP------DDLAT----------------------IIYTSGTTGRPKGVMLSHRNILSNALALAE--RLPATEGD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VWSLF--HSHAFDFAVWELwgAWLYGGRAVLVPEAvcrqPDAFLDLLAEYGVTVLNQTP-------SAFYALQSQAMRRE 3775
Cdd:cd05907    130 RHLSFlpLAHVFERRAGLY--VPLLAGARIYFASS----AETLLDDLSEVRPTVFLAVPrvwekvyAAIKVKAVPGLKRK 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3776 LAL-----NVRAVVFGGEALEPSRLqpwreRYPQAELVNM---YGITETTVHVSFHRLSDEDLQSptsrIGSALPDLAVH 3847
Cdd:cd05907    204 LFDlavggRLRFAASGGAPLPAELL-----HFFRALGIPVyegYGLTETSAVVTLNPPGDNRIGT----VGKPLPGVEVR 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VldaagqpvplGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLR-GYRI 3926
Cdd:cd05907    275 I----------ADDGEILVRGPNVMLGYYKNPEATAEALDADG---WLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNI 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQ---------------------GEGAWLMAYAVAADGAEPDPQSLREALRALLPDY 3985
Cdd:cd05907    342 SPEPIENALKASPLISQAVVIGDGRpflvalivpdpealeawaeehGIAYTDVAELAANPAVRAEIEAAVEAANARLSRY 421
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1246793773 3986 MLPRLIQLLPaLP-------LTANGKLDRKAL 4010
Cdd:cd05907    422 EQIKKFLLLP-EPftiengeLTPTLKLKRPVI 452
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1598-1948 5.12e-37

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: 147.17  E-value: 5.12e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTaIVWEGLSVPHQIVLADAAAP-WQ 1676
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRT-RFCEEAGRYEQVVLDKTVRFrIE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1677 TLDWSALDDaaQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQ 1756
Cdd:cd19066     81 IIDLRNLAD--PEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1757 GATLRLPPAPGFQAYLDW----RERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHP-VQREECERRLSAHDSERLRAF 1831
Cdd:cd19066    159 QKPTLPPPVGSYADYAAWlekqLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVAsYEVLTLEFFLRSEETKRLREV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1832 CRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPElaGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSL 1911
Cdd:cd19066    239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 1912 EVAENEAVGLGEILADSG----LDADRLFASLLVVENFPAM 1948
Cdd:cd19066    317 EAIEHQRVPFIELVRHLGvvpeAPKHPLFEPVFTFKNNQQQ 357
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3667-4007 5.56e-37

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: 145.11  E-value: 5.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNVerlFTAATQTG-RFSFDEHDVW----SLFHshAFDFAVWELwGAWLYGGRAVLVPEAVcrQ 3741
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNI---VNNGYFIGeRLGLTEQDRLcipvPLFH--CFGSVLGVL-ACLTHGATMVFPSPSF--D 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3742 PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhV 3820
Cdd:cd05917     81 PLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLsSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSP-V 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVP-LGVVGELVVEGDGVAQGYWQRPELTAErfvERGGQRFYRSGD 3899
Cdd:cd05917    160 STQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAE---AIDGDGWLHTGD 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREAL 3978
Cdd:cd05917    237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVgVPDERYGEEVCAWIRLKEGAELTEEDIKAYC 316
                          330       340
                   ....*....|....*....|....*....
gi 1246793773 3979 RALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd05917    317 KGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3520-4010 5.85e-37

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 148.88  E-value: 5.85e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK06145     3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGV-CLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEAPA-----YLIYTSGSTG 3673
Cdd:PRK06145    83 NYRLAADEVAYILGDAGAkLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAptdlvRLMYTSGTTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVErlFTAATQTGRFSFDEHD----VWSLFHSHAFDFAvwelwgawlygGRAVLVPEAVCR-----QPDA 3744
Cdd:PRK06145   163 RPKGVMHSYGNLH--WKSIDHVIALGLTASErllvVGPLYHVGAFDLP-----------GIAVLWVGGTLRihrefDPEA 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3745 FLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFH 3823
Cdd:PRK06145   230 VLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDsLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLM 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3824 RLSDEdlqspTSRIGS---ALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVerGGqrFYRSGDL 3900
Cdd:PRK06145   310 EAGRE-----IEKIGStgrALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY--GD--WFRSGDV 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAADGAEPDPQSLREA 3977
Cdd:PRK06145   381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI--GVHDDRWgerITAVVVLNPGATLTLEALDRH 458
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1246793773 3978 LRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06145   459 CRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3507-4008 6.19e-37

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 150.15  E-value: 6.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3507 AAWTSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVAL 3586
Cdd:PRK05605    20 APWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3587 LAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVS-----------------QRALAVELPG-------TALCLDDPF- 3641
Cdd:PRK05605   100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVwdkvaptverlrrttplETIVSVNMIAampllqrLALRLPIPAl 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3642 --TRAQLDAVEPG-------------------ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNverLFTAATQ-----T 3695
Cdd:PRK05605   180 rkARAALTGPAPGtvpwetlvdaaiggdgsdvSHPRPTPDDVALILYTSGTTGKPKGAQLTHRN---LFANAAQgkawvP 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3696 GRFSFDE--HDVWSLFHSHAF----DFAVwelwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQS 3769
Cdd:PRK05605   257 GLGDGPErvLAALPMFHAYGLtlclTLAV-------SIGGELVLLPAP---DIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3770 QAMRRELALN-VRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLSDEdlQSPTSrIGSALPDLAVHV 3848
Cdd:PRK05605   327 AAEERGVDLSgVRNAFSGAMALPVSTVELW-EKLTGGLLVEGYGLTETSPIIVGNPMSDD--RRPGY-VGVPFPDTEVRI 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDA--AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:PRK05605   403 VDPedPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLD----GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAVTVEGQGEGAW-LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK05605   479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558

                   ...
gi 1246793773 4006 DRK 4008
Cdd:PRK05605   559 RRR 561
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
648-1041 7.24e-37

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: 147.59  E-value: 7.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  648 PSVAIAVDELklDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVD 727
Cdd:cd05922     93 PGTVLDADGI--RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYD 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  728 TTLEQILAAWSRGACVVARPDELLePQRFLAFLSERAITVTDLAPAYANELVRAsvadDWRDLA---LRCLVVGGDVLPV 804
Cdd:cd05922    171 YGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAMLTRL----GFDPAKlpsLRYLTQAGGRLPQ 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  805 ALAQRWFELGLDRRCALInaYGPTEATISSHY---HRVqaidASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGG 881
Cdd:cd05922    246 ETIARLRELLPGAQVYVM--YGQTEATRRMTYlppERI----LEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  882 IGLAEGYRGDaaaserrfAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRA 961
Cdd:cd05922    320 PNVMKGYWND--------PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIE 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  962 AAAGVVGEGAAQRLVAWVEcagedgfgqADLNQTDSDQTeserwhRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05922    392 AAAVGLPDPLGEKLALFVT---------APDKIDPKDVL------RSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3529-4010 1.10e-36

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: 148.16  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDG----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGA---------- 3594
Cdd:cd12119      6 ARLHGDREIVSRTHEgevhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvlhtinprlf 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3595 ----AYV--------------------PVDPHAPAARRGFILEDSgvclsvsqRALAVELPGTALCLDDpftraQLDAVE 3650
Cdd:cd12119     86 peqiAYIinhaedrvvfvdrdflplleAIAPRLPTVEHVVVMTDD--------AAMPEPAGVGVLAYEE-----LLAAES 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3651 P-GELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVW----SLFHSHAfdfavwelWG-- 3723
Cdd:cd12119    153 PeYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVlpvvPMFHVNA--------WGlp 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3724 --AWLYGGRAVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELaLNVRAVVFGGEALEPSRLQPWR 3799
Cdd:cd12119    225 yaAAMVGAKLVLPGPYL--DPASLAELIEREGVTFAAGVPTVWQGLLDhlEANGRDL-SSLRRVVIGGSAVPRSLIEAFE 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3800 ERYpqAELVNMYGITETTVHVSFHRLSDEDLQSP-------TSRIGSALPDLAVHVLDAAGQPVPL--GVVGELVVEGDG 3870
Cdd:cd12119    302 ERG--VRVIHAWGMTETSPLGTVARPPSEHSNLSedeqlalRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPW 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveG 3950
Cdd:cd12119    380 VTKSYYKNDEESEALT--EDG--WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVI--G 453
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3951 QGEGAWL---MAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd12119    454 VPHPKWGerpLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
586-1041 1.12e-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: 146.85  E-value: 1.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  586 RSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQglagfapsvaiaVDELKLDGAGEN 665
Cdd:cd17654     42 RAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKE------------LDNAPLSFTPEH 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  666 GSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVA 745
Cdd:cd17654    110 RHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLI 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 RPDEL-LEPQRFLAFLSER-AITVTDLAPAYANELVRASVADDW--RDLALRCLVVGGDVLPVALAQR-WFELGLdrRCA 820
Cdd:cd17654    190 VPTSVkVLPSKLADILFKRhRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLVILSsWRGKGN--RTR 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  821 LINAYGPTEATISSHYHRVQAIDAsrPVPLGQLLPGRIAAVLDAHGrivpRGVCGELALGGIGLAeGYRGDaaaserrfa 900
Cdd:cd17654    268 IFNIYGITEVSCWALAYKVPEEDS--PVQLGSPLLGTVIEVRDQNG----SEGTGQVFLGGLNRV-CILDD--------- 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  901 PLRLPSGEslrMYRSGDRVRlLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagvvgegaaqrlVAWve 980
Cdd:cd17654    332 EVTVPKGT---MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA------------VTL-- 393
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773  981 cagedgFGQADLNQTDSDQTESERWHRAL-CERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17654    394 ------SDQQRLIAFIVGESSSSRIHKELqLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1142-1373 2.13e-36

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 139.79  E-value: 2.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDrYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQDWR 1221
Cdd:COG4908      1 LSPAQKRFLFLEPGSNA-YNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLP-LEVVDLS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1222 GAADlDSRVDAAFARMQE--ATPL---AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAW 1295
Cdd:COG4908     79 ALPE-PEREAELEELVAEeaSRPFdlaRGPLLRAALIRLGEDEhVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1296 TPSARGASYADYVEALREADDAQRFDA--GFWRELAAQ--PMQALPQDRPValADARQSNVGRIVQTLDAGLTADLLERA 1371
Cdd:COG4908    158 PLPELPIQYADYAAWQRAWLQSEALEKqlEYWRQQLAGapPVLELPTDRPR--PAVQTFRGATLSFTLPAELTEALKALA 235

                   ..
gi 1246793773 1372 GE 1373
Cdd:COG4908    236 KA 237
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1599-1940 4.94e-36

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: 143.73  E-value: 4.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19544      3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVEEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 DWSALDDAAqdAQLQRwLADDAAQGVDFAHAPLARMSLI-GRGGGRYWLVWSIHHLIVDGWSTPLLVGEmLQRYTAGaQG 1757
Cdd:cd19544     83 TLDPGDDAL--AQLRA-RFDPRRYRLDLRQAPLLRAHVAeDPANGRWLLLLLFHHLISDHTSLELLLEE-IQAILAG-RA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLrLPPAP--GFQAYLdwRERQDLARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCRER 1835
Cdd:cd19544    158 AAL-PPPVPyrNFVAQA--RLGASQAEHEAFFREMLGDVDEPTAPFGLLDVQGDGSDITEARLALDAELAQRLRAQARRL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1836 GCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDaGQPALDLLSALRSQSLEVAE 1915
Cdd:cd19544    235 GVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAELLR 313
                          330       340
                   ....*....|....*....|....*.
gi 1246793773 1916 NEAVGLGEILADSGLDADR-LFASLL 1940
Cdd:cd19544    314 HEHASLALAQRCSGVPAPTpLFSALL 339
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3529-4025 6.59e-36

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 146.64  E-value: 6.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAAR 3607
Cdd:PRK08314    20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3608 RGFILEDSG----VCLS-------------------VSQRA--------------LAVELPGTALclDDPFTRAQLDAVE 3650
Cdd:PRK08314   100 LAHYVTDSGarvaIVGSelapkvapavgnlrlrhviVAQYSdylpaepeiavpawLRAEPPLQAL--APGGVVAWKEALA 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3651 PGELPEVPTEAP---AYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFdfaVWELWG 3723
Cdd:PRK08314   178 AGLAPPPHTAGPddlAVLPYTSGTTGVPKGCMHTHRTV--MANAVGSVLWSNSTPESVVlavlPLFHVTGM---VHSMNA 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3724 AWLYGGRAVLVPeavcR-QPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPS----RLQpw 3798
Cdd:PRK08314   253 PIYAGATVVLMP----RwDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEavaeRLK-- 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3799 rERYpQAELVNMYGITETTVHVSFHRLSDEDLQSptsrIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQ 3877
Cdd:PRK08314   327 -ELT-GLDYVEGYGLTETMAQTHSNPPDRPKLQC----LGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQGEG 3954
Cdd:PRK08314   401 RPEATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAcviATPDPRRGET 480
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3955 AwlMAYAVAADGAE--PDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetQDRDEGVLES 4025
Cdd:PRK08314   481 V--KAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL-----QEQEKARAAK 546
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1138-1577 8.90e-36

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: 144.01  E-value: 8.90e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1138 GEVGLSPIQ--RWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQV---AAPGPA 1212
Cdd:pfam00668    3 DEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVileERPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1213 PAIQAQDWrGAADLDSRVDAaFARMQEATPL---AGPLV-ALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAA 1288
Cdd:pfam00668   83 EIIDISDL-SESEEEEAIEA-FIQRDLQSPFdleKGPLFrAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1289 LARGEAwTPSARGASYADYVEALREADDAQRF--DAGFWRELAAQ--PMQALPQDRPvALADaRQSNVGRIVQTLDAGlT 1364
Cdd:pfam00668  161 LLKGEP-LPLPPKTPYKDYAEWLQQYLQSEDYqkDAAYWLEQLEGelPVLQLPKDYA-RPAD-RSFKGDRLSFTLDED-T 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1365 ADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGRdvlDGRDWSSVLGWYTAVHPLPLDL-GVADGPAQI 1443
Cdd:pfam00668  237 EELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR---PSPDIERMVGMFVNTLPLRIDPkGGKTFSELI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1444 GALKEQIR-ALARRGLDYMPLVASARIPALPAGQLLF-------NYHGvvdagahPAFEVEPRTLASGN------GADNP 1509
Cdd:pfam00668  314 KRVQEDLLsAEPHQGYPFGDLVNDLRLPRDLSRHPLFdpmfsfqNYLG-------QDSQEEEFQLSELDlsvssvIEEEA 386
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1510 PGALvEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQARL 1577
Cdd:pfam00668  387 KYDL-SLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
3520-4020 1.76e-35

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 145.68  E-value: 1.76e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK05677    25 NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAARRGFILEDSG----VCLSVSQRALAVELPGTALC---------LDDPFTRAQLDA--------VEPGELPE- 3656
Cdd:PRK05677   105 TNPLYTAREMEHQFNDSGakalVCLANMAHLAEKVLPKTGVKhvivtevadMLPPLKRLLINAvvkhvkkmVPAYHLPQa 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 --------------VPTEAP-----AYLIYTSGSTGTPKGVVVTHRNV--ERLFTAATQTGRFSFDEHDVWS---LFHSH 3712
Cdd:PRK05677   185 vkfndalakgagqpVTEANPqaddvAVLQYTGGTTGVAKGAMLTHRNLvaNMLQCRALMGSNLNEGCEILIAplpLYHIY 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3713 AFDFAVWELwgaWLYGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRREL---ALNVRAVvfGGEA 3789
Cdd:PRK05677   265 AFTFHCMAM---MLIGNHNILISNP--RDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLdfsALKLTLS--GGMA 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3790 LEPSRLQPWRErYPQAELVNMYGITETTVHVSFHRLsdEDLQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD 3869
Cdd:PRK05677   338 LQLATAERWKE-VTGCAICEGYGMTETSPVVSVNPS--QAIQVGT--IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3870 GVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD-AAVTV 3948
Cdd:PRK05677   413 QVMKGYWQRPEATDEILDSDG---WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGV 489
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3949 EGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqdRDE 4020
Cdd:PRK05677   490 PDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL-------RDE 554
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3113-3397 2.93e-35

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: 142.07  E-value: 2.93e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3113 GALDREAFAAAWQQALERHPILRSGF-AVQGLPSprQLPHRQVSLPLAEQDWSGLEPAQArsrLSELQAQQCEAgFDLAA 3191
Cdd:cd20484     34 SKLDVEKFKQACQFVLEQHPILKSVIeEEDGVPF--QKIEPSKPLSFQEEDISSLKESEI---IAYLREKAKEP-FVLEN 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3192 PPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESRTP-QLPAAPPFRDYLHW----LRGQDEAAA 3266
Cdd:cd20484    108 GPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPtLASSPASYYDFVAWeqdmLAGAEGEEH 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3267 RAFWREQLTG----LE-PAALPEATEPAEGYASSTRRFDLAAAS---AWAQSHGLTASSLLQGALALVLQRYYGRDDFAL 3338
Cdd:cd20484    188 RAYWKQQLSGtlpiLElPADRPRSSAPSFEGQTYTRRLPSELSNqikSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIV 267
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3339 GITIAGRPPElaGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPL 3397
Cdd:cd20484    268 GMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPF 324
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
2061-2517 2.93e-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: 143.51  E-value: 2.93e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIG- 2139
Cdd:cd05911     10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 -------WGAAPAW--------VPASVRW-LDAESVLDVVSAYEE---PPRVDVDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05911     90 pdglekvKEAAKELgpkdkiivLDDKPDGvLSIEDLLSPTLGEEDedlPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2201 NL-ANY--VAGVLPVLDLGEDASLATLSTVAAdLGFTALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPS 2277
Cdd:cd05911    170 NLiANLsqVQTFLYGNDGSNDVILGFLPLYHI-YGLFTTLASLLNGATVIIMP---KFDSELFLDLIEKYKITFLYLVPP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2278 HLAGLLAAAGGTA-VLP--REcLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVgilTCTVPEEWPVEQGvPVGHP 2354
Cdd:cd05911    246 IAAALAKSPLLDKyDLSslRV-ILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGG---ILTVNPDGDDKPG-SVGRL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2355 LAGNEAWVLDRFG-LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLLyRSGDLARLDGEGRIVYLGRGD 2433
Cdd:cd05911    321 LPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDGWL-HTGDIGYFDEDGYLYIVDRKK 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2434 HQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA--------LPGANGVLQLGACIqgSLEGVAEALAQRLPEYlcpSRWRA 2505
Cdd:cd05911    395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGipdevsgeLPRAYVVRKPGEKL--TEKEVKDYVAKKVASY---KQLRG 469
                          490
                   ....*....|....*.
gi 1246793773 2506 ----VESMPRLGNGKI 2517
Cdd:cd05911    470 gvvfVDEIPKSASGKI 485
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
2061-2608 4.31e-35

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: 148.67  E-value: 4.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGW 2140
Cdd:TIGR03443  270 SFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVI 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAAPAWVPASVRWLDAE-------------------------SVLDVVSAYE----EPPRVDVDADTPAYLIYTSGSTGT 2191
Cdd:TIGR03443  350 EKAGTLDQLVRDYIDKElelrteipalalqddgslvggslegGETDVLAPYQalkdTPTGVVVGPDSNPTLSFTSGSEGI 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2192 PKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADL----GFTALFgallsgrrvrlLPAELafdaqalaahlqah 2267
Cdd:TIGR03443  430 PKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPiqrdMFTPLF-----------LGAQL-------------- 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 pvdclkIVPSHLAGLLAAAGGTAVLPRECLVTG-----GEALTGALVQQV---------------------RALAPTLRI 2321
Cdd:TIGR03443  485 ------LVPTADDIGTPGRLAEWMAKYGATVTHltpamGQLLSAQATTPIpslhhaffvgdiltkrdclrlQTLAENVCI 558
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2322 VNHYGPTETTVGILTCTVPeewPVEQG----------VPVGHPLAGNEAWVLDRFGLPAPVGVA--GELYLGGGNLSLGY 2389
Cdd:TIGR03443  559 VNMYGTTETQRAVSYFEIP---SRSSDstflknlkdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGY 635
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2390 WQRAEQTAERFVA----------------------HPLAP-DRLlYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:TIGR03443  636 LGLPELNAEKFVNnwfvdpshwidldkennkpereFWLGPrDRL-YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELG 714
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2447 EVEQVLAQLPGVE----------------VAAVLALPGANGVLQLGACIQGSLEG----------------VAEALAQRL 2494
Cdd:TIGR03443  715 EIDTHLSQHPLVRenvtlvrrdkdeeptlVSYIVPQDKSDELEEFKSEVDDEESSdpvvkglikyrklikdIREYLKKKL 794
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2495 PEYLCPSRWRAVESMPRLGNGKIDRQAL-----ADL-LQQDDADSSAEAIDETPVNEVLRELWQKLLGRE--HIGAHDNF 2566
Cdd:TIGR03443  795 PSYAIPTVIVPLKKLPLNPNGKVDKPALpfpdtAQLaAVAKNRSASAADEEFTETEREIRDLWLELLPNRpaTISPDDSF 874
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 2567 FALGGDSILSLQLVARARQAGLALMPRQL-YDHPTLAGLSAQV 2608
Cdd:TIGR03443  875 FDLGGHSILATRMIFELRKKLNVELPLGLiFKSPTIKGFAKEV 917
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
551-1041 5.70e-35

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: 141.45  E-value: 5.70e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  551 RAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAA 630
Cdd:cd05919      1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  631 SGCDAVLTDAqglagfapsvaiavdelkldgagengsgenaapNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEAL 710
Cdd:cd05919     81 CEARLVVTSA---------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  711 AL-SADDRVLHVAGLAVDTTL-EQILAAWSRGACVVARPdELLEPQRFLAFLSERAITVTDLAPA-YANELVRASVADDw 787
Cdd:cd05919    128 LGlTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNP-GWPTAERVLATLARFRPTVLYGVPTfYANLLDSCAGSPD- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  788 RDLALRCLVVGGDVLPVALAQRWFELGLdrrCALINAYGPTEatiSSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGR 867
Cdd:cd05919    206 ALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATE---VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGH 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  868 IVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpsGEslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELE 947
Cdd:cd05919    280 TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN------GG---WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPV 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  948 EIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECAGEdgfgqadlnqTDSDQTESERWHRALCERLPAYMVPTQFVALP 1026
Cdd:cd05919    351 EVESLIIQHPAVaEAAVVAVPESTGLSRLTAFVVLKSP----------AAPQESLARDIHRHLLERLSAHKVPRRIAFVD 420
                          490
                   ....*....|....*
gi 1246793773 1027 RLPRNASGKIDRRAL 1041
Cdd:cd05919    421 ELPRTATGKLQRFKL 435
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
3545-4013 6.19e-35

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 142.92  E-value: 6.19e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQ- 3623
Cdd:PRK12406    12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHa 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 ---RALAVELPGT--------------------ALCLDDPFT---RAQLDAVEPGELPevPTEAPAYLIYTSGSTGTPKG 3677
Cdd:PRK12406    92 dllHGLASALPAGvtvlsvptppeiaaayrispALLTPPAGAidwEGWLAQQEPYDGP--PVPQPQSMIYTSGTTGHPKG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3678 VVVTHRNVERLFTAATQTGRFSFDEHDVWS-----LFHSHAFDFAVwelwGAWLYGGRAVLVPEAvcrQPDAFLDLLAEY 3752
Cdd:PRK12406   170 VRRAAPTPEQAAAAEQMRALIYGLKPGIRAlltgpLYHSAPNAYGL----RAGRLGGVLVLQPRF---DPEELLQLIERH 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3753 GVTVLNQTPSAFYALQS--QAMRRELALN-VRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVhVSFHRlSDED 3829
Cdd:PRK12406   243 RITHMHMVPTMFIRLLKlpEEVRAKYDVSsLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA-VTFAT-SEDA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQ-GYWQRPELTAErfVERGGqrFYRSGDLGRYRADGS 3908
Cdd:PRK12406   320 LSHPGT-VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--IDRGG--FITSGDVGYLDADGY 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3909 LEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVAADGAEPDPQSLREALRALLPDYML 3987
Cdd:PRK12406   395 LFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfGEALMAVVEPQPGATLDEADIRAQLKARLAGYKV 474
                          490       500
                   ....*....|....*....|....*.
gi 1246793773 3988 PRLIQLLPALPLTANGKLDRKALPKP 4013
Cdd:PRK12406   475 PKHIEIMAELPREDSGKIFKRRLRDP 500
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3507-4010 8.99e-35

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: 144.17  E-value: 8.99e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3507 AAWTSRERYACTGNLVSRFAEIARRYPArIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLL 3583
Cdd:cd05968     52 AAWFVGGRMNIVEQLLDKWLADTRTRPA-LRWEGEDGTsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIV 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3584 VALLAILKTGAAYVPV--------------DPHAPA-------ARRGFILE-----------DSGVCLSVSQRALAVELP 3631
Cdd:cd05968    131 PAFLAVARIGGIVVPIfsgfgkeaaatrlqDAEAKAlitadgfTRRGREVNlkeeadkacaqCPTVEKVVVVRHLGNDFT 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3632 GTalcLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVErlfTAATQTGRFSFD--EHDVWSLF 3709
Cdd:cd05968    211 PA---KGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFP---LKAAQDMYFQFDlkPGDLLTWF 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HSHAFDFAVWELWGAWLYGGRAVL---VPEAvcRQPDAFLDLLAEYGVTVLNQTPS---AFYALQSQAMRRELALNVRav 3783
Cdd:cd05968    285 TDLGWMMGPWLIFGGLILGATMVLydgAPDH--PKADRLWRMVEDHEITHLGLSPTlirALKPRGDAPVNAHDLSSLR-- 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEAlEPSRLQPWR--------ERYPqaeLVNMYGITEttvhVSFHRLSDEDLQ--SPTSrIGSALPDLAVHVLDAAG 3853
Cdd:cd05968    361 VLGSTG-EPWNPEPWNwlfetvgkGRNP---IINYSGGTE----ISGGILGNVLIKpiKPSS-FNGPVPGMKADVLDESG 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3854 QPVPlGVVGELVVEGD--GVAQGYWQRPeltaERFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:cd05968    432 KPAR-PEVGELVLLAPwpGMTRGFWRDE----DRYLETYWSRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGP 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSD-AAVTVEGQGEGAWLMAYAVAADGAEPDPqSLREALRALLPDYM----LPRLIQLLPALPLTANG 4003
Cdd:cd05968    507 AEIESVLNAHPAVLEsAAIGVPHPVKGEAIVCFVVLKPGVTPTE-ALAEELMERVADELgkplSPERILFVKDLPKTRNA 585

                   ....*..
gi 1246793773 4004 KLDRKAL 4010
Cdd:cd05968    586 KVMRRVI 592
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3532-4004 9.19e-35

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: 142.05  E-value: 9.19e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3532 YPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFI 3611
Cdd:cd12118     17 YPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGVclsvsqRALAVelpgtalclDDPFTRAQLDAV-EPGELPEVPTEA--PAYLIYTSGSTGTPKGVVVTHRNVerl 3688
Cdd:cd12118     97 LRHSEA------KVLFV---------DREFEYEDLLAEgDPDFEWIPPADEwdPIALNYTSGTTGRPKGVVYHHRGA--- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATQTG-RFSFDEHDV--WSL--FHSHAFDFAvwelWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:cd12118    159 YLNALANIlEWEMKQHPVylWTLpmFHCNGWCFP----WTVAAVGGTNVCLRKV---DAKAIYDLIEKHKVTHFCGAPTV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELALNVRAVVFGGEALEPSRLqpwrerypqaeLVNM----------YGITETTVHVSF-------HRLS 3826
Cdd:cd12118    232 LNMLANAPPSDARPLPHRVHVMTAGAPPPAAV-----------LAKMeelgfdvthvYGLTETYGPATVcawkpewDELP 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3827 DEDLQSPTSRIGSALPDL-AVHVLDAAG-QPVPL-GV-VGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGR 3902
Cdd:cd12118    301 TEERARLKARQGVRYVGLeEVDVLDPETmKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF--RGG--WFHSGDLAV 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3903 YRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQGEGawLMAYAVAADGAEPDPQSLREALR 3979
Cdd:cd12118    377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVArpdEKWGEV--PCAFVELKEGAKVTEEEIIAFCR 454
                          490       500
                   ....*....|....*....|....*
gi 1246793773 3980 ALLPDYMLPRLIQLLPaLPLTANGK 4004
Cdd:cd12118    455 EHLAGFMVPKTVVFGE-LPKTSTGK 478
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3545-4012 9.42e-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: 140.73  E-value: 9.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV-DPHAPAArrgfiledsgvclsVSQ 3623
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLfTAFGPKA--------------IEH 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 RalaVELPGTALCLDDPFTRAQLDavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTGRFSFDEH 3703
Cdd:cd05973     67 R---LRTSGARLVVTDAANRHKLD------------SDPFVMMFTSGTTGLPKGVPVPLRAL----AAFGAYLRDAVDLR 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3704 DvwslfhshafDFAVWEL----WGAWLYggRAVLVPEAVCR---------QPDAFLDLLAEYGVTVLNQTPSAFYALQSQ 3770
Cdd:cd05973    128 P----------EDSFWNAadpgWAYGLY--YAITGPLALGHptilleggfSVESTWRVIERLGVTNLAGSPTAYRLLMAA 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3771 AMRRELALNV--RAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSriGSALPDLAVHV 3848
Cdd:cd05973    196 GAEVPARPKGrlRRVSSAGEPLTPEVIR-WFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSA--GRAMPGWRVAV 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LDAAGQPVPLGVVGELVVEGDGVA----QGYWQRPELTAErfverggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:cd05973    273 LDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAID-------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLPALPLT 4000
Cdd:cd05973    346 RIGPFDVESALIEHPAVAEAAVIgVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKT 425
                          490
                   ....*....|..
gi 1246793773 4001 ANGKLDRKALPK 4012
Cdd:cd05973    426 PSGKIQRFLLRR 437
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
2051-2524 1.87e-34

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 141.58  E-value: 1.87e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIA-VL 2129
Cdd:PRK07656    20 DKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY-TADEAAyIL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGA-APAWVPASVRWLDAESVldVVSAYEEPPRVD---------------------VDADTPAYLIYTSG 2187
Cdd:PRK07656    99 ARGDAKALFVLGLfLGVDYSATTRLPALEHV--VICETEEDDPHTekmktftdflaagdpaerapeVDPDDVADILFTSG 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2188 STGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLSTVAAdLGFTA-LFGALLSGRRVrlLPaELAFDaqalaahlq 2265
Cdd:PRK07656   177 TTGRPKGAMLTHRQLLSNAADWAEYLGLTEgDRYLAANPFFHV-FGYKAgVNAPLMRGATI--LP-LPVFD--------- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2266 ahPVDCLKIVPSHLAgllaaaggtAVLP-----------------------REClVTGGEALTGALVQQVRALAPTLRIV 2322
Cdd:PRK07656   244 --PDEVFRLIETERI---------TVLPgpptmynsllqhpdrsaedlsslRLA-VTGAASMPVALLERFESELGVDIVL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2323 NHYGPTETTvGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfva 2402
Cdd:PRK07656   312 TGYGLSEAS-GVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAA---- 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2403 hPLAPDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN-G-------VLQ 2474
Cdd:PRK07656   387 -AIDADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERlGevgkayvVLK 464
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2475 LGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK07656   465 PGAEL--TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
PRK05691 PRK05691
peptide synthase; Validated
537-1371 2.15e-34

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 147.24  E-value: 2.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  537 VVDAIARAADEFPERAAL-----ETAQGR-LSYRELLTAADARAAALRRRLGAQARSVaLCLPRGLDWYCLLLGAWRAGL 610
Cdd:PRK05691    11 LVQALQRRAAQTPDRLALrfladDPGEGVvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  611 SVIPL-----DTEWPQARRAEVVAASGCDAVLTDA----------QGLAGFAPSVaIAVDELKLDGAgENGSGENAAPNQ 675
Cdd:PRK05691    90 IAVPAyppesARRHHQERLLSIIADAEPRLLLTVAdlrdsllqmeELAAANAPEL-LCVDTLDPALA-EAWQEPALQPDD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  676 LAYILYTSGSTGIPKGVEVGHAALAAhidaaaealalsadDRVLHVAGLAVDTTLEQILAAW------------------ 737
Cdd:PRK05691   168 IAFLQYTSGSTALPKGVQVSHGNLVA--------------NEQLIRHGFGIDLNPDDVIVSWlplyhdmgliggllqpif 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  738 SRGACVVARPDELLE-PQRFLAFLSERAITVTDlAPAYANELVRASVADD---------WRDLALRCLVVGGDVLPvALA 807
Cdd:PRK05691   234 SGVPCVLMSPAYFLErPLRWLEAISEYGGTISG-GPDFAYRLCSERVSESalerldlsrWRVAYSGSEPIRQDSLE-RFA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  808 QRWFELGLDRRcALINAYGPTEAT-----------ISSHYHRVQAIDASRPVP-LGQLL-------PGRIAAVLD-AHGR 867
Cdd:PRK05691   312 EKFAACGFDPD-SFFASYGLAEATlfvsggrrgqgIPALELDAEALARNRAEPgTGSVLmscgrsqPGHAVLIVDpQSLE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  868 IVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLrlpsgESLRMYRSGDrVRLLDDGELQFLGRADFQVKLRGYRIELE 947
Cdd:PRK05691   391 VLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH-----DGRTWLRTGD-LGFLRDGELFVTGRLKDMLIVRGHNLYPQ 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  948 EIEHCLGQlpQVRAAAAGVVGEGAaqrlvawVECAGEDGFGQA-----DLNQTDSDQTESERWHRALCErlpAYMVPTQF 1022
Cdd:PRK05691   465 DIEKTVER--EVEVVRKGRVAAFA-------VNHQGEEGIGIAaeisrSVQKILPPQALIKSIRQAVAE---ACQEAPSV 532
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1023 VALPR---LPRNASGKIDRRA---------LPAPPVLAQAERTPPRTAEESA------LCEVWAEVLQCE-VGIHDSFFR 1083
Cdd:PRK05691   533 VLLLNpgaLPKTSSGKLQRSAcrlrladgsLDSYALFPALQAVEAAQTAASGdelqarIAAIWCEQLKVEqVAADDHFFL 612
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1084 LGGDSIRSLQVVARLRER-GYAVTPKLMYQYQS----AAELAPQLIALQAAPAEAAPLVGEVGL--SPIQR--WFFDSAP 1154
Cdd:PRK05691   613 LGGNSIAATQVVARLRDElGIDLNLRQLFEAPTlaafSAAVARQLAGGGAAQAAIARLPRGQALpqSLAQNrlWLLWQLD 692
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1155 AQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQDWRGAADLDSRVDAAF 1234
Cdd:PRK05691   693 PQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFA-LQRIDLSDLPEAEREARAAQ 771
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1235 ARMQEA-TPL---AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVE 1309
Cdd:PRK05691   772 IREEEArQPFdleKGPLLRVTLVRLDDEEhQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGA 851
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1310 ALRE---ADDAQRfDAGFWR-ELA-AQPMQALPQDRPvaLADARQSNVGRIVQTLDAGLTADLLERA 1371
Cdd:PRK05691   852 WQRQwlaQGEAAR-QLAYWKaQLGdEQPVLELATDHP--RSARQAHSAARYSLRVDASLSEALRGLA 915
PRK05691 PRK05691
peptide synthase; Validated
3521-4085 2.63e-34

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 146.85  E-value: 2.63e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVS--AEDGE----LDYATLDRRSSQLATLLIRQgAGPGQRVGLCLPRGCDLLVALLAILKTGA 3594
Cdd:PRK05691    11 LVQALQRRAAQTPDRLALRflADDPGegvvLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCLYAGV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3595 AYVPVDPHAPA--------------ARRGFILEDSGVCLSVSQ-RALAVELPGTALCLDdpftraQLDAV--EPGELPEV 3657
Cdd:PRK05691    90 IAVPAYPPESArrhhqerllsiiadAEPRLLLTVADLRDSLLQmEELAAANAPELLCVD------TLDPAlaEAWQEPAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3658 PTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDV---W-SLFHSHAFdfaVWELWGAWLYGGRAVL 3733
Cdd:PRK05691   164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVivsWlPLYHDMGL---IGGLLQPIFSGVPCVL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 V-PEAVCRQPDAFLDLLAEYGVTVlNQTPSAFYALQSQ-----AMRRELALNVRAVVFGGEALEPSRLQPWRERY----- 3802
Cdd:PRK05691   241 MsPAYFLERPLRWLEAISEYGGTI-SGGPDFAYRLCSErvsesALERLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgf 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3803 -PQAELVNmYGITETTVHVS---------FHRLSDEDLQ---------SPTSRIGSALPDLAVHVLDAA-GQPVPLGVVG 3862
Cdd:PRK05691   320 dPDSFFAS-YGLAEATLFVSggrrgqgipALELDAEALArnraepgtgSVLMSCGRSQPGHAVLIVDPQsLEVLGDNRVG 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVS 3942
Cdd:PRK05691   399 EIWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVV 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3943 D----AAVTVEGQGEGAWLMAYAVAADGAEP-DPQSLREALRALLPD--YMLPRLIQLLP--ALPLTANGKLDRKA---- 4009
Cdd:PRK05691   478 RkgrvAAFAVNHQGEEGIGIAAEISRSVQKIlPPQALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSAcrlr 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4010 -----------LPKPETQDRDEG-VLESASERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPL 4077
Cdd:PRK05691   558 ladgsldsyalFPALQAVEAAQTaASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNL 637

                   ....*...
gi 1246793773 4078 KSLFEQPR 4085
Cdd:PRK05691   638 RQLFEAPT 645
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
3528-4012 3.25e-34

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: 141.27  E-value: 3.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3528 IARRYPARIAVS-AEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:cd05906     19 AAERGPTKGITYiDADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPP 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 ----PAARRGFI-----LEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPT---EAPAYLIYTSGS 3671
Cdd:cd05906     99 tydePNARLRKLrhiwqLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQsrpDDLALLMLTSGS 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3672 TGTPKGVVVTHRNVERLFTAATQTGRFSFDE--------HDVWSLFHSHAFDFavwelwgawLYGGRAVLVP-EAVCRQP 3742
Cdd:cd05906    179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQDvflnwvplDHVGGLVELHLRAV---------YLGCQQVHVPtEEILADP 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVlNQTPSAFYALQSQAMRRE-----LALNVRAVVFGGEALEPS---RLQPWRERY--PQAELVNMYG 3812
Cdd:cd05906    250 LRWLDLIDRYRVTI-TWAPNFAFALLNDLLEEIedgtwDLSSLRYLVNAGEAVVAKtirRLLRLLEPYglPPDAIRPAFG 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVHVSFHRLSDEDLQSPTSR---IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVER 3889
Cdd:cd05906    329 MTETCSGVIYSRSFPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3890 GgqrFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV---SDAAVTVEGQGEGAWLMA--YAVAA 3964
Cdd:cd05906    409 G---WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEELAifFVPEY 484
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3965 DGAEPDPQSLREALRALL------PDYMLPrliqlLP--ALPLTANGKLDRKALPK 4012
Cdd:cd05906    485 DLQDALSETLRAIRSVVSrevgvsPAYLIP-----LPkeEIPKTSLGKIQRSKLKA 535
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
2923-3070 5.64e-34

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: 129.70  E-value: 5.64e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2923 DLGAALRSTKDRMRAVPDRGLGFGVLRYLHGE---LAELPVPQVCFNYLGQLRAGERDG-WALCEEPDGGGRAGGNRRRH 2998
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPeekLAASPQPEISFNYLGQFDADSNDElFQPSSYSPGEAISPESPRPY 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2999 LLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIACVQTAEPRP-TLADLPLAGLDNAPLDAL 3070
Cdd:TIGR01720   81 ALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGlTPSDFSLKDLTQDELDEL 153
PRK09274 PRK09274
peptide synthase; Provisional
3520-4010 7.18e-34

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 140.42  E-value: 7.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDG----------ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAI 3589
Cdd:PRK09274     7 NIARHLPRAAQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3590 LKTGAAYVPVDP-----------------------HAPAARRGFILEDSGV--CLSVSQRALaveLPGTALcldDPFTRA 3644
Cdd:PRK09274    87 FKAGAVPVLVDPgmgiknlkqclaeaqpdafigipKAHLARRLFGWGKPSVrrLVTVGGRLL---WGGTTL---ATLLRD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3645 QldAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSlfhshafdFAVWELWGA 3724
Cdd:PRK09274   161 G--AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPT--------FPLFALFGP 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3725 WLyGGRAVlVPEAVCRQP-----DAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPW 3798
Cdd:PRK09274   231 AL-GMTSV-IPDMDPTRPatvdpAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERF 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3799 RERYPQ-AELVNMYGITE----TTVHvsfhrlSDEDLQSPTSR--------IGSALPDLAVHVLD---------AAGQPV 3856
Cdd:PRK09274   309 RAMLPPdAEILTPYGATEalpiSSIE------SREILFATRAAtdngagicVGRPVDGVEVRIIAisdapipewDDALRL 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFY-RSGDLGRYRADGSLEYRGRGDDQVKLRGYRI--EPGEiaA 3933
Cdd:PRK09274   383 ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLytIPCE--R 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3934 KIASLPQVSDAA-VTVEGQGEGAWLMAYAVaADGAEPDPQSLREALRALLPDYMLPRLIQLL---PALPLTA--NGKLDR 4007
Cdd:PRK09274   461 IFNTHPGVKRSAlVGVGVPGAQRPVLCVEL-EPGVACSKSALYQELRALAAAHPHTAGIERFlihPSFPVDIrhNAKIFR 539

                   ...
gi 1246793773 4008 KAL 4010
Cdd:PRK09274   540 EKL 542
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3520-4010 7.47e-34

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 139.79  E-value: 7.47e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVgLCLPRGCD-LLVALLAILKTGAAYVP 3598
Cdd:PRK07470     8 NLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRI-LVHSRNCNqMFESMFAAFRLGAVWVP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAARRGFILEDSGVCLSVSQ-------RALAVELPGTALCLDDPFTRAQLD--------AVEPGELPEVPTEAPA 3663
Cdd:PRK07470    87 TNFRQTPDEVAYLAEASGARAMICHadfpehaAAVRAASPDLTHVVAIGGARAGLDyealvarhLGARVANAAVDHDDPC 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 YLIYTSGSTGTPKGVVVTH--------RNVERLFTAATqtgrfsfdEHDVwSLF---HSHafdfavwelwGAWLY----- 3727
Cdd:PRK07470   167 WFFFTSGTTGRPKAAVLTHgqmafvitNHLADLMPGTT--------EQDA-SLVvapLSH----------GAGIHqlcqv 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 --GGRAVLVPeAVCRQPDAFLDLLAEYGVTVLNQTPSAFYAL-QSQAMRRELALNVRAVVFGGEALepsrlqpWRERYPQ 3804
Cdd:PRK07470   228 arGAATVLLP-SERFDPAEVWALVERHRVTNLFTVPTILKMLvEHPAVDRYDHSSLRYVIYAGAPM-------YRADQKR 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 A------ELVNMYGITETTVHVS-----FHRLSDEdlqsPTSRIGS---ALPDLAVHVLDAAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK07470   300 AlaklgkVLVQYFGLGEVTGNITvlppaLHDAEDG----PDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPA 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveG 3950
Cdd:PRK07470   376 VFAGYYNNPEANAKAF--RDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL--G 449
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3951 QGEGAW---LMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07470   450 VPDPVWgevGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
89-507 8.01e-34

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: 137.50  E-value: 8.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDsvaagGG----------AA 158
Cdd:cd19533      3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-----GEpyqwidpytpVP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  159 VESADLRGRGQDEIDALV---EGFRlRPFELQRqRPL-RMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQ---D 231
Cdd:cd19533     78 IRHIDLSGDPDPEGAAQQwmqEDLR-KPLPLDN-DPLfRHALFTLGDN-----RHFWYQRVHHIVMDGFSFALFGQrvaE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  232 LSRAYRVECGLAAEPAPPL------PCQYGDYARWQRDTLdrldaslrHHVEALSGAPHLHELpldheRPAVLGQSGAKL 305
Cdd:cd19533    151 IYTALLKGRPAPPAPFGSFldlveeEQAYRQSERFERDRA--------FWTEQFEDLPEPVSL-----ARRAPGRSLAFL 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  306 R--LAFPPGLSERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQLHDD 383
Cdd:cd19533    218 RrtAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQ 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  384 PDFASLVARCRDHQLAALEHQALPLERVIETLQVERSSRH--APLFQLMfalRHDADLALDLHGVQAHAL-TLPEDvakh 460
Cdd:cd19533    298 QTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELHPlfGPTVNYM---PFDYGLDFGGVVGLTHNLsSGPTN---- 370
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773  461 ELTLEVL--VGAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19533    371 DLSIFVYdrDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
3529-4010 9.71e-34

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 138.56  E-value: 9.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK03640    12 AFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREEL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGV-CLSVSQRALAVELPGTALCLDDpftRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNveR 3687
Cdd:PRK03640    92 LWQLDDAEVkCLITDDDFEAKLIPGISVKFAE---LMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN--H 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3688 LFTAATQTGRFSFDEHDVW----SLFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:PRK03640   167 WWSAVGSALNLGLTEDDCWlaavPIFHISGLSILMRSV----IYGMRVVLVEKF---DAEKINKLLQTGGVTIISVVSTM 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERypQAELVNMYGITETTVHVSfhRLSDEDLQsptSRIGSA--- 3840
Cdd:PRK03640   240 LQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETASQIV--TLSPEDAL---TKLGSAgkp 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 LPDLAVHVLDaAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:PRK03640   313 LFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF--QDG--WFKTGDIGYLDEEGFLYVLDRRSDLII 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWLM---AYAVAadGAEPDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:PRK03640   388 SGGENIYPAEIEEVLLSHPGVAEAGVV--GVPDDKWGQvpvAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEEL 463
                          490
                   ....*....|...
gi 1246793773 3998 PLTANGKLDRKAL 4010
Cdd:PRK03640   464 PRNASGKLLRHEL 476
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
3665-4007 1.02e-33

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: 135.09  E-value: 1.02e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNverLFTAATQT-GRFSFDEHDVW----SLFHSHAFD--FAVWELwgawlyGGRAVLVPEA 3737
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGN---LIAANLQLiHAMGLTEADVYlnmlPLFHIAGLNlaLATFHA------GGANVVMEKF 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEAlePSRLQPWRERYPqAELVNMYGITETT 3817
Cdd:cd17637     76 ---DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDA--PETIQRFEETTG-ATFWSLYGQTETS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSFHRLSDEdlqsPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRS 3897
Cdd:cd17637    150 GLVTLSPYRER----PGS-AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--RNG--WHHT 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3898 GDLGRYRADGSLEYRGRG--DDQVKLRGYRIEPGEIAAKIASLPQVsdAAVTVEGQ-----GEGawLMAYAVAADGAEPD 3970
Cdd:cd17637    221 GDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAI--AEVCVIGVpdpkwGEG--IKAVCVLKPGATLT 296
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1246793773 3971 PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17637    297 ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3474-4012 1.42e-33

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 139.29  E-value: 1.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3474 VEQMLDDLDFVLQQVPALQRFDALPLLPSQTRSAAWTSRERYACTGNLVsRFAeiARRYPARIAVSAEDGELDYATLDRR 3553
Cdd:PRK07788     7 VSGYLTRGSAEAHYLRVMIRSGAVDLERPDNGLRLAADIRRYGPFAGLV-AHA--ARRAPDRAALIDERGTLTYAELDEQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3554 SSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP--HAP-----AARRG---------------FI 3611
Cdd:PRK07788    84 SNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTgfSGPqlaevAAREGvkalvyddeftdllsAL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGVCLSVSQRALAVELPG-TALCLDDpftraQLDAVEPGELPEVPTEApAYLIYTSGSTGTPKGVVvtHRNVERLFT 3690
Cdd:PRK07788   164 PPDLGRLRAWGGNPDDDEPSGsTDETLDD-----LIAGSSTAPLPKPPKPG-GIVILTSGTTGTPKGAP--RPEPSPLAP 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATQTGRFSFDEHDVWSLFHS--HAFDFAVWELwgAWLYGGRAVLV----PEAVcrqpdafLDLLAEYGVTVLNQTP--- 3761
Cdd:PRK07788   236 LAGLLSRVPFRAGETTLLPAPmfHATGWAHLTL--AMALGSTVVLRrrfdPEAT-------LEDIAKHKATALVVVPvml 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3762 SAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITEttvhVSFHRLSD-EDLQSPTSRIGSA 3840
Cdd:PRK07788   307 SRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTE----VAFATIATpEDLAEAPGTVGRP 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 LPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYwqrpelTAERFVER-GGqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:PRK07788   382 PKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGRDKQIiDG--LLSSGDVGYFDEDGLLFVDGRDDDMI 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3920 KLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:PRK07788   454 VSGGENVFPAEVEDLLAGHPDVVEAAVIgVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELP 533
                          570
                   ....*....|....
gi 1246793773 3999 LTANGKLDRKALPK 4012
Cdd:PRK07788   534 RNPTGKVLKRELRE 547
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
588-1041 1.71e-33

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: 136.70  E-value: 1.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQglagfapsvaiavdelkldgagengs 667
Cdd:cd05972     28 VAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE-------------------------- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 genaapnQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLA-VDTTLEQILAAWSRGACVVAR 746
Cdd:cd05972     82 -------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGwAKGAWSSFFGPWLLGATVFVY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  747 PDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRdLALRCLVVGGDVLPVALAQRWFE-LGLDRRcaliNAY 825
Cdd:cd05972    155 EGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF-SHLRLVVSAGEPLNPEVIEWWRAaTGLPIR----DGY 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  826 GPTEATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELA--LGGIGLAEGYRGDAAASERRFaplr 903
Cdd:cd05972    230 GQTETGLTVGNFPDMPV---KPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAikLPPPGLFLGYVGDPEKTEASI---- 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  904 lpSGEslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECA 982
Cdd:cd05972    303 --RGD---YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVaEAAVVGSPDPVRGEVVKAFVVLT 377
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  983 geDGFGQadlnqTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05972    378 --SGYEP-----SEELAEELQGHVK---KVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
536-1041 5.16e-33

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: 137.11  E-value: 5.16e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  536 NVVDAIARAADE-FPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIP 614
Cdd:cd05959      4 NAATLVDLNLNEgRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  615 LDTEWP--------QARRAEVVAASG-CDAVLTDAQGLAGFAPSVAIAVD---------ELKLDGAGENGSGENAA--PN 674
Cdd:cd05959     84 VNTLLTpddyayylEDSRARVVVVSGeLAPVLAAALTKSEHTLVVLIVSGgagpeagalLLAELVAAEAEQLKPAAthAD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKG-VEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTL-EQILAAWSRGACVVARPdELLE 752
Cdd:cd05959    164 DPAFWLYSSGSTGRPKGvVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLgNSLTFPLSVGATTVLMP-ERPT 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  753 PQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFEL-GLDrrcaLINAYGPTEAT 831
Cdd:cd05959    243 PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARfGLD----ILDGIGSTEML 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  832 issHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpSGEslr 911
Cdd:cd05959    319 ---HIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE--- 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  912 MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQRLVAWVECagedgfgqAD 991
Cdd:cd05959    387 WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAA--VVGVEDEDGLTKPKAF--------VV 456
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  992 LNQTDSDQTESERWHRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05959    457 LRPGYEDSEALEEELKEFVkDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2062-2522 7.25e-33

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: 134.73  E-value: 7.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgwg 2141
Cdd:cd05934      4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV--- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 aapawvpasvrwldaesvldvvsayeepprvdVDadtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DAS 2220
Cdd:cd05934     81 --------------------------------VD---PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEdDVY 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPREClvtG 2300
Cdd:cd05934    126 LTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAA---Y 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRAlAPTLRIVNHYGPTETTVGILTctvpeewPVEQGVPVGH---PLAGNEAWVLDRFGLPAPVGVAGE 2377
Cdd:cd05934    203 GAPNPPELHEEFEE-RFGVRLLEGYGMTETIVGVIG-------PRDEPRRPGSigrPAPGYEVRIVDDDGQELPAGEPGE 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2378 LYL---GGGNLSLGYWQRAEQTAERFvAHplapdrLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQ 2454
Cdd:cd05934    275 LVIrglRGWGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2455 LPGVEVAAVLALPGANGVLQLGACIQ----GSL--EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05934    348 HPAVREAAVVAVPDEVGEDEVKAVVVlrpgETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3520-4003 7.80e-33

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 137.18  E-value: 7.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV 3599
Cdd:PRK06164    11 TLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3600 DPHAPAARRGFILEDSGVCLSV------------------------SQRALAVELPGTALCLDDPFTRAQLDAVEPGE-- 3653
Cdd:PRK06164    91 NTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaavppdalppLRAIAVVDDAADATPAPAPGARVQLFALPDPApp 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3654 ----LPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVweLWGAwLYGG 3729
Cdd:PRK06164   171 aaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFST--LLGA-LAGG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 rAVLVPEAVCRQPDAfLDLLAEYGVTVLNQTPSAFYALQSQA-MRRELAlnvRAVVFGGEALEPSrlqpWRERYPQAE-- 3806
Cdd:PRK06164   248 -APLVCEPVFDAART-ARALRRHRVTHTFGNDEMLRRILDTAgERADFP---SARLFGFASFAPA----LGELAALARar 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3807 ---LVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELT 3882
Cdd:PRK06164   319 gvpLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPASPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3883 AERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQGEGAwlmA 3959
Cdd:PRK06164   399 ARALTDDG---YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAqvvGATRDGKTVPV---A 472
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1246793773 3960 YAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:PRK06164   473 FVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESA 516
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
2054-2522 1.02e-32

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: 136.34  E-value: 1.02e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2054 AVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSG 2133
Cdd:cd05959     22 AFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVIGWGA-APAWVPASVRWLDAESVLDVVSAYEEPPRVDV-----------------DADTPAYLIYTSGSTGTPKGV 2195
Cdd:cd05959    102 ARVVVVSGElAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLlaelvaaeaeqlkpaatHADDPAFWLYSSGSTGRPKGV 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2196 VVSQGNLanYVAGVL---PVLDLGEDASLatLStvAADLGFT-----ALFGALLSGRRVRLLPAELAFDAQALAAHLQAH 2267
Cdd:cd05959    182 VHLHADI--YWTAELyarNVLGIREDDVC--FS--AAKLFFAyglgnSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRP 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 PVdcLKIVPSHLAGLLAAAGGTAVLP---REClVTGGEALTGALVQQVRALApTLRIVNHYGPTETtVGILTCTVPEEwp 2344
Cdd:cd05959    256 TV--FFGVPTLYAAMLAAPNLPSRDLsslRLC-VSAGEALPAEVGERWKARF-GLDILDGIGSTEM-LHIFLSNRPGR-- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2345 VEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEG 2424
Cdd:cd05959    329 VRYGT-TGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-------WTRTGDKYVRDDDG 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2425 RIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI--------QGSL-EGVAEALAQRLP 2495
Cdd:cd05959    401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpgyedSEALeEELKEFVKDRLA 480
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 2496 EYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05959    481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
543-1038 1.51e-32

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: 134.27  E-value: 1.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  543 RAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQA 622
Cdd:cd17631      3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  623 RRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengsgenaapnqLAYILYTSGSTGIPKGVEVGHAALAAH 702
Cdd:cd17631     83 EVAYILADSGAKVLFDD------------------------------------LALLMYTSGTTGRPKGAMLTHRNLLWN 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  703 IDAAAEALALSADDRVLHVAGL----AVDTTLEQILAawsRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANEL 778
Cdd:cd17631    127 AVNALAALDLGPDDVLLVVAPLfhigGLGVFTLPTLL---RGGTVVILRK--FDPETVLDLIERHRVTSFFLVPTMIQAL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  779 VRASVADDWRDLALRCLVVGGDVLPVALAQRWfelgLDRRCALINAYGPTEAT-----ISSHYHRVQAIDASRPVPLGQl 853
Cdd:cd17631    202 LQHPRFATTDLSSLRAVIYGGAPMPERLLRAL----QARGVKFVQGYGMTETSpgvtfLSPEDHRRKLGSAGRPVFFVE- 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  854 lpgriAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRA 933
Cdd:cd17631    277 -----VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-----DG----WFHTGDLGRLDEDGYLYIVDRK 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  934 DFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQrlvaWVECagedgfGQAdLNQTDSDQTESERWHRALC-ER 1012
Cdd:cd17631    343 KDMIISGGENVYPAEVEDVLYEHPAVAEVA--VIGVPDEK----WGEA------VVA-VVVPRPGAELDEDELIAHCrER 409
                          490       500
                   ....*....|....*....|....*.
gi 1246793773 1013 LPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd17631    410 LARYKIPKSVEFVDALPRNATGKILK 435
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3537-4014 2.25e-32

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 134.35  E-value: 2.25e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3537 AVSAEDGELDYATLDRRSSQLATLLirqgaGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG 3616
Cdd:PRK07787    18 AVRIGGRVLSRSDLAGAATAVAERV-----AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3617 VclsvsqRALAVELPGTALCLddPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTG 3696
Cdd:PRK07787    93 A------QAWLGPAPDDPAGL--PHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3697 RFSFDEHDVWSL--FHSHAFdfaVWELWGAWLYGGRAVLV----PEAVCRQPDAFLDLLaeYGV-TV---LNQTPSAFYA 3766
Cdd:PRK07787   165 QWTADDVLVHGLplFHVHGL---VLGVLGPLRIGNRFVHTgrptPEAYAQALSEGGTLY--FGVpTVwsrIAADPEAARA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3767 LQSqamrrelalnVRAVVFGGEALePSrlqPWRERYPQA---ELVNMYGITETTVHVSFHrlSDEDLQSPTsrIGSALPD 3843
Cdd:PRK07787   240 LRG----------ARLLVSGSAAL-PV---PVFDRLAALtghRPVERYGMTETLITLSTR--ADGERRPGW--VGLPLAG 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAAGQPVPLGV--VGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGR-GDDQVK 3920
Cdd:PRK07787   302 VETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADG---WFRTGDVAVVDPDGMHRIVGReSTDLIK 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVAADgaEPDPQSLREALRALLPDYMLPRLIQLLPALPL 3999
Cdd:PRK07787   379 SGGYRIGAGEIETALLGHPGVREAAVVGVPDDDlGQRIVAYVVGAD--DVAADELIDFVAQQLSVHKRPREVRFVDALPR 456
                          490
                   ....*....|....*
gi 1246793773 4000 TANGKLDRKALPKPE 4014
Cdd:PRK07787   457 NAMGKVLKKQLLSEG 471
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
3108-3427 2.48e-32

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: 133.32  E-value: 2.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3108 TVALHGALDREAFAAAWQQALERHPILRSGF-AVQGLPSPRQLPHRQVSLPLAEQDwsgLEPAQARSRLSELqaqqCEAG 3186
Cdd:cd19540     29 ALRLTGALDVDALRAALADVVARHESLRTVFpEDDGGPYQVVLPAAEARPDLTVVD---VTEDELAARLAEA----ARRG 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3187 FDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESRTPQLPAAPP-FRDYLHWLR------ 3259
Cdd:cd19540    102 FDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLPVqYADYALWQRellgde 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3260 -GQDEAAAR--AFWREQLTGLePAALPEATE---PAE-GYASSTRRFDL-----AAASAWAQSHGLTASSLLQGALALVL 3327
Cdd:cd19540    182 dDPDSLAARqlAYWRETLAGL-PEELELPTDrprPAVaSYRGGTVEFTIdaelhARLAALAREHGATLFMVLHAALAVLL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3328 QRYYGRDDFALGITIAGRP-PELagvERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQragaa 3406
Cdd:cd19540    261 SRLGAGDDIPIGTPVAGRGdEAL---DDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFERLV----- 332
                          330       340       350
                   ....*....|....*....|....*....|
gi 1246793773 3407 DAVSP---------FDVLLVFENLPTESRE 3427
Cdd:cd19540    333 EALNPprstarhplFQVMLAFQNTAAATLE 362
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
2062-2524 3.29e-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: 132.85  E-value: 3.29e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIAV-LDDSGARIVIgw 2140
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLL-GPKDIEYrLEAAGAKAIV-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:cd05972     78 ---------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDI 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLG-FTALFGALLSGRRVrLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPR-ECLV 2298
Cdd:cd05972    125 HWNIADPGWAKGaWSSFFGPWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHlRLVV 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2299 TGGEALTGALVQQVRA-LAPTLRivNHYGPTETTvgiLTCTVPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPAPVGVAGE 2377
Cdd:cd05972    204 SAGEPLNPEVIEWWRAaTGLPIR--DGYGQTETG---LTVGNFPDMPVKPG-SMGRPTPGYDVAIIDDDGRELPPGEEGD 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2378 L--YLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:cd05972    278 IaiKLPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEH 350
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2456 PGVEVAAVLALPG--------ANGVLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05972    351 PAVAEAAVVGSPDpvrgevvkAFVVLTSGYEPSEELaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
2049-2522 3.70e-32

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: 133.37  E-value: 3.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAV 2128
Cdd:cd17654      4 PALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 LDDSGarivigwgaapawvpasVRWLDAESVLDVVSAYEEPPRVDVDADTP---AYLIYTSGSTGTPKGVVVSQGNLANY 2205
Cdd:cd17654     84 MKKCH-----------------VSYLLQNKELDNAPLSFTPEHRHFNIRTDeclAYVIHTSGTTGTPKIVAVPHKCILPN 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 VAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSG-------RRVRLLPAELAfdaqalAAHLQAHPVDCLKIVPSH 2278
Cdd:cd17654    147 IQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGatllivpTSVKVLPSKLA------DILFKRHRITVLQATPTL 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2279 LAGLLAAAGGTAVLPR----ECLVTGGEAL-TGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpvEQGVPVGH 2353
Cdd:cd17654    221 FRRFGSQSIKSTVLSAtsslRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEE---DSPVQLGS 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2354 PLAGNEAWVLDRFGLPapvgVAGELYLGGgnLSLGYWQRAEQTAerfvahplaPDRLLYRSGDLARLDgEGRIVYLGRGD 2433
Cdd:cd17654    298 PLLGTVIEVRDQNGSE----GTGQVFLGG--LNRVCILDDEVTV---------PKGTMRATGDFVTVK-DGELFFLGRKD 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2434 HQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAngvlQLGACIQGslEGVAEALAQRL-----PEYLCPSRWRAVES 2508
Cdd:cd17654    362 SQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ----RLIAFIVG--ESSSSRIHKELqltllSSHAIPDTFVQIDK 435
                          490
                   ....*....|....
gi 1246793773 2509 MPRLGNGKIDRQAL 2522
Cdd:cd17654    436 LPLTSHGKVDKSEL 449
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3525-4012 6.56e-32

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 134.49  E-value: 6.56e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:PRK06087    29 WQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSW 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSG----VCLSVSQR--------ALAVELP--GTALCLD------DPFTRAQ-LDAVEP-GELPEVPTEA 3661
Cdd:PRK06087   109 REAELVWVLNKCQakmfFAPTLFKQtrpvdlilPLQNQLPqlQQIVGVDklapatSSLSLSQiIADYEPlTTAITTHGDE 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHSHAFDFAVWelwGAWLYGGRAVLVPEA 3737
Cdd:PRK06087   189 LAAVLFTSGTEGLPKGVMLTHNNI--LASERAYCARLNLTWQDVFmmpaPLGHATGFLHGVT---APFLIGARSVLLDIF 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVT-VLNQTPSAF---YALQSQAMRRElalNVRAVVFGGEALePSRLQpwRERYPQA-ELVNMYG 3812
Cdd:PRK06087   264 ---TPDACLALLEQQRCTcMLGATPFIYdllNLLEKQPADLS---ALRFFLCGGTTI-PKKVA--RECQQRGiKLLSVYG 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVHVsFHRLSDedlqsPTSRI----GSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE 3888
Cdd:PRK06087   335 STESSPHA-VVNLDD-----PLSRFmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3889 RGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQGEGawLMAYAV-AA 3964
Cdd:PRK06087   409 EG---WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAmpdERLGER--SCAYVVlKA 483
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773 3965 DGAEPDPQSLREAL-RALLPDYMLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:PRK06087   484 PHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3527-4020 8.66e-32

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 134.39  E-value: 8.66e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3527 EIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK06710    32 QMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTER 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSG----VCLS-------------------VSQRALAVELPGTALClddPFTRAQ----------------LD 3647
Cdd:PRK06710   112 ELEYQLHDSGakviLCLDlvfprvtnvqsatkiehviVTRIADFLPFPKNLLY---PFVQKKqsnlvvkvsesetihlWN 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3648 AVEPG-----ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlfTAATQTG---RFSFDEHD-----VWSLFHSHAF 3714
Cdd:PRK06710   189 SVEKEvntgvEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNL----VSNTLMGvqwLYNCKEGEevvlgVLPFFHVYGM 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3715 DfAVWELwgAWLYGGRAVLVPEAVCRQpdaFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGGEALePS 3793
Cdd:PRK06710   265 T-AVMNL--SIMQGYKMVLIPKFDMKM---VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISsIRACISGSAPL-PV 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3794 RLQPWRERYPQAELVNMYGITETT--VHVSFhrLSDEdlQSPTSrIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK06710   338 EVQEKFETVTGGKLVEGYGLTESSpvTHSNF--LWEK--RVPGS-IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQ 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VE 3949
Cdd:PRK06710   413 IMKGYWNKPEETAA--VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIgVP 488
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3950 GQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDE 4020
Cdd:PRK06710   489 DPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
3554-4057 8.78e-32

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 135.93  E-value: 8.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3554 SSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVEL-PG 3632
Cdd:PRK06060    40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFqPS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3633 TALCLDDPFTRAQldAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVvtHRNVERL-FTAATQTGRFSFDEHDVWSLFHS 3711
Cdd:PRK06060   120 RVAEAAELMSEAA--RVAPGGYEPMGGDALAYATYTSGTTGPPKAAI--HRHADPLtFVDAMCRKALRLTPEDTGLCSAR 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3712 HAFDFAVW-ELWGAWLYGGRAVLVPEAVCRQPDAFLDllAEYGVTVLNQTPSaFYALQSQAMRRELALNVRAVVFGGEAL 3790
Cdd:PRK06060   196 MYFAYGLGnSVWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPN-FFARVIDSCSPDSFRSLRCVVSAGEAL 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPSRLQPWRERYPQAELVNmyGITETTVHVSFHRLSDEDLQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK06060   273 ELGLAERLMEFFGGIPILD--GIGSTEVGQTFVSNRVDEWRLGT--LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPA 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPeltaERFVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEG 3950
Cdd:PRK06060   349 IAKGYWNRP----DSPVANEG--WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3951 QGEGA-WLMAYAVAADGAEPDPQSLREALRALLPD---YMLPRLIQLLPALPLTANGKLDRKALpKPETQDRDEGVLESA 4026
Cdd:PRK06060   423 ESTGAsTLQAFLVATSGATIDGSVMRDLHRGLLNRlsaFKVPHRFAVVDRLPRTPNGKLVRGAL-RKQSPTKPIWELSLT 501
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1246793773 4027 SERRLAElwrqllgGELPGRGA-HFFARGGHS 4057
Cdd:PRK06060   502 EPGSGVR-------AQRDDLSAsNMTIAGGND 526
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
534-1041 8.87e-32

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 133.49  E-value: 8.87e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  534 VGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVI 613
Cdd:PRK07656     4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  614 PLDTEWPQARRAEVVAASGCDAVLtdaqGLAGFAPSVAIAVDEL-------------------------KLDGAGENGSG 668
Cdd:PRK07656    84 PLNTRYTADEAAYILARGDAKALF----VLGLFLGVDYSATTRLpalehvviceteeddphtekmktftDFLAAGDPAER 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  669 ENA-APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDttleqILAAWSRGA 741
Cdd:PRK07656   160 APEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLaanpffHVFGYKAG-----VNAPLMRGA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  742 CVVARPdeLLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDLA-LRCLVVGGDVLPVALAQRwF--ELGLDRr 818
Cdd:PRK07656   235 TILPLP--VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-EDLSsLRLAVTGAASMPVALLER-FesELGVDI- 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  819 caLINAYGPTEA----TISShyhrvqaIDASR---PVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGD 891
Cdd:PRK07656   310 --VLTGYGLSEAsgvtTFNR-------LDDDRktvAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDD 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  892 AAASErrfaplrlpsgESLRM---YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVV 967
Cdd:PRK07656   381 PEATA-----------AAIDAdgwLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaEAAVIGVP 449
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773  968 GEGAAQRLVAWVECAGEDGFGQADLNQtdsdqteserWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK07656   450 DERLGEVGKAYVVLKPGAELTEEELIA----------YCR---EHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
3499-4011 9.38e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 133.58  E-value: 9.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3499 LLPSQTRSAAWTSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPR 3578
Cdd:PRK13383    15 LNPPSPRAVLRLLREASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3579 GCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPGT--ALCLDDPFTraqLDAVEPGELPE 3656
Cdd:PRK13383    95 GRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGAddAVAVIDPAT---AGAEESGGRPA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEAPAYLIyTSGSTGTPKGV------------VVTHRNVERLFTAAtqtgRFSFdehdVWSLFHSHAFDFAVW--ELW 3722
Cdd:PRK13383   172 VAAPGRIVLL-TSGTTGKPKGVprapqlrsavgvWVTILDRTRLRTGS----RISV----AMPMFHGLGLGMLMLtiALG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3723 GAWL----YGGRAVLVPEAVCRQpDAFldllaeygvTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEALEPSRLQPW 3798
Cdd:PRK13383   243 GTVLthrhFDAEAALAQASLHRA-DAF---------TAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRF 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3799 RERYPQAeLVNMYGITETTVHVsfhRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGdgvaqgywqr 3878
Cdd:PRK13383   313 MDTYGDI-LYNGYGSTEVGIGA---LATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG---------- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3879 pELTAERFVERGGQR----FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGE 3953
Cdd:PRK13383   379 -ELAGTRYTDGGGKAvvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIgVPDERF 457
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 3954 GAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALP 4011
Cdd:PRK13383   458 GHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2630-3043 9.99e-32

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: 132.07  E-value: 9.99e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQH--WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGD-----WQADR 2702
Cdd:pfam00668    7 LSPAQKrmWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEerpfeLEIID 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2703 FAHREADAGQR-EDLLAQWQAGLSFD---GALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGR 2778
Cdd:pfam00668   87 ISDLSESEEEEaIEAFIQRDLQSPFDlekGPLFRA-GLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2779 SPALAAEAC--GFGAWQAALRQlSAATLDGwRSYWR-AQAADAEAIALPwqdsdNRYADTVhlHDRFERD--------WT 2847
Cdd:pfam00668  166 PLPLPPKTPykDYAEWLQQYLQ-SEDYQKD-AAYWLeQLEGELPVLQLP-----KDYARPA--DRSFKGDrlsftldeDT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2848 ERLLTQTARAYGNEPQEVLLTalalalrdggdAATLW-----------VEMEGHGRDdlgaGLDLSRTVGWFTARYPLAL 2916
Cdd:pfam00668  237 EELLRKLAKAHGTTLNDVLLA-----------AYGLLlsrytgqddivVGTPGSGRP----SPDIERMVGMFVNTLPLRI 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2917 HLPAGEDLGAALRSTKDRMR-AVPDRGLGFGVLRY---LHGELAELPVPQVCF---NYLGQLRagERDGWALCEEPDGGG 2989
Cdd:pfam00668  302 DPKGGKTFSELIKRVQEDLLsAEPHQGYPFGDLVNdlrLPRDLSRHPLFDPMFsfqNYLGQDS--QEEEFQLSELDLSVS 379
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2990 RAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:pfam00668  380 SVIEEEAKYDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIA 433
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3521-4010 1.19e-31

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 133.61  E-value: 1.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD 3600
Cdd:PRK07059    25 LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVN 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 P-HAP----------AARRGFILEDSGVCL-----SVSQRALAVELPGTALCLDDPF----TRAQLDAVEPGELP----- 3655
Cdd:PRK07059   105 PlYTPrelehqlkdsGAEAIVVLENFATTVqqvlaKTAVKHVVVASMGDLLGFKGHIvnfvVRRVKKMVPAWSLPghvrf 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3656 ------------EVPTEAP---AYLIYTSGSTGTPKGVVVTHRNV-----------ERLFTAATQTGRFSFdehdVWSLF 3709
Cdd:PRK07059   185 ndalaegarqtfKPVKLGPddvAFLQYTGGTTGVSKGATLLHRNIvanvlqmeawlQPAFEKKPRPDQLNF----VCALP 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HSHAFDFAVWELWGAWLyGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGE 3788
Cdd:PRK07059   261 LYHIFALTVCGLLGMRT-GGRNILIPNP--RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFsKLIVANGGGM 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3789 ALEPSRLQPWRERyPQAELVNMYGITETTVHVSFHRLSDEDLqspTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEG 3868
Cdd:PRK07059   338 AVQRPVAERWLEM-TGCPITEGYGLSETSPVATCNPVDATEF---SGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRG 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3869 DGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD-AAVT 3947
Cdd:PRK07059   414 PQVMAGYWNRPDETAKVMTADG---FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEvAAVG 490
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3948 VEGQGEGAWLMAYAVAADGAEPDpQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07059   491 VPDEHSGEAVKLFVVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
588-1041 2.44e-31

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 132.93  E-value: 2.44e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWpqarRAEVVA----ASGCDAVLTDAQGLAG-----FAPSVAIAVDELK 658
Cdd:COG0365     67 VAIYLPNIPEAVIAMLACARIGAVHSPVFPGF----GAEALAdrieDAEAKVLITADGGLRGgkvidLKEKVDEALEELP 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  659 -------LDGAGENGSGENA-------------------APNQLAYILYTSGSTGIPKGvevghaalaahidaaaealal 712
Cdd:COG0365    143 slehvivVGRTGADVPMEGDldwdellaaasaefepeptDADDPLFILYTSGTTGKPKG--------------------- 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  713 saddrVLHVAG---LAVDTTLEQIL-------------------------AAWSRGACVV---ARPDeLLEPQRFLAFLS 761
Cdd:COG0365    202 -----VVHTHGgylVHAATTAKYVLdlkpgdvfwctadigwatghsyivyGPLLNGATVVlyeGRPD-FPDPGRLWELIE 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  762 ERAITVTDLAPAYANELVRAsvADDWR---DL-ALRCLVVGGDVLPVALAQRWFE-LGldrrCALINAYGPTEAT--ISS 834
Cdd:COG0365    276 KYGVTVFFTAPTAIRALMKA--GDEPLkkyDLsSLRLLGSAGEPLNPEVWEWWYEaVG----VPIVDGWGQTETGgiFIS 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  835 HYhrvqAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGG--IGLAEGYRGDAAASERRFaplrlpSGESLRM 912
Cdd:COG0365    350 NL----PGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETY------FGRFPGW 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  913 YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAgeDGFgqad 991
Cdd:COG0365    420 YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAeAAVVGVPDEIRGQVVKAFVVLK--PGV---- 493
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773  992 lnqTDSDQTESERwHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:COG0365    494 ---EPSDELAKEL-QAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3529-4010 2.76e-31

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 132.32  E-value: 2.76e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIA--VSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK05852    26 ATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 R----------RGFILEDSGVC----LSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPT---EAPAYLIYTS 3669
Cdd:PRK05852   106 EqrvrsqaagaRVVLIDADGPHdraePTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglrPDDAMIMFTG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVVVTHRNVE---RLFTAATQTGrfsfdEHD----VWSLFHSHAFDFAVWelwgAWLYGGRAVLVPEAVCRQP 3742
Cdd:PRK05852   186 GTTGLPKMVPWTHANIAssvRAIITGYRLS-----PRDatvaVMPLYHGHGLIAALL----ATLASGGAVLLPARGRFSA 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYAL----QSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTV 3818
Cdd:PRK05852   257 HTFWDDIKAVGATWYTAVPTIHQILleraATEPSGRKPA-ALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATH 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3819 HVSFHRLSDEDL-QSPTSRIGSALPDLA--VHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFY 3895
Cdd:PRK05852   335 QVTTTQIEGIGQtENPVVSTGLVGRSTGaqIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD----GWL 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3896 RSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSL 3974
Cdd:PRK05852   411 RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEAVAAVIVPRESAPPTAEEL 490
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1246793773 3975 REALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK05852   491 VQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
3661-4010 4.88e-31

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: 127.06  E-value: 4.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 APAYLIYTSGSTGTPKGVVVTHRNverLFTAATQTG-RFSFDEHDVW--SLFHSHAFDFAVweLWgAWLYGGRAVLVPEa 3737
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAAN---LLASAAGLHsRLGFGGGDSWllSLPLYHVGGLAI--LV-RSLLAGAELVLLE- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcrQPDAFLDLLAEYGVTVLNQTPSAF-YALQSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERypQAELVNMYGITET 3816
Cdd:cd17630     74 ---RNQALAEDLAPPGVTHVSLVPTQLqRLLDSGQGPAALK-SLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTET 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDEDLQSptsrIGSALPDLAVHVLDAagqpvplgvvGELVVEGDGVAQGYWqRPELTAERFvergGQRFYR 3896
Cdd:cd17630    148 ASQVATKRPDGFGRGG----VGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFN----EDGWFT 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3897 SGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWLMAYAVAADGAEP-DPQSLR 3975
Cdd:cd17630    209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV--GVPDEELGQRPVAVIVGRGPaDPAELR 286
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1246793773 3976 EALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd17630    287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
2061-2522 5.08e-31

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: 129.50  E-value: 5.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgw 2140
Cdd:cd05919     10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV-AGVLPVLDLGEDA 2219
Cdd:cd05919     88 ---------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTPGD 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLSTV--AADLGfTALFGALLSGRRVRLLPAELAFDAQALAAHLQAHPVdcLKIVPSHLAGLLAAAGGTAVLPRE-- 2295
Cdd:cd05919    135 RVFSSAKMffGYGLG-NSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTV--LYGVPTFYANLLDSCAGSPDALRSlr 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 CLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETtVGILTCTVPEEWPVEQgvpVGHPLAGNEAWVLDRFGLPAPVGVA 2375
Cdd:cd05919    212 LCVSAGEALPRGLGERWME-HFGGPILDGIGATEV-GHIFLSNRPGAWRLGS---TGRPVPGYEIRLVDEEGHTIPPGEE 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:cd05919    287 GDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQH 359
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2456 PGVEVAAVLALPGANG--------VLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05919    360 PAVAEAAVVAVPESTGlsrltafvVLKSPAAPQESLaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
3520-4012 5.53e-31

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: 132.44  E-value: 5.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARR-YPARIAVSAEDGELD---YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAA 3595
Cdd:cd05967     54 NALDRHVEAGRGdQIALIYDSPVTGTERtytYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3596 YVPV----DPHAPAARrgfiLEDSGVCLSVSQRA-------------------LAVELPGTALCLDDPFTRAQLDAVE-- 3650
Cdd:cd05967    134 HSVVfggfAAKELASR----IDDAKPKLIVTASCgiepgkvvpykplldkaleLSGHKPHHVLVLNRPQVPADLTKPGrd 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3651 ---------PGELPEVPTEA--PAYLIYTSGSTGTPKGVVvthRNVERLFTAATQTGRFSFDEH---------DV-WSLF 3709
Cdd:cd05967    210 ldwsellakAEPVDCVPVAAtdPLYILYTSGTTGKPKGVV---RDNGGHAVALNWSMRNIYGIKpgdvwwaasDVgWVVG 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HShafdFAVWE--LWGAW--LYGGRAVLVPEavcrqPDAFLDLLAEYGVTVLNQTPSAFYALQSQ-----AMRRELALNV 3780
Cdd:cd05967    287 HS----YIVYGplLHGATtvLYEGKPVGTPD-----PGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgkYIKKYDLSSL 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3781 RAVVFGGEALEPSRLQpWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGV 3860
Cdd:cd05967    358 RTLFLAGERLDPPTLE-WAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNE 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 VGELVVEGD---GVAQGYWQRPEltaeRFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:cd05967    437 LGNIVIKLPlppGCLLTLWKNDE----RFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEES 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3935 IASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLP----RLIQLLPALPLTANGKLDRKA 4009
Cdd:cd05967    513 VLSHPAVAECAVVgVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSGKILRRT 592

                   ...
gi 1246793773 4010 LPK 4012
Cdd:cd05967    593 LRK 595
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
3507-4010 9.83e-31

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 134.28  E-value: 9.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3507 AAWTSRERYACTgnLVSRFAEIARRYPARIAVSAEDG-ELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVA 3585
Cdd:PRK08633   605 DSWKSRKEALPP--LAEAWIDTAKRNWSRLAVADSTGgELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALA 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3586 LLAILKTGAayVPVDPHAPAARRGFI--LEDSGVCLSVSQRA-----------LAVELPGTALCLDDPFTRAQ------- 3645
Cdd:PRK08633   682 NLALLLAGK--VPVNLNYTASEAALKsaIEQAQIKTVITSRKfleklknkgfdLELPENVKVIYLEDLKAKISkvdklta 759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 --------LDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTgrFSFDEHDV----WSLFHSha 3713
Cdd:PRK08633   760 llaarllpARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDV--FNLRNDDVilssLPFFHS-- 835
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3714 FDFAVwELWGAWLYGGRAVLVPEavcrqP-DAFL--DLLAEYGVTVLNQTPSAFYA-LQSQAMRRELALNVRAVVFGGEA 3789
Cdd:PRK08633   836 FGLTV-TLWLPLLEGIKVVYHPD-----PtDALGiaKLVAKHRATILLGTPTFLRLyLRNKKLHPLMFASLRLVVAGAEK 909
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3790 LEPSRLQPWRERYpQAELVNMYGITETTVHVSFH---RLSDEDLQSPTSRIGS---ALPDLAVHVLDA-AGQPVPLGVVG 3862
Cdd:PRK08633   910 LKPEVADAFEEKF-GIRILEGYGATETSPVASVNlpdVLAADFKRQTGSKEGSvgmPLPGVAVRIVDPeTFEELPPGEDG 988
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGR-------GDDQVKLRgyRIEPgEIAAKI 3935
Cdd:PRK08633   989 LILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRysrfakiGGEMVPLG--AVEE-ELAKAL 1065
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3936 -ASLPQVSDAAVTVEGQGEgawlmAYAVAADGAEPDPQSLREALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK08633  1066 gGEEVVFAVTAVPDEKKGE-----KLVVLHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
3541-4007 2.35e-30

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: 128.33  E-value: 2.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVcls 3620
Cdd:cd05914      4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA--- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 vsqralavelpgTALCLDDPftraqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSF 3700
Cdd:cd05914     81 ------------KAIFVSDE-------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGK 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3701 DEHDVWSLFHSHAFDFaVWELWGAWLYGGRAVLVPeavcRQPDAFLDLLAEYGVTV------------------LNQTPS 3762
Cdd:cd05914    130 GDKILSILPLHHIYPL-TFTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPtlgvpvplviekifkmdiIPKLTL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 A--------------FYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRE-RYPQAElvnMYGITETTVHVSFHRLSD 3827
Cdd:cd05914    205 KkfkfklakkinnrkIRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTiGFPYTI---GYGMTETAPIISYSPPNR 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3828 EDLQSptsrIGSALPDLAVHVLDaagqPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADG 3907
Cdd:cd05914    282 IRLGS----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDG---WFHTGDLGKIDAEG 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3908 SLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALR------- 3979
Cdd:cd05914    351 YLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKwevrdkv 430
                          490       500       510
                   ....*....|....*....|....*....|
gi 1246793773 3980 -ALLPDYMLPRLIQLLPA-LPLTANGKLDR 4007
Cdd:cd05914    431 nQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3529-4032 2.82e-30

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 129.49  E-value: 2.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK06155    31 AERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDSGVCLSVSQRALAVELPgTALCLDDPFTR--------AQLDAVEPGELPEVPTEAPA-----------YLIYTS 3669
Cdd:PRK06155   111 EHILRNSGARLLVVEAALLAALE-AADPGDLPLPAvwlldapaSVSVPAGWSTAPLPPLDAPApaaavqpgdtaAILYTS 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVVVTHrnvERLFTAATQTGR-FSFDEHDVW----SLFHSHAFDfavwELWGAWLYGGRAVLVPEAvcrQPDA 3744
Cdd:PRK06155   190 GTTGPSKGVCCPH---AQFYWWGRNSAEdLEIGADDVLyttlPLFHTNALN----AFFQALLAGATYVLEPRF---SASG 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3745 FLDLLAEYGVTVLNQTPSAFYALQSQAMR-RELALNVRAVVFGGEAlePSRLQPWRERYPQAeLVNMYGITETTVHVSFH 3823
Cdd:PRK06155   260 FWPAVRRHGATVTYLLGAMVSILLSQPAReSDRAHRVRVALGPGVP--AALHAAFRERFGVD-LLDGYGSTETNFVIAVT 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3824 RLSdedlQSPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD---GVAQGYWQRPELTaerfVERGGQRFYRSGDL 3900
Cdd:PRK06155   337 HGS----QRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKT----VEAWRNLWFHTGDR 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREALR 3979
Cdd:PRK06155   408 VVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfPVPSELGEDEVMAAVVLRDGTALEPVALVRHCE 487
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqdRDEGVLESASERRLA 4032
Cdd:PRK06155   488 PRLAYFAVPRYVEFVAALPKTENGKVQKFVL-------REQGVTADTWDREAA 533
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
3081-3403 2.97e-30

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: 127.10  E-value: 2.97e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3081 YPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF-AVQGLPSPRQLPHRQVSLPLA 3159
Cdd:cd19533      2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFtEEEGEPYQWIDPYTPVPIRHI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3160 eqDWSGLE-PAQARSRLSELQAQQceaGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALR 3238
Cdd:cd19533     82 --DLSGDPdPEGAAQQWMQEDLRK---PLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 ESRTPQLPAAPPFRDYL----------HWLRGqdeaaaRAFWREQLTGL-EPAALpeaTEPAEGYASSTRRFDL------ 3301
Cdd:cd19533    157 KGRPAPPAPFGSFLDLVeeeqayrqseRFERD------RAFWTEQFEDLpEPVSL---ARRAPGRSLAFLRRTAelppel 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3302 -AAASAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRppeLAGVER-MLGVFINSVPLRVTPAGEATPAPWL 3379
Cdd:cd19533    228 tRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR---LGAAARqTPGMVANTLPLRLTVDPQQTFAELV 304
                          330       340
                   ....*....|....*....|....
gi 1246793773 3380 QALQQRNLDLRTHGYLPLAQIQRA 3403
Cdd:cd19533    305 AQVSRELRSLLRHQRYRYEDLRRD 328
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1142-1559 3.18e-30

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: 127.14  E-value: 3.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDR--YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQD 1219
Cdd:cd19066      4 LSPMQRGMWFLKKLATDPsaFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEIID 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1220 WRGAADLDSRVDAAFARMQEaTPL---AGPLVALT-HAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAW 1295
Cdd:cd19066     84 LRNLADPEARLLELIDQIQQ-TIYdleRGPLVRVAlFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1296 TPSARGaSYADYVEAL---READDAQRfDAGFWRELAAQ--PMQALPQD-RPVALADARQsnvGRIVQTLDAGLTADLLE 1369
Cdd:cd19066    163 LPPPVG-SYADYAAWLekqLESEAAQA-DLAYWTSYLHGlpPPLPLPKAkRPSQVASYEV---LTLEFFLRSEETKRLRE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1370 RAGEAYRCRTDeVLLIALARALATRTGRNRLWLDRERHGR---DVLDgrdwssVLGWYTAVHPLPLDLGV-ADGPAQIGA 1445
Cdd:cd19066    238 VARESGTTPTQ-LLLAAFALALKRLTASIDVVIGLTFLNRpdeAVED------TIGLFLNLLPLRIDTSPdATFPELLKR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1446 LKEQIRALARRGLDYMPLV--ASARIPALPAGQL---LFNYH------GVVDAGAHPAFEVEPRTlasgngadnPPGALV 1514
Cdd:cd19066    311 TKEQSREAIEHQRVPFIELvrHLGVVPEAPKHPLfepVFTFKnnqqqlGKTGGFIFTTPVYTSSE---------GTVFDL 381
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773 1515 EINARVQA-GRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHC 1559
Cdd:cd19066    382 DLEASEDPdGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
3665-4005 3.50e-30

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: 124.54  E-value: 3.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHD--VWSLFHShafdFAVWELWGAWLYGGrAVLVPEAVCrQP 3742
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYliINPFFHT----FGYKAGIVACLLTG-ATVVPVAVF-DV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVS 3821
Cdd:cd17638     79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLsSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV-AT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 FHRLSDeDLQSPTSRIGSALPDLAVHVLDAagqpvplgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLG 3901
Cdd:cd17638    158 MCRPGD-DAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADG---WLHTGDVG 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3902 RYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRA 3980
Cdd:cd17638    224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRE 303
                          330       340
                   ....*....|....*....|....*
gi 1246793773 3981 LLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:cd17638    304 RLANYKVPRFVRFLDELPRNASGKV 328
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
3543-4010 4.45e-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: 127.83  E-value: 4.45e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3543 GELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGaaYVPVDPHAPAARRGFI--LEDSGVCLS 3620
Cdd:cd05909      6 TSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGLRELRacIKLAGIKTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3621 VSQRAL----------AVELPGTALCLDDpfTRAQL---DAVEPG------------ELPEVPTEA--PAYLIYTSGSTG 3673
Cdd:cd05909     83 LTSKQFieklklhhlfDVEYDARIVYLED--LRAKIskaDKCKAFlagkfppkwllrIFGVAPVQPddPAVILFTSGSEG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHShaFDFAVwELWGAWLYGGRAVLVPEAVcrQPDAFLDLL 3749
Cdd:cd05909    161 LPKGVVLSHKNL--LANVEQITAIFDPNPEDVVfgalPFFHS--FGLTG-CLWLPLLSGIKVVFHPNPL--DYKKIPELI 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3750 AEYGVTVLNQTPSAFYALQSQAMRRELAlNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRlsded 3829
Cdd:cd05909    234 YDKKATILLGTPTFLRGYARAAHPEDFS-SLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVNT----- 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPtSRIGSA---LPDLAVHVLDAAG-QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErggqRFYRSGDLGRYRA 3905
Cdd:cd05909    307 PQSP-NKEGTVgrpLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD----GWYDTGDIGKIDG 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3906 DGSLEYRGRGDDQVKLRG-----YRIEpgEIAAKIasLP-QVSDAAVTV--EGQGEgawlmAYAVAADGAEPDPQSLREA 3977
Cdd:cd05909    382 EGFLTITGRLSRFAKIAGemvslEAIE--DILSEI--LPeDNEVAVVSVpdGRKGE-----KIVLLTTTTDTDPSSLNDI 452
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1246793773 3978 LRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05909    453 LKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
3529-4010 1.30e-29

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 127.07  E-value: 1.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLI--RQGAGPgQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPhapaA 3606
Cdd:PRK13388    11 DRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIalADPDRP-LHVGVLLGNTPEMLFWLAAAALGGYVLVGLNT----T 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILE------DSGVCLSVSQ-RAL--AVELPGTALCLDDPFTRAQLDAVEPGELP--EVPTEAPAYLIYTSGSTGTP 3675
Cdd:PRK13388    86 RRGAALAadirraDCQLLVTDAEhRPLldGLDLPGVRVLDVDTPAYAELVAAAGALTPhrEVDAMDPFMLIFTSGTTGAP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3676 KGVVVTHRNVerLFTAATQTGRFSFDEHDV----WSLFHSHafdfAVWELWGAWLYGGRAVLVPEAVcrQPDAFLDLLAE 3751
Cdd:PRK13388   166 KAVRCSHGRL--AFAGRALTERFGLTRDDVcyvsMPLFHSN----AVMAGWAPAVASGAAVALPAKF--SASGFLDDVRR 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAFYALQSQAMRRELALNVRAVVFGGEAlEPSRLQPWRERYpQAELVNMYGITETTVHVSfhrlsdEDLQ 3831
Cdd:PRK13388   238 YGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEA-SPRDIAEFSRRF-GCQVEDGYGSSEGAVIVV------REPG 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3832 SPTSRIGSALPDLAVH-----------VLDAAGQPV-PLGVVGELV-VEGDGVAQGYWQRPELTAERFveRGGqrFYRSG 3898
Cdd:PRK13388   310 TPPGSIGRGAPGVAIYnpetltecavaRFDAHGALLnADEAIGELVnTAGAGFFEGYYNNPEATAERM--RHG--MYWSG 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3899 DLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREA 3977
Cdd:PRK13388   386 DLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyAVPDERVGDQVMAALVLRDGATFDPDAFAAF 465
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 3978 LRAL--LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK13388   466 LAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
673-1044 1.34e-29

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: 126.86  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGA-CVVARPDELL 751
Cdd:cd17647    108 PDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAqLLVPTQDDIG 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  752 EPQRFLAFLSERAITVTDLAPAYAnELVRASVADDWRDLaLRCLVVGgDVLPVALAQRWfeLGLDRRCALINAYGPTEAT 831
Cdd:cd17647    188 TPGRLAEWMAKYGATVTHLTPAMG-QLLTAQATTPFPKL-HHAFFVG-DILTKRDCLRL--QTLAENVRIVNMYGTTETQ 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  832 ISSHYHRVQA--------------IDASRPVPLGQLLpgriaaVLDAHGR--IVPRGVCGELALGGIGLAEGYRGDAAAS 895
Cdd:cd17647    263 RAVSYFEVPSrssdptflknlkdvMPAGRGMLNVQLL------VVNRNDRtqICGIGEVGEIYVRAGGLAEGYRGLPELN 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  896 ERRF-------------------APLRLPS-GESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQ 955
Cdd:cd17647    337 KEKFvnnwfvepdhwnyldkdnnEPWRQFWlGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQ 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  956 LPQVRAAAAGVVGEGAAQR-LVAWVECAGE--DGFGQADLNQTDSDQTES-----ERWHRA-------LCERLPAYMVPT 1020
Cdd:cd17647    417 HPLVRENITLVRRDKDEEPtLVSYIVPRFDkpDDESFAQEDVPKEVSTDPivkglIGYRKLikdirefLKKRLASYAIPS 496
                          410       420
                   ....*....|....*....|....
gi 1246793773 1021 QFVALPRLPRNASGKIDRRALPAP 1044
Cdd:cd17647    497 LIVVLDKLPLNPNGKVDKPKLQFP 520
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3115-3385 2.17e-29

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: 124.52  E-value: 2.17e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3115 LDREAFAAAWQQALERHPILRSGFavqgLPSPRQLPHRQVSLP-LAEQDWSGLEPAQARSRLSELQAQ---QCeagFDLA 3190
Cdd:cd19535     37 LDPDRLERAWNKLIARHPMLRAVF----LDDGTQQILPEVPWYgITVHDLRGLSEEEAEAALEELRERlshRV---LDVE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3191 APPL--MRLALLRRSAdehwlvwTRHH-----LIVDGWSSALLLDEVWRLYAALREsrtpQLPAAPP-FRDYLHWLRGQD 3262
Cdd:cd19535    110 RGPLfdIRLSLLPEGR-------TRLHlsidlLVADALSLQILLRELAALYEDPGE----PLPPLELsFRDYLLAEQALR 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3263 EAA---ARAFWREQLTGLEPA-ALPEATEPAE-GYASSTRRFDLAAASAW------AQSHGLTASSLLQGALALVLQRYY 3331
Cdd:cd19535    179 ETAyerARAYWQERLPTLPPApQLPLAKDPEEiKEPRFTRREHRLSAEQWqrlkerARQHGVTPSMVLLTAYAEVLARWS 258
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3332 GRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQR 3385
Cdd:cd19535    259 GQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQ 312
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3533-4010 2.46e-29

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 126.26  E-value: 2.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYV--------------- 3597
Cdd:PRK10946    37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnalfshqrselnaya 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 -PVDP--------HAPAARRGFILEDSGVCLSVSQRALavelpgtalcLDDPFTRAQLDAVEPGELPEVPTEAP----AY 3664
Cdd:PRK10946   117 sQIEPalliadrqHALFSDDDFLNTLVAEHSSLRVVLL----------LNDDGEHSLDDAINHPAEDFTATPSPadevAF 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLV--PEAVCRQP 3742
Cdd:PRK10946   187 FQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSPGALGVFLAGGTVVLApdPSATLCFP 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 dafldLLAEYGVTVLNQTPSAFyALQSQAM-----RRELA-LNVRAVvfGGEALEPSRLQpwreRYPQ---AELVNMYGI 3813
Cdd:PRK10946   267 -----LIEKHQVNVTALVPPAV-SLWLQAIaeggsRAQLAsLKLLQV--GGARLSETLAR----RIPAelgCQLQQVFGM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETTVhvSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PRK10946   335 AEGLV--NYTRLDDSDERIFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG--- 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAA-VTVEGQGEGAWLMAYAVAADGAEpdPQ 3972
Cdd:PRK10946   410 FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAAlVSMEDELMGEKSCAFLVVKEPLK--AV 487
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1246793773 3973 SLREALRAL-LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK10946   488 QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3082-3396 3.25e-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: 123.91  E-value: 3.25e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLF-HSLLnaeADPYINQTTVALH--GALDREAFAAAWQQALERHPILRSGFaVQGLPSPRQLPHRQVSLPL 3158
Cdd:cd20483      3 PMSTFQRRLWFlHNFL---EDKTFLNLLLVCHikGKPDVNLLQKALSELVRRHEVLRTAY-FEGDDFGEQQVLDDPSFHL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3159 AEQDWSglEPAQARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALR 3238
Cdd:cd20483     79 IVIDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3239 ESRTPQLPAAPP--FRDYLHW----LRGQDEAAARAFWREQLTGLEPAA--LPEATE---PAEGYASSTRRFDLAAASA- 3306
Cdd:cd20483    157 AGRDLATVPPPPvqYIDFTLWhnalLQSPLVQPLLDFWKEKLEGIPDASklLPFAKAerpPVKDYERSTVEATLDKELLa 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3307 ----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRP-PElagVERMLGVFINSVPLRVTPAGEATPAPWLQA 3381
Cdd:cd20483    237 rmkrICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPhPD---FDDLVGFFVNMLPIRCRMDCDMSFDDLLES 313
                          330
                   ....*....|....*
gi 1246793773 3382 LQQRNLDLRTHGYLP 3396
Cdd:cd20483    314 TKTTCLEAYEHSAVP 328
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
672-1041 4.03e-29

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: 124.08  E-value: 4.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGHAALA-AHIDAAAEALALSADDRVLH-------VAGLavdttLEQILAAWSRGACV 743
Cdd:cd05971     86 GSDDPALIIYTSGTTGPPKGALHAHRVLLgHLPGVQFPFNLFPRDGDLYWtpadwawIGGL-----LDVLLPSLYFGVPV 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  744 VARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQrWF--ELGLDrrcal 821
Cdd:cd05971    161 LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLG-WAreQFGVE----- 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  822 IN-AYGPTEAT--ISSHyhrvQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELAL---GGIGLAeGYRGDAAAS 895
Cdd:cd05971    235 VNeFYGQTECNlvIGNC----SALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVelpDPVAFL-GYWNNPSAT 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  896 ERRFAplrlpsGESLRmyrSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQR 974
Cdd:cd05971    310 EKKMA------GDWLL---TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLmAAVVGIPDPIRGEI 380
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  975 LVAWVEcagedgfgqadLNQTDSDQTESERWHRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05971    381 VKAFVV-----------LNPGETPSDALAREIQELVKtRLAAHEYPREIEFVNELPRTATGKIRRREL 437
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
588-1042 4.60e-29

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: 123.56  E-value: 4.60e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDaqglagfapsvaiavdelkldgagengs 667
Cdd:cd05934     31 VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD---------------------------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 genaapnqLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGA 741
Cdd:cd05934     83 --------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLtvlplfHINAQAV-----SVLAALSVGA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  742 CVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRClvVGGDVLPVALAQRWFElgldrR--C 819
Cdd:cd05934    150 TLVLLPR--FSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA--AYGAPNPPELHEEFEE-----RfgV 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  820 ALINAYGPTEATISShyhrVQAIDASRPVP-LGQLLPGRIAAVLDAHGRIVPRGVCGEL---ALGGIGLAEGYRGDAAAS 895
Cdd:cd05934    221 RLLEGYGMTETIVGV----IGPRDEPRRPGsIGRPAPGYEVRIVDDDGQELPAGEPGELvirGLRGWGFFKGYYNMPEAT 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  896 ERRFAPLrlpsgeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQR 974
Cdd:cd05934    297 AEAMRNG---------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvAVPDEVGEDE 367
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  975 LVAWVECagEDGfgqadlnQTDsDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:cd05934    368 VKAVVVL--RPG-------ETL-DPEELFAFCE---GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
2050-2527 4.63e-29

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 125.88  E-value: 4.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK05605    46 GDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPF 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWG-AAP----------------------------------------------AWVPASVRW---LDAESV 2159
Cdd:PRK05605   126 EDHGARVAIVWDkVAPtverlrrttpletivsvnmiaampllqrlalrlpipalrkaraaltGPAPGTVPWetlVDAAIG 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2160 LDVVSAyeEPPRVDvdADTPAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDAS--LATLSTVAA-DLGFTA 2235
Cdd:PRK05605   206 GDGSDV--SHPRPT--PDDVALILYTSGTTGKPKGAQLTHRNLfANAAQGKAWVPGLGDGPErvLAALPMFHAyGLTLCL 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2236 LFGALLSGRRVrLLPaelAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAV--------------LPREcLVTGG 2301
Cdd:PRK05605   282 TLAVSIGGELV-LLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVdlsgvrnafsgamaLPVS-TVELW 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2302 EALTGALvqqvralaptlrIVNHYGPTETTvgiltctvpeewPVEQGVP---------VGHPLAGNEAWVLDR--FGLPA 2370
Cdd:PRK05605   357 EKLTGGL------------LVEGYGLTETS------------PIIVGNPmsddrrpgyVGVPFPDTEVRIVDPedPDETM 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2371 PVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQ 2450
Cdd:PRK05605   413 PDGEEGELLVRGPQVFKGYWNRPEETAKSF-----LDG--WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE 485
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2451 VLAQLPGVEVAAVLALPGANG--------VLQLGACIQGslEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK05605   486 VLREHPGVEDAAVVGLPREDGseevvaavVLEPGAALDP--EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563

                   ....*
gi 1246793773 2523 ADLLQ 2527
Cdd:PRK05605   564 REELL 568
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3545-4010 6.71e-29

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: 123.06  E-value: 6.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPvdphapaarrgfiledSGVCLSVSQR 3624
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP----------------ATTLLTPDDL 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3625 ALAVELPGTALCLDDPFTRAqldavepgelpevptEAPAYLIYTSGSTGTPKGVVVTHR-----NVERLFTAATQTGrfs 3699
Cdd:cd05974     65 RDRVDRGGAVYAAVDENTHA---------------DDPMLLYFTSGTTSKPKLVEHTHRsypvgHLSTMYWIGLKPG--- 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3700 fdehDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRReLALN 3779
Cdd:cd05974    127 ----DVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLAS-FDVK 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3780 VRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVHVSfhrlsdedlQSP-----TSRIGSALPDLAVHVLDAAGQ 3854
Cdd:cd05974    202 LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTALVG---------NSPgqpvkAGSMGRPLPGYRVALLDPDGA 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3855 PVPLGVVGelVVEGD----GVAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGE 3930
Cdd:cd05974    272 PATEGEVA--LDLGDtrpvGLMKGYAGDPDKTAH--AMRGG--YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFE 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3931 IAAKIASLPQVSDAAVTVEGQGEG-AWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQLLpALPLTANGKLD 4006
Cdd:cd05974    346 LESVLIEHPAVAEAAVVPSPDPVRlSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIR 424

                   ....
gi 1246793773 4007 RKAL 4010
Cdd:cd05974    425 RVEL 428
PRK05691 PRK05691
peptide synthase; Validated
2373-2812 7.47e-29

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 128.75  E-value: 7.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2373 GVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlapDRLLYRSGDLARLDgEGRIVYLGRGDHQVKIRGYRVELGEVEQVL 2452
Cdd:PRK05691   395 NRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2453 AQlpGVEVA-----AVLALP--GANGV---LQLGACIQGSLEgvAEALAQRLPEYLCPSRWRAVE--------SMPRLGN 2514
Cdd:PRK05691   471 ER--EVEVVrkgrvAAFAVNhqGEEGIgiaAEISRSVQKILP--PQALIKSIRQAVAEACQEAPSvvlllnpgALPKTSS 546
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2515 GKIDRQALADLLQQDDADSSA---------EAIDETPVNEV---LRELWQKLLGREHIGAHDNFFALGGDSILSLQLVAR 2582
Cdd:PRK05691   547 GKLQRSACRLRLADGSLDSYAlfpalqaveAAQTAASGDELqarIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVAR 626
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2583 ARQA-GLALMPRQLYDHPTLAGLSAQV----QASSPAPATIkPATEAEQSFGLTPIQH--WFFEQALDQPAHWNMSLYLK 2655
Cdd:PRK05691   627 LRDElGIDLNLRQLFEAPTLAAFSAAVarqlAGGGAAQAAI-ARLPRGQALPQSLAQNrlWLLWQLDPQSAAYNIPGGLH 705
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2656 LPGALDTAAFAAALADVAAAHPMLRARF--------QR-DAAGQWQQTLGDWQADRFAHREADAGQ-REDllaqwQAGLS 2725
Cdd:PRK05691   706 LRGELDEAALRASFQRLVERHESLRTRFyerdgvalQRiDAQGEFALQRIDLSDLPEAEREARAAQiREE-----EARQP 780
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2726 FD---GALLRVlALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQ-LSA 2801
Cdd:PRK05691   781 FDlekGPLLRV-TLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQwLAQ 859
                          490
                   ....*....|.
gi 1246793773 2802 ATLDGWRSYWR 2812
Cdd:PRK05691   860 GEAARQLAYWK 870
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
2050-2524 9.93e-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: 123.96  E-value: 9.93e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT--FAqLAAMAAVWHRGAAwLPLDPQHPDARQIA 2127
Cdd:cd05926      3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGleFV-VAFLAAARAGAVV-APLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 VLDDSGARIVIGW--GAAPAWVPAS-VRWLDAESVLDVVSAYEEP----------------PRVDVDADTPAYLIYTSGS 2188
Cdd:cd05926     81 YLADLGSKLVLTPkgELGPASRAASkLGLAILELALDVGVLIRAPsaeslsnlladkknakSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2189 TGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLAT--LSTVAADLGftALFGALLSGRRVrLLPAelAFDAQALAAHLQ 2265
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPdDRTLVVmpLFHVHGLVA--SLLSTLAAGGSV-VLPP--RFSASTFWPDVR 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2266 AHPVDCLKIVPS--HLAGLLAAAGGTAVLP-----RECLVTGGEALTGALVQQVRalAPTLRIvnhYGPTETTVGIlTCT 2338
Cdd:cd05926    236 DYNATWYTAVPTihQILLNRPEPNPESPPPklrfiRSCSASLPPAVLEALEATFG--APVLEA---YGMTEAAHQM-TSN 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 vpeewPVEQGVP----VGHPlAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplaPDRLLyRS 2414
Cdd:cd05926    310 -----PLPPGPRkpgsVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF-----KDGWF-RT 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRgdhqVK---IRGyrvelGE------VEQVLAQLPGVEVAAVLALP--------GANGVLQLGA 2477
Cdd:cd05926    378 GDLGYLDADGYLFLTGR----IKeliNRG-----GEkispleVDGVLLSHPAVLEAVAFGVPdekygeevAAAVVLREGA 448
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1246793773 2478 CIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05926    449 SV--TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
3513-4020 1.06e-28

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 124.78  E-value: 1.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3513 ERYActgNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPrgcDLL---VALLA 3588
Cdd:PRK08974    20 DRYQ---SLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMP---NLLqypIALFG 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3589 ILKTGAAYVPVDP--------H------APA------------------ARRGFILEDSGVCLSVSQRALA--------- 3627
Cdd:PRK08974    94 ILRAGMIVVNVNPlytpreleHqlndsgAKAivivsnfahtlekvvfktPVKHVILTRMGDQLSTAKGTLVnfvvkyikr 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3628 ----VELPGtALCLDDPFTRA-QLDAVEPgelpEVPTEAPAYLIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGRFSFD 3701
Cdd:PRK08974   174 lvpkYHLPD-AISFRSALHKGrRMQYVKP----ELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAKAAYGPLLHP 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 EHD--VWSLFHSHAFDFAVWELWGAWLyGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL- 3778
Cdd:PRK08974   249 GKElvVTALPLYHIFALTVNCLLFIEL-GGQNLLITNP--RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFs 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLsdeDLQSPTSRIGSALPDLAVHVLDAAGQPVPL 3858
Cdd:PRK08974   326 SLKLSVGGGMAVQQAVAERW-VKLTGQYLLEGYGLTECSPLVSVNPY---DLDYYSGSIGLPVPSTEIKLVDDDGNEVPP 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3859 GVVGELVVEGDGVAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASL 3938
Cdd:PRK08974   402 GEPGELWVKGPQVMLGYWQRPEATDE--VIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLH 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3939 PQVSD-AAVTVEGQGEGAWLMAYAVAADgAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqd 4017
Cdd:PRK08974   478 PKVLEvAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL------- 549

                   ...
gi 1246793773 4018 RDE 4020
Cdd:PRK08974   550 RDE 552
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
2052-2522 1.07e-28

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 124.14  E-value: 1.07e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLP----LDPQhpdarQIA 2127
Cdd:PRK06187    22 KEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPinirLKPE-----EIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 -VLDDSGARIV-----------------------IGWGAAPAwVPASVRWLDAESVLDvvSAYEEPPRVDVDADTPAYLI 2183
Cdd:PRK06187    97 yILNDAEDRVVlvdsefvpllaailpqlptvrtvIVEGDGPA-APLAPEVGEYEELLA--AASDTFDFPDIDENDAAAML 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG-EDASLatlstVAADL----GFTALFGALLSGRRVrLLPAElaFDAQ 2258
Cdd:PRK06187   174 YTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSrDDVYL-----VIVPMfhvhAWGLPYLALMAGAKQ-VIPRR--FDPE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALApTLRIVNHYGPTETTvGILT 2336
Cdd:PRK06187   246 NLLDLIETERVTFFFAVPTiwQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETS-PVVS 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2337 CTVPEEWPVEQG---VPVGHPLAGNEAWVLDRFG--LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlL 2411
Cdd:PRK06187   324 VLPPEDQLPGQWtkrRSAGRPLPGVEARIVDDDGdeLPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG-------W 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2412 YRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP--------GANGVLQLGACIqgSL 2483
Cdd:PRK06187   397 LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPdekwgerpVAVVVLKPGATL--DA 474
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1246793773 2484 EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK06187   475 KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
539-1041 1.15e-28

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: 123.59  E-value: 1.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGlsVIPLdTE 618
Cdd:cd05920     19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPV-LA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  619 WPQARRAEVVAasgcdavltdaqgLAGFAPSVAIAV-DELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHA 697
Cdd:cd05920     96 LPSHRRSELSA-------------FCAHAEAVAYIVpDRHAGFDHRALARELAESIPEVALFLLSGGTTGTPKLIPRTHN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  698 ALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQ--ILAAWSRGACVVARPDEllEPQRFLAFLSERAITVTDLAPAYA 775
Cdd:cd05920    163 DYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPDP--SPDAAFPLIEREGVTVTALVPALV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  776 NELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE-LGldrrCALINAYGPTEATISshYHRVQAIDA------SRPV 848
Cdd:cd05920    241 SLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPvLG----CTLQQVFGMAEGLLN--YTRLDDPDEviihtqGRPM 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  849 -PLGQLLpgriaaVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpSGeslrMYRSGDRVRLLDDGEL 927
Cdd:cd05920    315 sPDDEIR------VVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP----DG----FYRTGDLVRRTPDGYL 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  928 QFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEdgfgqadlnqtdsdQTESERWH 1006
Cdd:cd05920    381 VVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVvAMPDELLGERSCAFVVLRDP--------------PPSAAQLR 446
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1246793773 1007 RALCER-LPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05920    447 RFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3547-4010 1.77e-28

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: 121.30  E-value: 1.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVclsvsqral 3626
Cdd:cd05912      4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV--------- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 avelpgtalclddpftraQLDAVepgelpevpteapAYLIYTSGSTGTPKGVVVTHRNveRLFTAATQTGRFSFDEHDVW 3706
Cdd:cd05912     75 ------------------KLDDI-------------ATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALNLGLTEDDNW 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 ----SLFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAlNVRA 3782
Cdd:cd05912    122 lcalPLFHISGLSILMRSV----IYGMTVYLVDKF---DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN-NLRC 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3783 VVFGGEALEPSRLQPWRER-YPqaeLVNMYGITETTVHVSfhRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPvplGVV 3861
Cdd:cd05912    194 ILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIV--TLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEV 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3862 GELVVEGDGVAQGYWQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV 3941
Cdd:cd05912    266 GEILLKGPNVTKGYLNRPDATEESF--ENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI 341
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3942 SDAAVTveGQGEGAWLM---AYAVAAdgAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05912    342 KEAGVV--GIPDDKWGQvpvAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2062-2522 1.96e-28

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: 121.77  E-value: 1.96e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQH-PDARQIAvLDDSGARIVIGW 2140
Cdd:cd05971      7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFgPEALEYR-LSNSGASALVTD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAapawvpasvrwldaesvldvvsayeepprvdvdaDTPAYLIYTSGSTGTPKGVVVSQgnlaNYVAGVLPVLDLGEDas 2220
Cdd:cd05971     86 GS----------------------------------DDPALIIYTSGTTGPPKGALHAH----RVLLGHLPGVQFPFN-- 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 latLSTVAADLGFT--------ALFGALLS---------GRRVRLLPAELAFDAQALAAHLQA-HPVDCLKIVPSHLAGL 2282
Cdd:cd05971    126 ---LFPRDGDLYWTpadwawigGLLDVLLPslyfgvpvlAHRMTKFDPKAALDLMSRYGVTTAfLPPTALKMMRQQGEQL 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2283 LAaaggtAVLPRECLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETTVGILTCTVpeEWPVEQGvPVGHPLAGNEAWV 2362
Cdd:cd05971    203 KH-----AQVKLRAIATGGESLGEELLGWARE-QFGVEVNEFYGQTECNLVIGNCSA--LFPIKPG-SMGKPIPGHRVAI 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2363 LDRFGLPAPVGVAGE--LYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllyRSGDLARLDGEGRIVYLGRGDHQVKIRG 2440
Cdd:cd05971    274 VDDNGTPLPPGEVGEiaVELPDPVAFLGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSG 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2441 YRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---QGslEGVAEALAQRLPEYLC--------PSRWRAVESM 2509
Cdd:cd05971    347 YRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVvlnPG--ETPSDALAREIQELVKtrlaaheyPREIEFVNEL 424
                          490
                   ....*....|...
gi 1246793773 2510 PRLGNGKIDRQAL 2522
Cdd:cd05971    425 PRTATGKIRRREL 437
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
3661-4006 2.05e-28

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: 119.33  E-value: 2.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 APAYLIYTSGSTGTPKGVVVTHRNverLFTAATQTGRF-SFDEHDVW----SLFHSHAFDFAVwelwGAWLYGGRAVLVP 3735
Cdd:cd17636      1 DPVLAIYTAAFSGRPNGALLSHQA---LLAQALVLAVLqAIDEGTVFlnsgPLFHIGTLMFTL----ATFHAGGTNVFVR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3736 EAVcrqPDAFLDLLAEYGVTvlnqtpSAFYALQSQAMRREL-------ALNVRAVVF--GGEALEPSRLQPWReRYPQAe 3806
Cdd:cd17636     74 RVD---AEEVLELIEAERCT------HAFLLPPTIDQIVELnadglydLSSLRSSPAapEWNDMATVDTSPWG-RKPGG- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3807 lvnmYGITETTVHVSFHRLSDEDLqsptSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERF 3886
Cdd:cd17636    143 ----YGQTEVMGLATFAALGGGAI----GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 veRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVA 3963
Cdd:cd17636    215 --RGG--WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI--GVPDPRWaqsVKAIVVL 288
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 3964 ADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:cd17636    289 KPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
3660-4007 3.15e-28

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: 118.90  E-value: 3.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRnverLFTAAT---QTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPE 3736
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANK----TFFAVPdilQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 AVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSqaMRRELALNV---RAVVFGGEALEPSRLQPWrERYPQAELVNMYGI 3813
Cdd:cd17635     77 NT--TYKSLFKILTTNAVTTTCLVPTLLSKLVS--ELKSANATVpslRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETT--VHVSFHRLSDEdlqspTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVErgg 3891
Cdd:cd17635    152 SETGtaLCLPTDDDSIE-----INAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID--- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3892 qRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVA-ADGAEP 3969
Cdd:cd17635    224 -GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVAsAELDEN 302
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1246793773 3970 DPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17635    303 AIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1599-1977 3.44e-28

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: 120.94  E-value: 3.44e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLL-ESLRGDGaDPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLsVPHQIVLADAAAPWQT 1677
Cdd:cd19533      3 PLTSAQRGVWFaEQLDPEG-SIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEG-EPYQWIDPYTPVPIRH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1678 LDWSAldDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG 1757
Cdd:cd19533     81 IDLSG--DPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLRLPPAPGF----QAYLDWRERQDLARQRGWWRERLSGyagtaALPAPVAAAHHPVQREECERR---LSAHDSERLRA 1830
Cdd:cd19533    159 RPAPPAPFGSFldlvEEEQAYRQSERFERDRAFWTEQFED-----LPEPVSLARRAPGRSLAFLRRtaeLPPELTRTLLE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1831 FCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRppelAGVES--MVGVFINTLPLRLRIDAGQPALDLLSALRS 1908
Cdd:cd19533    234 AAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR----LGAAArqTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 1909 QSLEVAENEAVGLGEILADSGL--DADRLFASLLVVENFpamaPAQLPFALrvRETRAANHYA-----LTLRVSER 1977
Cdd:cd19533    310 ELRSLLRHQRYRYEDLRRDLGLtgELHPLFGPTVNYMPF----DYGLDFGG--VVGLTHNLSSgptndLSIFVYDR 379
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3535-4005 3.99e-28

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 121.93  E-value: 3.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3535 RIAVSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILE 3613
Cdd:PRK08276     1 PAVIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3614 DSGVC-LSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELP------EVPTEAPA------YLIYTSGSTGTPKGVV- 3679
Cdd:PRK08276    81 DSGAKvLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSyeealaAQPDTPIAdetagaDMLYSSGTTGRPKGIKr 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3680 -VTHRNVER---LFTAATQTGRFSFDEHDVWS---LFHSHAFDFAVWELWGawlyGGRAVLVPEAvcrQPDAFLDLLAEY 3752
Cdd:PRK08276   161 pLPGLDPDEapgMMLALLGFGMYGGPDSVYLSpapLYHTAPLRFGMSALAL----GGTVVVMEKF---DAEEALALIERY 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3753 GVTVLNQTPSAFyalqsqamRRELAL--NVRA--------VVFGGEALEP----SRLQPW-----RERYPQAElvnMYGI 3813
Cdd:PRK08276   234 RVTHSQLVPTMF--------VRMLKLpeEVRArydvsslrVAIHAAAPCPvevkRAMIDWwgpiiHEYYASSE---GGGV 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3814 TETTvhvsfhrlSDEDLQSPTSrIGSALpDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PRK08276   303 TVIT--------SEDWLAHPGS-VGKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHG--- 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDP- 3971
Cdd:PRK08276   370 WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGERVKAVVQPADGADAGDa 449
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1246793773 3972 --QSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK08276   450 laAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
3082-3422 4.83e-28

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: 120.45  E-value: 4.83e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGF-AVQGLPSPRQLPHRQVSLPLAE 3160
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFpEEDGVPYQLILEEDEATPKLEI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3161 QDWSglepaqaRSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRES 3240
Cdd:cd19538     83 KEVD-------EEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3241 RTPQLPAAP-PFRDYLHWLR-------GQDEAAAR--AFWREQLTGLePAALPEATE---PAE-GYASSTRRFDLAAA-- 3304
Cdd:cd19538    156 EAPELAPLPvQYADYALWQQellgdesDPDSLIARqlAYWKKQLAGL-PDEIELPTDyprPAEsSYEGGTLTFEIDSElh 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3305 ---SAWAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRppELAGVERMLGVFINSVPLRVTPAGEATPAPWLQA 3381
Cdd:cd19538    235 qqlLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLER 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3382 LQQRNLDLRTHGYLPLAQIqragaADAVSP---------FDVLLVFENLP 3422
Cdd:cd19538    313 VKETNLEAYEHQDIPFERL-----VEALNPtrsrsrhplFQIMLALQNTP 357
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
2179-2526 5.06e-28

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: 118.20  E-value: 5.06e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG-EDASLATL--STVAadlGFTALFGALLSGRRVRLLPAELAF 2255
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGgGDSWLLSLplYHVG---GLAILVRSLLAGAELVLLERNQAL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2256 daqalAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQqvRALAPTLRIVNHYGPTETTVGI 2334
Cdd:cd17630     79 -----AEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSlRAVLLGGAPIPPELLE--RAADRGIPLYTTYGMTETASQV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwpvEQGVpVGHPLAGNEAWVLDRfglpapvgvaGELYLGGGNLSLGYWqraeqtaeRFVAHPLAPDRLLYRS 2414
Cdd:cd17630    152 ATKRPDGF---GRGG-VGVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTT 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGVLQLGACIQGSLEGVAEAL 2490
Cdd:cd17630    210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGRGPADPAELRAWL 289
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1246793773 2491 AQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLL 2526
Cdd:cd17630    290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2063-2522 7.40e-28

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: 120.32  E-value: 7.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL----DPQHPDARqiavLDDSGARIVI 2138
Cdd:cd05973      2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLftafGPKAIEHR----LRTSGARLVV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 gwgaapawvpasvrwLDAESvldvvsayeeppRVDVDADtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGED 2218
Cdd:cd05973     78 ---------------TDAAN------------RHKLDSD-PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPE 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2219 ASLATlstvAADLG-----FTALFGALLSGRRVRLLpaELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP 2293
Cdd:cd05973    130 DSFWN----AADPGwayglYYAITGPLALGHPTILL--EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARP 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2294 RECL---VTGGEALTGALVQQVRALAPTLrIVNHYGPTEttVGILTCTV-PEEWPVEQGvPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd05973    204 KGRLrrvSSAGEPLTPEVIRWFDAALGVP-IHDHYGQTE--LGMVLANHhALEHPVHAG-SAGRAMPGWRVAVLDDDGDE 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSL----GYWQRAEQtaerfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd05973    280 LGPGEPGRLAIDIANSPLmwfrGYQLPDTP----------AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2446 GEVEQVLAQLPGVEVAAVLALPGA--NGVLQLGACIQGSLEG---VAEALA----QRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05973    350 FDVESALIEHPAVAEAAVIGVPDPerTEVVKAFVVLRGGHEGtpaLADELQlhvkKRLSAHAYPRTIHFVDELPKTPSGK 429

                   ....*.
gi 1246793773 2517 IDRQAL 2522
Cdd:cd05973    430 IQRFLL 435
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
88-507 7.91e-28

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: 119.86  E-value: 7.91e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVES 161
Cdd:cd19536      2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvqvVHRQAQVPVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  162 ADLRG--RGQDEIDALVEGFRLRPFELQRQRPLRMQLLRLDGQGdgpvrHWLQVV-VHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19536     82 LDLTPleEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERE-----RFLLVIsDHHSILDGWSLYLLVKEILAVYN- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  239 ecGLAA----EPAPPLPcqYGDYARWQRDTLDRlDASLRHHVEALSGAPHLhelPLDHERPAVLGQSGAKLRLAFPPGLS 314
Cdd:cd19536    156 --QLLEykplSLPPAQP--YRDFVAHERASIQQ-AASERYWREYLAGATLA---TLPALSEAVGGGPEQDSELLVSVPLP 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  315 ERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRVRP--ELDSLVGLFVNTVVLRTQLHDDPdFASLVAR 392
Cdd:cd19536    228 VRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEttGAERLLGLFLNTLPLRVTLSEET-VEDLLKR 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  393 CRDHQLAALEHQALPLErvietlQVERSSRHAPLFQLMFALRH-DADLALDLHG---VQAHALTLPEDVAKHELTLEVLV 468
Cdd:cd19536    307 AQEQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHfDLDFGLPEWGsdeGMRRGLLFSEFKSNYDVNLSVLP 380
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1246793773  469 GAGGMSAVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19536    381 KQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
PRK13382 PRK13382
bile acid CoA ligase;
3523-4013 1.84e-27

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 120.63  E-value: 1.84e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3523 SRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPH 3602
Cdd:PRK13382    47 SGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 APAARRGFILEDSGV--------CLSVSQRALAvELPGTALCLD-----DPFTRAQLDAVEPGELPEVPTEAPAYLIYTS 3669
Cdd:PRK13382   127 FAGPALAEVVTREGVdtviydeeFSATVDRALA-DCPQATRIVAwtdedHDLTVEVLIAAHAGQRPEPTGRKGRVILLTS 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVvvTHRNVERLFTAATQTGRFSFDEHD----VWSLFHShafdfavwelWGAWLYGGRAVLVPEAVCRQ---P 3742
Cdd:PRK13382   206 GTTGTPKGA--RRSGPGGIGTLKAILDRTPWRAEEptviVAPMFHA----------WGFSQLVLAASLACTIVTRRrfdP 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3743 DAFLDLLAEYGVTVLNQTPSAF---YALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETTVH 3819
Cdd:PRK13382   274 EATLDLIDRHRATGLAVVPVMFdriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMI 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3820 VSfhrLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYwqrPELTAERFVERggqrFYRSGD 3899
Cdd:PRK13382   353 AT---ATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDG----FMASGD 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREAL 3978
Cdd:PRK13382   423 VGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIgVDDEQYGQRLAAFVVLKPGASATPETLKQHV 502
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 3979 RALLPDYMLPRLIQLLPALPLTANGKLDRKALPKP 4013
Cdd:PRK13382   503 RDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK07867 PRK07867
acyl-CoA synthetase; Validated
3552-4010 1.93e-27

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 120.56  E-value: 1.93e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGpgqRVGLCLPRGCDLLVALLAILKTGAAYVPVDP--HAPAARRGFILEDSGVCLSVS-QRALAV 3628
Cdd:PRK07867    40 ARAAALRARLDPTRPP---HVGVLLDNTPEFSLLLGAAALSGIVPVGLNPtrRGAALARDIAHADCQLVLTESaHAELLD 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3629 ELPGTALCLD-DPFTRAQLDAVEPGELPEVPTEAPA---YLIYTSGSTGTPKGVVVTHRNVErlFTAATQTGRFSFDEHD 3704
Cdd:PRK07867   117 GLDPGVRVINvDSPAWADELAAHRDAEPPFRVADPDdlfMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFGLGPDD 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 V----WSLFHSHafdfAVWELWGAWLYGGRAVlvpeAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL 3778
Cdd:PRK07867   195 VcyvsMPLFHSN----AVMAGWAVALAAGASI----ALRRKFSAsgFLPDVRRYGATYANYVGKPLSYVLATPERPDDAD 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEAlEPSRLQPWRERYpQAELVNMYGITETTvhVSFHRLSDedlqSPTSRIGSALPDLAvhVLDAA-GQPVP 3857
Cdd:PRK07867   267 NPLRIVYGNEG-APGDIARFARRF-GCVVVDGFGSTEGG--VAITRTPD----TPPGALGPLPPGVA--IVDPDtGTECP 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 LGV------------VGELV-VEGDGVAQGYWQRPELTAERFveRGGQrfYRSGDLGRYRADGSLEYRGRGDDQVKLRGY 3924
Cdd:PRK07867   337 PAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADAERM--RGGV--YWSGDLAYRDADGYAYFAGRLGDWMRVDGE 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3925 RIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEPDPQSLREALRAL--LPDYMLPRLIQLLPALPLTA 4001
Cdd:PRK07867   413 NLGTAPIERILLRYPDATEVAVyAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTA 492

                   ....*....
gi 1246793773 4002 NGKLDRKAL 4010
Cdd:PRK07867   493 TFKVLKRQL 501
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
3547-3935 2.47e-27

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: 119.00  E-value: 2.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGvclsvsqral 3626
Cdd:cd17640      8 YKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSE---------- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3627 avelpGTALCLDDpftraqldavEPGELpevpteapAYLIYTSGSTGTPKGVVVTHRNverlftaatqtgrFSFDEHDVW 3706
Cdd:cd17640     78 -----SVALVVEN----------DSDDL--------ATIIYTSGTTGNPKGVMLTHAN-------------LLHQIRSLS 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SLFHSHAFD--FAVWELWGAW---------LYGGravlvpEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYAL-------- 3767
Cdd:cd17640    122 DIVPPQPGDrfLSILPIWHSYersaeyfifACGC------SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLysgiqkqv 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3768 -QSQAMRRELAL------NVRAVVFGGEALEPSRlqpwrERYPQA---ELVNMYGITETTVHVSFHRLSDEDLQSptsrI 3837
Cdd:cd17640    196 sKSSPIKQFLFLfflsggIFKFGISGGGALPPHV-----DTFFEAigiEVLNGYGLTETSPVVSARRLKCNVRGS----V 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3838 GSALPDLAVHVLDA-AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd17640    267 GRPLPGTEIKIVDPeGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDG---WFNTGDLGWLTCGGELVLTGRAK 343
                          410       420
                   ....*....|....*....|
gi 1246793773 3917 DQVKLR-GYRIEPGEIAAKI 3935
Cdd:cd17640    344 DTIVLSnGENVEPQPIEEAL 363
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
3525-4010 3.71e-27

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 119.98  E-value: 3.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:PRK08751    31 FATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLY 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGV---------CLSVsQRALA------VELPGTALCLDdpFTRAQL---------------------- 3646
Cdd:PRK08751   111 TPRELKHQLIDSGAsvlvvidnfGTTV-QQVIAdtpvkqVITTGLGDMLG--FPKAALvnfvvkyvkklvpeyringair 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3647 --DAVEPGELPEVPT-----EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQ----TGRFSFDEHDVWS---LFHsh 3712
Cdd:PRK08751   188 frEALALGRKHSMPTlqiepDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEGCEVVITalpLYH-- 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3713 afdfaVWELWGAWL----YGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAVVFGG 3787
Cdd:PRK08751   266 -----IFALTANGLvfmkIGGCNHLISNP--RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSsLKMTLGGG 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3788 EALEPSRLQPWReRYPQAELVNMYGITETTVHVSFHRLsdeDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVE 3867
Cdd:PRK08751   339 MAVQRSVAERWK-QVTGLTLVEAYGLTETSPAACINPL---TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3868 GDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSD-AAV 3946
Cdd:PRK08751   415 GPQVMKGYWKRPEETAKVMDADG---WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAV 491
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3947 TVEGQGEGAWLMAYAVAADGAePDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK08751   492 GVPDEKSGEIVKVVIVKKDPA-LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1599-1949 4.20e-27

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: 117.87  E-value: 4.20e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 DWSAlDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGA 1758
Cdd:cd19539     83 DLSD-PDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1759 TLRLPPAPG-FQAYLDWRERQD----LARQRGWWRERLSGYAGTAALPAPVAAAHHPVQREECERRLSAHDSERLRAFCR 1833
Cdd:cd19539    162 AAPLPELRQqYKEYAAWQREALaaprAAELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1834 ERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAgvESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEV 1913
Cdd:cd19539    242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRF--ESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDA 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1246793773 1914 AENEAVGLGEILADSGLDADR----LFASLLVVENFPAMA 1949
Cdd:cd19539    320 QRHQELPFQQLVAELPVDRDAgrhpLVQIVFQVTNAPAGE 359
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
3527-4010 5.89e-27

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 118.63  E-value: 5.89e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3527 EIARRYPARIAVSAEDG-----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP 3601
Cdd:PRK08008    15 DLADVYGHKTALIFESSggvvrRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3602 HAPAARRGFILEDSGVCLSVSQ-------RALAVE--LPGTALCLDDP----------FTraQLDAVEPGELPEVP---T 3659
Cdd:PRK08008    95 RLLREESAWILQNSQASLLVTSaqfypmyRQIQQEdaTPLRHICLTRValpaddgvssFT--QLKAQQPATLCYAPplsT 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW----SLFHShafDFAVWELWGAWLYGGRAVLVP 3735
Cdd:PRK08008   173 DDTAEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWQCALRDDDVYltvmPAFHI---DCQCTAAMAAFSAGATFVLLE 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3736 EAVCRqpdAFLDLLAEYGVTVLNQTPSAFYALQSQ-AMRRELALNVRAVVFgGEALEPSRLQPWRERYpQAELVNMYGIT 3814
Cdd:PRK08008   248 KYSAR---AFWGQVCKYRATITECIPMMIRTLMVQpPSANDRQHCLREVMF-YLNLSDQEKDAFEERF-GVRLLTSYGMT 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTVHVSFHRLSDEDlQSPTsrIGSALPDLAVHVLDAAGQPVPLGVVGELVVE---GDGVAQGYWQRPELTAERFVERGg 3891
Cdd:PRK08008   323 ETIVGIIGDRPGDKR-RWPS--IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLEADG- 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3892 qrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPD 3970
Cdd:PRK08008   399 --WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVgIKDSIRDEAIKAFVVLNEGETLS 476
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1246793773 3971 PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK08008   477 EEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
3555-4015 6.10e-27

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: 118.72  E-value: 6.10e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3555 SQLATLLIRQGAG--PGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPG 3632
Cdd:cd05928     51 SRKAANVLSGACGlqRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDS 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3633 TALclDDPFTRAQL---DAVEPGELP---------------EVPTEAPAYLIYTSGSTGTPKGVVVTHRNverLFTAATQ 3694
Cdd:cd05928    131 VAS--ECPSLKTKLlvsEKSRDGWLNfkellneastehhcvETGSQEPMAIYFTSGTTGSPKMAEHSHSS---LGLGLKV 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3695 TGRFSFD--EHDV-WSLFHSHAFDFAVWELWGAWLYGGrAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQA 3771
Cdd:cd05928    206 NGRYWLDltASDImWNTSDTGWIKSAWSSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQD 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3772 MRRELALNVRAVVFGGEALEPSRLQPWRERyPQAELVNMYGITETTVHVSfhrlSDEDLQSPTSRIGSALPDLAVHVLDA 3851
Cdd:cd05928    285 LSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTETGLICA----NFKGMKIKPGSMGKASPPYDVQIIDD 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 AGQPVPLGVVGELVVEGD-----GVAQGYWQRPELTAErfVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRI 3926
Cdd:cd05928    360 NGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAA--TIRGD--FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRI 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3927 EPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAV-AADGAEPDPQSL----REALRALLPDYMLPRLIQLLPALPLT 4000
Cdd:cd05928    436 GPFEVESALIEHPAVVESAVvSSPDPIRGEVVKAFVVlAPQFLSHDPEQLtkelQQHVKSVTAPYKYPRKVEFVQELPKT 515
                          490
                   ....*....|....*
gi 1246793773 4001 ANGKLDRKALPKPET 4015
Cdd:cd05928    516 VTGKIQRNELRDKEW 530
PRK08315 PRK08315
AMP-binding domain protein; Validated
3525-4004 8.59e-27

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 118.76  E-value: 8.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAEIARRYPARIAVSAEDGEL--DYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPH 3602
Cdd:PRK08315    22 LDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 APAARRGFILEDSGVCLSVSQRA------------LAVEL----PGTALCLDDPFTR--------------------AQL 3646
Cdd:PRK08315   102 YRLSELEYALNQSGCKALIAADGfkdsdyvamlyeLAPELatcePGQLQSARLPELRrviflgdekhpgmlnfdellALG 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3647 DAVEPGELPEV-----PTEApaylI---YTSGSTGTPKGVVVTHRNV--ERLFTAATQtgRFSfdEHD-----VwSLFH- 3710
Cdd:PRK08315   182 RAVDDAELAARqatldPDDP----IniqYTSGTTGFPKGATLTHRNIlnNGYFIGEAM--KLT--EEDrlcipV-PLYHc 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3711 -----------SH---------AFDfavwelwgawlyggrAVLVPEAV----CRqpdafldllAEYGVtvlnqtPSAFYA 3766
Cdd:PRK08315   253 fgmvlgnlacvTHgatmvypgeGFD---------------PLATLAAVeeerCT---------ALYGV------PTMFIA 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3767 LQSQAMRRELALN-VRAVVFGG-----EALEpsRLQpwrerypqaELVNM------YGITETTvHVSFHRLSDEDLQSPT 3834
Cdd:PRK08315   303 ELDHPDFARFDLSsLRTGIMAGspcpiEVMK--RVI---------DKMHMsevtiaYGMTETS-PVSTQTRTDDPLEKRV 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3835 SRIGSALPDLAVHVLDAA-GQPVPLGVVGELVVEGDGVAQGYWQRPELTAERfVERGGqrFYRSGDLGRYRADGSLEYRG 3913
Cdd:PRK08315   371 TTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADG--WMHTGDLAVMDEEGYVNIVG 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3914 RGDDQVkLR-GYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLI 3991
Cdd:PRK08315   448 RIKDMI-IRgGENIYPREIEEFLYTHPKIQDVQVVgVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYI 526
                          570
                   ....*....|...
gi 1246793773 3992 QLLPALPLTANGK 4004
Cdd:PRK08315   527 RFVDEFPMTVTGK 539
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
2061-2522 8.80e-27

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: 116.81  E-value: 8.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgw 2140
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldAESVLDvvsayeepprvDVdadtpAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL-GEDA 2219
Cdd:cd05935     79 ---------------VGSELD-----------DL-----ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLtPSDV 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLST--VAadlGFTALFGALLSGRRVRLLPA----ELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLp 2293
Cdd:cd05935    128 ILACLPLfhVT---GFVGSLNTAVYVGGTYVLMArwdrETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKV- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2294 recLVTGGEALTGALVQQVRALApTLRIVNHYGPTETTVGilTCTVPEEWPVEQGVpvGHPLAGNEAWVLD-RFGLPAPV 2372
Cdd:cd05935    204 ---LTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQ--THTNPPLRPKLQCL--GIP*FGVDARVIDiETGRELPP 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2373 GVAGELYLGGGNLSLGYWQRAEQTAERFVAhplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVL 2452
Cdd:cd05935    276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2453 AQLPGVEVAAVLALPG--------ANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05935    353 YKHPAI*EVCVISVPDervgeevkAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
3547-4010 8.90e-27

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 118.84  E-value: 8.90e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAARrgfiLEDSGVCLSVS 3622
Cdd:PRK04319    76 YKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDR----LEDSEAKVLIT 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 QRAL-----AVELPG--TALCLDDP---------FTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVe 3686
Cdd:PRK04319   152 TPALlerkpADDLPSlkHVLLVGEDveegpgtldFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM- 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3687 rlfTAATQTGRFSFDEH--DV--------WSLFHSHAfdfavweLWGAWLYGgrAVLVPEAVCRQPDAFLDLLAEYGVTV 3756
Cdd:PRK04319   231 ---LQHYQTGKYVLDLHedDVywctadpgWVTGTSYG-------IFAPWLNG--ATNVIDGGRFSPERWYRILEDYKVTV 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3757 LNQTPSAFYALqsqaMRR--ELA-----------------LNVRAVVFGGEALEpsrlQPWRERYPQaelvnmygiTETT 3817
Cdd:PRK04319   299 WYTAPTAIRML----MGAgdDLVkkydlsslrhilsvgepLNPEVVRWGMKVFG----LPIHDNWWM---------TETG 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHV-----SFhrlsdeDLQsPTSrIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGD--GVAQGYWQRPELTAERFVerG 3890
Cdd:PRK04319   362 GIMianypAM------DIK-PGS-MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYFA--G 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 GqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGE---GAWLMAYAVAADGA 3967
Cdd:PRK04319   432 D--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVI--GKPDpvrGEIIKAFVALRPGY 507
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1246793773 3968 EPDpQSLREALRAL----LPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK04319   508 EPS-EELKEEIRGFvkkgLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
2063-2517 1.17e-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: 116.71  E-value: 1.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIgwga 2142
Cdd:cd05903      3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2143 apawVPASVRWLDaesvldvvsaYEEPPrvdvdaDTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLA 2222
Cdd:cd05903     79 ----VPERFRQFD----------PAAMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2223 TLSTVAADLGFT-ALFGALLSGRRVRLLpaelafdaqalaahLQAHPVDCLKIVPSHLA-------------GLLAAAGG 2288
Cdd:cd05903    139 VASPMAHQTGFVyGFTLPLLLGAPVVLQ--------------DIWDPDKALALMREHGVtfmmgatpfltdlLNAVEEAG 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2289 TAVLPRECLVTGGEALTGALVQQVRALAPTLrIVNHYGPTETTvGILTCTVPEEwPVEQGVPVGHPLAGNEAWVLDRFGL 2368
Cdd:cd05903    205 EPLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECP-GAVTSITPAP-EDRRLYTDGRPLPGVEIKVVDDTGA 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2369 PAPVGVAGELYLGGGNLSLGYWQRAEQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRgDHQVKIR-GYRVELGE 2447
Cdd:cd05903    282 TLAPGVEGELLSRGPSVFLGYLDRPDLTAD-------AAPEGWFRTGDLARLDEDGYLRITGR-SKDIIIRgGENIPVLE 353
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2448 VEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIqgSLEGVAEAL-AQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd05903    354 VEDLLLGHPGVIEAAVVALPDerlgeracAVVVTKSGALL--TFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
3520-4010 1.65e-26

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 118.00  E-value: 1.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK12492    25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVN 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAARRGFILEDSG----VCLSVSQRALAVELPGTALcldDPFTRAQLDAVEPGE--------LPEVPTEAPAY-- 3664
Cdd:PRK12492   105 TNPLYTAREMRHQFKDSGaralVYLNMFGKLVQEVLPDTGI---EYLIEAKMGDLLPAAkgwlvntvVDKVKKMVPAYhl 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 ------------------------------LIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGRFSFDEHDVWS------ 3707
Cdd:PRK12492   182 pqavpfkqalrqgrglslkpvpvglddiavLQYTGGTTGLAKGAMLTHGNlVANMLQVRACLSQLGPDGQPLMKegqevm 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3708 -----LFHSHAFDFAVWELWgawLYGGRAVLVPEAvcRQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVR 3781
Cdd:PRK12492   262 iaplpLYHIYAFTANCMCMM---VSGNHNVLITNP--RDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFsALK 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3782 AVVFGGEALEPSRLQPWrERYPQAELVNMYGITETTVHVSFHRLSDedlQSPTSRIGSALPDLAVHVLDAAGQPVPLGVV 3861
Cdd:PRK12492   337 LTNSGGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGE---LARLGTVGIPVPGTALKVIDDDGNELPLGER 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3862 GELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV 3941
Cdd:PRK12492   413 GELCIKGPQVMKGYWQQPEATAEALDAEG---WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3942 SD-AAVTVEGQGEGAWLMAYAVAADGAePDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK12492   490 ANcAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3497-4008 2.23e-26

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 118.05  E-value: 2.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3497 LPLLPSQTRSAAWTSR-ERYACTGnLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLC 3575
Cdd:PRK08279    15 LPDLPGILRGLKRTALiTPDSKRS-LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3576 LPRGCDLLVALLAILKTGAAYVPVDPHApaarRGFILEDsgvCLSVSQ-RALAVE--------------LPGTALCLDDP 3640
Cdd:PRK08279    94 MENRPEYLAAWLGLAKLGAVVALLNTQQ----RGAVLAH---SLNLVDaKHLIVGeelveafeearadlARPPRLWVAGG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3641 FTRAQLDAVE-------------PGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVER------LFTAATQTGRFsfd 3701
Cdd:PRK08279   167 DTLDDPEGYEdlaaaaagapttnPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKamggfgGLLRLTPDDVL--- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 eHDVWSLFHSHAFDFAvwelWGAWLYGGRAVlvpeAVCRQPDA--FLDLLAEYGVTV-----------LNQTPSAfyalq 3768
Cdd:PRK08279   244 -YCCLPLYHNTGGTVA----WSSVLAAGATL----ALRRKFSAsrFWDDVRRYRATAfqyigelcrylLNQPPKP----- 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3769 sqamrRELALNVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITETTVHvsfhrLSDEDlqsptSRIGSA--LPDLAV 3846
Cdd:PRK08279   310 -----TDRDHRLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEGNVG-----FINVF-----NFDGTVgrVPLWLA 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3847 H--------------VLDAAG--QPVPLGVVGELVVEGDGVAQ--GYWQrPELTAE---RFVERGGQRFYRSGDLGRYRA 3905
Cdd:PRK08279   373 HpyaivkydvdtgepVRDADGrcIKVKPGEVGLLIGRITDRGPfdGYTD-PEASEKkilRDVFKKGDAWFNTGDLMRDDG 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3906 DGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQG-EGAWLMAYAVAADGAEPDPQSLREALRALLP 3983
Cdd:PRK08279   452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVyGVEVPGtDGRAGMAAIVLADGAEFDLAALAAHLYERLP 531
                          570       580
                   ....*....|....*....|....*
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKLdRK 4008
Cdd:PRK08279   532 AYAVPLFVRLVPELETTGTFKY-RK 555
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
675-1041 3.87e-26

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: 112.42  E-value: 3.87e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQILAAWsrgacvvarpd 748
Cdd:cd17630      1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLlslplyHVGGLAI--LVRSLLAGA----------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  749 ELLEPQRFLAFLSERA---ITVTDLAPAYANELVRASVADDWRDlALRCLVVGGDVLPVALAQRwfelGLDRRCALINAY 825
Cdd:cd17630     68 ELVLLERNQALAEDLAppgVTHVSLVPTQLQRLLDSGQGPAALK-SLRAVLLGGAPIPPELLER----AADRGIPLYTTY 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  826 GPTE--ATISshyhrVQAIDASRPVPLGQLLPGRiaavldaHGRIVPRgvcGELALGGIGLAEGYRgdaaasERRFAPLR 903
Cdd:cd17630    143 GMTEtaSQVA-----TKRPDGFGRGGVGVLLPGR-------ELRIVED---GEIWVGGASLAMGYL------RGQLVPEF 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  904 LPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAA---QRLVAWVE 980
Cdd:cd17630    202 NEDG----WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAF--VVGVPDEelgQRPVAVIV 275
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  981 CAGEdgfgqadlnqtdsdqTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd17630    276 GRGP---------------ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
588-1043 4.68e-26

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: 114.91  E-value: 4.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLdtewpqarraevVAASGCDAVLtdaQGLAGFAPSVAIAVDELKldgagengs 667
Cdd:cd05969     28 VFVLSPRSPELYFSMLGIGKIGAVICPL------------FSAFGPEAIR---DRLENSEAKVLITTEELY--------- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 gENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLA-VDTTLEQILAAWSRGACVVAR 746
Cdd:cd05969     84 -ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTADPGwVTGTVYGIWAPWLNGVTNVVY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  747 PDElLEPQRFLAFLSERAITVTDLAPAYANELVRASV--ADDWRDLALRCLVVGGDVL-PVALaqRWFELGLDRRcaLIN 823
Cdd:cd05969    163 EGR-FDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelARKYDLSSLRFIHSVGEPLnPEAI--RWGMEVFGVP--IHD 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  824 AYGPTE-ATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELAL--GGIGLAEGYRGDAAASERRFa 900
Cdd:cd05969    238 TWWQTEtGSIMIANYPCMPI---KPGSMGKPLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSF- 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  901 plrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEG---AAQRLVA 977
Cdd:cd05969    314 ----IDG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAV--AEAGVIGKPdplRGEIIKA 383
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773  978 WVecAGEDGFgqadlNQTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:cd05969    384 FI--SLKEGF-----EPSDELKEEIINFVR---QKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3082-3457 5.18e-26

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: 114.09  E-value: 5.18e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLF-HSLLNaeaDP--YINQTTVALHGALDREAFAAAWQQALERHPILRSGF--------AVQG-LPSPR-Q 3148
Cdd:cd19532      3 PMSFGQSRFWFlQQYLE---DPttFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftdpedgePMQGvLASSPlR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3149 LPHRQVSlplaeqdwsglEPAQARSRLSELQAQQceagFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLD 3228
Cdd:cd19532     80 LEHVQIS-----------DEAEVEEEFERLKNHV----YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLR 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3229 EVWRLYaalreSRTPQLPAAPPFRDYLHWLRGQDE----AAARAFWREQLTGLePAALP-------EATEPAEGYASSTR 3297
Cdd:cd19532    145 DLERAY-----NGQPLLPPPLQYLDFAARQRQDYEsgalDEDLAYWKSEFSTL-PEPLPllpfakvKSRPPLTRYDTHTA 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3298 RFDLAAASA-----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPElaGVERMLGVFINSVPLRVTPAGE 3372
Cdd:cd19532    219 ERRLDAALAarikeASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPS 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3373 ATPApwlQALQQ-RNldlrthgylplaQIQRAGAADAVsPFDVLL----------------VFENLPTESREERS--GMR 3433
Cdd:cd19532    297 QTFA---DVLKEtRD------------KAYAALAHSRV-PFDVLLdelgvprsathsplfqVFINYRQGVAESRPfgDCE 360
                          410       420
                   ....*....|....*....|....*
gi 1246793773 3434 IEELD-HRAHSNYPLMLTAIPDAGG 3457
Cdd:cd19532    361 LEGEEfEDARTPYDLSLDIIDNPDG 385
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
3544-4009 1.11e-25

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 115.99  E-value: 1.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV-DPHAP--AARRGFILEDS--GVC 3618
Cdd:PRK12476    68 ELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAepTVV 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3619 LSVSQRALAVE-----LPG----TALCLDD-------PFTRAQLDavepgelpevpTEAPAYLIYTSGSTGTPKGVVVTH 3682
Cdd:PRK12476   147 LTTTAAAEAVEgflrnLPRlrrpRVIAIDAipdsageSFVPVELD-----------TDDVSHLQYTSGSTRPPVGVEITH 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 RNV-ERLFTAATQTGRFSFDEHDV-W-SLFHshafDFAVWELWGAWLYGGRAVLV-PEAVCRQPDAFLDLLAEYGVT--V 3756
Cdd:PRK12476   216 RAVgTNLVQMILSIDLLDRNTHGVsWlPLYH----DMGLSMIGFPAVYGGHSTLMsPTAFVRRPQRWIKALSEGSRTgrV 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3757 LNQTPSAFYALQSQ----AMRRELALNVRAVVFGGEALEPSRLQPWRERY-----PQAELVNMYGITETTVHVS------ 3821
Cdd:PRK12476   292 VTAAPNFAYEWAAQrglpAEGDDIDLSNVVLIIGSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFVAtiapda 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3822 ------FHRlsDEDLQSPTSRIGSALPDLAVHVL--------------DAAGQPVPLGVVGELVVEGDGVAQGYWQRPEL 3881
Cdd:PRK12476   372 epsvvyLDR--EQLGAGRAVRVAADAPNAVAHVScgqvarsqwavivdPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEE 449
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3882 TAERFVERGGQR---------------FYRSGDLGRYRaDGSLEYRGRGDDQVKLRGYRIEPGEIAAKIA-SLPQVSD-- 3943
Cdd:PRK12476   450 TERTFGAKLQSRlaegshadgaaddgtWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAeASPMVRRgy 528
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3944 -AAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPD-YMLP-RLIQLLPA--LPLTANGKLDRKA 4009
Cdd:PRK12476   529 vTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRrHGLAvADVRLVPAgaIPRTTSGKLARRA 599
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3664-4006 2.45e-25

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: 110.93  E-value: 2.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 YLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWS----------------LFHShafdfAVWELWGAWLY 3727
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagtvmfpappLMHG-----TGSWTAFGGLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3728 GGRAVLVPEAVCRqPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELALNV---RAVVFGGEALEPSRLQPWRERYPQ 3804
Cdd:cd05924     82 GGQTVVLPDDRFD-PEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLsslFAISSGGALLSPEVKQGLLELVPN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 AELVNMYGITETTVHVSFHrlSDEDLQSPTSRIGSAlPDLAVhvLDAAGQPVPLGVVGELVVEGDG-VAQGYWQRPELTA 3883
Cdd:cd05924    161 ITLVDAFGSSETGFTGSGH--SAGSGPETGPFTRAN-PDTVV--LDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3884 ERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAY 3960
Cdd:cd05924    236 ETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV--GRPDERWgqeVVAV 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773 3961 AVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:cd05924    314 VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
2050-2522 4.52e-25

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: 112.60  E-value: 4.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDARQIAV 2128
Cdd:cd05923     17 ACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRlKAAELAELI 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 LDDSGARIVIGWGA--APAWVPASVRWLdAESVLD------VVSAYEEPPRVDVDAdtPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05923     97 ERGEMTAAVIAVDAqvMDAIFQSGVRVL-ALSDLVglgepeSAGPLIEDPPREPEQ--PAFVFYTSGTTGLPKGAVIPQR 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2201 NLANYVAGVLPVLDL--GEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAElaFDAQALAAHLQAHPVDCLKIVPSH 2278
Cdd:cd05923    174 AAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEE--FDPADALKLIEQERVTSLFATPTH 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2279 --LAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTlRIVNHYGPTEttvgILTCTVPEEWPVEQGVPVGHPLA 2356
Cdd:cd05923    252 ldALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTE----AMNSLYMRDARTGTEMRPGFFSE 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLDRFGLPAPVGVAGELY--LGGGNLSLGYWQRAEQTAERFVahplapDRLlYRSGDLARLDGEGRIVYLGRGDH 2434
Cdd:cd05923    327 VRIVRIGGSPDEALANGEEGELIvaAAADAAFTGYLNQPEATAKKLQ------DGW-YRTGDVGYVDPSGDVRILGRVDD 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2435 QVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAE------ALAQRLPEYLCPSRWRAVES 2508
Cdd:cd05923    400 MIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAdeldqfCRASELADFKRPRRYFFLDE 479
                          490
                   ....*....|....
gi 1246793773 2509 MPRLGNGKIDRQAL 2522
Cdd:cd05923    480 LPKNAMNKVLRRQL 493
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
3661-4007 6.97e-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: 108.65  E-value: 6.97e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 APAYLIYTSGSTGTPKGVVVTHRNVERLFTAatQTGRFSFDEHDVW----SLFHSHAfdfavweLWGAW--LYGGRAVLV 3734
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVC--NEDLFNISGEDAIlapgPLSHSLF-------LYGAIsaLYLGGTFIG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3735 PEAVcrQPDAFLDLLAEYGVTVLNQTPSAfyaLQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGIT 3814
Cdd:cd17633     72 QRKF--NPKSWIRKINQYNATVIYLVPTM---LQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTvHVSFhrLSDEDLQSPTSrIGSALPDLAVHVLDAAGqpvplGVVGELVVEGDGVAQGYwqrpelTAERFVERGGqrF 3894
Cdd:cd17633    147 ELS-FITY--NFNQESRPPNS-VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGY------VRGGFSNPDG--W 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3895 YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVaadGAEPDPQS 3973
Cdd:cd17633    210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVgIPDARFGEIAVALYS---GDKLTYKQ 286
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1246793773 3974 LREALRALLPDYMLPRLIQLLPALPLTANGKLDR 4007
Cdd:cd17633    287 LKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK07638 PRK07638
acyl-CoA synthetase; Validated
3533-4012 7.09e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 111.79  E-value: 7.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL 3612
Cdd:PRK07638    15 PNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3613 EDSGVCLSVSQRALAVELPG--TALCLDD---PFTRAQLDAVEPGELPEvptEAPAYLIYTSGSTGTPKGVVVTHRNVER 3687
Cdd:PRK07638    94 AISNADMIVTERYKLNDLPDeeGRVIEIDewkRMIEKYLPTYAPIENVQ---NAPFYMGFTSGSTGKPKAFLRAQQSWLH 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3688 LFTAATQTGRFSFDEHDV--WSLFHSHafdFavweLWGA--WLY-GGRAVLVPEAVcrqPDAFLDLLAEYGVTVLNQTPS 3762
Cdd:PRK07638   171 SFDCNVHDFHMKREDSVLiaGTLVHSL---F----LYGAisTLYvGQTVHLMRKFI---PNQVLDKLETENISVMYTVPT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 AFYALQSQAMRRElalNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVSFhrLSDEDLQSPTSRIGSALP 3842
Cdd:PRK07638   241 MLESLYKENRVIE---NKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTA--LVDEESERRPNSVGRPFH 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGY----WQRPELTAERFVErggqrfyrSGDLGRYRADGSLEYRGRGDDQ 3918
Cdd:PRK07638   315 NVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYiiggVLARELNADGWMT--------VRDVGYEDEEGFIYIVGREKNM 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWlMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALP 3998
Cdd:PRK07638   387 ILFGGINIFPEEIESVLHEHPAVDEIVVI--GVPDSYW-GEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIP 463
                          490
                   ....*....|....
gi 1246793773 3999 LTANGKLDRKALPK 4012
Cdd:PRK07638   464 YTNSGKIARMEAKS 477
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3542-4004 7.24e-25

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: 111.29  E-value: 7.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAayvpvdphaPAArrgfiledsgvCLSV 3621
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------VAA-----------LINY 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3622 SQRALAVelpgtALCLDdpFTRAQLDAVEPgelpevpteapAYLIYTSGSTGTPKGVVVTHRNVER-LFTAATQTGRFSF 3700
Cdd:cd05940     61 NLRGESL-----AHCLN--VSSAKHLVVDA-----------ALYIYTSGTTGLPKAAIISHRRAWRgGAFFAGSGGALPS 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3701 DE-HDVWSLFHSHAFDFAvwelWGAWLYGGRAVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAF-YALQSQAMRRELAL 3778
Cdd:cd05940    123 DVlYTCLPLYHSTALIVG----WSACLASGATLVIRKKF--SASNFWDDIRKYQATIFQYIGELCrYLLNQPPKPTERKH 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITETTvhVSFHRLSDEDlqSPTSRIGSALPDLA----VHVLDAAGQ 3854
Cdd:cd05940    197 KVRMIF--GNGLRPDIWEEFKERFGVPRIAEFYAATEGN--SGFINFFGKP--GAIGRNPSLLRKVAplalVKYDLESGE 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3855 P----------VPLGVVGELVVEGDGVA--QGYWQRPELTAE--RFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVK 3920
Cdd:cd05940    271 PirdaegrcikVPRGEPGLLISRINPLEpfDGYTDPAATEKKilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDA---AVTVEGQgEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPAL 3997
Cdd:cd05940    351 WKGENVSTTEVAAVLGAFPGVEEAnvyGVQVPGT-DGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEM 429

                   ....*..
gi 1246793773 3998 PLTANGK 4004
Cdd:cd05940    430 EITGTFK 436
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3529-4010 8.18e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 112.09  E-value: 8.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAV-SAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK13391     7 AQTTPDKPAViMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQ-------RALAVELPGTALCL--DDPFTRAQLDAVEP--GELPEVPTEAP---AYLIYTSGST 3672
Cdd:PRK13391    87 EAAYIVDDSGARALITSaakldvaRALLKQCPGVRHRLvlDGDGELEGFVGYAEavAGLPATPIADEslgTDMLYSSGTT 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3673 GTPKGV--------VVTHRNVERLFTAAtqtgrFSFDEHDVW----SLFHShAFDFAVwelwGAWLYGGRAVLVPEAVcr 3740
Cdd:PRK13391   167 GRPKGIkrplpeqpPDTPLPLTAFLQRL-----WGFRSDMVYlspaPLYHS-APQRAV----MLVIRLGGTVIVMEHF-- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 QPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELALNVRAVVFGGEALEPSRLQ--------PWRERYpqaelvnm 3810
Cdd:PRK13391   235 DAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKeqmidwwgPIIHEY-------- 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3811 YGITEtTVHVSFHRlSDEDLQSPTSrIGSALPDLaVHVLDAAGQPVPLGVVGELVVEGdGVAQGYWQRPELTAERFVERG 3890
Cdd:PRK13391   307 YAATE-GLGFTACD-SEEWLAHPGT-VGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 GqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVEGQGEGAWLMAYAVAADGAEP 3969
Cdd:PRK13391   382 T--WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfGVPNEDLGEEVKAVVQPVDGVDP 459
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1246793773 3970 DP---QSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK13391   460 GPalaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
3520-4021 8.78e-25

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: 113.04  E-value: 8.78e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEiarRYPARIAV--SAEDGE----LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTG 3593
Cdd:cd05966     57 NCLDRHLK---ERGDKVAIiwEGDEPDqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3594 AAYVPV----DPHAPAARrgfiLEDSGVCL-----SVSQRALAVEL-----------PGTALCL-------DDPFTRAQ- 3645
Cdd:cd05966    134 AVHSVVfagfSAESLADR----INDAQCKLvitadGGYRGGKVIPLkeivdealekcPSVEKVLvvkrtggEVPMTEGRd 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 --LDAVEPGELPEVPTEA-----PAYLIYTSGSTGTPKGVVvtHRNVERLFTAATqTGRFSFDEH--DV--------WSL 3708
Cdd:cd05966    210 lwWHDLMAKQSPECEPEWmdsedPLFILYTSGSTGKPKGVV--HTTGGYLLYAAT-TFKYVFDYHpdDIywctadigWIT 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3709 FHSHAfdfavwelwgawLYG----GRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQA----MRRELA- 3777
Cdd:cd05966    287 GHSYI------------VYGplanGATTVMFEGTPTYPDPgrYWDIVEKHKVTIFYTAPTAIRALMKFGdewvKKHDLSs 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LNVRAVVfgGEALEPSrlqPWR--------ERYPqaeLVNMYGITETTVHVSfhrlsdedlqSP-----TSRIGSA---L 3841
Cdd:cd05966    355 LRVLGSV--GEPINPE---AWMwyyevigkERCP---IVDTWWQTETGGIMI----------TPlpgatPLKPGSAtrpF 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAAGQPVPLGVVGELVVEGD--GVAQGYWQRPEltaeRFVERGGQRF---YRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd05966    417 FGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFpgyYFTGDGARRDEDGYYWITGRVD 492
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-----VEGQGegawLMAYAVAADGAEPDP---QSLREALRALLPDYMLP 3988
Cdd:cd05966    493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVgrphdIKGEA----IYAFVTLKDGEEPSDelrKELRKHVRKEIGPIATP 568
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1246793773 3989 RLIQLLPALPLTANGKLDRKALPKPETQDRDEG 4021
Cdd:cd05966    569 DKIQFVPGLPKTRSGKIMRRILRKIAAGEEELG 601
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
3520-4028 8.78e-25

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: 113.11  E-value: 8.78e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:TIGR02188   61 NCVDRHLEARPDKVAIIWEGDEPGEvrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIH 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPV----DPHAPAARrgfiLEDSGVCLSVS-----QRALAVELPGT---AL---------CL--------DDPFTRAQ-- 3645
Cdd:TIGR02188  141 SVVfggfSAEALADR----INDAGAKLVITadeglRGGKVIPLKAIvdeALekcpvsvehVLvvrrtgnpVVPWVEGRdv 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 -LDAVEPGELPEVPTEA-----PAYLIYTSGSTGTPKGVVvtHRNVERLFTAATqTGRFSFDEH---------DV-WSLF 3709
Cdd:TIGR02188  217 wWHDLMAKASAYCEPEPmdsedPLFILYTSGSTGKPKGVL--HTTGGYLLYAAM-TMKYVFDIKdgdifwctaDVgWITG 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3710 HSHAfdfavwelwgawLYG----GRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQA----MRRELA-L 3778
Cdd:TIGR02188  294 HSYI------------VYGplanGATTVMFEGVPTYPDPgrFWEIIEKHKVTIFYTAPTAIRALMRLGdewvKKHDLSsL 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVfgGEALEPSrlqPWR--------ERYPqaeLVNMYGITETTVHVSFHRLSDEDLQSptsriGSA---LPDLAVH 3847
Cdd:TIGR02188  362 RLLGSV--GEPINPE---AWMwyykvvgkERCP---IVDTWWQTETGGIMITPLPGATPTKP-----GSAtlpFFGIEPA 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3848 VLDAAGQPVP-LGVVGELVVEGD--GVAQGYWQRPeltaERFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKL 3921
Cdd:TIGR02188  429 VVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFpgyYFTGDGARRDKDGYIWITGRVDDVINV 504
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3922 RGYRIEPGEIAAKIASLPQVSDAAV-----TVEGQGegawLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQL 3993
Cdd:TIGR02188  505 SGHRLGTAEIESALVSHPAVAEAAVvgipdDIKGQA----IYAFVTLKDGYEPDDelrKELRKHVRKEIGPIAKPDKIRF 580
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773 3994 LPALPLTANGKLDRKALPK------PETQD----RDEGVLESASE 4028
Cdd:TIGR02188  581 VPGLPKTRSGKIMRRLLRKiaageaEILGDtstlEDPSVVEELIE 625
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
2062-2522 8.92e-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: 8.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGwg 2141
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 aapawvpasvrwldAESVLDvvsayeepprvDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDasl 2221
Cdd:cd05969     79 --------------TEELYE-----------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPD--- 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2222 aTLSTVAADLG-----FTALFGALLSGrrVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPREC 2296
Cdd:cd05969    131 -DIYWCTADPGwvtgtVYGIWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLS 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2297 ----LVTGGEALTGALVQ-QVRALAptLRIVNHYGPTETTvGILTCTVPEEwPVEQGvPVGHPLAGNEAWVLDRFGLPAP 2371
Cdd:cd05969    208 slrfIHSVGEPLNPEAIRwGMEVFG--VPIHDTWWQTETG-SIMIANYPCM-PIKPG-SMGKPLPGVKAAVVDENGNELP 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2372 VGVAGELYLGGGNLSL--GYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd05969    283 PGTKGILALKPGWPSMfrGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGangvLQLGACIQG--SL-EGV--AEALA--------QRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05969    356 SALMEHPAVAEAGVIGKPD----PLRGEIIKAfiSLkEGFepSDELKeeiinfvrQKLGAHVAPREIEFVDNLPKTRSGK 431

                   ....*.
gi 1246793773 2517 IDRQAL 2522
Cdd:cd05969    432 IMRRVL 437
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3544-4010 1.34e-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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 110.63  E-value: 1.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPhapaarrgfiledsgvclSVSQ 3623
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP------------------GMGR 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 RALAVelpgtalCLDDpftraqldaVEPGELPEVP-TEAPAYLIYTSGSTGTPKGVVVTHRNverlFTAATQTGRFSFD- 3701
Cdd:cd05910     64 KNLKQ-------CLQE---------AEPDAFIGIPkADEPAAILFTSGSTGTPKGVVYRHGT----FAAQIDALRQLYGi 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3702 ---EHDVWSlfhshafdFAVWELWGAWLygGRAVLVPEAVCRQ-----PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMR 3773
Cdd:cd05910    124 rpgEVDLAT--------FPLFALFGPAL--GLTSVIPDMDPTRparadPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3774 RELAL-NVRAVVFGGEALEPSRLQPWRER-YPQAELVNMYGITETTVHVSfhrLSDEDL----QSPTSR-----IGSALP 3842
Cdd:cd05910    194 HGITLpSLRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGATEALPVSS---IGSRELlattTAATSGgagtcVGRPIP 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3843 DLAVHVLDAAGQP---------VPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRF-YRSGDLGRYRADGSLEYR 3912
Cdd:cd05910    271 GVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFwHRMGDLGYLDDEGRLWFC 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRI--EPGEIAAKIAslPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRL 3990
Cdd:cd05910    351 GRKAHRVITTGGTLytEPVERVFNTH--PGVRRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYPHTQR 428
                          490       500
                   ....*....|....*....|....*
gi 1246793773 3991 IQLL---PALPLTA--NGKLDRKAL 4010
Cdd:cd05910    429 IGRFlihPSFPVDIrhNAKIFREKL 453
PRK06188 PRK06188
acyl-CoA synthetase; Validated
2050-2522 1.36e-24

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 111.62  E-value: 1.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK06188    26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVI--------GWGAAPAWVPASVRWL------DAESVLDVVSAYEEPPRVDVDADT-PAYLIYTSGSTGTPKG 2194
Cdd:PRK06188   106 EDAGISTLIvdpapfveRALALLARVPSLKHVLtlgpvpDGVDLLAAAAKFGPAPLVAAALPPdIAGLAYTGGTTGKPKG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2195 VVVSQGNLANYVAGVLPVLDLGEDASL---ATLSTVAAdlgftALF-GALLSGRRVRLLPAelaFDAQALAAHLQAHPVD 2270
Cdd:PRK06188   186 VMGTHRSIATMAQIQLAEWEWPADPRFlmcTPLSHAGG-----AFFlPTLLRGGTVIVLAK---FDPAEVLRAIEEQRIT 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2271 CLKIVPS-------HLAGLlaaaggTAVLPR-ECLVTGGEALTGA-LVQQVRALAPTLriVNHYGPTETTVGILTCTVPE 2341
Cdd:PRK06188   258 ATFLVPTmiyalldHPDLR------TRDLSSlETVYYGASPMSPVrLAEAIERFGPIF--AQYYGQTEAPMVITYLRKRD 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2342 EWPVEQGV--PVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllyRSGDLAR 2419
Cdd:PRK06188   330 HDPDDPKRltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWL-------HTGDVAR 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2420 LDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGAciQGSLEGVAEALA 2491
Cdd:PRK06188   403 EDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDekwgeavtAVVVLRPGA--AVDAAELQAHVK 480
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1246793773 2492 QRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK06188   481 ERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
588-1041 1.40e-24

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: 111.25  E-value: 1.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGF---APSVAIAVDELKLDGAG- 663
Cdd:cd05926     42 VAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGELGPAsraASKLGLAILELALDVGVl 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  664 -----------------ENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------H 720
Cdd:cd05926    122 irapsaeslsnlladkkNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfH 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  721 VAGLAVdtTLEQILAAwsrGACVVArpdellePQRFLA--FLSE---------------RAITVTDLAPAYANEL----- 778
Cdd:cd05926    202 VHGLVA--SLLSTLAA---GGSVVL-------PPRFSAstFWPDvrdynatwytavptiHQILLNRPEPNPESPPpklrf 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  779 VRASVADdwrdlalrclvvggdvLPVALAQRwFELGLdrRCALINAYGPTEATisshyHRVqaidASRPVPLGQLLPGRI 858
Cdd:cd05926    270 IRSCSAS----------------LPPAVLEA-LEATF--GAPVLEAYGMTEAA-----HQM----TSNPLPPGPRKPGSV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  859 -------AAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRMYRSGDRVRLLDDGELQFLG 931
Cdd:cd05926    322 gkpvgveVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA--------FKDGWFRTGDLGYLDADGYLFLTG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  932 RADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC 1010
Cdd:cd05926    394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfGVPDEKYGEEVAAAVVLREGASVTEEEL--------------RAFC 459
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1246793773 1011 -ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05926    460 rKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
681-1041 1.48e-24

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: 110.26  E-value: 1.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  681 YTSGSTGIPKGVEVGHAALAAHIDA-AAEALALSADDRVLHVAGLAVDTTLEQILA-AWSRGACVVARPDELlePQRFLA 758
Cdd:cd05958    104 FTSGTTGAPKATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGLGGVLLfPFGVGASGVLLEEAT--PDLLLS 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  759 FLSERAITVTDLAP-AYANELvrASVADDWRDLA-LRCLVVGGDVLPVALAQRWFE-LGLDrrcaLINAYGPTEATissH 835
Cdd:cd05958    182 AIARYKPTVLFTAPtAYRAML--AHPDAAGPDLSsLRKCVSAGEALPAALHRAWKEaTGIP----IIDGIGSTEMF---H 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  836 YHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGiglAEGYRGDAAASERRFAplrlpSGESLrmyRS 915
Cdd:cd05958    253 IFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYV-----QGGWN---IT 321
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  916 GDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAAQRLV---AWVECAGEDGFGQADL 992
Cdd:cd05958    322 GDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAV--AECAVVGHPDESRGVvvkAFVVLRPGVIPGPVLA 399
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773  993 NQTDSDQTeserwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05958    400 RELQDHAK----------AHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
PRK07514 PRK07514
malonyl-CoA synthase; Validated
2049-2525 1.72e-24

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 111.12  E-value: 1.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVE-EGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpqhpDARQIA 2127
Cdd:PRK07514    15 DRDAPFIEtPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN----TAYTLA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 VLD----DSGARIVIGWGAAPAWVPA--------SVRWLDAE---SVLDVvsAYEEPPR---VDVDADTPAYLIYTSGST 2189
Cdd:PRK07514    91 ELDyfigDAEPALVVCDPANFAWLSKiaaaagapHVETLDADgtgSLLEA--AAAAPDDfetVPRGADDLAAILYTSGTT 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2190 GTPKGVVVSQGNLA-NYVA-----GVLPvldlgEDASLATLSTVAADLGFTALFGALLSGRRVRLLPaelAFDAQALAah 2263
Cdd:PRK07514   169 GRSKGAMLSHGNLLsNALTlvdywRFTP-----DDVLIHALPIFHTHGLFVATNVALLAGASMIFLP---KFDPDAVL-- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2264 lqahpvdclkivpshlagllaaaggtAVLPRECLVTG----------GEALTGALVQQVRAL----APTL---------- 2319
Cdd:PRK07514   239 --------------------------ALMPRATVMMGvptfytrllqEPRLTREAAAHMRLFisgsAPLLaethrefqer 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2320 ---RIVNHYGPTETtvGILTCTvpeewPVE---QGVPVGHPLAGNEAWVLDR-FGLPAPVGVAGELYLGGGNLSLGYWQR 2392
Cdd:PRK07514   293 tghAILERYGMTET--NMNTSN-----PYDgerRAGTVGFPLPGVSLRVTDPeTGAELPPGEIGMIEVKGPNVFKGYWRM 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFvahplAPDRlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----- 2467
Cdd:PRK07514   366 PEKTAEEF-----RADG-FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPhpdfg 439
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2468 -GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID----RQALADL 2525
Cdd:PRK07514   440 eGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQknllREQYADL 502
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
550-1041 2.37e-24

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: 109.69  E-value: 2.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  550 ERAALETAQGRLSYRELLTAADARAAA-LRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRaevv 628
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRlLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL---- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 aasgcDAVLTDAQglagfapsVAIAVDelkldgagengsgenaapnqLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE 708
Cdd:cd05941     77 -----EYVITDSE--------PSLVLD--------------------PALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  709 ALALSADDRVL------HVAGL--AVDTTLeqilaaWSRGACVVARPDellEPQRFLAFLSERAITVTDLAPAYANEL-- 778
Cdd:cd05941    124 AWRWTEDDVLLhvlplhHVHGLvnALLCPL------FAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYTRLlq 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  779 -VRASVADDWRDLA-----LRCLVVGGDVLPVALAQRWFELGLDRrcaLINAYGPTEA--TISSHYHrvqaiDASRPVPL 850
Cdd:cd05941    195 yYEAHFTDPQFARAaaaerLRLMVSGSAALPVPTLEEWEAITGHT---LLERYGMTEIgmALSNPLD-----GERRPGTV 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  851 GQLLPG---RIAAvlDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLpsgeslrmYRSGDRVRLLDDGEL 927
Cdd:cd05941    267 GMPLPGvqaRIVD--EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYY 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  928 QFLGR-ADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAA---QRLVAWVecAGEDGFGQADLNqtdsdqtESE 1003
Cdd:cd05941    337 WILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECA--VIGVPDPdwgERVVAVV--VLRAGAAALSLE-------ELK 405
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 1004 RWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05941    406 EWAK---QRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK09088 PRK09088
acyl-CoA synthetase; Validated
2049-2526 2.45e-24

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 110.28  E-value: 2.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVE-EGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIA 2127
Cdd:PRK09088     9 PQRLAAVDlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2128 VLDDSGARIVIGwGAAPAwvPASVRWLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL----A 2203
Cdd:PRK09088    89 LLQDAEPRLLLG-DDAVA--AGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLqqtaH 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2204 NY------------------------VAGVLPVLDLG----------EDASLATLSTVAadLGFTALFGALLSGRRVRLL 2249
Cdd:PRK09088   166 NFgvlgrvdahssflcdapmfhiiglITSVRPVLAVGgsilvsngfePKRTLGRLGDPA--LGITHYFCVPQMAQAFRAQ 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 PAelaFDAQALAAHlqahpvdclkivpshlagllaaaggTAvlprecLVTGGEAltgALVQQVRA-LAPTLRIVNHYGPT 2328
Cdd:PRK09088   244 PG---FDAAALRHL-------------------------TA------LFTGGAP---HAAEDILGwLDDGIPMVDGFGMS 286
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 E--TTVGIltctvpeewPVEQGV------PVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERF 2400
Cdd:PRK09088   287 EagTVFGM---------SVDCDVirakagAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2401 VAHPlapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGVLQLg 2476
Cdd:PRK09088   358 TGDG------WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAdaqwGEVGYLAI- 430
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2477 ACIQGS---LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLL 2526
Cdd:PRK09088   431 VPADGApldLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
2050-2525 2.74e-24

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 110.75  E-value: 2.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK05852    32 APALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRS 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGAAPA-WVPASVR-WLDAESVLDVVSAYEEPPRVDVDA---------------DTPAYLIYTSGSTGTP 2192
Cdd:PRK05852   112 QAAGARVVLIDADGPHdRAEPTTRwWPLTVNVGGDSGPSGGTLSVHLDAateptpatstpeglrPDDAMIMFTGGTTGLP 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2193 KGVVVSQGNLANYVAGVLPVLDLG-EDASLATLSTVAADLGFTALFGALLSGRRVrLLPAELAFDAQALAAHLQAHPVDC 2271
Cdd:PRK05852   192 KMVPWTHANIASSVRAIITGYRLSpRDATVAVMPLYHGHGLIAALLATLASGGAV-LLPARGRFSAHTFWDDIKAVGATW 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2272 LKIVPS------HLAGLLAAAGGTAVLP--REClvtgGEALTGALVQ--QVRALAPtlrIVNHYGPTETTVGILTCTVP- 2340
Cdd:PRK05852   271 YTAVPTihqillERAATEPSGRKPAALRfiRSC----SAPLTAETAQalQTEFAAP---VVCAFGMTEATHQVTTTQIEg 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2341 ---EEWPVEQGVPVGHPlAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllyRSGDL 2417
Cdd:PRK05852   344 igqTENPVVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-------RTGDL 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2418 ARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI--QGSLEGVAEALAQ--- 2492
Cdd:PRK05852   416 GSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIvpRESAPPTAEELVQfcr 495
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1246793773 2493 -RLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK05852   496 eRLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
2061-2522 4.29e-24

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: 109.91  E-value: 4.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGW 2140
Cdd:cd17647     20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAApawvpasvrwldaesvlDVVsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDAS 2220
Cdd:cd17647    100 RAA-----------------GVV----------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADL----GFTALF-GA--LLSGRRVRLLPAELAfdaqalaAHLQAHPVDCLKIVPSHLAGLLAAAGGTAV-L 2292
Cdd:cd17647    153 FTMLSGIAHDPiqrdMFTPLFlGAqlLVPTQDDIGTPGRLA-------EWMAKYGATVTHLTPAMGQLLTAQATTPFPkL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 PRECLVtgGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWP-------VEQGVPVGHPLAGNEAWVLDR 2365
Cdd:cd17647    226 HHAFFV--GDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSdptflknLKDVMPAGRGMLNVQLLVVNR 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2366 FGLPAPVGVA--GELYLGGGNLSLGYWQRAEQTAERFV----AHP------------------LAPDRLLYRSGDLARLD 2421
Cdd:cd17647    304 NDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfwLGPRDRLYRTGDLGRYL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2422 GEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-------------------QGS 2482
Cdd:cd17647    384 PNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIvprfdkpddesfaqedvpkEVS 463
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2483 LEGVA--------------EALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd17647    464 TDPIVkgligyrklikdirEFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2047-2536 4.60e-24

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 110.22  E-value: 4.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPR----TFAQLAAMAAvwhrGAAWLPLDPQHPD 2122
Cdd:PRK06087    35 AMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGwcefTIIYLACLKV----GAVSVPLLPSWRE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIVIgwgaAPAWVpASVRWLD--------------------------AESVLDVVSAYE---EPPrvD 2173
Cdd:PRK06087   111 AELVWVLNKCQAKMFF----APTLF-KQTRPVDlilplqnqlpqlqqivgvdklapatsSLSLSQIIADYEpltTAI--T 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2174 VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFT-ALFGALLSGRRVRLL--- 2249
Cdd:PRK06087   184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLhGVTAPFLIGARSVLLdif 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 -PAELA--FDAQALAAHLQAHP--VDCLKIVPSHLagllaaaggTAVLPRECLVTGGEALTGALVQQvrALAPTLRIVNH 2324
Cdd:PRK06087   264 tPDACLalLEQQRCTCMLGATPfiYDLLNLLEKQP---------ADLSALRFFLCGGTTIPKKVARE--CQQRGIKLLSV 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTVGILtctVPEEWPVEQ-GVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfvah 2403
Cdd:PRK06087   333 YGSTESSPHAV---VNLDDPLSRfMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR----- 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2404 PLAPDRLLYrSGDLARLDGEGRIVYLGRgDHQVKIR-GYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQ 2474
Cdd:PRK06087   405 ALDEEGWYY-SGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDerlgerscAYVVLK 482
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2475 lGACIQGSLEGVAEALA-QRLPEYLCPSRWRAVESMPRLGNGKIDRQALA-DLLQQDDADSSAE 2536
Cdd:PRK06087   483 -APHHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMRRLTQDVCEE 545
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
2063-2467 5.86e-24

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: 109.25  E-value: 5.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDP-QHPD--ARQIavlDDSGARIVIg 2139
Cdd:cd05904     34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPlSTPAeiAKQV---KDSGAKLAF- 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 wgAAPAWVPaSVRWLDAESVL----DVVSAYE----------EPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL--- 2202
Cdd:cd05904    110 --TTAELAE-KLASLALPVVLldsaEFDSLSFsdllfeadeaEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLiam 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 -ANYVAGVLPVLDlGEDASLATL--STVaadLGFTALFGALLS-GRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVP-- 2276
Cdd:cd05904    187 vAQFVAGEGSNSD-SEDVFLCVLpmFHI---YGLSSFALGLLRlGATVVVMP---RFDLEELLAAIERYKVTHLPVVPpi 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 -----SHLAGLLAAaggtaVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEWPVEQGvPV 2351
Cdd:cd05904    260 vlalvKSPIVDKYD-----LSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYG-SV 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplaPDRLLyRSGDLARLDGEGRIVYLG 2430
Cdd:cd05904    334 GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID-----KEGWL-HTGDLCYIDEDGYLFIVD 407
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1246793773 2431 RGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:cd05904    408 RLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
2170-2525 6.54e-24

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: 108.96  E-value: 6.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2170 PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFT-ALFGALLSGRRVRL 2248
Cdd:cd05909    140 GVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSGIKVVF 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2249 LPaelafdaqalaahlqaHPVDCLKIVPSHLAGLLAAAGGTAVLPR--------ECL------VTGGEALTGALVQQVRA 2314
Cdd:cd05909    220 HP----------------NPLDYKKIPELIYDKKATILLGTPTFLRgyaraahpEDFsslrlvVAGAEKLKDTLRQEFQE 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2315 LApTLRIVNHYGPTETTvGILTCTVPEEwPVEQGVpVGHPLAGNEAWVLDRFGL-PAPVGVAGELYLGGGNLSLGYWQRA 2393
Cdd:cd05909    284 KF-GIRILEGYGTTECS-PVISVNTPQS-PNKEGT-VGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEP 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2394 EQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPG--VEVAAVL---ALPG 2468
Cdd:cd05909    360 ELTSF-------AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPedNEVAVVSvpdGRKG 432
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2469 ANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:cd05909    433 EKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
2061-2465 6.87e-24

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: 108.45  E-value: 6.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPR----TFAQLAAMAAvwhrGAAWLPLDPQHPdARQIA-VLDDSGAR 2135
Cdd:cd05907      5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNrpewTIADLAILAI----GAVPVPIYPTSS-AEQIAyILNDSEAK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2136 IVIgwgaapawvpasvrwldaesvldvvsayeepprVDvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL 2215
Cdd:cd05907     80 ALF---------------------------------VE-DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2216 GEDASLAT---LSTVAADLgfTALFGALLSGRRVRLLP-AELAFDAQALAAHLQAHPVD------CLKIVPSHLAGLLAA 2285
Cdd:cd05907    126 TEGDRHLSflpLAHVFERR--AGLYVPLLAGARIYFASsAETLLDDLSEVRPTVFLAVPrvwekvYAAIKVKAVPGLKRK 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 AGGTAVLPR-ECLVTGGEALTGALVQQVRALAPTLRIVnhYGPTETTvGILTCTVPEEWPVEQgvpVGHPLAGNEawvld 2364
Cdd:cd05907    204 LFDLAVGGRlRFAASGGAPLPAELLHFFRALGIPVYEG--YGLTETS-AVVTLNPPGDNRIGT---VGKPLPGVE----- 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2365 rfglpAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGR-GDHQVKIRGYRV 2443
Cdd:cd05907    273 -----VRIADDGEILVRGPNVMLGYYKNPEATAEALDA-----DGWL-HTGDLGEIDEDGFLHITGRkKDLIITSGGKNI 341
                          410       420
                   ....*....|....*....|..
gi 1246793773 2444 ELGEVEQVLAQLPGVEVAAVLA 2465
Cdd:cd05907    342 SPEPIENALKASPLISQAVVIG 363
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2053-2527 7.46e-24

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 108.79  E-value: 7.46e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK06839    19 IAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIV---------IGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPrvdvDADTPAYLIYTSGSTGTPKGVVVSQGNL 2202
Cdd:PRK06839    99 SGTTVLfvektfqnmALSMQKVSYVQRVISITSLKEIEDRKIDNFVEK----NESASFIICYTSGTTGKPKGAVLTQENM 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 A-NYVAGVLpVLDL-GEDASLATLSTVaaDLGFTALFG--ALLSGRRVrLLPAElaFDAQALAAHLQAHPVDCLKIVPS- 2277
Cdd:PRK06839   175 FwNALNNTF-AIDLtMHDRSIVLLPLF--HIGGIGLFAfpTLFAGGVI-IVPRK--FEPTKALSMIEKHKVTVVMGVPTi 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2278 HLAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQVRALAptLRIVNHYGPTET--TVGILTctvpEEWPVEQGVPVGHP 2354
Cdd:PRK06839   249 HQALINCSKFETTNLQSvRWFYNGGAPCPEELMREFIDRG--FLFGQGFGMTETspTVFMLS----EEDARRKVGSIGKP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2355 LAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplaPDRLLYrSGDLARLDGEGRIVYLGRGDH 2434
Cdd:PRK06839   323 VLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI------QDGWLC-TGDLARVDEDGFVYIVGRKKE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2435 QVKIRGYRVELGEVEQVLAQLPGVEVAAVLA--------LPGANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAV 2506
Cdd:PRK06839   396 MIISGGENIYPLEVEQVINKLSDVYEVAVVGrqhvkwgeIPIAFIVKKSSSVL--IEKDVIEHCRLFLAKYKIPKEIVFL 473
                          490       500
                   ....*....|....*....|.
gi 1246793773 2507 ESMPRLGNGKIDRQALADLLQ 2527
Cdd:PRK06839   474 KELPKNATGKIQKAQLVNQLK 494
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
3529-4005 9.16e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 108.94  E-value: 9.16e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAV-SAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PRK13390     7 AQIAPDRPAViVAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVSQRAL--AVELPGTALCLDDPFTR-----AQLDAVEPGELPEVpTEAP--AYLIYTSGSTGTPKG 3677
Cdd:PRK13390    87 EADYIVGDSGARVLVASAALdgLAAKVGADLPLRLSFGGeidgfGSFEAALAGAGPRL-TEQPcgAVMLYSSGTTGFPKG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3678 VV--VTHRNVERLF--TAATQTGRFSFDEHDVWslFHSHAFDFAVWELWGAWLY--GGRAVLVPEAvcrQPDAFLDLLAE 3751
Cdd:PRK13390   166 IQpdLPGRDVDAPGdpIVAIARAFYDISESDIY--YSSAPIYHAAPLRWCSMVHalGGTVVLAKRF---DAQATLGHVER 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3752 YGVTVLNQTPSAF---YALQSQAMRRELALNVRAVVFGGeALEPSRLQPWRERYPQAELVNMYGITEttVHVSFHRLSDE 3828
Cdd:PRK13390   241 YRITVTQMVPTMFvrlLKLDADVRTRYDVSSLRAVIHAA-APCPVDVKHAMIDWLGPIVYEYYSSTE--AHGMTFIDSPD 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3829 DLQSPTSRIGSALPDLavHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAErfVERGGQRFYRS-GDLGRYRADG 3907
Cdd:PRK13390   318 WLAHPGSVGRSVLGDL--HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHPFWTTvGDLGSVDEDG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3908 SLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREAL---RALLP 3983
Cdd:PRK13390   394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgVPDPEMGEQVKAVIQLVEGIRGSDELARELIdytRSRIA 473
                          490       500
                   ....*....|....*....|..
gi 1246793773 3984 DYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK13390   474 HYKAPRSVEFVDELPRTPTGKL 495
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
539-1041 9.18e-24

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: 109.08  E-value: 9.18e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  539 DAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGlsVIPLDTe 618
Cdd:COG1021     29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFA- 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  619 WPQARRAE---VVAASGCDAVLTDAQ----GLAGFAPSVAIAVDELK----------------LDGAGENGSGENAAPNQ 675
Cdd:COG1021    106 LPAHRRAEishFAEQSEAVAYIIPDRhrgfDYRALARELQAEVPSLRhvlvvgdageftsldaLLAAPADLSEPRPDPDD 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  676 LAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQ--ILAAWSRGACVVARPDelLEP 753
Cdd:COG1021    186 VAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpgVLGVLYAGGTVVLAPD--PSP 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  754 QRFLAFLSERAITVTDLAPAYANELVRASVADDWrDLA-LRCLVVGGDVLPVALAQRWF-ELGldrrCALINAYGPTEAT 831
Cdd:COG1021    264 DTAFPLIERERVTVTALVPPLALLWLDAAERSRY-DLSsLRVLQVGGAKLSPELARRVRpALG----CTLQQVFGMAEGL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  832 ISshYHRvqaIDAS---------RPV-PLGQLLpgriaaVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAp 901
Cdd:COG1021    339 VN--YTR---LDDPeevilttqgRPIsPDDEVR------IVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT- 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  902 lrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEgaaqRLV 976
Cdd:COG1021    407 ---PDG----FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVvampdEYLGE----RSC 475
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773  977 AWVECAGEDgFGQADLNqtdsdqteserwhRALCER-LPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:COG1021    476 AFVVPRGEP-LTLAELR-------------RFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK07470 PRK07470
acyl-CoA synthetase; Validated
2051-2528 1.02e-23

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 108.98  E-value: 1.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLD-PQHPDarQIAVL 2129
Cdd:PRK07470    22 DRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfRQTPD--EVAYL 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 -DDSGARIVIGWGAAPAWVPA---------SVRWLDA----ESVLDVVSAY--EEPPRVDVDADTPAYLIYTSGSTGTPK 2193
Cdd:PRK07470   100 aEASGARAMICHADFPEHAAAvraaspdltHVVAIGGaragLDYEALVARHlgARVANAAVDHDDPCWFFFTSGTTGRPK 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2194 GVVVSQGNLA----NYVAGVLPVLDlGEDASLatlstVAADLGFTALFGALLS---GRRVRLLPAElAFDAQALAAHLQA 2266
Cdd:PRK07470   180 AAVLTHGQMAfvitNHLADLMPGTT-EQDASL-----VVAPLSHGAGIHQLCQvarGAATVLLPSE-RFDPAEVWALVER 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2267 HPVDCLKIVPShlaGLLAAAGGTAVLPRE-----CLVTGGEALTGAlvQQVRALAPTLR-IVNHYGPTETTVGIltcTV- 2339
Cdd:PRK07470   253 HRVTNLFTVPT---ILKMLVEHPAVDRYDhsslrYVIYAGAPMYRA--DQKRALAKLGKvLVQYFGLGEVTGNI---TVl 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2340 ------PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYR 2413
Cdd:PRK07470   325 ppalhdAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG-------WFR 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2414 SGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIQGslEG 2485
Cdd:PRK07470   398 TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpvwgevgvAVCVARDGAPVDE--AE 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 2486 VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK07470   476 LLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
2053-2526 1.05e-23

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 108.13  E-value: 1.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIAV-LDD 2131
Cdd:PRK03640    19 TAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN-TRLSREELLWqLDD 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGAAPA--WVPASVRWLDAESvldvvSAYEEP-PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNlaNYVAG 2208
Cdd:PRK03640    98 AEVKCLITDDDFEAklIPGISVKFAELMN-----GPKEEAeIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN--HWWSA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLG---EDASLATL-----StvaadlGFTALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPShla 2280
Cdd:PRK03640   171 VGSALNLGlteDDCWLAAVpifhiS------GLSILMRSVIYGMRVVLVE---KFDAEKINKLLQTGGVTIISVVST--- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2281 gllAAAGGTAVLPRE-------CLVTGGEALTGALVQQVRalAPTLRIVNHYGPTETTVGIltCTVPEEWPVEQGVPVGH 2353
Cdd:PRK03640   239 ---MLQRLLERLGEGtypssfrCMLLGGGPAPKPLLEQCK--EKGIPVYQSYGMTETASQI--VTLSPEDALTKLGSAGK 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2354 PLAGNEAWVLDRfGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplapDRLLYrSGDLARLDGEGRIVYLGRGD 2433
Cdd:PRK03640   312 PLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ------DGWFK-TGDIGYLDEEGFLYVLDRRS 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2434 HQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANGVlqlgACIQGSLEGVAEALAQ----RLPEYLCPSRWRA 2505
Cdd:PRK03640   384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPV----AFVVKSGEVTEEELRHfceeKLAKYKVPKRFYF 459
                          490       500
                   ....*....|....*....|.
gi 1246793773 2506 VESMPRLGNGKIDRQALADLL 2526
Cdd:PRK03640   460 VEELPRNASGKLLRHELKQLV 480
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3533-4010 2.56e-23

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 107.83  E-value: 2.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP-------- 3601
Cdd:PRK13295    41 TAVTAVRLGTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPifrerels 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3602 ----HA-------PAARRGFILEDSGvclsvsqRALAVELP----------GTALCLDDPFTRAQLDAvEPGELPEVPTE 3660
Cdd:PRK13295   121 fmlkHAeskvlvvPKTFRGFDHAAMA-------RRLRPELPalrhvvvvggDGADSFEALLITPAWEQ-EPDAPAILARL 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3661 AP-----AYLIYTSGSTGTPKGVVVTHRN--------VERL--------FTAAT---QTGrfsfdehdvwslfhshafdf 3716
Cdd:PRK13295   193 RPgpddvTQLIYTSGTTGEPKGVMHTANTlmanivpyAERLglgaddviLMASPmahQTG-------------------- 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3717 avwelwgaWLYGGR-AVLVPEAVCRQ----PDAFLDLLAEYGVT-VLNQTPSAFYALQSQAMRRELALNVRAVVFGGEAL 3790
Cdd:PRK13295   253 --------FMYGLMmPVMLGATAVLQdiwdPARAAELIRTEGVTfTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPSRLQPWRERYpQAELVNMYGITETTVhVSFHRLSDEDLQSPTSRiGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDG 3870
Cdd:PRK13295   325 PGALVERARAAL-GAKIVSAWGMTENGA-VTLTKLDDPDERASTTD-GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3871 VAQGYWQRPELTAERFverggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV-- 3948
Cdd:PRK13295   402 NFGGYLKRPQLNGTDA-----DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAyp 476
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3949 -EGQGEGAwlMAYAVAADGAEPDPQSLREALRA--LLPDYMLPRLIqLLPALPLTANGKLDRKAL 4010
Cdd:PRK13295   477 dERLGERA--CAFVVPRPGQSLDFEEMVEFLKAqkVAKQYIPERLV-VRDALPRTPSGKIQKFRL 538
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1142-1371 3.31e-23

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: 105.90  E-value: 3.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDS-APAQPDrYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQ 1218
Cdd:cd19531      4 LSFAQQrlWFLDQlEPGSAA-YNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLP-LPVV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRGAADLDSRVDAAFARMQEA-TP--LA-GPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGE 1293
Cdd:cd19531     82 DLSGLPEAEREAEAQRLAREEArRPfdLArGPLLRATLLRLGEDEhVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1294 AWTPSARGASYADYVEALREADDAQRFDA--GFWRE-LA-AQPMQALPQDRPVAladARQSNVGRIVQ-TLDAGLTADLL 1368
Cdd:cd19531    162 PSPLPPLPIQYADYAVWQREWLQGEVLERqlAYWREqLAgAPPVLELPTDRPRP---AVQSFRGARVRfTLPAELTAALR 238

                   ...
gi 1246793773 1369 ERA 1371
Cdd:cd19531    239 ALA 241
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
2056-2517 4.21e-23

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: 107.66  E-value: 4.21e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAAS--WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSG 2133
Cdd:cd17634     77 DDTSQSrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVIGW------------------------------------GAAPAWVPAsvRWLDAESVLDVVSAYEEPPRVDvdAD 2177
Cdd:cd17634    157 SRLLITAdggvragrsvplkknvddalnpnvtsvehvivlkrtGSDIDWQEG--RDLWWRDLIAKASPEHQPEAMN--AE 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP-VLDLGEdaslATLSTVAADLGFTA-----LFGALLSGRRVRLLPA 2251
Cdd:cd17634    233 DPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGP----GDIYWCTADVGWVTghsylLYGPLACGATTLLYEG 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 elafdaqalaAHLQAHPVDCLKIVPSHLAGLLAAAGgTAVlpRECLVTGGEALTGALVQQVRALAPT------------- 2318
Cdd:cd17634    309 ----------VPNWPTPARMWQVVDKHGVNILYTAP-TAI--RALMAAGDDAIEGTDRSSLRILGSVgepinpeayewyw 375
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2319 -------LRIVNHYGPTETTVGILTcTVPEEWPVEQGVPVgHPLAGNEAWVLDRFGLPAPVGVAGELYLGGG--NLSLGY 2389
Cdd:cd17634    376 kkigkekCPVVDTWWQTETGGFMIT-PLPGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTL 453
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2390 WQRAEqtaeRFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGA 2469
Cdd:cd17634    454 FGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA 529
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2470 -NG-------VLQLGACIQGSLEG-VAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd17634    530 iKGqapyayvVLNHGVEPSPELYAeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK09192 PRK09192
fatty acyl-AMP ligase;
3515-4007 5.51e-23

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 107.01  E-value: 5.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3515 YACTG----NLVSRFAEIARRYPariavsaedgeldYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAIL 3590
Cdd:PRK09192    29 YAALGeagmNFYDRRGQLEEALP-------------YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3591 KTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALA---------VELPGTALCLDDPFTRAQLDAVE--PGELPEVPT 3659
Cdd:PRK09192    96 YAGLVPVPLPLPMGFGGRESYIAQLRGMLASAQPAAIitpdellpwVNEATHGNPLLHVLSHAWFKALPeaDVALPRPTP 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGrFSFDEHD---VW-SLFHshafDFAVWELWGAWLYGGRAV--L 3733
Cdd:PRK09192   176 DDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDG-LKVRPGDrcvSWlPFYH----DMGLVGFLLTPVATQLSVdyL 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPEAVCRQPDAFLDLLAEYGVTVlNQTPSAFYALQSQAMR--RELALNV---RAVVFGGEALEPSRLQPWRERYPQA--- 3805
Cdd:PRK09192   251 PTRDFARRPLQWLDLISRNRGTI-SYSPPFGYELCARRVNskDLAELDLscwRVAGIGADMIRPDVLHQFAEAFAPAgfd 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3806 --ELVNMYGITETTVHVSF--------------HRLS----DEDLQSPTSRI------GSALPDLAVHVLDAAGQPVPLG 3859
Cdd:PRK09192   330 dkAFMPSYGLAEATLAVSFsplgsgivveevdrDRLEyqgkAVAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPER 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3860 VVGELVVEGDGVAQGYWQRPEltAERFVERGGqrFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLP 3939
Cdd:PRK09192   410 VVGHICVRGPSLMSGYFRDEE--SQDVLAADG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEP 484
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3940 QV--SDAAV-TVEGQGEGAwlMAYAVAADGAEPDP-QSLREALRALLpdYM---LPRLIQLLP--ALPLTANGKLDR 4007
Cdd:PRK09192   485 ELrsGDAAAfSIAQENGEK--IVLLVQCRISDEERrGQLIHALAALV--RSefgVEAAVELVPphSLPRTSSGKLSR 557
PRK05850 PRK05850
acyl-CoA synthetase; Validated
3521-3952 6.19e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 106.95  E-value: 6.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDGELD---------YATLDRRSSQLATLLIRQGAgPGQRVGLCLPRGCDLLVALLAILK 3591
Cdd:PRK05850     3 VPSLLRERASLQPDDAAFTFIDYEQDpagvaetltWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3592 TGAAYVPVDPHAPAA---RRGFILEDSG--VCLSVSQRALAVELPGTALCLDDPFTRAQLDAVE---PGELPEVPTEAP- 3662
Cdd:PRK05850    82 AGLIAVPLSVPQGGAhdeRVSAVLRDTSpsVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDldsPRGSDARPRDLPs 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 -AYLIYTSGSTGTPKGVVVTHRNV----ERLFTA--ATQTGRFSFDEHDV-W-SLFHSHAFDFAVWelwgAWLYGGR-AV 3732
Cdd:PRK05850   162 tAYLQYTSGSTRTPAGVMVSHRNVianfEQLMSDyfGDTGGVPPPDTTVVsWlPFYHDMGLVLGVC----APILGGCpAV 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3733 LV-PEAVCRQPDAFLDLLAEYgvtvlnqtPSAFYALQSQAMrrELAL--------------NVRAVVFGGEALEPSRLQP 3797
Cdd:PRK05850   238 LTsPVAFLQRPARWMQLLASN--------PHAFSAAPNFAF--ELAVrktsdddmagldlgGVLGIISGSERVHPATLKR 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WRERY-----PQAELVNMYGITETTVHVS--------------FHRLSDEDLQSPTSRIGSAL------PDLAVHVLDA- 3851
Cdd:PRK05850   308 FADRFapfnlRETAIRPSYGLAEATVYVAtrepgqppesvrfdYEKLSAGHAKRCETGGGTPLvsygspRSPTVRIVDPd 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFverGGQ-----------RFYRSGDLGrYRADGSLEYRGRGDDQVK 3920
Cdd:PRK05850   388 TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTF---GATlvdpspgtpegPWLRTGDLG-FISEGELFIVGRIKDLLI 463
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1246793773 3921 LRGYRIEPGEIAAKIASLPQVSDAAVTVEGQG 3952
Cdd:PRK05850   464 VDGRNHYPDDIEATIQEITGGRVAAISVPDDG 495
PRK08162 PRK08162
acyl-CoA synthetase; Validated
3529-4010 6.71e-23

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 106.57  E-value: 6.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK08162    28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASI 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILE--DSGVCL------SVSQRALAvELPGTALCL----DDPFTRAQL-------DAVEPGElPEVPTEAPA------ 3663
Cdd:PRK08162   108 AFMLRhgEAKVLIvdtefaEVAREALA-LLPGPKPLVidvdDPEYPGGRFigaldyeAFLASGD-PDFAWTLPAdewdai 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 YLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDV--WSL--FHSHAFDFAvWELwgawlyggrAVLVPEAVC 3739
Cdd:PRK08162   186 ALNYTSGTTGNPKGVVYHHRGA--YLNALSNILAWGMPKHPVylWTLpmFHCNGWCFP-WTV---------AARAGTNVC 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 -R--QPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELALNVRAVVfGGEALEPSRLQPWRERypQAELVNMYGIT 3814
Cdd:PRK08162   254 lRkvDPKLIFDLIREHGVTHYCGAPIVLSALINapAEWRAGIDHPVHAMV-AGAAPPAAVIAKMEEI--GFDLTHVYGLT 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ET----TV---HVSFHRLSDEDLQSPTSRIGSALPDL-AVHVLDAA-GQPVPLG--VVGELVVEGDGVAQGYWQRPELTA 3883
Cdd:PRK08162   331 ETygpaTVcawQPEWDALPLDERAQLKARQGVRYPLQeGVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATE 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3884 ERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVklrgyrIEPGEiaaKIASL---------PQVSDAAVTV---EGQ 3951
Cdd:PRK08162   411 EAF--AGG--WFHTGDLAVLHPDGYIKIKDRSKDII------ISGGE---NISSIevedvlyrhPAVLVAAVVAkpdPKW 477
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3952 GEGAwlMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPaLPLTANGKLDRKAL 4010
Cdd:PRK08162   478 GEVP--CAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVL 533
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
588-1036 7.83e-23

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: 105.76  E-value: 7.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGL-------AGFAPSVAIAVDELKLD 660
Cdd:cd05911     38 VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLekvkeaaKELGPKDKIIVLDDKPD 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  661 GAGENGSG---------------ENAAPNQLAYILYTSGSTGIPKGVEVGHAA--LAAHIDAAAEALALSADDRVL---- 719
Cdd:cd05911    118 GVLSIEDLlsptlgeededlpppLKDGKDDTAAILYSSGTTGLPKGVCLSHRNliANLSQVQTFLYGNDGSNDVILgflp 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  720 --HVAGLavDTTLEQILaawsRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWrDLA-LRCLV 796
Cdd:cd05911    198 lyHIYGL--FTTLASLL----NGATVIIMPK--FDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKY-DLSsLRVIL 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  797 VGGDvlpvALAQRWFEL--GLDRRCALINAYGPTEAT-ISSHYHRVQAIDASrpvpLGQLLPGRIAAVLDAHGR-IVPRG 872
Cdd:cd05911    269 SGGA----PLSKELQELlaKRFPNATIKQGYGMTETGgILTVNPDGDDKPGS----VGRLLPNVEAKIVDDDGKdSLGPN 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  873 VCGELALGGIGLAEGYRGDAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHC 952
Cdd:cd05911    341 EPGEICVRGPQVMKGYYNNPEATKETFD----EDG----WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAV 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  953 LGQLPQVR-AAAAGVVGEGAAQRLVAWVECAgedgfgqadlnqtDSDQTESERWHRALCERLPAYM-----VptQFValP 1026
Cdd:cd05911    413 LLEHPGVAdAAVIGIPDEVSGELPRAYVVRK-------------PGEKLTEKEVKDYVAKKVASYKqlrggV--VFV--D 475
                          490
                   ....*....|
gi 1246793773 1027 RLPRNASGKI 1036
Cdd:cd05911    476 EIPKSASGKI 485
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
2090-2531 8.10e-23

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 106.29  E-value: 8.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2090 ALCLPRTFAQL--AAMAAvwhrgaawlPLDPQHPDARQIAVLDDSGARIVIGWGAAPAWVPASvrwlDAESVLDvvsaye 2167
Cdd:PRK13295   130 VLVVPKTFRGFdhAAMAR---------RLRPELPALRHVVVVGGDGADSFEALLITPAWEQEP----DAPAILA------ 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2168 eppRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLanyVAGVLPV---LDLGEDASLATLSTVAADLGF----------- 2233
Cdd:PRK13295   191 ---RLRPGPDDVTQLIYTSGTTGEPKGVMHTANTL---MANIVPYaerLGLGADDVILMASPMAHQTGFmyglmmpvmlg 264
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2234 ----------TALFGALLSGRRVRLLPAELAF-DAQALAAHLQAHPVDCLKIvpshlagllaaaggtavlprecLVTGGE 2302
Cdd:PRK13295   265 atavlqdiwdPARAAELIRTEGVTFTMASTPFlTDLTRAVKESGRPVSSLRT----------------------FLCAGA 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2303 ALTGALVQQVRALAPTlRIVNHYGPTETtvGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG 2382
Cdd:PRK13295   323 PIPGALVERARAALGA-KIVSAWGMTEN--GAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRG 399
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2383 GNLSLGYWQRAEQTAERFVAhplapdrlLYRSGDLARLDGEGRIVYLGRgDHQVKIRG-YRVELGEVEQVLAQLPGVEVA 2461
Cdd:PRK13295   400 CSNFGGYLKRPQLNGTDADG--------WFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQV 470
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2462 AVLALPGANgvLQLGACI-----QGS---LEGVAEAL-AQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDA 2531
Cdd:PRK13295   471 AIVAYPDER--LGERACAfvvprPGQsldFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
PLN02574 PLN02574
4-coumarate--CoA ligase-like
3545-4010 1.31e-22

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 105.69  E-value: 1.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3545 LDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQ 3623
Cdd:PLN02574    67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 -------RALAVELPGT--ALCLDD------PFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNverl 3688
Cdd:PLN02574   147 penveklSPLGVPVIGVpeNYDFDSkriefpKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRN---- 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3689 FTAATQTG-RFSFDEHD----------VWSLFHSHAFDFAVWELwgawLYGGRAVLVpeavCRQPDA--FLDLLAEYGVT 3755
Cdd:PLN02574   223 LIAMVELFvRFEASQYEypgsdnvylaALPMFHIYGLSLFVVGL----LSLGSTIVV----MRRFDAsdMVKVIDRFKVT 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3756 VLNQTPSAFYAL--QSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVhVSFHRLSDEDLQSP 3833
Cdd:PLN02574   295 HFPVVPPILMALtkKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTA-VGTRGFNTEKLSKY 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3834 TSrIGSALPDLAVHVLD-AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYR 3912
Cdd:PLN02574   374 SS-VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG---WLRTGDIAYFDEDGYLYIV 449
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGE-GAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLI 3991
Cdd:PLN02574   450 DRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKEcGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKV 529
                          490
                   ....*....|....*....
gi 1246793773 3992 QLLPALPLTANGKLDRKAL 4010
Cdd:PLN02574   530 VFVQSIPKSPAGKILRREL 548
PRK07787 PRK07787
acyl-CoA synthetase; Validated
2049-2523 1.43e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 104.69  E-value: 1.43e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAASWTYAQLRAAAGRIAGAL---DAVGVQPGAHVALCLPRTFAQLAAMAAVwhrgaawlPLDPQHPDARQ 2125
Cdd:PRK07787    13 ADIADAVRIGGRVLSRSDLAGAATAVAERVagaRRVAVLATPTLATVLAVVGALIAGVPVV--------PVPPDSGVAER 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2126 IAVLDDSGARIVIGwgaAPAWVPASVRWLDAESVLDVVSAYEEPprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLAny 2205
Cdd:PRK07787    85 RHILADSGAQAWLG---PAPDDPAGLPHVPVRLHARSWHRYPEP-----DPDAPALIVYTSGTTGPPKGVVLSRRAIA-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 vagvlpvldlgedaslATLSTVAADLGFTA---------LF----------GALLSGRRVRLL----PAELAFDAQALAA 2262
Cdd:PRK07787   155 ----------------ADLDALAEAWQWTAddvlvhglpLFhvhglvlgvlGPLRIGNRFVHTgrptPEAYAQALSEGGT 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2263 HLQAHPVDCLKIVpshlaglLAAAGGTAVLPRECLVTGGEALTGALVQQVRALApTLRIVNHYGPTETtvgILTCTVPEE 2342
Cdd:PRK07787   219 LYFGVPTVWSRIA-------ADPEAARALRGARLLVSGSAALPVPVFDRLAALT-GHRPVERYGMTET---LITLSTRAD 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2343 WPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVA--GELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllYRSGDLARL 2420
Cdd:PRK07787   288 GERRPGW-VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVV 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2421 DGEG--RIVylGRGDHQ-VKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAEAL----AQR 2493
Cdd:PRK07787   361 DPDGmhRIV--GRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELidfvAQQ 438
                          490       500       510
                   ....*....|....*....|....*....|
gi 1246793773 2494 LPEYLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:PRK07787   439 LSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
PRK06178 PRK06178
acyl-CoA synthetase; Validated
2051-2529 1.84e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 105.51  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLD 2130
Cdd:PRK06178    48 QRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELN 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWG----------------------------AAPAW-VPASVR--------WLDAESVLDVVSAYEEPPRVD 2173
Cdd:PRK06178   128 DAGAEVLLALDqlapvveqvraetslrhvivtsladvlpAEPTLpLPDSLRaprlaaagAIDLLPALRACTAPVPLPPPA 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2174 VDAdtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVlDLGEDASLATLSTVA----ADLGFTALFgALLSGRRVRLL 2249
Cdd:PRK06178   208 LDA--LAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAV-AVVGGEDSVFLSFLPefwiAGENFGLLF-PLFSGATLVLL 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 paelafdaqalaahLQAHPVDCLKIVPSHLAGLLAAAGGTAV---------------LPRECLVTGGEALTGALVQQVRA 2314
Cdd:PRK06178   284 --------------ARWDAVAFMAAVERYRVTRTVMLVDNAVelmdhprfaeydlssLRQVRVVSFVKKLNPDYRQRWRA 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2315 LAPTLRIVNHYGPTET-TVGILTC--TVPEEWPVEQGVPVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYW 2390
Cdd:PRK06178   350 LTGSVLAEAAWGMTEThTCDTFTAgfQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYW 429
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2391 QRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA----- 2465
Cdd:PRK06178   430 NKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGrpdpd 502
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2466 ---LPGANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSrWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK06178   503 kgqVPVAFVQLKPGADL--TAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALAEEL 566
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
3529-4010 1.98e-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: 104.38  E-value: 1.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:cd05929      2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEdsgvclsVSQRALAVELPGTALCLDDPFTraqlDAVEPGELPEVPTE---APAYLIYTSGSTGTPKGVVVTH--- 3682
Cdd:cd05929     82 CAIIE-------IKAAALVCGLFTGGGALDGLED----YEAAEGGSPETPIEdeaAGWKMLYSGGTTGRPKGIKRGLpgg 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3683 -RNVERLFTAATQTGrFSFDEHDVWS--LFHSHAFDFAVwelwGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQ 3759
Cdd:cd05929    151 pPDNDTLMAAALGFG-PGADSVYLSPapLYHAAPFRWSM----TALFMGGTLVLMEKF---DPEEFLRLIERYRVTFAQF 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3760 TPSAF---YALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAeLVNMYGITETtVHVSFHRlSDEDLQSPTSr 3836
Cdd:cd05929    223 VPTMFvrlLKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEG-QGLTIIN-GEEWLTHPGS- 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 IGSALPDlAVHVLDAAGQPVPLGVVGELVVEGdGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGD 3916
Cdd:cd05929    299 VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGG---WSTLGDVGYLDEDGYLYLTDRRS 373
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ---SLREALRALLPDYMLPRLIQ 3992
Cdd:cd05929    374 DMIISGGVNIYPQEIENALIAHPKVLDAAVVgVPDEELGQRVHAVVQPAPGADAGTAlaeELIAFLRDRLSRYKCPRSIE 453
                          490
                   ....*....|....*...
gi 1246793773 3993 LLPALPLTANGKLDRKAL 4010
Cdd:cd05929    454 FVAELPRDDTGKLYRRLL 471
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3663-4010 3.27e-22

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: 101.79  E-value: 3.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKgvVVTHRNVERLFTAATQTGRFSFDEHDV----WSLFHSHAfdfAVWELWGAWLYGGRAVLVPEAV 3738
Cdd:cd05944      5 AAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVllcgLPLFHVNG---SVVTLLTPLASGAHVVLAGPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3739 CRQPDAFLD---LLAEYGVTVLNQTPSAFYALQSQAMRRELAlNVRAVVFGGEALePSRLQPWRERYPQAELVNMYGITE 3815
Cdd:cd05944     80 YRNPGLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADIS-SLRFAMSGAAPL-PVELRARFEDATGLPVVEGYGLTE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3816 TTvhvSFHRLSDEDLQSPTSRIGSALPDLAVH--VLDAAGQ---PVPLGVVGELVVEGDGVAQGYWQRpELTAERFVERG 3890
Cdd:cd05944    158 AT---CLVAVNPPDGPKRPGSVGLRLPYARVRikVLDGVGRllrDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADG 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3891 gqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGE---GAWLMAYAVAADGA 3967
Cdd:cd05944    234 ---WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAV--GQPDahaGELPVAYVQLKPGA 308
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1246793773 3968 EPDPQSLREALRALLPDY-MLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:cd05944    309 VVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
513-1057 4.17e-22

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 104.07  E-value: 4.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  513 SWPWPADELALDDKREPAprtvgnvvdAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCL 592
Cdd:PRK06155     8 LAARAVDPLPPSERTLPA---------MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  593 PRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGF--------------------APSVAI 652
Cdd:PRK06155    79 GNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadpgdlplpavwlldapaSVSVPA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  653 AVDELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQ 732
Cdd:PRK06155   159 GWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  733 ILAAWSRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGdvLPVALAQRWFE 812
Cdd:PRK06155   239 FFQALLAGATYVLEPR--FSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRE 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  813 lgldrRC--ALINAYGPTEATISSHyhrvQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGG---IGLAEG 887
Cdd:PRK06155   315 -----RFgvDLLDGYGSTETNFVIA----VTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATG 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  888 YRGDAAASERRFAPLrlpsgeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV 967
Cdd:PRK06155   386 YFGMPEKTVEAWRNL---------WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  968 GEGAAQRLVAwVECAGEDGfgqadlnqTDSDQTESERWhralCE-RLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPV 1046
Cdd:PRK06155   457 PSELGEDEVM-AAVVLRDG--------TALEPVALVRH----CEpRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
                          570
                   ....*....|....*..
gi 1246793773 1047 LAQ------AERTPPRT 1057
Cdd:PRK06155   524 TADtwdreaAGVQLPRS 540
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1644-1906 5.63e-22

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: 102.39  E-value: 5.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1644 TVRRQ-PMLRTAIVWEGlSVPHQIVLADAAAPWQTLDWSALDDAaqdaQLQRWLADDAAQGVDFAHAPLARMSLIGRGGG 1722
Cdd:cd20484     47 FVLEQhPILKSVIEEED-GVPFQKIEPSKPLSFQEEDISSLKES----EIIAYLREKAKEPFVLENGPLMRVHLFSRSEQ 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1723 RYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPG-FQAYLDWrERQDLARQRG-----WWRERLSGyaG 1796
Cdd:cd20484    122 EHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPAsYYDFVAW-EQDMLAGAEGeehraYWKQQLSG--T 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1797 TAALPAPVAAAHHPVQR---EECERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPEl 1873
Cdd:cd20484    199 LPILELPADRPRSSAPSfegQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEE- 277
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1246793773 1874 aGVESMVGVFINTLPLRLRIDAGQPALDLLSAL 1906
Cdd:cd20484    278 -RFDSLIGYFINMLPIRSRILGEETFSDFIRKL 309
PRK07529 PRK07529
AMP-binding domain protein; Validated
3529-4029 1.00e-21

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 103.50  E-value: 1.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVS--------AEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAyVPVD 3600
Cdd:PRK07529    35 AARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPIN 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3601 PHAPAARRGFILEDSG----VCLS------VSQRALAV--ELPG--TALCLD------------DPFTR----------- 3643
Cdd:PRK07529   114 PLLEPEQIAELLRAAGakvlVTLGpfpgtdIWQKVAEVlaALPElrTVVEVDlarylpgpkrlaVPLIRrkaharildfd 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3644 AQLDAvEPGELPEVPTEA----PAYLIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGrfsFDEHDV----WSLFHSHAf 3714
Cdd:PRK07529   194 AELAR-QPGDRLFSGRPIgpddVAAYFHTGGTTGMPKLAQHTHGNeVANAWLGALLLG---LGPGDTvfcgLPLFHVNA- 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3715 dfAVWELWGAWLYGGRAVLVPEAVCRQP---DAFLDLLAEYGVTVLNQTPSAFYALqsqaMRREL-ALNVRAV--VFGGE 3788
Cdd:PRK07529   269 --LLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAAL----LQVPVdGHDISSLryALCGA 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3789 ALEPSRLqpwRERYPQA---ELVNMYGITETTVHVSFHRLSDEdlqsptSRIGSA---LP--DLAVHVLDAAG---QPVP 3857
Cdd:PRK07529   343 APLPVEV---FRRFEAAtgvRIVEGYGLTEATCVSSVNPPDGE------RRIGSVglrLPyqRVRVVILDDAGrylRDCA 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 LGVVGELVVEGDGVAQGYwqrpeLTAERfvERG---GQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:PRK07529   414 VDEVGVLCIAGPNVFSGY-----LEAAH--NKGlwlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEA 486
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3935 IASLPQVSDAAVTveGQGE---GAWLMAYAVAADGAEPDPQSLREALRALLPD-YMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07529   487 LLRHPAVALAAAV--GRPDahaGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL 564
                          570
                   ....*....|....*....
gi 1246793773 4011 PKPETQDRDEGVLESASER 4029
Cdd:PRK07529   565 RRDAIRRVLRAALRDAGVE 583
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2063-2634 2.12e-21

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 102.80  E-value: 2.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDARQIAVLDDSGARIVIGWG 2141
Cdd:PRK06060    32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPElHRDDHALAARNTEPALVVTSDA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 AAPAWVPASVrwLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV------LPVLDL 2215
Cdd:PRK06060   112 LRDRFQPSRV--AEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrkalrLTPEDT 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2216 GEDASLATLstvAADLGFTALFgALLSGRRVRLLPAELAFDAQALAAHLQAHPVdcLKIVPSHLAGLLAAAGGTAVLPRE 2295
Cdd:PRK06060   190 GLCSARMYF---AYGLGNSVWF-PLATGGSAVINSAPVTPEAAAILSARFGPSV--LYGVPNFFARVIDSCSPDSFRSLR 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVpEEWPVEQgvpVGHPLAGNEAWVLDRFGLPAPVGVA 2375
Cdd:PRK06060   264 CVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRV-DEWRLGT---LGRVLPPYEIRVVAPDGTTAGPGVE 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGNLSLGYWQRAEqtaerfvahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:PRK06060   340 GDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIED 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2456 PGVEVAAVLALPGANGVLQL--------GACIQGS-LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL---- 2522
Cdd:PRK06060   411 EAVAEAAVVAVRESTGASTLqaflvatsGATIDGSvMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqs 490
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2523 --------------ADLLQQDDADSSAEAID------ETPVNEVLRELWQ---------------KLLGREHIGAHDN-- 2565
Cdd:PRK06060   491 ptkpiwelsltepgSGVRAQRDDLSASNMTIaggndgGATLRERLVALRQerqrlvvdavcaeaaKMLGEPDPWSVDQdl 570
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2566 -FFALGGDSILSLQLVAR-ARQAGLALMPRQLYDHPTLAGLS----AQVQASSPAPATikPATEAEQSFGLTPIQ 2634
Cdd:PRK06060   571 aFSELGFDSQMTVTLCKRlAAVTGLRLPETVGWDYGSISGLAqyleAELAGGHGRLKS--AGPVNSGATGLWAIE 643
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
1441-1585 2.13e-21

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: 93.49  E-value: 2.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1441 AQIGALKEQIRALARRGLDYMPL----VASARIPALPAGQLLFNYHGVVDAGAHPAFeVEPRTLASGNGAD--NPPGALV 1514
Cdd:TIGR01720    4 RLIKAVKEQLRRIPNKGVGYGVLryltEPEEKLAASPQPEISFNYLGQFDADSNDEL-FQPSSYSPGEAISpeSPRPYAL 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1515 EINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQARLQADEFALL 1585
Cdd:TIGR01720   83 EINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
2173-2525 2.53e-21

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 103.08  E-value: 2.53e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2173 DVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLSTVAAdLGFTA-LFGALLSGRRVRLLP 2250
Cdd:PRK08633   778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNdDVILSSLPFFHS-FGLTVtLWLPLLEGIKVVYHP 856
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2251 aelafdaqalaahlqaHPVDCLKIVPSHLAGLLAAAGGTAVLPRECL----------------VTGGEALTGALVQQVRa 2314
Cdd:PRK08633   857 ----------------DPTDALGIAKLVAKHRATILLGTPTFLRLYLrnkklhplmfaslrlvVAGAEKLKPEVADAFE- 919
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2315 LAPTLRIVNHYGPTETTvGILTCTVPEEwpVEQGVP---------VGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGN 2384
Cdd:PRK08633   920 EKFGIRILEGYGATETS-PVASVNLPDV--LAADFKrqtgskegsVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQ 996
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2385 LSLGYWQRAEQTAErfVAHPLAPDRlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVE--VAA 2462
Cdd:PRK08633   997 VMKGYLGDPEKTAE--VIKDIDGIG-WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEevVFA 1073
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2463 VLALP----GANGVLqLGACIQGSLEGVAEALAQ-RLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK08633  1074 VTAVPdekkGEKLVV-LHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2630-3043 3.03e-21

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: 99.79  E-value: 3.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQ--HWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRFA--- 2704
Cdd:cd19066      4 LSPMQrgMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEiid 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2705 ---HREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAY--AERRAGRS 2779
Cdd:cd19066     84 lrnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYdaAERQKPTL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2780 PALAAEACGFGAWQAALRQLSA--ATLDGWRSYWRAQAADAEAIALPwQDSDNRYADTVHLHDRFERDWTERlLTQTARA 2857
Cdd:cd19066    164 PPPVGSYADYAAWLEKQLESEAaqADLAYWTSYLHGLPPPLPLPKAK-RPSQVASYEVLTLEFFLRSEETKR-LREVARE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2858 YGNEPQEVLLTALALALRDGGDAATLWVEMEGHGRDDlgagLDLSRTVGWFTARYPLALHLPAGEDLGAALRSTKDRMRA 2937
Cdd:cd19066    242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD----EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2938 VPDRGLGFGVLRYLH----GELAELPVPQVCFNYLGQlraGERDGWALCEEPDGGGRAGGNRRRHLLDVNAM-LVDGELR 3012
Cdd:cd19066    318 AIEHQRVPFIELVRHlgvvPEAPKHPLFEPVFTFKNN---QQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASeDPDGDLL 394
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1246793773 3013 LDWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:cd19066    395 LRLEYSRGVYDERTIDRFAERYMTALRQLIE 425
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
3522-4009 3.28e-21

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 101.73  E-value: 3.28e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3522 VSRFAE-----IARRYparIAVSAE-DG---ELDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKT 3592
Cdd:PRK07769    27 VERWAKvrgdkLAYRF---LDFSTErDGvarDLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYA 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3593 GAAYVPV-DPHAP--AARRGFILEDS--GVCLSVSQRALAVE-----LPGTalclDDPFTRAqLDAVePGEL------PE 3656
Cdd:PRK07769   103 GRIAVPLfDPAEPghVGRLHAVLDDCtpSAILTTTDSAEGVRkffraRPAK----ERPRVIA-VDAV-PDEVgatwvpPE 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEAPAYLIYTSGSTGTPKGVVVTHRNVErlfTAATQT-GRFSFDEHD---VW-SLFHshafDFAVWELWGAWLYGGR- 3730
Cdd:PRK07769   177 ANEDTIAYLQYTSGSTRIPAGVQITHLNLP---TNVLQViDALEGQEGDrgvSWlPFFH----DMGLITVLLPALLGHYi 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3731 AVLVPEAVCRQPDAFLDLLA---EYGVTVLNQTPSafYALQSQAMR-----RELAL---NVRAVVFGGEALEPSRLQPWR 3799
Cdd:PRK07769   250 TFMSPAAFVRRPGRWIRELArkpGGTGGTFSAAPN--FAFEHAAARglpkdGEPPLdlsNVKGLLNGSEPVSPASMRKFN 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3800 ERY-----PQAELVNMYGITETTVHVSFHRLSDE-------------------DLQSPTS--RIGS---ALPDLAVHVLD 3850
Cdd:PRK07769   328 EAFapyglPPTAIKPSYGMAEATLFVSTTPMDEEptviyvdrdelnagrfvevPADAPNAvaQVSAgkvGVSEWAVIVDP 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQR--------------FYRSGDLGRYrADGSLEYRGRGD 3916
Cdd:PRK07769   408 ETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRlseshaegapddalWVRTGDYGVY-FDGELYITGRVK 486
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3917 DQVKLRGYR----------------IEPGEIAA---KIASLPQV----SDAAVTVEGQGEGAWLMAYAVAADGA-EPDPQ 3972
Cdd:PRK07769   487 DLVIIDGRNhypqdleytaqeatkaLRTGYVAAfsvPANQLPQVvfddSHAGLKFDPEDTSEQLVIVAERAPGAhKLDPQ 566
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 3973 SLREALRALLPDY--MLPRLIQLLPA--LPLTANGKLDRKA 4009
Cdd:PRK07769   567 PIADDIRAAIAVRhgVTVRDVLLVPAgsIPRTSSGKIARRA 607
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
2061-2522 3.64e-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: 99.34  E-value: 3.64e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSgarivigw 2140
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gaapawvpasvrwldaesvldvvsayeepprvDVDADTPAYLIYTSGSTGTPKGVVVSQGNlaNYVAGVLPVLDLG---E 2217
Cdd:cd05912     73 --------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGN--HWWSAIGSALNLGlteD 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2218 DASLATLSTVAADlGFTALFGALLSGRRVRLLPaelAFDAQALAAHLQAHPVDCLKIVPShlagllAAAGGTAVLPR--- 2294
Cdd:cd05912    119 DNWLCALPLFHIS-GLSILMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPT------MLQRLLEILGEgyp 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2295 ---ECLVTGGEALTGALVQQVRALAptLRIVNHYGPTETTVGILTCTvPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPAP 2371
Cdd:cd05912    189 nnlRCILLGGGPAPKPLLEQCKEKG--IPVYQSYGMTETCSQIVTLS-PEDALNKIG-SAGKPLFPVELKIEDDGQPPYE 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2372 VgvaGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQV 2451
Cdd:cd05912    265 V---GEILLKGPNVTKGYLNRPDATEESFENG-------WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2452 LAQLPGVEVAAVLALP----GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05912    335 LLSHPAIKEAGVVGIPddkwGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2329-2616 4.28e-21

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 97.13  E-value: 4.28e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 ETTVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLAPD 2408
Cdd:COG3433      1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2409 RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAE 2488
Cdd:COG3433     81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQA-----LADLLQQDDADSSAEAIDETPVNEVLRELWQKLLG--REHIG 2561
Cdd:COG3433    161 ALAALDKVPPDVVAASAVVALDALLLLALKVVAraapaLAAAEALLAAASPAPALETALTEEELRADVAELLGvdPEEID 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2562 AHDNFFALGGDSILSLQLVARARQAGLALMPRQLYDHPTLAGLSAQVQASSPAPA 2616
Cdd:COG3433    241 PDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PRK07798 PRK07798
acyl-CoA synthetase; Validated
2052-2518 5.07e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 100.34  E-value: 5.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK07798    19 RVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGAR-------------------------IVIGWGAAPAWVPASVRWLDAesvldVVSAYEEPPRVDVDADTpAYLIYTS 2186
Cdd:PRK07798    99 SDAValvyerefaprvaevlprlpklrtlVVVEDGSGNDLLPGAVDYEDA-----LAAGSPERDFGERSPDD-LYLLYTG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2187 GSTGTPKGVV-------VSQGNLANYVAGVlPVLDLGEDASLATLST-----VAADL----GFTALFGALLSGRRVRLLP 2250
Cdd:PRK07798   173 GTTGMPKGVMwrqedifRVLLGGRDFATGE-PIEDEEELAKRAAAGPgmrrfPAPPLmhgaGQWAAFAALFSGQTVVLLP 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2251 AElAFDaqalaahlqahPVDCLKIVPSHLAGLLAAA-------GGTAVLPRE--------CLVTGGEALTGALVQQVRAL 2315
Cdd:PRK07798   252 DV-RFD-----------ADEVWRTIEREKVNVITIVgdamarpLLDALEARGpydlsslfAIASGGALFSPSVKEALLEL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVGILTCTVPEEwpveqgVPVGHPL--AGNEAWVLDRFGLPAPVGVAGELYLG-GGNLSLGYWQR 2392
Cdd:PRK07798   320 LPNVVLTDSIGSSETGFGGSGTVAKGA------VHTGGPRftIGPRTVVLDEDGNPVEPGSGEIGWIArRGHIPLGYYKD 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFvahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN-- 2470
Cdd:PRK07798   394 PEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERwg 470
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2471 ----GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:PRK07798   471 qevvAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK06145 PRK06145
acyl-CoA synthetase; Validated
2054-2527 5.19e-21

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 100.35  E-value: 5.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2054 AVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSG 2133
Cdd:PRK06145    20 ALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVI--GWGAAPAWVPASVRWLDAESVLDV---VSAYEEPPRVDVDADTPAY-LIYTSGSTGTPKGVVVSQGNLANYVA 2207
Cdd:PRK06145   100 AKLLLvdEEFDAIVALETPKIVIDAAAQADSrrlAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYGNLHWKSI 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2208 GVLPVLDLGEDASLATLSTV----AADL-GFTALF-GALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAG 2281
Cdd:PRK06145   180 DHVIALGLTASERLLVVGPLyhvgAFDLpGIAVLWvGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2282 LLAAAGGTAVlpreclVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPEEwpVEQGVPVGHPLAGNEAW 2361
Cdd:PRK06145   260 RFDLDSLAWC------IGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGRE--IEKIGSTGRALAHVEIR 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2362 VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:PRK06145   332 IADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-------WFRSGDVGYLDEEGFLYLTDRKKDMIISGGE 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPGANG--------VLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:PRK06145   405 NIASSEVERVIYELPEVAEAAVIGVHDDRWgeritavvVLNPGATL--TLEALDRHCRQRLASFKVPRQLKVRDELPRNP 482
                          490
                   ....*....|....
gi 1246793773 2514 NGKIDRQALADLLQ 2527
Cdd:PRK06145   483 SGKVLKRVLRDELN 496
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
598-1041 6.10e-21

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: 100.43  E-value: 6.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  598 WYCLLLGAWRAGLSVIPLDTEwpQARRAE----VVAASGCDAVLTDAQGLAGFAP--------SVAIAVDELKLDGAGEN 665
Cdd:cd05906     82 WACVLAGFVPAPLTVPPTYDE--PNARLRklrhIWQLLGSPVVLTDAELVAEFAGletlsglpGIRVLSIEELLDTAADH 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  666 gSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGL------AVDTTLEQI 733
Cdd:cd05906    160 -DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLnwvpldHVGGLvelhlrAVYLGCQQV 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  734 LAAwsrgacvvarPDELL-EPQRFLAFLSERAITVTdLAPAYA----NELVRASVADDWRDLALRCLVVGGDVLPVALAQ 808
Cdd:cd05906    239 HVP----------TEEILaDPLRWLDLIDRYRVTIT-WAPNFAfallNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIR 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  809 RWFEL----GLdRRCALINAYGPTE----ATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALG 880
Cdd:cd05906    308 RLLRLlepyGL-PPDAIRPAFGMTEtcsgVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR 386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  881 GIGLAEGYRGDAAASERRFaplrLPSGeslrMYRSGDrVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR 960
Cdd:cd05906    387 GPVVTKGYYNNPEANAEAF----TEDG----WFRTGD-LGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  961 ---AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTESERWHRAlcerlPAYMVPtqfvaLPR--LPRNASGK 1035
Cdd:cd05906    458 psfTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVGVS-----PAYLIP-----LPKeeIPKTSLGK 527

                   ....*.
gi 1246793773 1036 IDRRAL 1041
Cdd:cd05906    528 IQRSKL 533
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
2047-2517 6.41e-21

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 100.24  E-value: 6.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQI 2126
Cdd:PRK07786    28 LMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2127 AVLDDSGARIVIGwGAAPAWVPASVRwlDAESVLDVV-------------------SAYEEPPRVDVDADTPAYLIYTSG 2187
Cdd:PRK07786   108 FLVSDCGAHVVVT-EAALAPVATAVR--DIVPLLSTVvvaggssddsvlgyedllaEAGPAHAPVDIPNDSPALIMYTSG 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2188 STGTPKGVVVSQGNLANYVAGVLPV--LDLGEDASLAT--LSTVAAdLGFTALFgaLLSGRRVRLLPAElAFDAQALAAH 2263
Cdd:PRK07786   185 TTGRPKGAVLTHANLTGQAMTCLRTngADINSDVGFVGvpLFHIAG-IGSMLPG--LLLGAPTVIYPLG-AFDPGQLLDV 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2264 LQAHPVDCLKIVPSHLAGLLAAAGgtaVLPRE----CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVgiLTCTV 2339
Cdd:PRK07786   261 LEAEKVTGIFLVPAQWQAVCAEQQ---ARPRDlalrVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSP--VTCML 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2340 PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplapDRLLYRSGDLAR 2419
Cdd:PRK07786   336 LGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-------AGGWFHSGDLVR 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2420 LDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPG-VEVA--------------AVLALPGANGVLqlgaciqgSLE 2484
Cdd:PRK07786   409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDiVEVAvigradekwgevpvAVAAVRNDDAAL--------TLE 480
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1246793773 2485 GVAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK07786   481 DLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1625-1934 7.32e-21

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: 98.87  E-value: 7.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1625 VAELDGEIDAAALAQAWQQTVRRQPMLRTAIVwEGLSVPHQIVLADAAAPWQTLDWSalDDAAQDAQLQRWLADDAAQGV 1704
Cdd:cd20483     29 VCHIKGKPDVNLLQKALSELVRRHEVLRTAYF-EGDDFGEQQVLDDPSFHLIVIDLS--EAADPEAALDQLVRNLRRQEL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1705 DFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPGFQaYLD---WRER--QD 1779
Cdd:cd20483    106 DIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDLATVPPPPVQ-YIDftlWHNAllQS 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1780 LARQR--GWWRERLSGYAGTAALPAPVAAAHHPV---QREECERRLSAHDSERLRAFCRERGCT-----LSDLIAMVWgl 1849
Cdd:cd20483    185 PLVQPllDFWKEKLEGIPDASKLLPFAKAERPPVkdyERSTVEATLDKELLARMKRICAQHAVTpfmflLAAFRAFLY-- 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1850 anaRYGNHDDVVLGATRSGRP-PElagVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGEILadS 1928
Cdd:cd20483    263 ---RYTEDEDLTIGMVDGDRPhPD---FDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVPFDYIV--D 334

                   ....*.
gi 1246793773 1929 GLDADR 1934
Cdd:cd20483    335 ALDVPR 340
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
3529-4010 7.91e-21

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 100.05  E-value: 7.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIA-VSAEDGE-LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAA 3606
Cdd:PLN02330    38 AELYADKVAfVEAVTGKaVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALES 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3607 RRGFILEDSGVCLSVS-----QRALAVELPGTAL---CLDDPFTRAQL-----DAVEPGELPEVPTEAPAYLIYTSGSTG 3673
Cdd:PLN02330   118 EIKKQAEAAGAKLIVTndtnyGKVKGLGLPVIVLgeeKIEGAVNWKELleaadRAGDTSDNEEILQTDLCALPFSSGTTG 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3674 TPKGVVVTHRNV-----ERLFTAATQT-------GRFSFdehdvwslFHShafdFAVWELWGAWLYG-GRAVLVPEAVCR 3740
Cdd:PLN02330   198 ISKGVMLTHRNLvanlcSSLFSVGPEMigqvvtlGLIPF--------FHI----YGITGICCATLRNkGKVVVMSRFELR 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 qpdAFLDLLAEYGVTVLNQTPSAFYALQSQAMRREL---ALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETT 3817
Cdd:PLN02330   266 ---TFLNALITQEVSFAPIVPPIILNLVKNPIVEEFdlsKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSFHrlSDEDLQSPTSR---IGSALPDLAVHVLDA-AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqr 3893
Cdd:PLN02330   343 CITLTH--GDPEKGHGIAKknsVGFILPNLEVKFIDPdTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDG--- 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3894 FYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQ 3972
Cdd:PLN02330   418 WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVpLPDEEAGEIPAACVVINPKAKESEE 497
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 3973 SLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PLN02330   498 DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
3552-4009 8.07e-21

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 100.07  E-value: 8.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVdpHAPAARRGFIL--EDSGVCLSVSQRALAVe 3629
Cdd:PRK07768    37 ERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML--HQPTPRTDLAVwaEDTLRVIGMIGAKAVV- 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3630 lpgtalcLDDPF---------------TRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERlfTAATQ 3694
Cdd:PRK07768   114 -------VGEPFlaaapvleekgirvlTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYA--NAEAM 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3695 TGRFSFD-EHDV---W-SLFHSHAFdfaVWELWGAWLYGGRAVLV-PEAVCRQPDAFLDLLAEYGVTVLnQTPSAFYALQ 3768
Cdd:PRK07768   185 FVAAEFDvETDVmvsWlPLFHDMGM---VGFLTVPMYFGAELVKVtPMDFLRDPLLWAELISKYRGTMT-AAPNFAYALL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3769 SQAMRR---ELALN---VRAVVFGGEALEPSRLQPW-----RERYPQAELVNMYGITETTVHVSFHRLS--------DED 3829
Cdd:PRK07768   261 ARRLRRqakPGAFDlssLRFALNGAEPIDPADVEDLldagaRFGLRPEAILPAYGMAEATLAVSFSPCGaglvvdevDAD 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSR--------------IGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYwqrpeLTAERFVE-RGGQRF 3894
Cdd:PRK07768   341 LLAALRRavpatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaQDADGW 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3895 YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV-SDAAVTVE----GQGEGawlmaYAVAADGAEP 3969
Cdd:PRK07768   416 LDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVrPGNAVAVRldagHSREG-----FAVAVESNAF 490
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773 3970 DPQSLREALRALLPDYML------PRLIQLLPA--LPLTANGKLDRKA 4009
Cdd:PRK07768   491 EDPAEVRRIRHQVAHEVVaevgvrPRNVVVLGPgsIPKTPSGKLRRAN 538
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
2056-2426 1.27e-20

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: 99.24  E-value: 1.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAASWTYAQLRAAAGRIAGALDAVGvQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL---DPQHPDARQIAVLDDS 2132
Cdd:cd05931     19 GGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAILADA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2133 GARIVIGWGAAPAWVPASV---------RWLDAESVLDVVSAYEEPPrvDVDADTPAYLIYTSGSTGTPKGVVVSQGNLA 2203
Cdd:cd05931     98 GPRVVLTTAAALAAVRAFAasrpaagtpRLLVVDLLPDTSAADWPPP--SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLL 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2204 NYVAGVLPVLDLGEDASLATLSTVAADLG-FTALFGALLSGRRVRLLPAE-------------------------LAFDA 2257
Cdd:cd05931    176 ANVRQIRRAYGLDPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSPAaflrrplrwlrlisryratisaapnFAYDL 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 -QALAAHLQAHPVD--CLKIV-----PSHLAGLLAAAGGTAV--LPREC------------LVTGGEALTGALVQQVRAL 2315
Cdd:cd05931    256 cVRRVRDEDLEGLDlsSWRVAlngaePVRPATLRRFAEAFAPfgFRPEAfrpsyglaeatlFVSGGPPGTGPVVLRVDRD 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVGILTCtvpeewpveqgvpvGHPLAGNEAWVLDRFGL-PAPVGVAGELYLGGGNLSLGYWQRAE 2394
Cdd:cd05931    336 ALAGRAVAVAADDPAARELVSC--------------GRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPE 401
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1246793773 2395 QTAERFVAHPLAPDRLLYRSGDLARL-DGE----GRI 2426
Cdd:cd05931    402 ATAETFGALAATDEGGWLRTGDLGFLhDGElyitGRL 438
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
544-1041 1.30e-20

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: 98.85  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  544 AADEFPERAAL-ETAQGR-LSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDtewPQ 621
Cdd:cd05904     14 FASAHPSRPALiDAATGRaLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN---PL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  622 ARRAEV---VAASGCDAVLTDAQG---LAGFAPSVaIAVDELKLDGAGE----NGSGENAAPNQ------LAYILYTSGS 685
Cdd:cd05904     91 STPAEIakqVKDSGAKLAFTTAELaekLASLALPV-VLLDSAEFDSLSFsdllFEADEAEPPVVvikqddVAALLYSSGT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  686 TGIPKGVEVGHA--ALAAHIDAAAEALALSADDRVL------HVAGLAVDTtleqiLAAWSRGACVVARPDelLEPQRFL 757
Cdd:cd05904    170 TGRSKGVMLTHRnlIAMVAQFVAGEGSNSDSEDVFLcvlpmfHIYGLSSFA-----LGLLRLGATVVVMPR--FDLEELL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  758 AFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRwFElgldRR---CALINAYGPTEATISS 834
Cdd:cd05904    243 AAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEA-FR----AKfpnVDLGQGYGMTESTGVV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  835 HYHRVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERrfaplrlpSGESLRMY 913
Cdd:cd05904    318 AMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA--------TIDKEGWL 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  914 RSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVecagedgfgqa 990
Cdd:cd05904    390 HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAA--VIPypdEEAGEVPMAFV----------- 456
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773  991 dLNQTDSDQTESErwhralcerlpaYMvptQFVA--------------LPRLPRNASGKIDRRAL 1041
Cdd:cd05904    457 -VRKPGSSLTEDE------------IM---DFVAkqvapykkvrkvafVDAIPKSPSGKILRKEL 505
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
2179-2519 2.24e-20

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: 95.79  E-value: 2.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDASLATLSTVAADLGF----TALF--GALLSGRRVRLLPA 2251
Cdd:cd17635      3 PLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLwwilTCLIhgGLCVTGGENTTYKS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 ---ELAFDAqalaahlqahpVDCLKIVPSHLAGLLAAAGGT-AVLPR-ECLVTGGEALTGALVQqVRALAPTLRIVNHYG 2326
Cdd:cd17635     83 lfkILTTNA-----------VTTTCLVPTLLSKLVSELKSAnATVPSlRLIGYGGSRAIAADVR-FIEATGLTNTAQVYG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2327 PTETTVgilTCTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahpla 2406
Cdd:cd17635    151 LSETGT---ALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2407 pDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN--GVLQLGACIQGSLE 2484
Cdd:cd17635    223 -DGWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfgELVGLAVVASAELD 300
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1246793773 2485 -----GVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17635    301 enairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK08316 PRK08316
acyl-CoA synthetase; Validated
2053-2517 3.60e-20

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 97.70  E-value: 3.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIA-VLDD 2131
Cdd:PRK08316    28 TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN-FMLTGEELAyILDH 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVI---------------------GWGAAPAWVPASVRWLDAESVLDvvSAYEEPPRVDVDADTPAYLIYTSGSTG 2190
Cdd:PRK08316   107 SGARAFLvdpalaptaeaalallpvdtlILSLVLGGREAPGGWLDFADWAE--AGSVAEPDVELADDDLAQILYTSGTES 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2191 TPKGVVVSQGNL-ANYVAGVLpVLDLG-EDASLATLStvaadLGFTA-----LFGALLSGRRVRLLPAelafdaqalaah 2263
Cdd:PRK08316   185 LPKGAMLTHRALiAEYVSCIV-AGDMSaDDIPLHALP-----LYHCAqldvfLGPYLYVGATNVILDA------------ 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2264 lqAHPVDCLKIVPSHLAG------------LLAAAGGTAVLP--RECLVtGGEALTGALVQQVRALAPTLRIVNHYGPTE 2329
Cdd:PRK08316   247 --PDPELILRTIEAERITsffapptvwislLRHPDFDTRDLSslRKGYY-GASIMPVEVLKELRERLPGLRFYNCYGQTE 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2330 ttVGILTcTV--PEEwPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplap 2407
Cdd:PRK08316   324 --IAPLA-TVlgPEE-HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG---- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2408 drlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI---QGSLE 2484
Cdd:PRK08316   396 ---WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVvpkAGATV 472
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1246793773 2485 GVAEALA---QRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK08316   473 TEDELIAhcrARLAGFKVPKRVIFVDELPRNPSGKI 508
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
2056-2535 3.97e-20

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: 98.33  E-value: 3.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAA-SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGA 2134
Cdd:cd05968     85 EDGTSrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2135 RIVI-----------------------------------GWGAAPAWVPASVRWLDAEsvldVVSAYEEPPRVDvdADTP 2179
Cdd:cd05968    165 KALItadgftrrgrevnlkeeadkacaqcptvekvvvvrHLGNDFTPAKGRDLSYDEE----KETAGDGAERTE--SEDP 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2180 AYLIYTSGSTGTPKGVV-VSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAq 2258
Cdd:cd05968    239 LMIIYTSGTTGKPKGTVhVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPK- 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 alaahlqahPVDCLKIVPSHLAGLLAAaggTAVLPRECLVTGGEALTGALVQQVRALAPT-------------------- 2318
Cdd:cd05968    318 ---------ADRLWRMVEDHEITHLGL---SPTLIRALKPRGDAPVNAHDLSSLRVLGSTgepwnpepwnwlfetvgkgr 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2319 LRIVNHYGPTETTVGILTCTvpeewPVEQGVPVGH--PLAGNEAWVLDRFGLPAPVGVaGELYLGGG--NLSLGYWQRAE 2394
Cdd:cd05968    386 NPIINYSGGTEISGGILGNV-----LIKPIKPSSFngPVPGMKADVLDESGKPARPEV-GELVLLAPwpGMTRGFWRDED 459
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2395 QTAERFVahplapDRL--LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG---- 2468
Cdd:cd05968    460 RYLETYW------SRFdnVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkg 533
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2469 ----ANGVLQLGACIQGSL-EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL-ADLLQQDDADSSA 2535
Cdd:cd05968    534 eaivCFVVLKPGVTPTEALaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIrAAYLGKELGDLSS 606
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
3082-3400 6.88e-20

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: 96.01  E-value: 6.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFavqglPSPRQLPHRQVSLPLAEQ 3161
Cdd:cd19546      6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-----PGDGGDVHQRILDADAAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3162 DWSGLEPAqARSRLSELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLYAALRESR 3241
Cdd:cd19546     81 PELPVVPA-TEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3242 TPQ-LPAAPPFRDYLHW----LRGQDEAAAR-----AFWREQLTGLEPAALPEATEPAEGYASstRRFDLAAASAWAQSH 3311
Cdd:cd19546    160 APErAPLPLQFADYALWerelLAGEDDRDSLigdqiAYWRDALAGAPDELELPTDRPRPVLPS--RRAGAVPLRLDAEVH 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 ----------GLTASSLLQGALALVLQRYYGRDDFALGiTIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQA 3381
Cdd:cd19546    238 arlmeaaesaGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGR 316
                          330
                   ....*....|....*....
gi 1246793773 3382 LQQRNLDLRTHGYLPLAQI 3400
Cdd:cd19546    317 VREAVREARRHQDVPFERL 335
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
2063-2517 6.93e-20

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 96.95  E-value: 6.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVI--- 2138
Cdd:PRK08314    37 SYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIvgs 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 ------------------------------GWGAAPAW--VPASVRWLDAESVL---DVVSAYEEPPRVDVDADTPAYLI 2183
Cdd:PRK08314   117 elapkvapavgnlrlrhvivaqysdylpaePEIAVPAWlrAEPPLQALAPGGVVawkEALAAGLAPPPHTAGPDDLAVLP 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDASLATLSTVAAdLGF-TALFGALLSGRRVRLLP---AELAFDAQ 2258
Cdd:PRK08314   197 YTSGTTGVPKGCMHTHRTVmANAVGSVLWSNSTPESVVLAVLPLFHV-TGMvHSMNAPIYAGATVVLMPrwdREAAARLI 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 alaahlqahpvdclkivpSHLAGLLAAAGGTAVL-----PR---------ECLVTGGEALTGALVQQVRALApTLRIVNH 2324
Cdd:PRK08314   276 ------------------ERYRVTHWTNIPTMVVdflasPGlaerdlsslRYIGGGGAAMPEAVAERLKELT-GLDYVEG 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTVGILTCtvPEEWPVEQGvpVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAh 2403
Cdd:PRK08314   337 YGLTETMAQTHSN--PPDRPKLQC--LGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE- 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2404 pLAPDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQL 2475
Cdd:PRK08314   412 -IDGKRFF-RTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDprrgetvkAVVVLRP 489
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1246793773 2476 GACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK08314   490 EARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
99-507 7.30e-20

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: 95.45  E-value: 7.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   99 FLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHE------------------VLDRCiqgedsvaagggaAVE 160
Cdd:cd19542     11 MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDilrtvfvessaegtflqvVLKSL-------------DPP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  161 SADLRGRGQDEIDALVEGFRLRpfELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRvec 240
Cdd:cd19542     78 IEEVETDEDSLDALTRDLLDDP--TLFGQPPHRLTLLETSSG-----EVYLVLRISHALYDGVSLPIILRDLAAAYN--- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  241 GLAAEPAPPlpcqYGDYARWQRDTldRLDASLRHHVEALSGAPHLHElpldherPAVLGQSGAKLRLAFPPGLSERVAAY 320
Cdd:cd19542    148 GQLLPPAPP----FSDYISYLQSQ--SQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAF 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  321 AQASR---ATAFHVLQAAFAALLARCgagDDLLIGTPVAGR--VRPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRD 395
Cdd:cd19542    215 CASLGvtlASLFQAAWALVLARYTGS---RDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQ 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  396 HQLAALEHQALPLERVIETLqveRSSRHAPLFQLMFALRHDADLALDLHGVQAHALTL-PEDVAKHELTLEVLVGAGGMS 474
Cdd:cd19542    292 QYLRSLPHQHLSLREIQRAL---GLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSaAEDPTEYPVAVEVEPSGDSLK 368
                          410       420       430
                   ....*....|....*....|....*....|...
gi 1246793773  475 AVWEYNTALWNPATVARWAERYFVALAAMLENP 507
Cdd:cd19542    369 VSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
PLN02654 PLN02654
acetate-CoA ligase
3542-4020 7.46e-20

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 97.66  E-value: 7.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY----------------VPVDPH--- 3602
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHsvvfagfsaeslaqriVDCKPKvvi 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3603 -APAARRGF-------ILEDS-----------GVCLSVSQRalavelpgTALCLDDPFTRAQLDAVEPGELPEVPT---- 3659
Cdd:PLN02654   198 tCNAVKRGPktinlkdIVDAAldesakngvsvGICLTYENQ--------LAMKREDTKWQEGRDVWWQDVVPNYPTkcev 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 -----EAPAYLIYTSGSTGTPKGVVVTHRNVeRLFTAATQTGRFSFDEHDV--------WSLFHSHAfdfavweLWGAWL 3726
Cdd:PLN02654   270 ewvdaEDPLFLLYTSGSTGKPKGVLHTTGGY-MVYTATTFKYAFDYKPTDVywctadcgWITGHSYV-------TYGPML 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3727 yGGRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQ---SQAMRRELALNVRAVVFGGEALEPSrlqPWRER 3801
Cdd:PLN02654   342 -NGATVLVFEGAPNYPDSgrCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPINPS---AWRWF 417
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3802 YpqaelvNMYGITETTVhvsfhrlSDEDLQSPTS-------------RIGSA-LPDLAVhvldaagQPVplgVVGELVVE 3867
Cdd:PLN02654   418 F------NVVGDSRCPI-------SDTWWQTETGgfmitplpgawpqKPGSAtFPFFGV-------QPV---IVDEKGKE 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3868 GDGVAQGY------W-----------QRPELTaeRFVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGE 3930
Cdd:PLN02654   475 IEGECSGYlcvkksWpgafrtlygdhERYETT--YFKPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAE 550
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3931 IAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGaEPDPQSLREAL----RALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PLN02654   551 VESALVSHPQCAEAAVVgIEHEVKGQGIYAFVTLVEG-VPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKI 629
                          570
                   ....*....|....*
gi 1246793773 4006 DRKALPKPETQDRDE 4020
Cdd:PLN02654   630 MRRILRKIASRQLDE 644
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
3111-3461 8.16e-20

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: 94.94  E-value: 8.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3111 LHGALDREAFAAAWQQALERHPILRSGFavqgLPSPRQlPHRQVSlplaeqdwsglEPAQARSRLSELQAQQcEAG--FD 3188
Cdd:cd19537     32 LSGDVDRDRLASAWNTVLARHRILRSRY----VPRDGG-LRRSYS-----------SSPPRVQRVDTLDVWK-EINrpFD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3189 LAAPPLMRLALLRRSadehwLVWTRHHLIVDGWSSALLLDEVWRLYAalresrtpQLPAAPPFRDYLHWLRGQDEAAA-- 3266
Cdd:cd19537     95 LEREDPIRVFISPDT-----LLVVMSHIICDLTTLQLLLREVSAAYN--------GKLLPPVRREYLDSTAWSRPASPed 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3267 RAFWREQLTGLEPAALPEATEPAeGYASSTRRFDLAAASA-----WAQSHGLTASSLLQGALALVLQRYYGRDDFALGIT 3341
Cdd:cd19537    162 LDFWSEYLSGLPLLNLPRRTSSK-SYRGTSRVFQLPGSLYrsllqFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3342 IAGRPPElaGVERMLGVFINSVPLRV--TPAGEATPAPWLQALQQRNLDLRTHgYLPLAQIQRAGAADAVSP----FDVL 3415
Cdd:cd19537    241 YLNRTSE--EDMETVGLFLEPLPIRIrfPSSSDASAADFLRAVRRSSQAALAH-AIPWHQLLEHLGLPPDSPnhplFDVM 317
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3416 LVFEnlptESREERSGMRIEELDHRAH----SNYPLML--TAIPDAG-GLRIE 3461
Cdd:cd19537    318 VTFH----DDRGVSLALPIPGVEPLYTwaegAKFPLMFefTALSDDSlLLRLE 366
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
529-1041 9.58e-20

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 96.41  E-value: 9.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  529 PAPRTVGNVVDAIARaadEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALclprgLDWYC-----LLL 603
Cdd:PRK06187     3 DYPLTIGRILRHGAR---KHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAV-----FDWNSheyleAYF 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  604 GAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDA------QGLAGFAPSVA--IAVDELKLDGAGENGSG----ENA 671
Cdd:PRK06187    75 AVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSefvpllAAILPQLPTVRtvIVEGDGPAAPLAPEVGEyeelLAA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 AP----------NQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleqILA 735
Cdd:PRK06187   155 ASdtfdfpdideNDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpmfHVHAWGL------PYL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  736 AWSRGACVVArPDElLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDLA-LRCLVVGGDVLPVALAQRWFELg 814
Cdd:PRK06187   229 ALMAGAKQVI-PRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYF-VDFSsLRLVIYGGAALPPALLREFKEK- 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  815 ldRRCALINAYGPTEA--TIS-SHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPR--GVCGELALGGIGLAEGYR 889
Cdd:PRK06187   305 --FGIDLVQGYGMTETspVVSvLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYW 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  890 GDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG- 968
Cdd:PRK06187   383 NRPEATAETID-----GG----WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA--VIGv 451
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773  969 --EGAAQRLVAWVECAGEDGFGQADLnqtdsdqtesERWhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06187   452 pdEKWGERPVAVVVLKPGATLDAKEL----------RAF---LRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
537-1041 1.09e-19

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: 96.04  E-value: 1.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  537 VVDAIARAADEFPERAALETAQG--RLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIP 614
Cdd:cd05923      3 VFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  615 LDtewPQARRAEVVA----ASGCDAVLT-DAQGLAGFAPSVAIAVDELKLDGAGENGSGENA------APNQLAYILYTS 683
Cdd:cd05923     83 IN---PRLKAAELAElierGEMTAAVIAvDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLiedpprEPEQPAFVFYTS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  684 GSTGIPKGVEVGHAALAAHIDAAAEALALSADD--RVL------HVAG--------LAVDTTLeqilaawsrgaCVVarp 747
Cdd:cd05923    160 GTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhnVVLglmplyHVIGffavlvaaLALDGTY-----------VVV--- 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  748 dELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRcalINAYGP 827
Cdd:cd05923    226 -EEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK---VNIYGT 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  828 TEATISSHYHRVQAIDASRPvplGQLLPGRIAAVLDAHGRIVPRGVCGELALggiglaegyrgDAAASERRFAPLRLP-- 905
Cdd:cd05923    302 TEAMNSLYMRDARTGTEMRP---GFFSEVRIVRIGGSPDEALANGEEGELIV-----------AAAADAAFTGYLNQPea 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  906 SGESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVEca 982
Cdd:cd05923    368 TAKKLQdgWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTeVVVIGVADERWGQSVTACVV-- 445
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  983 gedgfgqadLNQTDSDQTESERWHRAlcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05923    446 ---------PREGTLSADELDQFCRA--SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
3544-3982 1.46e-19

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: 95.61  E-value: 1.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLcLPRGC-DLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG--VCL- 3619
Cdd:cd05932      6 EFTWGEVADKARRLAAALRALGLEPGSKIAL-ISKNCaEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSEskALFv 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3620 ------SVSQRALAVELPGTALCLDDP----FTRAQLDAVEPGELPEVPTEAP--AYLIYTSGSTGTPKGVVVTHRNVEr 3687
Cdd:cd05932     85 gklddwKAMAPGVPEGLISISLPPPSAancqYQWDDLIAQHPPLEERPTRFPEqlATLIYTSGTTGQPKGVMLTFGSFA- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3688 lFTAATQTGRFSFDEHD--VWSLFHSHAFDFAVWElwGAWLYGGRAVLVPEAVcrqpDAFLDLLAEYGVTVLNQTPSAFY 3765
Cdd:cd05932    164 -WAAQAGIEHIGTEENDrmLSYLPLAHVTERVFVE--GGSLYGGVLVAFAESL----DTFVEDVQRARPTLFFSVPRLWT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3766 ALQ---------------------SQAMRRE----LALNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHV 3820
Cdd:cd05932    237 KFQqgvqdkipqqklnlllkipvvNSLVKRKvlkgLGLDQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTENFAYS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3821 SFHRLSDEDlqspTSRIGSALPDLAVHVLDAagqpvplgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDL 3900
Cdd:cd05932    316 HLNYPGRDK----IGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADG---FLRTGDK 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3901 GRYRADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSdaAVTVEGQGEGAWLmayAVAADGAEPDPQSL---RE 3976
Cdd:cd05932    379 GELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVE--MVCVIGSGLPAPL---ALVVLSEEARLRADafaRA 453

                   ....*.
gi 1246793773 3977 ALRALL 3982
Cdd:cd05932    454 ELEASL 459
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
588-1040 2.72e-19

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: 95.38  E-value: 2.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPL--DTEWPQARRAEVVAA-SGCDAVLTDAQGLAGFAPSVA---------IAVD 655
Cdd:cd05931     51 VLLLAPPGLDFVAAFLGCLYAGAIAVPLppPTPGRHAERLAAILAdAGPRVVLTTAAALAAVRAFAAsrpaagtprLLVV 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  656 ELKLDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------H----VAGLa 725
Cdd:cd05931    131 DLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlplyHdmglIGGL- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  726 vdttleqILAAWSRGACVVARP-DELLEPQRFLAFLSERAITVTdLAPAYANEL-VRASVADDWRDLAL---RCLVVGGD 800
Cdd:cd05931    210 -------LTPLYSGGPSVLMSPaAFLRRPLRWLRLISRYRATIS-AAPNFAYDLcVRRVRDEDLEGLDLsswRVALNGAE 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  801 vlPV------ALAQRWFELGLDRRcALINAYGPTEATI------------------SSHYHRVQAIDASRP-----VPLG 851
Cdd:cd05931    282 --PVrpatlrRFAEAFAPFGFRPE-AFRPSYGLAEATLfvsggppgtgpvvlrvdrDALAGRAVAVAADDPaarelVSCG 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  852 QLLPG-RIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLdDGELQFL 930
Cdd:cd05931    359 RPLPDqEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG--GWLRTGDLGFLH-DGELYIT 435
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  931 GRADFQVKLRGYRIELEEIEHCLGQLPQVR---AAAAGVVGEGAAQRLVAWVECAGedGFGQADLnqtdsdqteserwhR 1007
Cdd:cd05931    436 GRLKDLIIVRGRNHYPQDIEATAEEAHPALrpgCVAAFSVPDDGEERLVVVAEVER--GADPADL--------------A 499
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 1008 ALCERLPAY------MVPTQFVALPR--LPRNASGKIDRRA 1040
Cdd:cd05931    500 AIAAAIRAAvarehgVAPADVVLVRPgsIPRTSSGKIQRRA 540
prpE PRK10524
propionyl-CoA synthetase; Provisional
3520-4010 2.72e-19

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 95.79  E-value: 2.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDGE---LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAY 3596
Cdd:PRK10524    57 NAVDRHLAKRPEQLALIAVSTETDEertYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIH 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3597 VPV----DPHAPAARrgfiLEDSGVCLSVSQRA-------------------LAVELPGTALCLD---DPFT-------- 3642
Cdd:PRK10524   137 SVVfggfASHSLAAR----IDDAKPVLIVSADAgsrggkvvpykplldeaiaLAQHKPRHVLLVDrglAPMArvagrdvd 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3643 ----RAQ-LDAVEPGELpeVPTEAPAYLIYTSGSTGTPKGV--------VVTHRNVERLFTAatQTGRFSFDEHDV-WSL 3708
Cdd:PRK10524   213 yatlRAQhLGARVPVEW--LESNEPSYILYTSGTTGKPKGVqrdtggyaVALATSMDTIFGG--KAGETFFCASDIgWVV 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3709 FHShafdFAVWelwgAWLYGGRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALQSQ---AMRRELALNVRAV 3783
Cdd:PRK10524   289 GHS----YIVY----APLLAGMATIMYEGLPTRPDAgiWWRIVEKYKVNRMFSAPTAIRVLKKQdpaLLRKHDLSSLRAL 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEAL-EPSrlQPWRERYPQAELVNMYGITETTVHV-SFHRlsdeDLQSPTSRIGSalPDLAVH-----VLD-AAGQP 3855
Cdd:PRK10524   361 FLAGEPLdEPT--ASWISEALGVPVIDNYWQTETGWPIlAIAR----GVEDRPTRLGS--PGVPMYgynvkLLNeVTGEP 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3856 VPLGVVGELVVEG---DGVAQGYWQrpelTAERFV----ERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEP 3928
Cdd:PRK10524   433 CGPNEKGVLVIEGplpPGCMQTVWG----DDDRFVktywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGT 508
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3929 GEIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALL---PDYML-----PRLIQLLPALPL 3999
Cdd:PRK10524   509 REIEESISSHPAVAEVAVVgVKDALKGQVAVAFVVPKDSDSLADREARLALEKEImalVDSQLgavarPARVWFVSALPK 588
                          570
                   ....*....|.
gi 1246793773 4000 TANGKLDRKAL 4010
Cdd:PRK10524   589 TRSGKLLRRAI 599
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
115-506 3.01e-19

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: 93.40  E-value: 3.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  115 LFELRGELDAAALERAVHGLLIRHEVLdRCiqgeDSVAAGGGAA------------VESADLrgrgQDEIDalvegfrlR 182
Cdd:cd19537     29 ACRLSGDVDRDRLASAWNTVLARHRIL-RS----RYVPRDGGLRrsyssspprvqrVDTLDV----WKEIN--------R 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  183 PFELQRQRPLRM-----QLLrldgqgdgpvrhwlqVVVHHIACDGVSLGLLTQDLSRAYRvecglaAEPAPPLPCQYGDY 257
Cdd:cd19537     92 PFDLEREDPIRVfispdTLL---------------VVMSHIICDLTTLQLLLREVSAAYN------GKLLPPVRREYLDS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  258 ARWQRdtldRLDASLRHH-VEALSGAPHLHelplDHERPAVLGQSGAKLRLAFPPGLSERVAAYAQASRATaFHVLQAAF 336
Cdd:cd19537    151 TAWSR----PASPEDLDFwSEYLSGLPLLN----LPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGIT-LHQLALAA 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  337 AALLARCGAG-DDLLIGTPVAGRVRPELDSLVGLFVNTVVLRTQL--HDDPDFASLVARCRDHQLAALEHqALPLERVIE 413
Cdd:cd19537    222 VALALQDLSDrTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFpsSSDASAADFLRAVRRSSQAALAH-AIPWHQLLE 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  414 TLQVERSSRHAPLFQLM--FALRHDADLALDLHGVQAHaLTLPEDvAKHELTLE-VLVGAGGMSAVWEYNTALWNPATVA 490
Cdd:cd19537    301 HLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPL-YTWAEG-AKFPLMFEfTALSDDSLLLRLEYDTDCFSEEEID 378
                          410
                   ....*....|....*.
gi 1246793773  491 RWAERYFVALAAMLEN 506
Cdd:cd19537    379 RIESLILAALELLVEG 394
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3082-3384 3.44e-19

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: 93.86  E-value: 3.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3082 PLAPLQEglLFHSLLNAEADPYiNQT-TVALHGALDREAFAAAWQQALERHPILRSGFA------VQGLPSPRQLPHRqv 3154
Cdd:cd19534      3 PLTPIQR--WFFEQNLAGRHHF-NQSvLLRVPQGLDPDALRQALRALVEHHDALRMRFRredggwQQRIRGDVEELFR-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3155 slpLAEQDWSGLEPAQARsrlsELQAQQCEAGFDLAAPPLMRLALLRRSADEHWLVWTRHHLIVDGWSSALLLDEVWRLY 3234
Cdd:cd19534     78 ---LEVVDLSSLAQAAAI----EALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAY 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3235 AALRESRTPQLPAAPPFRDylhWLRGQDEAAA-------RAFWREQLTGlEPAALPEATEPAEGyASSTRRFDLAAAsaw 3307
Cdd:cd19534    151 EQALAGEPIPLPSKTSFQT---WAELLAEYAQspalleeLAYWRELPAA-DYWGLPKDPEQTYG-DARTVSFTLDEE--- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3308 aqshglTASSLLQG---------------ALALVLQRYYGRDDFALGITIAGRPPELAGVE--RMLGVFINSVPLRVTPA 3370
Cdd:cd19534    223 ------ETEALLQEanaayrteindlllaALALAFQDWTGRAPPAIFLEGHGREEIDPGLDlsRTVGWFTSMYPVVLDLE 296
                          330
                   ....*....|....
gi 1246793773 3371 GEATpapWLQALQQ 3384
Cdd:cd19534    297 ASED---LGDTLKR 307
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
588-1041 4.13e-19

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: 94.45  E-value: 4.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWP--------QARRAEVVAASgcDAVLTDAQGLAGFAPSVAIA--VDEL 657
Cdd:cd05928     70 VAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTakdilyrlQASKAKCIVTS--DELAPEVDSVASECPSLKTKllVSEK 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  658 KLDGAG----------------ENGSGENAApnqlayILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRV--- 718
Cdd:cd05928    148 SRDGWLnfkellneastehhcvETGSQEPMA------IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDImwn 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  719 LHVAGLAVdTTLEQILAAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADdWRDLALR-CLVV 797
Cdd:cd05928    222 TSDTGWIK-SAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS-YKFPSLQhCVTG 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  798 GGDVLPVALAQRWFELGLDrrcaLINAYGPTEATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGEL 877
Cdd:cd05928    300 GEPLNPEVLEKWKAQTGLD----IYEGYGQTETGLICANFKGMKI---KPGSMGKASPPYDVQIIDDNGNVLPPGTEGDI 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  878 AL-----GGIGLAEGYRGD---AAASERRfaplrlpsgeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEI 949
Cdd:cd05928    373 GIrvkpiRPFGLFSGYVDNpekTAATIRG------------DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEV 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  950 EHCLGQLPQVraAAAGVVGEGAAQR---LVAWVECAgedgfgqADLNQTDSDQTESERWHRALCERLPaYMVPTQFVALP 1026
Cdd:cd05928    441 ESALIEHPAV--VESAVVSSPDPIRgevVKAFVVLA-------PQFLSHDPEQLTKELQQHVKSVTAP-YKYPRKVEFVQ 510
                          490
                   ....*....|....*
gi 1246793773 1027 RLPRNASGKIDRRAL 1041
Cdd:cd05928    511 ELPKTVTGKIQRNEL 525
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
588-1041 4.79e-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: 93.31  E-value: 4.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCdavltdaqglagfapSVAIAVDELkldgagengs 667
Cdd:cd05935     29 VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA---------------KVAVVGSEL---------- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 genaapNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLavdttLEQILAAWSRGA 741
Cdd:cd05935     84 ------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILaclplfHVTGF-----VGSLNTAVYVGG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  742 CVV--ARPDELLEPQRFlaflSERAITVTDLAPAYANELVrASVADDWRDLA-LRCLVVGGDVLPVALAQRWFEL-GLDr 817
Cdd:cd05935    153 TYVlmARWDRETALELI----EKYKVTFWTNIPTMLVDLL-ATPEFKTRDLSsLKVLTGGGAPMPPAVAEKLLKLtGLR- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  818 rcaLINAYGPTEATISSHYHRVQAIDASrpvPLGQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASE 896
Cdd:cd05935    227 ---FVEGYGLTETMSQTHTNPPLRPKLQ---CLGIP*FGVDARVIDIEtGRELPPNEVGEIVVRGPQIFKGYWNRPEETE 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  897 RRFAPLrlpSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRL 975
Cdd:cd05935    301 ESFIEI---KGR--RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*eVCVISVPDERVGEEV 375
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  976 VAWV----ECAGEdgfgqadlnqtdSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05935    376 KAFIvlrpEYRGK------------VTEEDIIEWAR---EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK06145 PRK06145
acyl-CoA synthetase; Validated
536-1041 5.07e-19

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 93.80  E-value: 5.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  536 NVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPL 615
Cdd:PRK06145     3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  616 DTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAV-------DELKLDGAGENGSGENA-APNQLAYILYTSGSTG 687
Cdd:PRK06145    83 NYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVidaaaqaDSRRLAQGGLEIPPQAAvAPTDLVRLMYTSGTTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  688 IPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGL----AVDttLEQILAAWSRGACVVARPdelLEPQRFLAFLSER 763
Cdd:PRK06145   163 RPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFD--LPGIAVLWVGGTLRIHRE---FDPEAVLAAIERH 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  764 AITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPvalAQRWFELG-LDRRCALINAYGPTEaTISSHYHRVQAI 842
Cdd:PRK06145   238 RLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTP---ESRIRDFTrVFTRARYIDAYGLTE-TCSGDTLMEAGR 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  843 DASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLL 922
Cdd:PRK06145   314 EIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG---------DWFRSGDVGYLD 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  923 DDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVEcagedgfgqadLNQTDSDQTE 1001
Cdd:PRK06145   385 EEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAViGVHDDRWGERITAVVV-----------LNPGATLTLE 453
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 1002 SERWHralCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06145   454 ALDRH---CRqRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
588-1036 7.11e-19

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: 92.83  E-value: 7.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLdteWPQARRAEVVAasgcdaVLTDAQGLAGFAPSVAIAVDELkldgagengs 667
Cdd:cd05903     29 VAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHELAF------ILRRAKAKVFVVPERFRQFDPA---------- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 genAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDT-TLEQILAAWSRGACVVAr 746
Cdd:cd05903     90 ---AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  747 pDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRRCAlinAYG 826
Cdd:cd05903    166 -QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS---AYG 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  827 PTEatissHYHRVQAIDASRP----VPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGY--RGDAAASErrfa 900
Cdd:cd05903    242 STE-----CPGAVTSITPAPEdrrlYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYldRPDLTADA---- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  901 plrLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVA 977
Cdd:cd05903    313 ---APEG----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAA--VVAlpdERLGERACA 383
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  978 WVECAGEDGFGQADLNQTDSDQteserwhralceRLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:cd05903    384 VVVTKSGALLTFDELVAYLDRQ------------GVAKQYWPERLVHVDDLPRTPSGKV 430
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1627-1934 8.40e-19

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: 92.52  E-value: 8.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1627 ELDGEIDAAALAQAWQQTVRRQPMLRTAIVW-EGLSVPHQIVLADAAAPWQTLDWSALDDAAQdaqlqrwLADDAAQGV- 1704
Cdd:cd19532     31 RLTGPLDVARLERAVRAVGQRHEALRTCFFTdPEDGEPMQGVLASSPLRLEHVQISDEAEVEE-------EFERLKNHVy 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1705 DFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYtagaQGATLrlpPAPGFQaYLDWRERQDLARQR 1784
Cdd:cd19532    104 DLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY----NGQPL---LPPPLQ-YLDFAARQRQDYES 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1785 G-------WWRERLSG---------YAGTAALPAPVAAAHHpvqreECERRLSAHDSERLRAFCRERGCT-----LSDLI 1843
Cdd:cd19532    176 GaldedlaYWKSEFSTlpeplpllpFAKVKSRPPLTRYDTH-----TAERRLDAALAARIKEASRKLRVTpfhfyLAALQ 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1844 AMVwglanARYGNHDDVVLGATRSGRPPElaGVESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLGE 1923
Cdd:cd19532    251 VLL-----ARLLDVDDICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVPFDV 323
                          330
                   ....*....|.
gi 1246793773 1924 ILADsgLDADR 1934
Cdd:cd19532    324 LLDE--LGVPR 332
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
3498-3947 8.60e-19

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: 93.36  E-value: 8.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3498 PLLPSQTRSAAwtSRERYActgnlVSRFAEIarryPARIA-VSAEDG-ELDYATLDRRSSQLATLLIRQGAGPGQRVGLC 3575
Cdd:cd17642      7 PFYPLEDGTAG--EQLHKA-----MKRYASV----PGTIAfTDAHTGvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVC 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3576 LPRGCDLLVALLAILKTGAAYVPVDP--------HAPAARRGFILEDSGVCLsvsQRALAVE--LP--GTALCLD----- 3638
Cdd:cd17642     76 SENSLQFFLPVIAGLFIGVGVAPTNDiynereldHSLNISKPTIVFCSKKGL---QKVLNVQkkLKiiKTIIILDskedy 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3639 ------DPFTRAQLDAVEPGELPEVPT----EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQT--GRFSFDEHDVW 3706
Cdd:cd17642    153 kgyqclYTFITQNLPPGFNEYDFKPPSfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPifGNQIIPDTAIL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3707 SL--FHsHAFdfAVWELWGAWLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAV 3783
Cdd:cd17642    233 TVipFH-HGF--GMFTTLGYLICGFRVVLMYKF---EEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLsNLHEI 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSfhrLSDEDLQSPTSrIGSALPDLAVHVLDA-AGQPVPLGVVG 3862
Cdd:cd17642    307 ASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAIL---ITPEGDDKPGA-VGKVVPFFYAKVVDLdTGKTLGPNERG 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVS 3942
Cdd:cd17642    383 ELCVKGPMIMKGYVNNPEATKALIDKDG---WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459

                   ....*
gi 1246793773 3943 DAAVT 3947
Cdd:cd17642    460 DAGVA 464
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
678-1039 9.31e-19

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: 91.29  E-value: 9.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  678 YILYTSGSTGIPKGVEVGHA--ALAAHIDAAAEALALSADDRVLHVAGLAVDTTL---------EQILAAWS--RGACVV 744
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEdiFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMfpapplmhgTGSWTAFGglLGGQTV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  745 ARPDELLEPQRFLAFLS-ERAITVTDLAPAYANELVRASVADDWRDL-ALRCLVVGGDVLPVALAQRWFELGLDRrcALI 822
Cdd:cd05924     87 VLPDDRFDPEEVWRTIEkHKVTSMTIVGDAMARPLIDALRDAGPYDLsSLFAISSGGALLSPEVKQGLLELVPNI--TLV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  823 NAYGPTEATISSHYHRVQAIDASRPvplgQLLPGRIAAVLDAHGRIVP--RGVCGELALGGIgLAEGYRGDAAASERRFa 900
Cdd:cd05924    165 DAFGSSETGFTGSGHSAGSGPETGP----FTRANPDTVVLDDDGRVVPpgSGGVGWIARRGH-IPLGYYGDEAKTAETF- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  901 plrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWV 979
Cdd:cd05924    239 ----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYdVLVVGRPDERWGQEVVAVV 314
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  980 ecAGEDGFGqADLNQTDsdqteserwhRALCERLPAYMVPTQFVALPRLPRNASGKIDRR 1039
Cdd:cd05924    315 --QLREGAG-VDLEELR----------EHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
588-1051 9.79e-19

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 94.33  E-value: 9.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGA-GENG 666
Cdd:PRK06060    58 VLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAArVAPG 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  667 SGENAAPNQLAYILYTSGSTGIPKGVEVGHA-------ALAAHIDAAAEALALSADDRVLHVAGLA------VDTTLEQI 733
Cdd:PRK06060   138 GYEPMGGDALAYATYTSGTTGPPKAAIHRHAdpltfvdAMCRKALRLTPEDTGLCSARMYFAYGLGnsvwfpLATGGSAV 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  734 LAAWSRGACVVARPDELLEPqrflaflseraiTVTDLAPAYANELVRASVADDWRdlALRCLVVGGDVLPVALAQRWFEL 813
Cdd:PRK06060   218 INSAPVTPEAAAILSARFGP------------SVLYGVPNFFARVIDSCSPDSFR--SLRCVVSAGEALELGLAERLMEF 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  814 --GLdrrcALINAYGPTEA--TISSHyhrvqAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYR 889
Cdd:PRK06060   284 fgGI----PILDGIGSTEVgqTFVSN-----RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYW 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  890 GdaaaserRFAPLrLPSGESLRmyrSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVG 968
Cdd:PRK06060   355 N-------RPDSP-VANEGWLD---TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVaEAAVVAVRE 423
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  969 EGAAQRLVAWVECAGEDGFgqadlnqtdsDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL----PAP 1044
Cdd:PRK06060   424 STGASTLQAFLVATSGATI----------DGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsPTK 493

                   ....*....
gi 1246793773 1045 PV--LAQAE 1051
Cdd:PRK06060   494 PIweLSLTE 502
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
3524-4084 1.02e-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: 94.38  E-value: 1.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHA 3603
Cdd:COG3319     10 AAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3604 PAARRGFILEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHR 3683
Cdd:COG3319     90 AAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 NVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSA 3763
Cdd:COG3319    170 ALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3764 FYALQSQAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSPTSRIGSALPD 3843
Cdd:COG3319    250 LLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLV 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRG 3923
Cdd:COG3319    330 LLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRG 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3924 YRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANG 4003
Cdd:COG3319    410 LREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLA 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 4004 KLDRKALPKPE-TQDRDEGVLESASERRLAELWRQLLGGELPGRGAHFFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFE 4082
Cdd:COG3319    490 ALLLAAAAPAAaAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLL 569

                   ..
gi 1246793773 4083 QP 4084
Cdd:COG3319    570 AP 571
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
3547-4022 2.08e-18

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: 91.72  E-value: 2.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAyvpvdphaPAArrgfiledsgvclsvsqra 3625
Cdd:cd05937      8 YSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PAF------------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3626 LAVELPGTAL--CLDdpFTRAQLDAVEPgelpevptEAPAYLIYTSGSTGTPKGVVVTHRnveRLFTAATQTGR-FSFDE 3702
Cdd:cd05937     61 INYNLSGDPLihCLK--LSGSRFVIVDP--------DDPAILIYTSGTTGLPKAAAISWR---RTLVTSNLLSHdLNLKN 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3703 HDVW----SLFHSHAFDFAVWELWGAwlyGGRAVLVPEAVCRQpdaFLDLLAEYGVTVLNQTPSAF-YALQSQAMRRELA 3777
Cdd:cd05937    128 GDRTytcmPLYHGTAAFLGACNCLMS---GGTLALSRKFSASQ---FWKDVRDSGATIIQYVGELCrYLLSTPPSPYDRD 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LNVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITE-------------TTVHVSFH----RLSDEDLQSPtsrigsa 3840
Cdd:cd05937    202 HKVRVAW--GNGLRPDIWERFRERFNVPEIGEFYAATEgvfaltnhnvgdfGAGAIGHHglirRWKFENQVVL------- 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 lpdlaVHVLDAAGQP-----------VPLGVVGELVV----EGDGVAQGYWQRPELTAERFVE---RGGQRFYRSGDLGR 3902
Cdd:cd05937    273 -----VKMDPETDDPirdpktgfcvrAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRdvfRKGDIYFRTGDLLR 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3903 YRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA---AVTV---EGQGEGAWLMAYAVAADGAEPDPQSLRE 3976
Cdd:cd05937    348 QDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvyGVKVpghDGRAGCAAITLEESSAVPTEFTKSLLAS 427
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773 3977 ALRALLPDYMLPRLIQLLPALPLTANGKLDRKALpkpetqdRDEGV 4022
Cdd:cd05937    428 LARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL-------RDEGV 466
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2176-2524 2.43e-18

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: 91.37  E-value: 2.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL-GEDASLATLSTVA---ADLGFTALFGALLSGRRVRLLPA 2251
Cdd:cd05910     84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIrPGEVDLATFPLFAlfgPALGLTSVIPDMDPTRPARADPQ 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 ELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAaggtavLPR-ECLVTGGEALTGALVQQVR-ALAPTLRIVNHYGPTE 2329
Cdd:cd05910    164 KLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT------LPSlRRVLSAGAPVPIALAARLRkMLSDEAEILTPYGATE 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2330 ----TTVG---ILTCTVPeewPVEQ--GVPVGHPLAGNEAWVL--DRFGLPA-------PVGVAGELYLGGGNLSLGYWQ 2391
Cdd:cd05910    238 alpvSSIGsreLLATTTA---ATSGgaGTCVGRPIPGVRVRIIeiDDEPIAEwddtlelPRGEIGEITVTGPTVTPTYVN 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2392 RAEQTAerFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLAL--PGA 2469
Cdd:cd05910    315 RPVATA--LAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGC 392
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2470 N---GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRL-----GNGKIDRQALAD 2524
Cdd:cd05910    393 QlpvLCVEPLPGTITPRARLEQELRALAKDYPHTQRIGRFLIHPSFpvdirHNAKIFREKLAV 455
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2630-2859 3.23e-18

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 87.02  E-value: 3.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQHWFFEqALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAaGQWQQTL---GDWQADRFAHR 2706
Cdd:COG4908      1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIdpdADLPLEVVDLS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2707 EADAGQREDLLAQWQAGL---SFD---GALLRVLALPDPQDGDtRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSP 2780
Cdd:COG4908     79 ALPEPEREAELEELVAEEasrPFDlarGPLLRAALIRLGEDEH-VLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2781 ALAAEACGFGAWQAALRQ-LSAATLDGWRSYWRAQ-AADAEAIALPW--QDSDNRYADTVHLHDRFERDWTERLLtQTAR 2856
Cdd:COG4908    158 PLPELPIQYADYAAWQRAwLQSEALEKQLEYWRQQlAGAPPVLELPTdrPRPAVQTFRGATLSFTLPAELTEALK-ALAK 236

                   ...
gi 1246793773 2857 AYG 2859
Cdd:COG4908    237 AHG 239
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
2049-2431 4.04e-18

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 91.70  E-value: 4.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLP-R---TFAQLAAMAAvwhrGAAWLPLDPQHPdAR 2124
Cdd:COG1022     28 VALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDnRpewVIADLAILAA----GAVTVPIYPTSS-AE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2125 QIA-VLDDSGARIVI------------GWGAAPA----WV------PASVRWLDAESVLDVVSAYEEPPRVD-----VDA 2176
Cdd:COG1022    103 EVAyILNDSGAKVLFvedqeqldklleVRDELPSlrhiVVldprglRDDPRLLSLDELLALGREVADPAELEarraaVKP 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2177 DTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASlaTLS------------------------------T 2226
Cdd:COG1022    183 DDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR--TLSflplahvfertvsyyalaagatvafaespdT 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2227 VAADLG------FTA---LFGALLSG--RRVRLLPA------ELAFDAQALAAHLQAHPVDclkivPSHLAGLLAAAGGT 2289
Cdd:COG1022    261 LAEDLRevkptfMLAvprVWEKVYAGiqAKAEEAGGlkrklfRWALAVGRRYARARLAGKS-----PSLLLRLKHALADK 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 AVLPR---------ECLVTGGEALTGALVQQVRALAptLRIVNHYGPTETTvGILTCTVPEEwpVEQGVpVGHPLAGNEa 2360
Cdd:COG1022    336 LVFSKlrealggrlRFAVSGGAALGPELARFFRALG--IPVLEGYGLTETS-PVITVNRPGD--NRIGT-VGPPLPGVE- 408
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2361 wvldrfglpapVGVA--GELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGR 2431
Cdd:COG1022    409 -----------VKIAedGEILVRGPNVMKGYYKNPEATAEAFDA-----DGWL-HTGDIGELDEDGFLRITGR 464
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
2047-2528 4.14e-18

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 90.70  E-value: 4.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALC----LPRTFAQLAAMAAvwhrGAAWLPLDPQHPD 2122
Cdd:PRK09029    14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRgknsPETLLAYLALLQC----GARVLPLNPQLPQ 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIvigwgaapAWVPASVRWLDAESVLdVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVS-QGN 2201
Cdd:PRK09029    90 PLLEELLPSLTLDF--------ALVLEGENTFSALTSL-HLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTaQAH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2202 LANyVAGVLPVLDLGEDAS-LATLstvaadlgftALFGA---------LLSGRRVrLLPAELAFDaqalaahlqahpvDC 2271
Cdd:PRK09029   161 LAS-AEGVLSLMPFTAQDSwLLSL----------PLFHVsgqgivwrwLYAGATL-VVRDKQPLE-------------QA 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2272 LKIVpSHL-----------AGLLAAAGGTAVLpreclvTGGEALTGALVQQVRALAptLRIVNHYGPTE--TTVgiltCT 2338
Cdd:PRK09029   216 LAGC-THAslvptqlwrllDNRSEPLSLKAVL------LGGAAIPVELTEQAEQQG--IRCWCGYGLTEmaSTV----CA 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEEwpveqGVP-VGHPLAGNEAWVldrfglpapvgVAGELYLGGGNLSLGYWQRAEQTaerfvahPLAPDRLLYRSGDL 2417
Cdd:PRK09029   283 KRAD-----GLAgVGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDR 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2418 ARLDGeGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN------GVLQLGAciQGSLEGVAEALA 2491
Cdd:PRK09029   340 GEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfgqrpvAVVESDS--EAAVVNLAEWLQ 416
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1246793773 2492 QRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK09029   417 DKLARFQQPVAYYLLPPELKNGGIKISRQALKEWVAQ 453
PLN02479 PLN02479
acetate-CoA ligase
3532-4010 1.04e-17

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 90.29  E-value: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3532 YPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFI 3611
Cdd:PLN02479    33 HPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFL 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3612 LEDSGVCL--------SVSQRAL---------AVELP-----GTALCLDDPFTRA-QLDAVEPGEL-----PEVPTEAPA 3663
Cdd:PLN02479   113 LEHSKSEVvmvdqeffTLAEEALkilaekkksSFKPPlliviGDPTCDPKSLQYAlGKGAIEYEKFletgdPEFAWKPPA 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3664 ------YLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDV--WSL--FHSHAFDFAvWELwgawlyggrAVL 3733
Cdd:PLN02479   193 dewqsiALGYTSGTTASPKGVVLHHRGA--YLMALSNALIWGMNEGAVylWTLpmFHCNGWCFT-WTL---------AAL 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPEAVC-RQ--PDAFLDLLAEYGVTVLNQTPSAFYALQSqAMRRELAL---NVRAVVFGGEALEPSRLQPWRERypQAEL 3807
Cdd:PLN02479   261 CGTNIClRQvtAKAIYSAIANYGVTHFCAAPVVLNTIVN-APKSETILplpRVVHVMTAGAAPPPSVLFAMSEK--GFRV 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3808 VNMYGITET----TV---HVSFHRLSDEDLQSPTSRIG---SALPDLAVhVLDAAGQPVPL--GVVGELVVEGDGVAQGY 3875
Cdd:PLN02479   338 THTYGLSETygpsTVcawKPEWDSLPPEEQARLNARQGvryIGLEGLDV-VDTKTMKPVPAdgKTMGEIVMRGNMVMKGY 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3876 WQRPELTAERFveRGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTV---EGQG 3952
Cdd:PLN02479   417 LKNPKANEEAF--ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVArpdERWG 492
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 3953 EGAwlMAYAVAADGAE-PDPQSLREAL----RALLPDYMLPRLIQLLPaLPLTANGKLDRKAL 4010
Cdd:PLN02479   493 ESP--CAFVTLKPGVDkSDEAALAEDImkfcRERLPAYWVPKSVVFGP-LPKTATGKIQKHVL 552
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
2050-2522 1.13e-17

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: 89.69  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:cd05920     29 PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFC 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVIGWGaapawvpasvRWLDAESVLDVVSAYEEPPrvdvdadTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05920    109 AHAEAVAYIVPD----------RHAGFDHRALARELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRAS 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLDLGEDASLATLSTVAADLGFTA--LFGALLSGRRVRLLP---AELAFDAQALAAhlqahpVDCLKIVPSHLAG--L 2282
Cdd:cd05920    172 AEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLAPdpsPDAAFPLIEREG------VTVTALVPALVSLwlD 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2283 LAAAGGTAVLPRECLVTGGEALTGALVQQVRA-LAPTLRIVnhYGPTEttvGILTCTV---PEEWPVE-QGVPVGhplAG 2357
Cdd:cd05920    246 AAASRRADLSSLRLLQVGGARLSPALARRVPPvLGCTLQQV--FGMAE---GLLNYTRlddPDEVIIHtQGRPMS---PD 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2358 NEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLlYRSGDLARLDGEGRIVYLGRGDHQVK 2437
Cdd:cd05920    318 DEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF-----TPDGF-YRTGDLVRRTPDGYLVVEGRIKDQIN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2438 IRGYRVELGEVEQVLAQLPGVEVAAVLALPgaNGVLQLGACI-------QGSLEGVAEALAQR-LPEYLCPSRWRAVESM 2509
Cdd:cd05920    392 RGGEKIAAEEVENLLLRHPAVHDAAVVAMP--DELLGERSCAfvvlrdpPPSAAQLRRFLRERgLAAYKLPDRIEFVDSL 469
                          490
                   ....*....|...
gi 1246793773 2510 PRLGNGKIDRQAL 2522
Cdd:cd05920    470 PLTAVGKIDKKAL 482
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
2179-2519 1.18e-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: 87.46  E-value: 1.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2179 PAYLIYTSGSTGTPKGVVVSQGN-LANYVAGVLPVLDLGEDAsLATLSTVAADLGFTALFGALLSGRRVRLLPAelaFDA 2257
Cdd:cd17633      2 PFYIGFTSGTTGLPKAYYRSERSwIESFVCNEDLFNISGEDA-ILAPGPLSHSLFLYGAISALYLGGTFIGQRK---FNP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAHLQAHPVDCLKIVPShlAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTvgILTC 2337
Cdd:cd17633     78 KSWIRKINQYNATVIYLVPT--MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELS--FITY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2338 TVPEE-WPVEQgvpVGHPLAGNEAWVLDRFGlpapvGVAGELYLGGGNLSLGYWQRAEQTAERFvahplapdrllYRSGD 2416
Cdd:cd17633    154 NFNQEsRPPNS---VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGD 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2417 LARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQG---SLEGVAEALAQR 2493
Cdd:cd17633    215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGdklTYKQLKRFLKQK 294
                          330       340
                   ....*....|....*....|....*.
gi 1246793773 2494 LPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17633    295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
3529-3982 1.35e-17

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: 89.80  E-value: 1.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGE-----LDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP-- 3601
Cdd:cd05921      5 ARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPay 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3602 ------HAPAARRGFILEDSGVCLSVS---QRAL-AVELPGTALCL-------DDPFTRAQLDAVEPGE-----LPEVPT 3659
Cdd:cd05921     85 slmsqdLAKLKHLFELLKPGLVFAQDAapfARALaAIFPLGTPLVVsrnavagRGAISFAELAATPPTAavdaaFAAVGP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDV------WS--LFHSHAFDFAVWElwGAWLY--GG 3729
Cdd:cd05921    165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVlvdwlpWNhtFGGNHNFNLVLYN--GGTLYidDG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 RAVlvpeavcrqPDAF---LDLLAEYGVTVLNQTPSAFYALqSQAMRRELAL------NVRAVVFGGEALEPS---RLQP 3797
Cdd:cd05921    243 KPM---------PGGFeetLRNLREISPTVYFNVPAGWEML-VAALEKDEALrrrffkRLKLMFYAGAGLSQDvwdRLQA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3798 WR-----ERYPqaeLVNMYGITETTVHVSFhrlsdedLQSPTSR---IGSALPDLAVHVldaagqpVPLGVVGELVVEGD 3869
Cdd:cd05921    313 LAvatvgERIP---MMAGLGATETAPTATF-------THWPTERsglIGLPAPGTELKL-------VPSGGKYEVRVKGP 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3870 GVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYrADGS-----LEYRGRGDDQVKLRG---YRIEPGEIAAKIASLPQV 3941
Cdd:cd05921    376 NVTPGYWRQPELTAQAFDEEG---FYCLGDAAKL-ADPDdpakgLVFDGRVAEDFKLASgtwVSVGPLRARAVAACAPLV 451
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3942 SDAAVTVEGQGE-GA--WLMAYAVAA--DGAEPDP------QSLREALRALL 3982
Cdd:cd05921    452 HDAVVAGEDRAEvGAlvFPDLLACRRlvGLQEASDaevlrhAKVRAAFRDRL 503
PLN03102 PLN03102
acyl-activating enzyme; Provisional
3662-4023 1.37e-17

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 90.08  E-value: 1.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVERLFTAAT---QTGRFSFdehDVWSL--FHSHAFDFAvwelWGAWLYGGRAVLVPE 3736
Cdd:PLN03102   188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIigwEMGTCPV---YLWTLpmFHCNGWTFT----WGTAARGGTSVCMRH 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 AVCrqPDAFLDlLAEYGVTVLNQTPSAFYALQsQAMRRELALNVRAV-VFGGEALEPSRLQPWRERYpQAELVNMYGITE 3815
Cdd:PLN03102   261 VTA--PEIYKN-IEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSGPVhVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTE 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3816 TTVHVSFHRLSDEDLQSP-------TSRIGSALPDLA-VHVLDAAGQ---PVPLGVVGELVVEGDGVAQGYWQRPELTAE 3884
Cdd:PLN03102   336 ATGPVLFCEWQDEWNRLPenqqmelKARQGVSILGLAdVDVKNKETQesvPRDGKTMGEIVIKGSSIMKGYLKNPKATSE 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3885 RFvERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQ---GEGAwlMAYA 3961
Cdd:PLN03102   416 AF-KHG---WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHptwGETP--CAFV 489
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3962 VAADGAEPDPQ----------SLREALRALLPDYMLPRLIQLLPALPLTANGKldrkaLPKPETQDRDEGVL 4023
Cdd:PLN03102   490 VLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGK-----ILKPKLRDIAKGLV 556
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3529-3946 1.51e-17

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 88.78  E-value: 1.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3529 ARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARR 3608
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3609 GFILEDsgvclsvsqraLAVELpgtALCLDDPFTRAQLDAVEPGELPEVPT-----EAPAYLIYTSGSTGTPKGVVVTHR 3683
Cdd:PRK09029    93 EELLPS-----------LTLDF---ALVLEGENTFSALTSLHLQLVEGAHAvawqpQRLATMTLTSGSTGLPKAAVHTAQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3684 NveRLFTAATQTGRFSFDEHDVW----SLFH--SHAFdfaVWElwgaWLYGGrAVLvpeaVCRQPDAFLDLLAeyGVTVL 3757
Cdd:PRK09029   159 A--HLASAEGVLSLMPFTAQDSWllslPLFHvsGQGI---VWR----WLYAG-ATL----VVRDKQPLEQALA--GCTHA 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3758 NQTPSAFYALQSQamrRELALNVRAVVFGGEALEPSRLQpwrerypQAELVNM-----YGITE--TTVhvsFHRLSDEdl 3830
Cdd:PRK09029   223 SLVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVELTE-------QAEQQGIrcwcgYGLTEmaSTV---CAKRADG-- 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3831 qspTSRIGSALPdlavhvldaaGQPVPLgVVGELVVEGDGVAQGYWQRPELTAerFVERGGqrFYRSGDLGRYRaDGSLE 3910
Cdd:PRK09029   288 ---LAGVGSPLP----------GREVKL-VDGEIWLRGASLALGYWRQGQLVP--LVNDEG--WFATRDRGEWQ-NGELT 348
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1246793773 3911 YRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:PRK09029   349 ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFV 384
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
588-1041 1.63e-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: 1.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEW-PQARrAEVVAASGCDAVLTDAQGLAgfapsvaiavdelKLDgageng 666
Cdd:cd05973     28 VAGLLPRTPELVVTILGIWRLGAVYQPLFTAFgPKAI-EHRLRTSGARLVVTDAANRH-------------KLD------ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  667 sgenaapNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGlavdttleqilAAWSRGA-CVVA 745
Cdd:cd05973     88 -------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAAD-----------PGWAYGLyYAIT 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 RPDELLEPQRFLA--FLSE------RAITVTDLA--PAYANELVRASVADDWR-DLALRCLVVGGDVLPVALAqRWFE-- 812
Cdd:cd05973    150 GPLALGHPTILLEggFSVEstwrviERLGVTNLAgsPTAYRLLMAAGAEVPARpKGRLRRVSSAGEPLTPEVI-RWFDaa 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  813 LGLdrrcALINAYGPTE--ATISSHYHRVQAIDASrpvPLGQLLPGRIAAVLDAHGRIVPRGVCGELALggiglaegyrg 890
Cdd:cd05973    229 LGV----PIHDHYGQTElgMVLANHHALEHPVHAG---SAGRAMPGWRVAVLDDDGDELGPGEPGRLAI----------- 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  891 DAAASERRF------APLRLPSGeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAa 964
Cdd:cd05973    291 DIANSPLMWfrgyqlPDTPAIDG---GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAA- 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  965 gVVGEGAAQR---LVAWVE-CAGEDGfgqadlnqTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRA 1040
Cdd:cd05973    367 -VIGVPDPERtevVKAFVVlRGGHEG--------TPALADELQLHVK---KRLSAHAYPRTIHFVDELPKTPSGKIQRFL 434

                   .
gi 1246793773 1041 L 1041
Cdd:cd05973    435 L 435
PRK08308 PRK08308
acyl-CoA synthetase; Validated
3542-4015 2.11e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 88.17  E-value: 2.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAgPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAP--AARRgfiledsgvcl 3619
Cdd:PRK08308     6 DEEYSKSDFDLRLQRYEEMEQFQEA-AGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPkeAAIR----------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3620 svsqraLAVELPGTALCLDDP-FTRaqldavepGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRF 3698
Cdd:PRK08308    74 ------MAKRAGCHGLLYGESdFTK--------LEAVNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNE--AL 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3699 SFDEHDV----WSLFHSHAFDFAVwelwgawLYGGRAVLVPEAVCRQ-PDAFLDLLAEYGVTVLNQTPSAFYALQSQAMR 3773
Cdd:PRK08308   138 NCEQDETpivaCPVTHSYGLICGV-------LAALTRGSKPVIITNKnPKFALNILRNTPQHILYAVPLMLHILGRLLPG 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3774 RElalNVRAVVFGGEALEPSRLQPWRERYPQaeLVNMYGITETTVhVSFHrlsdEDLQSPTSrIGSALPDLAVHVLDAAG 3853
Cdd:PRK08308   211 TF---QFHAVMTSGTPLPEAWFYKLRERTTY--MMQQYGCSEAGC-VSIC----PDMKSHLD-LGNPLPHVSVSAGSDEN 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3854 QPvplgvvGELVVegdgvaqgywqrpeltaerfveRGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAA 3933
Cdd:PRK08308   280 AP------EEIVV----------------------KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVED 331
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3934 KIASLPQVSDaAVTVEGQ----GEgawLMAYAVAADGaEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKA 4009
Cdd:PRK08308   332 VMLRLPGVQE-AVVYRGKdpvaGE---RVKAKVISHE-EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKL 406

                   ....*.
gi 1246793773 4010 LPKPET 4015
Cdd:PRK08308   407 LELGEV 412
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3520-3903 2.15e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 89.72  E-value: 2.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3520 NLVSRFAEIARRYPARIAVSAEDG------ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTG 3593
Cdd:PRK12582    50 SIPHLLAKWAAEAPDRPWLAQREPghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3594 AAYVPVDP--------HAP------AARRGFILEDSGVCLSvsqRAL-AVELPG------TALCLDDPFTR-AQLDAVEP 3651
Cdd:PRK12582   130 VPAAPVSPayslmshdHAKlkhlfdLVKPRVVFAQSGAPFA---RALaALDLLDvtvvhvTGPGEGIASIAfADLAATPP 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3652 GELPEVPTEA-----PAYLIYTSGSTGTPKGVVVTHRnverLFTA--ATQTGRFSFDEHDV------WSLFH-----SHA 3713
Cdd:PRK12582   207 TAAVAAAIAAitpdtVAKYLFTSGSTGMPKAVINTQR----MMCAniAMQEQLRPREPDPPppvsldWMPWNhtmggNAN 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3714 FDFAVWELWGAWLYGGRAVlvpeavcrqPDAF---LDLLAEYGVTVLNQTPSAFYAL-----QSQAMRRELALNVRAVVF 3785
Cdd:PRK12582   283 FNGLLWGGGTLYIDDGKPL---------PGMFeetIRNLREISPTVYGNVPAGYAMLaeameKDDALRRSFFKNLRLMAY 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3786 GGEALEP---SRLQPW--RERYPQAELVNMYGITETT-VHVSFHRlsdedlqsPTSR---IGSALPDLAVHVldaagqpV 3856
Cdd:PRK12582   354 GGATLSDdlyERMQALavRTTGHRIPFYTGYGATETApTTTGTHW--------DTERvglIGLPLPGVELKL-------A 418
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1246793773 3857 PLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRY 3903
Cdd:PRK12582   419 PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEG---FYRLGDAARF 462
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2184-2519 2.79e-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: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 86.56  E-value: 2.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNLAN--YVAG-----------VLPV-------LDLGEDASLATLST-VAADLGF--------- 2233
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNngYFIGerlglteqdrlCIPVplfhcfgSVLGVLACLTHGATmVFPSPSFdplavleai 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2234 -----TALFG------ALLSgrrvrlLPAELAFDaqalaahlqahpVDCLKivpshlagllaaaggTAVLpreclvtGGE 2302
Cdd:cd05917     89 ekekcTALHGvptmfiAELE------HPDFDKFD------------LSSLR---------------TGIM-------AGA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2303 ALTGALVQQVRALAPTLRIVNHYGPTETTVGIlTCTVPEEwPVEQGV-PVGHPLAGNEAWVLDRFGLP-APVGVAGELYL 2380
Cdd:cd05917    129 PCPPELMKRVIEVMNMKDVTIAYGMTETSPVS-TQTRTDD-SIEKRVnTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCI 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAEQTAErfvahPLAPDRlLYRSGDLARLDGEGRIVYLGRgdhqVK---IRGyrvelG------EVEQV 2451
Cdd:cd05917    207 RGYSVMKGYWNDPEKTAE-----AIDGDG-WLHTGDLAVMDEDGYCRIVGR----IKdmiIRG-----GeniyprEIEEF 271
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2452 LAQLPGVEVAAVLALPGANGVLQLGACIQG------SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd05917    272 LHTHPKVSDVQVVGVPDERYGEEVCAWIRLkegaelTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
2078-2524 2.85e-17

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 88.60  E-value: 2.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIA-VLDDSGARIVIGW-----GAAPAwVPASV 2151
Cdd:PRK12406    28 LAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVN-WHFKPEEIAyILEDSGARVLIAHadllhGLASA-LPAGV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2152 RWLDAESVLDVVSAYE------EPPRVDVDADT---------------PAYLIYTSGSTGTPKGV-----VVSQGNLANY 2205
Cdd:PRK12406   106 TVLSVPTPPEIAAAYRispallTPPAGAIDWEGwlaqqepydgppvpqPQSMIYTSGTTGHPKGVrraapTPEQAAAAEQ 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 VAGVLPVLDLGEDASLATLSTVAADLGFtalfgALLSGRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAa 2285
Cdd:PRK12406   186 MRALIYGLKPGIRALLTGPLYHSAPNAY-----GLRAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLK- 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2286 aggtavLPREC----------LVTGGEALTGALVQQ--VRALAPTlrIVNHYGPTETtvGILTCTVPEEWPVEQGVpVGH 2353
Cdd:PRK12406   260 ------LPEEVrakydvsslrHVIHAAAPCPADVKRamIEWWGPV--IYEYYGSTES--GAVTFATSEDALSHPGT-VGK 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2354 PLAGNEAWVLDRFGLPAPVGVAGELYL-GGGNLSLGYWQRAEQTAErfvahplaPDRL-LYRSGDLARLDGEGRIVYLGR 2431
Cdd:PRK12406   329 AAPGAELRFVDEDGRPLPQGEIGEIYSrIAGNPDFTYHNKPEKRAE--------IDRGgFITSGDVGYLDADGYLFLCDR 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2432 GDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN------GVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRA 2505
Cdd:PRK12406   401 KRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEfgealmAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEI 480
                          490
                   ....*....|....*....
gi 1246793773 2506 VESMPRLGNGKIDRQALAD 2524
Cdd:PRK12406   481 MAELPREDSGKIFKRRLRD 499
PLN02246 PLN02246
4-coumarate--CoA ligase
3544-3946 3.79e-17

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 88.50  E-value: 3.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3544 ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQ 3623
Cdd:PLN02246    50 VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQ 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3624 -------RALAVELPGTALCLDDPFTR----AQLDAVEPGELPEV---PTEAPAyLIYTSGSTGTPKGVVVTHRNverLF 3689
Cdd:PLN02246   130 scyvdklKGLAEDDGVTVVTIDDPPEGclhfSELTQADENELPEVeisPDDVVA-LPYSSGTTGLPKGVMLTHKG---LV 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3690 TAATQ-----TGRFSFDEHD----VWSLFHSHAFDFAVweLWGawLYGGRAVLvpeaVCRQPD--AFLDLLAEYGVTVLN 3758
Cdd:PLN02246   206 TSVAQqvdgeNPNLYFHSDDvilcVLPMFHIYSLNSVL--LCG--LRVGAAIL----IMPKFEigALLELIQRHKVTIAP 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3759 QTPSAFYAL-QSQAMRRELALNVRAVVFG----GEALEPSrlqpWRERYPQAELVNMYGITET----TVHVSFhrlSDED 3829
Cdd:PLN02246   278 FVPPIVLAIaKSPVVEKYDLSSIRMVLSGaaplGKELEDA----FRAKLPNAVLGQGYGMTEAgpvlAMCLAF---AKEP 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3830 LQSPTSRIGSALPDLAVHVLDA-AGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGS 3908
Cdd:PLN02246   351 FPVKSGSCGTVVRNAELKIVDPeTGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDG---WLHTGDIGYIDDDDE 427
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1246793773 3909 LEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:PLN02246   428 LFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV 465
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1142-1558 3.79e-17

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: 87.26  E-value: 3.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWF-FDSAPAQ-PDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFE-RADGQWRQQVAAPGPAPaIQAQ 1218
Cdd:cd19543      4 LSPMQEGMlFHSLLDPgSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLP-WREL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRG--AADLDSRVDAAFARMQEAT--PLAGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGELFDGLAALARGE 1293
Cdd:cd19543     83 DLSHlsEAEQEAELEALAEEDRERGfdLARAPLMRLTLIRLGDDRyRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1294 AwTPSARGASYADYVEAL--READDAQRfdagFWRE-LAAQPMQA-LPQDRPVALADARQsnVGRIVQTLDAGLTADLLE 1369
Cdd:cd19543    163 P-PSLPPVRPYRDYIAWLqrQDKEAAEA----YWREyLAGFEEPTpLPKELPADADGSYE--PGEVSFELSAELTARLQE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1370 RAgeayrcRTDEVllialaralatrTGRNRL---W---LDRERHGRDVL-----DGRDwSSVLGWYTAV----HPLPLDL 1434
Cdd:cd19543    236 LA------RQHGV------------TLNTVVqgaWallLSRYSGRDDVVfgttvSGRP-AELPGIETMVglfiNTLPVRV 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1435 GVADGPAQIGALKE-QIRALARRGLDYMPLvasARIPAL-PAGQLLFNyHGVVdagahpaFEVEPRTLASGNGADNPPGA 1512
Cdd:cd19543    297 RLDPDQTVLELLKDlQAQQLELREHEYVPL---YEIQAWsEGKQALFD-HLLV-------FENYPVDESLEEEQDEDGLR 365
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1513 LVEINARVQ-----------AGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAH 1558
Cdd:cd19543    366 ITDVSAEEQtnypltvvaipGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
3547-3989 6.42e-17

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: 87.90  E-value: 6.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLL-IRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSG---VCLSVS 3622
Cdd:cd17632     70 YAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEprlLAVSAE 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 QRALAVEL------PGTALCLD----DPFTRAQLDA------------------------VEPGEL--PEVPTEAPAYLI 3666
Cdd:cd17632    150 HLDLAVEAvleggtPPRLVVFDhrpeVDAHRAALESarerlaavgipvttltliavrgrdLPPAPLfrPEPDDDPLALLI 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNVERLFTAATQT-GRFSFDEHDVWSLFHSHAFDFAVweLWGAWLYGGRAVLVPE--------- 3736
Cdd:cd17632    230 YTSGSTGTPKGAMYTERLVATFWLKVSSIqDIRPPASITLNFMPMSHIAGRIS--LYGTLARGGTAYFAAAsdmstlfdd 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 -AVCRQPDAFL-----DLL-----AEYGVTVLNQTPSAFYALQSQAMRRELALNVR-AVVFGGEALEPSRLQPWRERYPQ 3804
Cdd:cd17632    308 lALVRPTELFLvprvcDMLfqryqAELDRRSVAGADAETLAERVKAELRERVLGGRlLAAVCGSAPLSAEMKAFMESLLD 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3805 AELVNMYGITETTV----------HVSFHRLSDedlqsptsrigsaLPDLAVHVLDaagQPVPLgvvGELVVEGDGVAQG 3874
Cdd:cd17632    388 LDLHDGYGSTEAGAvildgvivrpPVLDYKLVD-------------VPELGYFRTD---RPHPR---GELLVKTDTLFPG 448
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3875 YWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSDaaVTVEGQGE 3953
Cdd:cd17632    449 YYKRPEVTAEVFDEDG---FYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQ--IFVYGNSE 523
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 1246793773 3954 GAWLMAYAVAADGA---EPDPQ---SLREALRAL-----LPDYMLPR 3989
Cdd:cd17632    524 RAYLLAVVVPTQDAlagEDTARlraALAESLQRIareagLQSYEIPR 570
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
2047-2522 7.45e-17

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 87.51  E-value: 7.45e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2047 QMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVAL-CLPRtfaqlAAMAAVWhRGAAWLP--LDPQHPDA 2123
Cdd:PRK06155    32 ERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALmCGNR-----IEFLDVF-LGCAWLGaiAVPINTAL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2124 R--QIA-VLDDSGAR-IVIGWGAAPAWVPASVRWLDAESV--LDVVSAYEEPPRVDV----------------DADTPAy 2181
Cdd:PRK06155   106 RgpQLEhILRNSGARlLVVEAALLAALEAADPGDLPLPAVwlLDAPASVSVPAGWSTaplppldapapaaavqPGDTAA- 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2182 LIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPAELAFDAQALA 2261
Cdd:PRK06155   185 ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWPAV 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2262 AHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGGEAltgALVQQVRALApTLRIVNHYGPTETTVGILTctvpe 2341
Cdd:PRK06155   265 RRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPA---ALHAAFRERF-GVDLLDGYGSTETNFVIAV----- 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2342 EWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG---GNLSLGYWQRAEQTAErfvahplAPDRLLYRSGDLA 2418
Cdd:PRK06155   336 THGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE-------AWRNLWFHTGDRV 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIqGSLEGVA---EALAQ--- 2492
Cdd:PRK06155   409 VRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAV-VLRDGTAlepVALVRhce 487
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1246793773 2493 -RLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK06155   488 pRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
3557-4007 7.65e-17

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 87.55  E-value: 7.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3557 LATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVD-----PHAPAAR---RGFILEDSGVCLSVSQRALAV 3628
Cdd:PLN02860    45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsfEEAKSAMllvRPVMLVTDETCSSWYEELQND 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3629 ELP--GTALCLDDPFTR---AQLDAVEPGELPE---VPTE-----AP--AYLI-YTSGSTGTPKGVVVTHRN--VERLFT 3690
Cdd:PLN02860   125 RLPslMWQVFLESPSSSvfiFLNSFLTTEMLKQralGTTEldyawAPddAVLIcFTSGTTGRPKGVTISHSAliVQSLAK 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3691 AATqtgrFSFDEHDVW----SLFHSHAFDFAVWELwgawLYGGRAVLVPEAvcrQPDAFLDLLAEYGVTVLNQTPSAFYA 3766
Cdd:PLN02860   205 IAI----VGYGEDDVYlhtaPLCHIGGLSSALAML----MVGACHVLLPKF---DAKAALQAIKQHNVTSMITVPAMMAD 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3767 LQS---QAMRRELALNVRAVVFGGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHRLSDEDLQSP--TSRIGSAL 3841
Cdd:PLN02860   274 LISltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPkqTLQTVNQT 353
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 PDLAVHVLDAA--GQPVP---LGV-------VGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSL 3909
Cdd:PLN02860   354 KSSSVHQPQGVcvGKPAPhveLKIgldessrVGRILTRGPHVMLGYWGQNSETASVLSNDG---WLDTGDIGWIDKAGNL 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3910 EYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEgAWLMAYAVA----------ADGAEPD--------P 3971
Cdd:PLN02860   431 WLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV--GVPD-SRLTEMVVAcvrlrdgwiwSDNEKENakknltlsS 507
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 3972 QSLREALRAL-LPDYMLPRLI-QLLPALPLTANGKLDR 4007
Cdd:PLN02860   508 ETLRHHCREKnLSRFKIPKLFvQWRKPFPLTTTGKIRR 545
PRK13382 PRK13382
bile acid CoA ligase;
542-1044 8.17e-17

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 87.12  E-value: 8.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  542 ARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQ 621
Cdd:PRK13382    50 AIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  622 ARRAEVVAASGCDAVLTDAQglagFAPSVAIAVD----------------ELKLDGAGENGSGEN--AAPNQLAYILYTS 683
Cdd:PRK13382   130 PALAEVVTREGVDTVIYDEE----FSATVDRALAdcpqatrivawtdedhDLTVEVLIAAHAGQRpePTGRKGRVILLTS 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  684 GSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARpdELLEPQRFLAFLSER 763
Cdd:PRK13382   206 GTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTR--RRFDPEATLDLIDRH 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  764 AITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDrrcALINAYGPTEA---TISSHYHR 838
Cdd:PRK13382   284 RATGLAVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---VIYNNYNATEAgmiATATPADL 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  839 VQAID-ASRPvPLGQLLpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYrgdAAASERRFAplrlpSGeslrMYRSGD 917
Cdd:PRK13382   361 RAAPDtAGRP-AEGTEI-----RILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFH-----DG----FMASGD 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  918 RVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQTD 996
Cdd:PRK13382   423 VGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVaEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHV 502
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773  997 SDQteserwhralcerLPAYMVPTQFVALPRLPRNASGKIDRRALPAP 1044
Cdd:PRK13382   503 RDN-------------LANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK06164 PRK06164
acyl-CoA synthetase; Validated
2052-2528 8.58e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 87.11  E-value: 8.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPR------TFAQLAAMAA----VWHR------------ 2109
Cdd:PRK06164    26 AVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNciewvvLFLACARLGAtviaVNTRyrshevahilgr 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2110 -GAAWLPLDPQH-----------------PDARQIAVLDDSGArivigwgAAPAWVPASVRWLDAESVLDVVSAYEEPPR 2171
Cdd:PRK06164   106 gRARWLVVWPGFkgidfaailaavppdalPPLRAIAVVDDAAD-------ATPAPAPGARVQLFALPDPAPPAAAGERAA 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2172 vdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALFGALLSGRRVRLLPA 2251
Cdd:PRK06164   179 ---DPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPV 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2252 elaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVtGGEALTGA---LVQQVRALAPTLRIVnhYGPT 2328
Cdd:PRK06164   256 ---FDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF-GFASFAPAlgeLAALARARGVPLTGL--YGSS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 EttVGILTCTVPEEWPVEQGVPVGHPLAGNEAWVLDR---FGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPL 2405
Cdd:PRK06164   330 E--VQALVALQPATDPVSVRIEGGGRPASPEARVRARdpqDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2406 apdrllYRSGDLARLDGEGRIVYLGR-GDHqVKIRGYRVELGEVEQVLAQLPGVEVAAVLAL-------PGANGVLQLGA 2477
Cdd:PRK06164   408 ------FRTGDLGYTRGDGQFVYQTRmGDS-LRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrdgktvPVAFVIPTDGA 480
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2478 ciQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRL--GNG-KIDRQALADLLQQ 2528
Cdd:PRK06164   481 --SPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLREMAQA 532
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1142-1557 8.75e-17

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: 86.28  E-value: 8.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERAD-GQWRQQVAAPGPAPAIQAQ 1218
Cdd:cd19539      4 LSFAQErlWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLEVRD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRGAADLDsRVDAAFARMQEATP--LAG--PLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEA 1294
Cdd:cd19539     84 LSDPDSDRE-RRLEELLRERESRGfdLDEepPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1295 WTPSARGASYADYVEALREADDAQRFDA--GFWRE-LAAQPMQALPQDRPVALADARQSNVGRIVqtLDAGLTADLLERA 1371
Cdd:cd19539    163 APLPELRQQYKEYAAWQREALAAPRAAEllDFWRRrLRGAEPTALPTDRPRPAGFPYPGADLRFE--LDAELVAALRELA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1372 GEAyRCRTDEVLLIALARALATRTGRNRLWLDRERHGRDvldgRDW-SSVLGWYTAVHPLPLDLGvadgpaQIGALKEQI 1450
Cdd:cd19539    241 KRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRN----HPRfESTVGFFVNLLPLRVDVS------DCATFRDLI 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1451 RALARRgldympLVASARIPALPAGQLLFNYHGVVDAGAHPAFEV---------EPRTLASGN----GADNPPGALVEIN 1517
Cdd:cd19539    310 ARVRKA------LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIvfqvtnapaGELELAGGLsyteGSDIPDGAKFDLN 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1246793773 1518 ARV--QAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVA 1557
Cdd:cd19539    384 LTVteEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
3540-4033 1.13e-16

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 87.12  E-value: 1.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3540 AEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPV----DPHAPAAR------RG 3609
Cdd:PRK00174    94 GDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADRiidagaKL 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3610 FILEDSGV------------------CLSVsQRALAVELPGTALCLDDP-------FTRAQLDAVEPgelPEVPTEAPAY 3664
Cdd:PRK00174   174 VITADEGVrggkpiplkanvdealanCPSV-EKVIVVRRTGGDVDWVEGrdlwwheLVAGASDECEP---EPMDAEDPLF 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVThrnverlfTA-----ATQTGRFSFDEH---------DV-WSLFHSHAfdfavwelwgawLYG- 3728
Cdd:PRK00174   250 ILYTSGSTGKPKGVLHT--------TGgylvyAAMTMKYVFDYKdgdvywctaDVgWVTGHSYI------------VYGp 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3729 ---GRAVLVPEAVCRQPDA--FLDLLAEYGVTVLNQTPSAFYALqsqaMR--------RELA-LNVRAVVfgGEALEPsr 3794
Cdd:PRK00174   310 lanGATTLMFEGVPNYPDPgrFWEVIDKHKVTIFYTAPTAIRAL----MKegdehpkkYDLSsLRLLGSV--GEPINP-- 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3795 lQPWR--------ERYPqaeLVNMYGITETTVHvsfhrlsdedLQSPT-----SRIGSA---LPDLAVHVLDAAGQPVPL 3858
Cdd:PRK00174   382 -EAWEwyykvvggERCP---IVDTWWQTETGGI----------MITPLpgatpLKPGSAtrpLPGIQPAVVDEEGNPLEG 447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3859 GVVGELVVEGD--GVAQGYWQRPeltaERFVERGGQRF---YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAA 3933
Cdd:PRK00174   448 GEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFkgmYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3934 KIASLPQVSDAAVT-----VEGQGegawLMAYAVAADGAEPDPQsLREALRALLPDYM----LPRLIQLLPALPLTANGK 4004
Cdd:PRK00174   524 ALVAHPKVAEAAVVgrpddIKGQG----IYAFVTLKGGEEPSDE-LRKELRNWVRKEIgpiaKPDVIQFAPGLPKTRSGK 598
                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1246793773 4005 LDRKALPK-----PETQD----RDEGVLESASERRLAE 4033
Cdd:PRK00174   599 IMRRILRKiaegeEILGDtstlADPSVVEKLIEARQNR 636
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
530-1038 1.48e-16

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: 86.40  E-value: 1.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  530 APRTVGNVVDAIARAADEFPERAAL-----ETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLD-WYCLLl 603
Cdd:cd05970     12 VPENFNFAYDVVDAMAKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEfWYSLL- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  604 GAWRAGLSVIPL-------DTEWpQARRAEV--VAASGCDAVLTDAQGLAGFAPSVAIAV-------------DELKLDG 661
Cdd:cd05970     91 ALHKLGAIAIPAthqltakDIVY-RIESADIkmIVAIAEDNIPEEIEKAAPECPSKPKLVwvgdpvpegwidfRKLIKNA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  662 AG--ENGSGENAAPNQLAYILY-TSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVA----GLAVdttLEQIL 734
Cdd:cd05970    170 SPdfERPTANSYPCGEDILLVYfSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVAdtgwGKAV---WGKIY 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  735 AAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADdwRDLA-LRCLVVGGDVLPVALAQRWFEL 813
Cdd:cd05970    247 GQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR--YDLSsLRYCTTAGEALNPEVFNTFKEK 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  814 -GLDrrcaLINAYGPTEATISshyhrVQAIDASRPVP--LGQLLPGRIAAVLDAHGRIVPRGVCGELALG-----GIGLA 885
Cdd:cd05970    325 tGIK----LMEGFGQTETTLT-----IATFPWMEPKPgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLF 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  886 EGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAA 964
Cdd:cd05970    396 GGYYKDAEKTAEVWH-----DG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVlECAVT 466
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  965 GVVGEGAAQRLVAWVECAgedgfgqadlnqtdSDQTESERWHRAL---CERLPA-YMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd05970    467 GVPDPIRGQVVKATIVLA--------------KGYEPSEELKKELqdhVKKVTApYKYPRIVEFVDELPKTISGKIRR 530
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
2063-2522 2.18e-16

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: 85.76  E-value: 2.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDarQIA-VLDDSGARIV--- 2137
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRlFPE--QIAyIINHAEDRVVfvd 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2138 -----IGWGAAPAW----------------VPASVRWLDAESVLDVVSAYEEPPrvDVDADTPAYLIYTSGSTGTPKGVV 2196
Cdd:cd12119    105 rdflpLLEAIAPRLptvehvvvmtddaampEPAGVGVLAYEELLAAESPEYDWP--DFDENTAAAICYTSGTTGNPKGVV 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2197 VSQGNLANYVAGVLPVLDLGEDASLATLSTV------AADLGFTA-LFGA--LLSGRrvRLLPAELAfdaqalaAHLQAH 2267
Cdd:cd12119    183 YSHRSLVLHAMAALLTDGLGLSESDVVLPVVpmfhvnAWGLPYAAaMVGAklVLPGP--YLDPASLA-------ELIERE 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2268 PVDCLKIVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQqvRALAPTLRIVNHYGPTET----TVGILTCTVPE 2341
Cdd:cd12119    254 GVTFAAGVPTvwQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIE--AFEERGVRVIHAWGMTETsplgTVARPPSEHSN 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2342 EwPVEQGVPV----GHPLAGNEAWVLDRFG--LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplapDRLLyRSG 2415
Cdd:cd12119    332 L-SEDEQLALrakqGRPVPGVELRIVDDDGreLPWDGKAVGELQVRGPWVTKSYYKNDEESEALTE------DGWL-RTG 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2416 DLARLDGEG--RIVylGRGDHQVKIRG---YRVELgevEQVLAQLPGVEVAAVLALPG--------ANGVLQLGAciQGS 2482
Cdd:cd12119    404 DVATIDEDGylTIT--DRSKDVIKSGGewiSSVEL---ENAIMAHPAVAEAAVIGVPHpkwgerplAVVVLKEGA--TVT 476
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1246793773 2483 LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd12119    477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
673-1041 2.26e-16

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: 85.46  E-value: 2.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQILaawsrGACVVAR 746
Cdd:cd05909    146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFgalpffHSFGLTGCLWLPLLS-----GIKVVFH 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  747 PDElLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRdlALRCLVVGGDVLPVALAQRWFEL-GLdrrcALINAY 825
Cdd:cd05909    221 PNP-LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDFS--SLRLVVAGAEKLKDTLRQEFQEKfGI----RILEGY 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  826 GPTEATISSHYHRVQAidASRPVPLGQLLPGRIAAVLDAHGRI-VPRGVCGELALGGIGLAEGYrgdaaaserrfapLRL 904
Cdd:cd05909    294 GTTECSPVISVNTPQS--PNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGY-------------LNE 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  905 PSGESLRM----YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQL--PQVRAAAAGVVGEGAAQRLVAW 978
Cdd:cd05909    359 PELTSFAFgdgwYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGEKIVLL 438
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773  979 VecagedgfgqadlnqTDSDQTESErWHRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05909    439 T---------------TTTDTDPSS-LNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1645-1977 2.70e-16

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: 84.78  E-value: 2.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1645 VRRQPMLRTAIVwEGLSVPHQIVLADAAAPwqtLDWSALDDAAQDaqLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRY 1724
Cdd:cd19540     49 VARHESLRTVFP-EDDGGPYQVVLPAAEAR---PDLTVVDVTEDE--LAARLAEAARRGFDLTAELPLRARLFRLGPDEH 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1725 WLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLPPAPgFQaYLD---WRERQ---------DLARQRGWWRERLS 1792
Cdd:cd19540    123 VLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWAPLP-VQ-YADyalWQRELlgdeddpdsLAARQLAYWRETLA 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1793 G------------------YAGtaalpapvaaAHHPVqreecerRLSAHDSERLRAFCRERGCTLSdliaMVW--GLAN- 1851
Cdd:cd19540    201 GlpeelelptdrprpavasYRG----------GTVEF-------TIDAELHARLAALAREHGATLF----MVLhaALAVl 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1852 -ARYGNHDDVVLGATRSGRP-PELagvESMVGVFINTLPLRLRIDAGQPALDLLSALRSQSLEVAENEAVGLgEILADSg 1929
Cdd:cd19540    260 lSRLGAGDDIPIGTPVAGRGdEAL---DDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPF-ERLVEA- 334
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1930 LDADR------LFASLLVVENFPAmAPAQLPfALRVRETRAANHYA---LTLRVSER 1977
Cdd:cd19540    335 LNPPRstarhpLFQVMLAFQNTAA-ATLELP-GLTVEPVPVDTGVAkfdLSFTLTER 389
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2181-2518 3.40e-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: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 83.59  E-value: 3.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2181 YLIYTSGSTGTPKGVV-------VSQGNLANYVAGVLPVLDLGEDASLATLSTV---AADL----GFTALFGALLSGRRV 2246
Cdd:cd05924      7 YILYTGGTTGMPKGVMwrqedifRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVmfpAPPLmhgtGSWTAFGGLLGGQTV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2247 rLLPaELAFDAQALAAHLQAHPVDCLKIVpSHLAGLLAAAGGTAVLPREC-----LVTGGEALTGALVQQVRALAPTLRI 2321
Cdd:cd05924     87 -VLP-DDRFDPEEVWRTIEKHKVTSMTIV-GDAMARPLIDALRDAGPYDLsslfaISSGGALLSPEVKQGLLELVPNITL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2322 VNHYGPTETtvGILTCTVPEEWPVEQGVPVghpLAGNEAWVLDRFGLPAPVGVAGELYLG-GGNLSLGYWQRAEQTAERF 2400
Cdd:cd05924    164 VDAFGSSET--GFTGSGHSAGSGPETGPFT---RANPDTVVLDDDGRVVPPGSGGVGWIArRGHIPLGYYGDEAKTAETF 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2401 vahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV---------------EVAAVLA 2465
Cdd:cd05924    239 ---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVydvlvvgrpderwgqEVVAVVQ 315
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2466 LPGANGVlqlgaciqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID 2518
Cdd:cd05924    316 LREGAGV---------DLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK07788 PRK07788
acyl-CoA synthetase; Validated
535-1043 3.42e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 85.36  E-value: 3.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  535 GNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALcLPRGLDWYCL-LLGAWRAGLSVI 613
Cdd:PRK07788    49 GPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRGFVLaLYAAGKVGARII 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  614 PLDTEWPQARRAEVVAASGCDAVLTDAQ--GLAGFAP-------SVAIAVDELKLDGAG--------ENGSGEN--AAPN 674
Cdd:PRK07788   128 LLNTGFSGPQLAEVAAREGVKALVYDDEftDLLSALPpdlgrlrAWGGNPDDDEPSGSTdetlddliAGSSTAPlpKPPK 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARpdELLEPQ 754
Cdd:PRK07788   208 PGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLR--RRFDPE 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  755 RFLAFLSERAITVTDLAPAYANELVRasVADDWR---DL-ALRCLVVGGDVLPVALAQRWFELGLDRRCaliNAYGPTE- 829
Cdd:PRK07788   286 ATLEDIAKHKATALVVVPVMLSRILD--LGPEVLakyDTsSLKIIFVSGSALSPELATRALEAFGPVLY---NLYGSTEv 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  830 --ATISSHYHRVQAidasrPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDaaaserrfaplrlPSG 907
Cdd:PRK07788   361 afATIATPEDLAEA-----PGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDG-------------RDK 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  908 ESLR-MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVecAGED 985
Cdd:PRK07788   423 QIIDgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVeAAVIGVDDEEFGQRLRAFV--VKAP 500
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  986 GfgqADLnqtDSDQTesERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK07788   501 G---AAL---DEDAI--KDYVR---DNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
2320-2522 3.51e-16

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 85.12  E-value: 3.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2320 RIVNHYGPTETTVGILTCTVPEE--WPveqgvPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG---GNLSLGYWQRAE 2394
Cdd:PRK08008   314 RLLTSYGMTETIVGIIGDRPGDKrrWP-----SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPK 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2395 QTAErfvahPLAPDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG------ 2468
Cdd:PRK08008   389 ATAK-----VLEADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDsirdea 462
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2469 --ANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK08008   463 ikAFVVLNEGETL--SEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK09274 PRK09274
peptide synthase; Provisional
2134-2528 3.78e-16

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 85.34  E-value: 3.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2134 ARIVIGWGAAPA--WVPASVRWLDAESVLD---VVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYV-- 2206
Cdd:PRK09274   126 ARRLFGWGKPSVrrLVTVGGRLLWGGTTLAtllRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIea 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2207 -----------------------------AGVLPVLDLGEDASL--ATLSTVAADLGFTALFG--ALLSgrrvRLLPAEL 2253
Cdd:PRK09274   206 lredygiepgeidlptfplfalfgpalgmTSVIPDMDPTRPATVdpAKLFAAIERYGVTNLFGspALLE----RLGRYGE 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2254 AfdaqalaahlQAHPVDCLKIVPShlagllaaaggtavlpreclvtGGEALTGALVQQVRA-LAPTLRIVNHYGPTE--- 2329
Cdd:PRK09274   282 A----------NGIKLPSLRRVIS----------------------AGAPVPIAVIERFRAmLPPDAEILTPYGATEalp 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2330 -TTVG---ILTCTVpEEWPVEQGVPVGHPLAGNE------------AWVLDrfgLPAPVGVAGELYLGGGNLSLGYWQRA 2393
Cdd:PRK09274   330 iSSIEsreILFATR-AATDNGAGICVGRPVDGVEvriiaisdapipEWDDA---LRLATGEIGEIVVAGPMVTRSYYNRP 405
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2394 EQTAERFVAHPLAPDRllYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVL 2473
Cdd:PRK09274   406 EATRLAKIPDGQGDVW--HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPGAQR 483
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2474 --------QLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMP---RlGNGKIDRQALADLLQQ 2528
Cdd:PRK09274   484 pvlcvelePGVACSKSALYQELRALAAAHPHTAGIERFLIHPSFPvdiR-HNAKIFREKLAVWAAK 548
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
2062-2528 5.16e-16

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: 84.64  E-value: 5.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDP----QHPDAR-----QIAVLDDS 2132
Cdd:cd05906     40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARlrklrHIWQLLGS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2133 gARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPR----VDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAG 2208
Cdd:cd05906    120 -PVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAAdhdlPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2209 VLPVLDLGEDAslATLSTVAAD----LGFTALFGALLSGRRVRLLPAELAFDaqalaahlqahPVDCLKIVPSH------ 2278
Cdd:cd05906    199 KIQHNGLTPQD--VFLNWVPLDhvggLVELHLRAVYLGCQQVHVPTEEILAD-----------PLRWLDLIDRYrvtitw 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2279 ---------LAGLLAAAGGTAVLPR-ECLVTGGEALTGALVQQ-VRALAPT-LR---IVNHYGPTETTVGILTCTVPEEW 2343
Cdd:cd05906    266 apnfafallNDLLEEIEDGTWDLSSlRYLVNAGEAVVAKTIRRlLRLLEPYgLPpdaIRPAFGMTETCSGVIYSRSFPTY 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2344 PVEQG---VPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPlapdrlLYRSGDLARL 2420
Cdd:cd05906    346 DHSQAlefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDG------WFRTGDLGFL 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2421 DgEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV-----------------EVAAVLALPGANGVLQLGACIQgSL 2483
Cdd:cd05906    420 D-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsftaafavrdpgaetEELAIFFVPEYDLQDALSETLR-AI 497
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773 2484 EGVAEALAQRLPEYLCPSrwrAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:cd05906    498 RSVVSREVGVSPAYLIPL---PKEEIPKTSLGKIQRSKLKAAFEA 539
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
2062-2524 6.98e-16

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: 84.47  E-value: 6.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLP----LDP-------QHPDARQIAVLD 2130
Cdd:cd05970     48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqLTAkdivyriESADIKMIVAIA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGwGAAP--------AWVPASVR--WLDAESVLDVVSAYEEPPRVDVDA--DTPAYLIYTSGSTGTPKgvVVS 2198
Cdd:cd05970    128 EDNIPEEIE-KAAPecpskpklVWVGDPVPegWIDFRKLIKNASPDFERPTANSYPcgEDILLVYFSSGTTGMPK--MVE 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2199 QGNLanYVAGVLPVLDLGEDASLATLSTVAADLGFTA-----LFGALLSGRRVRLLPAELaFDAQALAAHLQAHPVDCLK 2273
Cdd:cd05970    205 HDFT--YPLGHIVTAKYWQNVREGGLHLTVADTGWGKavwgkIYGQWIAGAAVFVYDYDK-FDPKALLEKLSKYGVTTFC 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2274 IVPSHLAGLLAAAGGTAVLP--REClVTGGEALTGALVQQVRALApTLRIVNHYGPTETTVGILTCTVPEEWPVEqgvpV 2351
Cdd:cd05970    282 APPTIYRFLIREDLSRYDLSslRYC-TTAGEALNPEVFNTFKEKT-GIKLMEGFGQTETTLTIATFPWMEPKPGS----M 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGNEAWVLDRFGLPAPVGVAGELYL---GGGNLSL--GYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRI 2426
Cdd:cd05970    356 GKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAEKTAEVWHDG-------YYHTGDAAWMDEDGYL 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2427 VYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIQGSLEGVAEALAQRLPE-Y 2497
Cdd:cd05970    429 WFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDpirgqvvkATIVLAKGYEPSEELKKELQDHVKKVTApY 508
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 2498 LCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05970    509 KYPRIVEFVDELPKTISGKIRRVEIRE 535
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
2050-2529 1.45e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 83.28  E-value: 1.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVL 2129
Cdd:PRK12583    34 REALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYAL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2130 DDSGARIVI------------------------GWGA---------------APAWVPASVRWLDAESVLDVVSAYEEPP 2170
Cdd:PRK12583   114 GQSGVRWVIcadafktsdyhamlqellpglaegQPGAlacerlpelrgvvslAPAPPPGFLAWHELQARGETVSREALAE 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2171 R-VDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLAT-------LSTVAADLGFTALfGALLs 2242
Cdd:PRK12583   194 RqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpvplyhcFGMVLANLGCMTV-GACL- 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2243 grrvrLLPAElAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAvLPRECLVTG---GEALTGALVQQVRALAPTL 2319
Cdd:PRK12583   272 -----VYPNE-AFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGN-FDLSSLRTGimaGAPCPIEVMRRVMDEMHMA 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2320 RIVNHYGPTETT-VGILTCTvpeEWPVEQGV-PVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTA 2397
Cdd:PRK12583   345 EVQIAYGMTETSpVSLQTTA---ADDLERRVeTVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATA 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2398 ERFVAhplapDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGA 2477
Cdd:PRK12583   422 ESIDE-----DGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVA 495
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2478 CI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK12583   496 WVrlhpghAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEE 553
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
512-1043 1.54e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 83.12  E-value: 1.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  512 LSWPWPADELALddKREpAPRTVGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALC 591
Cdd:PRK13383    15 LNPPSPRAVLRL--LRE-ASRGGTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVM 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  592 LPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD---AQGLAGFAPSVAIaVDELKLDGAGENGSG 668
Cdd:PRK13383    92 CRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADnefAERIAGADDAVAV-IDPATAGAEESGGRP 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  669 ENAAPNQLayILYTSGSTGIPKGVE--------VGHAALAAHIDAAAEALALSADDRVLHVAGLAVdttleqILAAWSRG 740
Cdd:PRK13383   171 AVAAPGRI--VLLTSGTTGKPKGVPrapqlrsaVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGM------LMLTIALG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  741 ACVVARPDellepqrflaFLSERAITVTDLAPAYANELVRASVA------DDWRDL----ALRCLVVGGDVLPVALAQRW 810
Cdd:PRK13383   243 GTVLTHRH----------FDAEAALAQASLHRADAFTAVPVVLArilelpPRVRARnplpQLRVVMSSGDRLDPTLGQRF 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  811 FELGLDrrcALINAYGPTEATISSHYHRVQAIDAsrPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRG 890
Cdd:PRK13383   313 MDTYGD---ILYNGYGSTEVGIGALATPADLRDA--PETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  891 DAAASerrfaplrLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGE 969
Cdd:PRK13383   388 GGGKA--------VVDG----MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIGVPDE 455
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773  970 GAAQRLVAWVecAGEDGFGqadlnqTDSDQTESerwhrALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK13383   456 RFGHRLAAFV--VLHPGSG------VDAAQLRD-----YLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
2052-2528 1.57e-15

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: 83.27  E-value: 1.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT-------FAQLAA-----MAAVWHR---------- 2109
Cdd:COG1021     41 RIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVaefvivfFALFRAgaipvFALPAHRraeishfaeq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2110 -GAAWLPLDPQHP--DARQIA--VLDD-SGARIVIGWGAAPAWVPasvrwLDAesvldVVSAYEEPPRVDVDADTPAYLI 2183
Cdd:COG1021    121 sEAVAYIIPDRHRgfDYRALAreLQAEvPSLRHVLVVGDAGEFTS-----LDA-----LLAAPADLSEPRPDPDDVAFFQ 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGED-ASLATLsTVA--ADLGFTALFGALLSGRRVRLLP---AELAFDA 2257
Cdd:COG1021    191 LSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADtVYLAAL-PAAhnFPLSSPGVLGVLYAGGTVVLAPdpsPDTAFPL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAhlqahpVDCLKIVPSHLAGLLAAAGGTAVLPR--ECLVTGGEALTGALVQQVR-ALAPTLRIVnhYGPTEttvGI 2334
Cdd:COG1021    270 IERER------VTVTALVPPLALLWLDAAERSRYDLSslRVLQVGGAKLSPELARRVRpALGCTLQQV--FGMAE---GL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwPVE-----QGVPVGhplAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDR 2409
Cdd:COG1021    339 VNYTRLDD-PEEvilttQGRPIS---PDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAF-----TPDG 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 LlYRSGDLARLDGEGRIVYLGRGDHQVkIRGyrvelGE------VEQVLAQLPGVEVAAVLALPGAngvlQLG----ACI 2479
Cdd:COG1021    410 F-YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVHDAAVVAMPDE----YLGerscAFV 478
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2480 QG-----SLEGVAEALAQR-LPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:COG1021    479 VPrgeplTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
2082-2524 1.59e-15

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: 82.81  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2082 GVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGwgAAPAWvPASVRWLDAESVLD 2161
Cdd:cd05929     38 GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCG--LFTGG-GALDGLEDYEAAEG 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2162 vvsAYEEPPRVDVDAdtPAYLIYTSGSTGTPKGVVVS-QGNLANYVAGVLPVLDLGEDASLATLSTV----AAdlGFTAL 2236
Cdd:cd05929    115 ---GSPETPIEDEAA--GWKMLYSGGTTGRPKGIKRGlPGGPPDNDTLMAAALGFGPGADSVYLSPAplyhAA--PFRWS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2237 FGALLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLlaaaggtAVLPREclVTGGEALTG---------- 2306
Cdd:cd05929    188 MTALFMGGTLVLMEK---FDPEEFLRLIERYRVTFAQFVPTMFVRL-------LKLPEA--VRNAYDLSSlkrvihaaap 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2307 ---ALVQQVRALAPTlRIVNHYGPTETtVGiLTCTVPEEWPVEQGvPVGHPLAGnEAWVLDRFGLPAPVGVAGELYLGGG 2383
Cdd:cd05929    256 cppWVKEQWIDWGGP-IIWEYYGGTEG-QG-LTIINGEEWLTHPG-SVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANG 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2384 NLSLgYWQRAEQTAERFVAHPlapdrllYRS-GDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAA 2462
Cdd:cd05929    331 PGFE-YTNDPEKTAAARNEGG-------WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAA 402
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2463 VLALPGANGVLQLGACIQGSLEGV-----AEALA----QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05929    403 VVGVPDEELGQRVHAVVQPAPGADagtalAEELIaflrDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
PRK05857 PRK05857
fatty acid--CoA ligase;
3521-4010 1.86e-15

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 83.13  E-value: 1.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARIAVSAEDG--ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK05857    16 VLDRVFEQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDPHAPAA---RRGFILEDSGVCLSVSQRALAVELPGTALCL---------DDPFTRAQLDAVEPGELPEVPTEAPAYLI 3666
Cdd:PRK05857    96 ADGNLPIAaieRFCQITDPAAALVAPGSKMASSAVPEALHSIpviavdiaaVTRESEHSLDAASLAGNADQGSEDPLAMI 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3667 YTSGSTGTPKGVVVTHRNverlFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAW------LYGGRAVLVPEavcr 3740
Cdd:PRK05857   176 FTSGTTGEPKAVLLANRT----FFAVPDILQKEGLNWVTWVVGETTYSPLPATHIGGLWwiltclMHGGLCVTGGE---- 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3741 QPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGealepSRLQPWRERYPQAELV---NMYGITET 3816
Cdd:PRK05857   248 NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVpSLRLVGYGG-----SRAIAADVRFIEATGVrtaQVYGLSET 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDEDLQS-PTSRIGSALPDLAVHVLDAAG------QPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVEr 3889
Cdd:PRK05857   323 GCTALCLPTDDGSIVKiEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID- 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3890 ggqRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAWLMAYAVAAdGAEP 3969
Cdd:PRK05857   402 ---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVA-SAEL 477
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773 3970 DPQSLREALRALLPDY-------MLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK05857   478 DESAARALKHTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
3525-4004 2.14e-15

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: 83.09  E-value: 2.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3525 FAE--IARRYPARIAV--SAEDG---ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYV 3597
Cdd:cd05943     72 YAEnlLRHADADDPAAiyAAEDGertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 PVDP----HAPAARRG-----FILEDSGV-------CLSVSQRALAVELPGT--ALCLDDPFTRAQLDA----------- 3648
Cdd:cd05943    152 SCSPdfgvPGVLDRFGqiepkVLFAVDAYtyngkrhDVREKVAELVKGLPSLlaVVVVPYTVAAGQPDLskiakaltled 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3649 -VEPGELPE-----VPTEAPAYLIYTSGSTGTPK-------GVVVTHRNVERLFTAATQTGRFSFdehdvwslfhshaFD 3715
Cdd:cd05943    232 fLATGAAGElefepLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCDLRPGDRLFY-------------YT 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3716 FAVWELWGaWLYGGRA-----VLVPEA-VCRQPDAFLDLLAEYGVTVLNqTPSAFYALQSQA---MRRELALN-VRAVVF 3785
Cdd:cd05943    299 TCGWMMWN-WLVSGLAvgatiVLYDGSpFYPDTNALWDLADEEGITVFG-TSAKYLDALEKAglkPAETHDLSsLRTILS 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3786 GGEALEPSrLQPW--RERYPQAELVNMYGITE-------TTVHVSFHRlsdEDLQSPTsrIGsalpdLAVHVLDAAGQPV 3856
Cdd:cd05943    377 TGSPLKPE-SFDYvyDHIKPDVLLASISGGTDiiscfvgGNPLLPVYR---GEIQCRG--LG-----MAVEAFDEEGKPV 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PlGVVGELVVEGDGVAQ--GYWQRPELTAER---FVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEI 3931
Cdd:cd05943    446 W-GEKGELVCTKPFPSMpvGFWNDPDGSRYRaayFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEI 522
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3932 AAKIASLPQVSDA-AVTVEGQGEGAWLMAYAVAADGAEPDP---QSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:cd05943    523 YRVVEKIPEVEDSlVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
3656-3921 3.35e-15

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 82.17  E-value: 3.35e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3656 EVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlftAATQTGRFSF---DEHDVWSLFHS--HAFDFAVWELWgAWLYGGR 3730
Cdd:PRK06334   179 DKDPEDVAVILFTSGTEKLPKGVPLTHANL-----LANQRACLKFfspKEDDVMMSFLPpfHAYGFNSCTLF-PLLSGVP 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3731 AVLVPEAVcrQPDAFLDLLAEYGVTVLNQTPSAFYALQSQAMRRELAL-NVRAVVFGGEALEPSRLQPWRERYPQAELVN 3809
Cdd:PRK06334   253 VVFAYNPL--YPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLpSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQ 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3810 MYGITETTVHVSfhrLSDEDLQSPTSRIGSALPDLAVHVLDAAGQ-PVPLGVVGELVVEGDGVAQGYWQRPEltAERFVE 3888
Cdd:PRK06334   331 GYGTTECSPVIT---INTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE 405
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1246793773 3889 RGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKL 3921
Cdd:PRK06334   406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
3663-3921 4.36e-15

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: 81.49  E-value: 4.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFS--FDEHDVW--SLFHSHAFDFAVwEL----WGAWL-YGGRAVL 3733
Cdd:cd17639     91 ACIMYTSGSTGNPKGVMLTHGNL--VAGIAGLGDRVPelLGPDDRYlaYLPLAHIFELAA-ENvclyRGGTIgYGSPRTL 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 VPeAVCRQPDAflDLLaEY------GV---------TVLNQTPSA-------F---YALQSQAM---------------- 3772
Cdd:cd17639    168 TD-KSKRGCKG--DLT-EFkptlmvGVpaiwdtirkGVLAKLNPMgglkrtlFwtaYQSKLKALkegpgtplldelvfkk 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3773 -RRELALNVRAVVFGGEALEPSrlqpwrerypQAELVNM--------YGITETTVHVSFHRLSDEDlqspTSRIGSALPD 3843
Cdd:cd17639    244 vRAALGGRLRYMLSGGAPLSAD----------TQEFLNIvlcpviqgYGLTETCAGGTVQDPGDLE----TGRVGPPLPC 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3844 LAVHVLD------AAGQPVPLGvvgELVVEGDGVAQGYWQRPELTAERFVergGQRFYRSGDLGRYRADGSLEYRGRGDD 3917
Cdd:cd17639    310 CEIKLVDweeggySTDKPPPRG---EILIRGPNVFKGYYKNPEKTKEAFD---GDGWFHTGDIGEFHPDGTLKIIDRKKD 383

                   ....
gi 1246793773 3918 QVKL 3921
Cdd:cd17639    384 LVKL 387
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
2170-2524 4.39e-15

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 81.85  E-value: 4.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2170 PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLanyvagvlpvldlgedasLATLSTVAADLGFTalfGALLSGRRVRL- 2248
Cdd:PRK08751   201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNL------------------VANMQQAHQWLAGT---GKLEEGCEVVIt 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2249 -LPA---------ELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLVTGG----------EALTGAL 2308
Cdd:PRK08751   260 aLPLyhifaltanGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGfdqidfsslkMTLGGGM 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2309 VQQvRALAPT------LRIVNHYGPTETTVGilTCTVPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG 2382
Cdd:PRK08751   340 AVQ-RSVAERwkqvtgLTLVEAYGLTETSPA--ACINPLTLKEYNG-SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKG 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2383 GNLSLGYWQRAEQTAERFVAHPLapdrllYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV-EVA 2461
Cdd:PRK08751   416 PQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVlEVA 489
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2462 AVlALPGANGVLQLGACIQG-----SLEGVAEALAQRLPEYLCPsrwRAVE---SMPRLGNGKIDRQALAD 2524
Cdd:PRK08751   490 AV-GVPDEKSGEIVKVVIVKkdpalTAEDVKAHARANLTGYKQP---RIIEfrkELPKTNVGKILRRELRD 556
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1143-1361 4.85e-15

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: 80.43  E-value: 4.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1143 SPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASF--ERADGQWRQQVAAPGPAPAIQAQDw 1220
Cdd:cd19542      5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLKSLDPPIEEVET- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1221 rgaaDLDSRVDAAFARMQEATPLAGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGElfdgLAALARGeawTPSA 1299
Cdd:cd19542     84 ----DEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEvYLVLRISHALYDGVSLPIILRD----LAAAYNG---QLLP 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 1300 RGASYADYVEALREADDAQRFDagFWRE-LAAQPMQALPQDRPVALADARQSNVGRIVQTLDA 1361
Cdd:cd19542    153 PAPPFSDYISYLQSQSQEESLQ--YWRKyLQGASPCAFPSLSPKRPAERSLSSTRRSLAKLEA 213
PRK09088 PRK09088
acyl-CoA synthetase; Validated
601-1041 5.22e-15

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 81.39  E-value: 5.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDELKLDGAgENGSGENAAPNQLAYIL 680
Cdd:PRK09088    63 LHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADAL-EPADTPSIPPERVSLIL 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  681 YTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAvdTTLEQILAawsRGACVVARPDelLEPQ 754
Cdd:PRK09088   142 FTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLcdapmfHIIGLI--TSVRPVLA---VGGSILVSNG--FEPK 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  755 RFLAFLSERAITVTDL--APAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPTEATI 832
Cdd:PRK09088   215 RTLGRLGDPALGITHYfcVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGI----PMVDGFGMSEAGT 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  833 SSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRM 912
Cdd:PRK09088   291 VFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF--------TGDGW 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  913 YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQrlvaWVECagedgfGQADL 992
Cdd:PRK09088   363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECA--VVGMADAQ----WGEV------GYLAI 430
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773  993 NQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK09088   431 VPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
679-1036 5.75e-15

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: 79.47  E-value: 5.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDttleqILAAWSRGACVVarPDELLE 752
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpffHTFGYKAG-----IVACLLTGATVV--PVAVFD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  753 PQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWF-ELGLDrrcALINAYGPTEAT 831
Cdd:cd17638     78 VDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRsELGFE---TVLTAYGLTEAG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  832 ISShyhrvqaidASRP--------VPLGQLLPGRIAAVLDAhgrivprgvcGELALGGIGLAEGYRGDAAASERRFaplr 903
Cdd:cd17638    155 VAT---------MCRPgddaetvaTTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI---- 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  904 lpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECA 982
Cdd:cd17638    212 ----DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAqVAVIGVPDERMGEVGKAFVVAR 287
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246793773  983 GEDGFGQADLNQtdsdqteserWHRalcERLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:cd17638    288 PGVTLTEEDVIA----------WCR---ERLANYKVPRFVRFLDELPRNASGKV 328
PRK07798 PRK07798
acyl-CoA synthetase; Validated
533-1039 5.78e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 81.47  E-value: 5.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  533 TVGNVVDAIARAadeFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSV 612
Cdd:PRK07798     4 NIADLFEAVADA---VPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  613 IPLDTEWPQARRAEVVAASGCDAVLTDAQglagFAPSVAIAVDEL-KL-------DGAGENGSG---------ENAAPNQ 675
Cdd:PRK07798    81 VNVNYRYVEDELRYLLDDSDAVALVYERE----FAPRVAEVLPRLpKLrtlvvveDGSGNDLLPgavdyedalAAGSPER 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  676 LA--------YILYTSGSTGIPKGVEVGHA-ALAAHIDAAAEALALSADDRVLHVAGLAVD--------------TTLEQ 732
Cdd:PRK07798   157 DFgerspddlYLLYTGGTTGMPKGVMWRQEdIFRVLLGGRDFATGEPIEDEEELAKRAAAGpgmrrfpapplmhgAGQWA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  733 ILAAWSRGACVVARPDELLEPQRFLAFLS-ERAITVTDLAPAYANELVRASVADDWRDL-ALRCLVVGGDVLPVALAQRW 810
Cdd:PRK07798   237 AFAALFSGQTVVLLPDVRFDADEVWRTIErEKVNVITIVGDAMARPLLDALEARGPYDLsSLFAIASGGALFSPSVKEAL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  811 FELGLDRrcALINAYGPTEATISSHyhrvqAIDASRPVPLGQLL--PGRIAAVLDAHGRIVPRG--VCGELALGG-IGLa 885
Cdd:PRK07798   317 LELLPNV--VLTDSIGSSETGFGGS-----GTVAKGAVHTGGPRftIGPRTVVLDEDGNPVEPGsgEIGWIARRGhIPL- 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  886 eGYRGDAAASERRFaplrlPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAA 964
Cdd:PRK07798   389 -GYYKDPEKTAETF-----PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAdALVV 462
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773  965 GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRR 1039
Cdd:PRK07798   463 GVPDERWGQEVVAVVQLREGARPDLAEL--------------RAHCrSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
3524-3980 6.15e-15

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 81.46  E-value: 6.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3524 RFAEIARRYPARIAVSAEDG-----ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVP 3598
Cdd:PRK08180    44 RLVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3599 VDP------HAPAARR--------GFILEDSGvclSVSQRAL-AVELPGTALC-----LDDPFTRAQLDAVEPGELPEVP 3658
Cdd:PRK08180   124 VSPayslvsQDFGKLRhvlelltpGLVFADDG---AAFARALaAVVPADVEVVavrgaVPGRAATPFAALLATPPTAAVD 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3659 T-------EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDV------WSlfH----SHAFDFAVWel 3721
Cdd:PRK08180   201 AahaavgpDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVlvdwlpWN--HtfggNHNLGIVLY-- 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3722 WGAWLY--GGRAVlvpeavcrqPDAF---LDLLAEYGVTVLNQTPSAFYALqSQAMRRELAL------NVRAVVFGGEAL 3790
Cdd:PRK08180   277 NGGTLYidDGKPT---------PGGFdetLRNLREISPTVYFNVPKGWEML-VPALERDAALrrrffsRLKLLFYAGAAL 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPS---RLQPWRERYpQAELVNM---YGITETTVHVSF-HRlsdedlqsPTSR---IGSALPDLAVHVldaagqpVPLGV 3860
Cdd:PRK08180   347 SQDvwdRLDRVAEAT-CGERIRMmtgLGMTETAPSATFtTG--------PLSRagnIGLPAPGCEVKL-------VPVGG 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 VGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRY----RADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKI 3935
Cdd:PRK08180   411 KLEVRVKGPNVTPGYWRAPELTAEAFDEEG---YYRSGDAVRFvdpaDPERGLMFDGRIAEDFKLsSGTWVSVGPLRARA 487
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3936 ASL--PQVSDAAVTVEGQGE-GA--WLMAYAVAADGAEPDPQSLREALRA 3980
Cdd:PRK08180   488 VSAgaPLVQDVVITGHDRDEiGLlvFPNLDACRRLAGLLADASLAEVLAH 537
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
831-1120 6.69e-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: 78.64  E-value: 6.69e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  831 TISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESL 910
Cdd:COG3433      1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  911 RMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGFGQA 990
Cdd:COG3433     81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  991 DLNQTDsdqteserwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPPVLAQAERTPPRTAEESA-----LCE 1065
Cdd:COG3433    161 ALAALD--------------KVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRA 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1066 VWAEVLQC---EVGIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQYQSAAELA 1120
Cdd:COG3433    227 DVAELLGVdpeEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
3541-4005 6.74e-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: 81.18  E-value: 6.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3541 EDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTG--AAYVPvdphaPAARRGFIL---ED 3614
Cdd:cd05938      2 EGETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN-----TNIRSKSLLhcfRC 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3615 SG----------------VCLSVSQRALAV-------ELPGTAlCLDDPFTRAQLDAVePGELPEVPT-EAPAYLIYTSG 3670
Cdd:cd05938     77 CGakvlvvapelqeaveeVLPALRADGVSVwylshtsNTEGVI-SLLDKVDAASDEPV-PASLRAHVTiKSPALYIYTSG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3671 STGTPKGVVVTHrnvERLFTAATQTGRFSFDEHDV----WSLFHSHAFdfaVWELWGAWLYGGRAVLVPEAVCRQpdaFL 3746
Cdd:cd05938    155 TTGLPKAARISH---LRVLQCSGFLSLCGVTADDViyitLPLYHSSGF---LLGIGGCIELGATCVLKPKFSASQ---FW 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3747 DLLAEYGVTVL-----------NQTPSAfyalqsqamrRELALNVRAVVfgGEALepsRLQPWRE---RYPQAELVNMYG 3812
Cdd:cd05938    226 DDCRKHNVTVIqyigellrylcNQPQSP----------NDRDHKVRLAI--GNGL---RADVWREflrRFGPIRIREFYG 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3813 ITETTVhvSFHRLsdedlqspTSRIG-----SALPDLAVH-------------VLDAAGQ--PVPLGVVGELVVEgdgVA 3872
Cdd:cd05938    291 STEGNI--GFFNY--------TGKIGavgrvSYLYKLLFPfelikfdvekeepVRDAQGFciPVAKGEPGLLVAK---IT 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3873 Q-----GYWQRPELTAE---RFVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA 3944
Cdd:cd05938    358 QqspflGYAGDKEQTEKkllRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3945 ---AVTVEGQgEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:cd05938    438 nvyGVTVPGH-EGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQ 500
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1142-1558 8.54e-15

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: 81.83  E-value: 8.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQ----VAAPGPAPAIQA 1217
Cdd:COG1020     22 AAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQViqpvVAAPLPVVVLLV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHAHCDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTP 1297
Cdd:COG1020    102 DLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPL 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1298 SARGASYADYVEALREADDAQRFDAG----FWRELAAQPMQALPQDRPvaLADARQSNVGRIVQTLDAGLTADLLERAGE 1373
Cdd:COG1020    182 PPLPIQYADYALWQREWLQGEELARQlaywRQQLAGLPPLLELPTDRP--RPAVQSYRGARVSFRLPAELTAALRALARR 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1374 -----------AYrcrtdevllialaralatrtgrnRLWLDRERHGRDVL--------DGRDWSSVLGWYTAVHPLPLDL 1434
Cdd:COG1020    260 hgvtlfmvllaAF-----------------------ALLLARYSGQDDVVvgtpvagrPRPELEGLVGFFVNTLPLRVDL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1435 gvaDGPAQIGALKEQIRALARRGLDY--MP---LVASARIPALPAGQLLFNYHGVVDAGAHPAFEVEPRTLASGNGADNP 1509
Cdd:COG1020    317 ---SGDPSFAELLARVRETLLAAYAHqdLPferLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGT 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773 1510 PGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAH 1558
Cdd:COG1020    394 AKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2063-2522 2.76e-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: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 78.38  E-value: 2.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPldpqhpdARQIAVLDDSGARIVIGWGa 2142
Cdd:cd05974      2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------ATTLLTPDDLRDRVDRGGA- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2143 apawvpasvrwldaesvldVVSAYEEPPRvdvdADTPAYLIYTSGSTGTPKGVVVSQ-----GNLAN-YVAGVLPvldlg 2216
Cdd:cd05974     74 -------------------VYAAVDENTH----ADDPMLLYFTSGTTSKPKLVEHTHrsypvGHLSTmYWIGLKP----- 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2217 EDASLATLSTVAADLGFTALFGALLSGRRVRLLpAELAFDAQALAAHLQAHPVDCLKIVPS-HLAGLLAAAGGTAVLPRE 2295
Cdd:cd05974    126 GDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTvWRMLIQQDLASFDVKLRE 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 cLVTGGEALTGALVQQVRAlAPTLRIVNHYGPTETTVgiLTCTVPEEwPVEQGvPVGHPLAGNEAWVLDRFGLPAPvgvA 2375
Cdd:cd05974    205 -VVGAGEPLNPEVIEQVRR-AWGLTIRDGYGQTETTA--LVGNSPGQ-PVKAG-SMGRPLPGYRVALLDPDGAPAT---E 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGN-----LSLGYWQRAEQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQ 2450
Cdd:cd05974    276 GEVALDLGDtrpvgLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2451 VLAQLPGVEVAAV--------LALPGANGVLqlgacIQGSLEGVAEALA--QRLPEYLCP-SRWRAVE--SMPRLGNGKI 2517
Cdd:cd05974    349 VLIEHPAVAEAAVvpspdpvrLSVPKAFIVL-----RAGYEPSPETALEifRFSRERLAPyKRIRRLEfaELPKTISGKI 423

                   ....*
gi 1246793773 2518 DRQAL 2522
Cdd:cd05974    424 RRVEL 428
PRK07787 PRK07787
acyl-CoA synthetase; Validated
604-1044 3.22e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 78.49  E-value: 3.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  604 GAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVAIAVDelkldgAGENGSGENAAPNQLAYILYTS 683
Cdd:PRK07787    64 GALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPAGLPHVPVRLH------ARSWHRYPEPDPDAPALIVYTS 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  684 GSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDttleqILAAWSRGACVV--ARPDellePQR 755
Cdd:PRK07787   138 GTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVhglplfHVHGLVLG-----VLGPLRIGNRFVhtGRPT----PEA 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  756 FLAFLSERAiTVTDLAPAyanelVRASVADDwRDLAL-----RCLVVGGDVLPVALAQRWFELGLDRrcaLINAYGPTEA 830
Cdd:PRK07787   209 YAQALSEGG-TLYFGVPT-----VWSRIAAD-PEAARalrgaRLLVSGSAALPVPVFDRLAALTGHR---PVERYGMTET 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  831 TISShyhRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGV--CGELALGGIGLAEGYRGDAAASERRFAplrlPSGe 908
Cdd:PRK07787   279 LITL---STRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFT----ADG- 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  909 slrMYRSGDRVRLLDDGELQFLGRADFQ-VKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAA---QRLVAWVecAGE 984
Cdd:PRK07787   351 ---WFRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAA--VVGVPDDdlgQRIVAYV--VGA 423
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  985 DGFGQADLnqTDsdqteserwHRAlcERLPAYMVPTQFVALPRLPRNASGKIDRRALPAP 1044
Cdd:PRK07787   424 DDVAADEL--ID---------FVA--QQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
3539-4010 6.02e-14

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 78.29  E-value: 6.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3539 SAEDGELDYATLDRRSSQLATLLIRQ-GAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGV 3617
Cdd:PRK05620    33 GAEQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAED 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3618 CLSVSQRALAVEL-------PGTALCL---DDPFTRAQLDAVEPGEL----------------PEVPTEAPAYLIYTSGS 3671
Cdd:PRK05620   113 EVIVADPRLAEQLgeilkecPCVRAVVfigPSDADSAAAHMPEGIKVysyealldgrstvydwPELDETTAAAICYSTGT 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3672 TGTPKGVVVTHRNverLFTAAtqtgrFSFDEHDVWSLFHSHAFDFAV--WEL--WG----AWLYGGRAVLVPEAVcrQPD 3743
Cdd:PRK05620   193 TGAPKGVVYSHRS---LYLQS-----LSLRTTDSLAVTHGESFLCCVpiYHVlsWGvplaAFMSGTPLVFPGPDL--SAP 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3744 AFLDLLAEYGVTVLNQTPSAFYALQSQAMR---RELALnvRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITET---- 3816
Cdd:PRK05620   263 TLAKIIATAMPRVAHGVPTLWIQLMVHYLKnppERMSL--QEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETspvg 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3817 TVHVSFHRLSDE---DLQSPTSRIGSALPDLAV---HVLDAAGQPVplgvvGELVVEGDGVAQGYWQRPELT----AERF 3886
Cdd:PRK05620   340 TVARPPSGVSGEarwAYRVSQGRFPASLEYRIVndgQVMESTDRNE-----GEIQVRGNWVTASYYHSPTEEgggaASTF 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 ----VERGGQRF-----YRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAWL 3957
Cdd:PRK05620   415 rgedVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVI--GYPDDKWG 492
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3958 ---MAYAVAADGAEPD---PQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK05620   493 erpLAVTVLAPGIEPTretAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
2182-2517 7.80e-14

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: 76.00  E-value: 7.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2182 LIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTA-LFGALLSGRRVrlLPaELAFDAQAL 2260
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGATV--VP-VAVFDVDAI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2261 AAHLQAHPVDCLKIVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGilTCT 2338
Cdd:cd17638     82 LEAIERERITVLPGPPTlfQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA--TMC 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEEWPVEQGVPVGHPLAGNEAWVLDrfglpapvgvAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLYrSGDLA 2418
Cdd:cd17638    160 RPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDA-----DGWLH-TGDVG 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----GANG----VLQLGACIqgSLEGVAEAL 2490
Cdd:cd17638    224 ELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGkafvVARPGVTL--TEEDVIAWC 301
                          330       340
                   ....*....|....*....|....*..
gi 1246793773 2491 AQRLPEYLCPSRWRAVESMPRLGNGKI 2517
Cdd:cd17638    302 RERLANYKVPRFVRFLDELPRNASGKV 328
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
2325-2519 9.23e-14

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: 75.77  E-value: 9.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTvGILTCTVPEEWPVEqgvpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahp 2404
Cdd:cd17637    143 YGQTETS-GLVTLSPYRERPGS----AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---- 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2405 lapDRLLYRSGDLARLDGEGRIVYLGRGDHQ--VKIRGYRVELGEVEQVLAQLPGVEVAAVLALP------GANGVLQLG 2476
Cdd:cd17637    214 ---RNGWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPdpkwgeGIKAVCVLK 290
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 2477 ACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDR 2519
Cdd:cd17637    291 PGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
596-1041 9.53e-14

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 77.21  E-value: 9.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  596 LDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDA---------QGLAGFAPSVAIA----VDELKLDGA 662
Cdd:PRK06839    64 LEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKtfqnmalsmQKVSYVQRVISITslkeIEDRKIDNF 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  663 gENGSGENAApnqlaYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR------VLHVAGLAVDTtleqiLAA 736
Cdd:PRK06839   144 -VEKNESASF-----IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRsivllpLFHIGGIGLFA-----FPT 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  737 WSRGACVVArPDELlEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLd 816
Cdd:PRK06839   213 LFAGGVIIV-PRKF-EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGF- 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  817 rrcALINAYGPTEAT-----ISSHYHRVQAIDASRPVPLGQLlpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGD 891
Cdd:PRK06839   290 ---LFGQGFGMTETSptvfmLSEEDARRKVGSIGKPVLFCDY------ELIDENKNKVEVGEVGELLIRGPNVMKEYWNR 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  892 AAASErrfaplrlpsgESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGe 969
Cdd:PRK06839   361 PDATE-----------ETIQdgWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVA--VVG- 426
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  970 gaaQRLVAWVECAGedgfgQADLNQTDSDQTESERwhRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06839   427 ---RQHVKWGEIPI-----AFIVKKSSSVLIEKDV--IEHCRlFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
107-511 1.04e-13

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: 76.57  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  107 GHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIqgeDSVAAGGG--AAVESADLRGRGQDEIDALVEGFRLRPF 184
Cdd:cd19545     19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRI---VQSDSGGLlqVVVKESPISWTESTSLDEYLEEDRAAPM 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  185 ELQrQRPLRMQLLRldgqgDGPVRHWLQVVVHHIACDGVSLGLLTQDLSRAYRvecglaaEPAPPLPCQYGDYARWQRDT 264
Cdd:cd19545     96 GLG-GPLVRLALVE-----DPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ-------GEPVPQPPPFSRFVKYLRQL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  265 ldRLDASLRHHVEALSGAPHLHELPLDHERPAVLGQSGAKLRLAFPPGLSERV--AAYAQA------SRATafhvlqaaf 336
Cdd:cd19545    163 --DDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLEHSISLPSSASSGVtlATVLRAawalvlSRYT--------- 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  337 aallarcgAGDDLLIGTPVAGR---VrPELDSLVGLFVNTVVLRTQLHDDPDFASLVARCRDHQLAALEHQALPLERVie 413
Cdd:cd19545    232 --------GSDDVVFGVTLSGRnapV-PGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNI-- 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  414 tLQVERSSRHAPLFQLMFALRHDADLALDlhgvQAHALTLPEDVAKHE------LTLEVLVGAGGMSAvweynTALWNPA 487
Cdd:cd19545    301 -RRLGPDARAACNFQTLLVVQPALPSSTS----ESLELGIEEESEDLEdfssygLTLECQLSGSGLRV-----RARYDSS 370
                          410       420
                   ....*....|....*....|....*
gi 1246793773  488 TVARW-AERYFVALAAMLENPHEPA 511
Cdd:cd19545    371 VISEEqVERLLDQFEHVLQQLASAP 395
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1142-1374 1.09e-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: 76.69  E-value: 1.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WF---FDsaPAQPDrYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPA-PAI 1215
Cdd:cd19540      4 LSFAQQrlWFlnrLD--GPSAA-YNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEArPDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1216 QAQDwRGAADLDSRVDAAFAR---MQEATPLAGPLVALThahcDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARG 1292
Cdd:cd19540     81 TVVD-VTEDELAARLAEAARRgfdLTAELPLRARLFRLG----PDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1293 EA--WTPSArgASYADYV----EALREADDAQRFDA---GFWRE-LAAQPMQ-ALPQDRPVAladARQSNVGRIVQ-TLD 1360
Cdd:cd19540    156 RApdWAPLP--VQYADYAlwqrELLGDEDDPDSLAArqlAYWREtLAGLPEElELPTDRPRP---AVASYRGGTVEfTID 230
                          250
                   ....*....|....
gi 1246793773 1361 AGLTADLLERAGEA 1374
Cdd:cd19540    231 AELHARLAALAREH 244
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1598-1927 1.13e-13

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: 76.37  E-value: 1.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRGVLL-----ESLRGDGADPYFqqtvaELDGE-IDAAALAQAWQQTVRRQPMLRTAIVWEGlsvpHQIVLADA 1671
Cdd:cd19535      2 FPLTDVQYAYWIgrqddQELGGVGCHAYL-----EFDGEdLDPDRLERAWNKLIARHPMLRAVFLDDG----TQQILPEV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1672 AAP-WQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQR 1750
Cdd:cd19535     73 PWYgITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAAL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1751 YtagaQGATLRLPPAP-GFQAYL-DWRERQDLARQRG--WWRERLS---GYAGTAALPAPVAAAHHPVQReeCERRLSAH 1823
Cdd:cd19535    153 Y----EDPGEPLPPLElSFRDYLlAEQALRETAYERAraYWQERLPtlpPAPQLPLAKDPEEIKEPRFTR--REHRLSAE 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1824 DSERLRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGATRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLL 1903
Cdd:cd19535    227 QWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERA 306
                          330       340
                   ....*....|....*....|....
gi 1246793773 1904 SALRSQSLEVAENEAVGLGEILAD 1927
Cdd:cd19535    307 RRLQQQLWEDLDHSSYSGVVVVRR 330
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3521-4006 1.23e-13

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 78.08  E-value: 1.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3521 LVSRFAEIARRYPARiAVSAEDGE---LDYATLDRRSSQLATLLiRQGAGPGQRVGLCLPRGCDLLVALLAILKTGaaYV 3597
Cdd:PRK06814   633 LFEALIEAAKIHGFK-KLAVEDPVngpLTYRKLLTGAFVLGRKL-KKNTPPGENVGVMLPNANGAAVTFFALQSAG--RV 708
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3598 P-----------VDPHAPAAR-------RGFI----LEDSGVCLSVSQRALAVELPGTALCLDDpftraQLDAVEPGELP 3655
Cdd:PRK06814   709 PaminfsagianILSACKAAQvktvltsRAFIekarLGPLIEALEFGIRIIYLEDVRAQIGLAD-----KIKGLLAGRFP 783
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3656 EVPT-----EAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHD----VWSLFHShaFDFAVWELWGAwL 3726
Cdd:PRK06814   784 LVYFcnrdpDDPAVILFTSGSEGTPKGVVLSHRNL--LANRAQVAARIDFSPEDkvfnALPVFHS--FGLTGGLVLPL-L 858
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3727 YGGRAVL---------VPEAVCRQ-------PDAFLDLLAEYGvtvlnqTPSAFYALqsqamrrelalnvRAVVFGGEAL 3790
Cdd:PRK06814   859 SGVKVFLypsplhyriIPELIYDTnatilfgTDTFLNGYARYA------HPYDFRSL-------------RYVFAGAEKV 919
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3791 EPSRLQPWRERYpQAELVNMYGITETTVHVSfhrlsdedLQSPT-SRIGSA---LPDlavhvLDAAGQPVPlGVV--GEL 3864
Cdd:PRK06814   920 KEETRQTWMEKF-GIRILEGYGVTETAPVIA--------LNTPMhNKAGTVgrlLPG-----IEYRLEPVP-GIDegGRL 984
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3865 VVEGDGVAQGYwqrpeLTAER--FVERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASL-PQV 3941
Cdd:PRK06814   985 FVRGPNVMLGY-----LRAENpgVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDA 1059
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3942 SDAAVTVEGQGEGAWLMAYAVAADGAEPDPQslREALRALLPDYMLPRLIQLLPALPLTANGKLD 4006
Cdd:PRK06814  1060 LHAAVSIPDARKGERIILLTTASDATRAAFL--AHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
2152-2479 1.33e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 77.15  E-value: 1.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2152 RWLDAESVLDVVSAYEEpprvdvdadtpAYLI-YTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAAD 2230
Cdd:PLN02860   157 QRALGTTELDYAWAPDD-----------AVLIcFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHI 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2231 LGFTALFGALLSGRRVRLLP---AELAFDAQALAAhlqahpVDCLKIVP-------SHLAGLLAAAGGTAVLPrecLVTG 2300
Cdd:PLN02860   226 GGLSSALAMLMVGACHVLLPkfdAKAALQAIKQHN------VTSMITVPammadliSLTRKSMTWKVFPSVRK---ILNG 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNHYGPTET-------TVGILTCTVPEEWPVE------------QGVPVGHPLAGNEAw 2361
Cdd:PLN02860   297 GGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmTLHDPTLESPKQTLQTvnqtksssvhqpQGVCVGKPAPHVEL- 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2362 vldRFGLPAPVGVaGELYLGGGNLSLGYWQRAEQTAErfvahpLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:PLN02860   376 ---KIGLDESSRV-GRILTRGPHVMLGYWGQNSETAS------VLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGE 445
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI 2479
Cdd:PLN02860   446 NVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV 483
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1604-1919 1.71e-13

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: 76.15  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1604 QRGVLLESLRGDGAdPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGlSVPHQIVLADAAApwqTLDWSAL 1683
Cdd:cd19538      9 RRLWFLHQLEGPSA-TYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED-GVPYQLILEEDEA---TPKLEIK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1684 DdaAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQGATLRLP 1763
Cdd:cd19538     84 E--VDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1764 PAP-GFQAYLDWRERQ---------DLARQRGWWRERLsgyAGTAALPAPVAAAHHPVQREECERRLS----AHDSERLR 1829
Cdd:cd19538    162 PLPvQYADYALWQQELlgdesdpdsLIARQLAYWKKQL---AGLPDEIELPTDYPRPAESSYEGGTLTfeidSELHQQLL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1830 AFCRERGCTLsdliAMVW--GLAN--ARYGNHDDVVLGATRSGRppELAGVESMVGVFINTLPlrLRID-AGQPA-LDLL 1903
Cdd:cd19538    239 QLAKDNNVTL----FMVLqaGFAAllTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLV--LRTDtSGNPSfRELL 310
                          330
                   ....*....|....*.
gi 1246793773 1904 SALRSQSLEVAENEAV 1919
Cdd:cd19538    311 ERVKETNLEAYEHQDI 326
PRK06178 PRK06178
acyl-CoA synthetase; Validated
612-1041 1.90e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 76.62  E-value: 1.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  612 VIPLDTEWPQAR--RAEV----VAASGCDAVLTDA------QGLAGFAPSVAIAVDELK-LDGAGENGSGENAAPNQLAY 678
Cdd:PRK06178   134 LLALDQLAPVVEqvRAETslrhVIVTSLADVLPAEptlplpDSLRAPRLAAAGAIDLLPaLRACTAPVPLPPPALDALAA 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL-------HVAGlaVDTTLeqILAAWSrGACVV--ARPDe 749
Cdd:PRK06178   214 LNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFlsflpefWIAG--ENFGL--LFPLFS-GATLVllARWD- 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  750 llePQRFLAFLSERAITVTDLAPAYANELVRASvadDWRDLALRCLVVGGDV-----LPVALAQRWFEL-GLDRRCAlin 823
Cdd:PRK06178   288 ---AVAFMAAVERYRVTRTVMLVDNAVELMDHP---RFAEYDLSSLRQVRVVsfvkkLNPDYRQRWRALtGSVLAEA--- 358
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  824 AYGPTEATISSHYHR-VQAID---ASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASerr 898
Cdd:PRK06178   359 AWGMTETHTCDTFTAgFQDDDfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEAT--- 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  899 faplrlpsGESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVG---EGAAQ 973
Cdd:PRK06178   436 --------AEALRdgWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAV--LGSAVVGrpdPDKGQ 505
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  974 RLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFVaLPRLPRNASGKIDRRAL 1041
Cdd:PRK06178   506 VPVAFVQLKPGADLTAAAL--------------QAWCrENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
3542-4012 2.10e-13

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: 75.92  E-value: 2.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3542 DGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAyvpvdphAPAARRGFILEDSGVCLSV 3621
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVE-------TALINSNLRLESLLHCITV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3622 SQ-RALAVELpgtalcLDDPFTRAQLdavEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHrnVERLFTAATQTGRFSF 3700
Cdd:cd05939     74 SKaKALIFNL------LDPLLTQSST---EPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVH--SRYYRIAAGAYYAFGM 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3701 DEHDVW----SLFHSHAFDFAVwelwGAWLYGGRAVlvpeaVCRQ---PDAFLDLLAEYGVTV-----------LNQTPS 3762
Cdd:cd05939    143 RPEDVVydclPLYHSAGGIMGV----GQALLHGSTV-----VIRKkfsASNFWDDCVKYNCTIvqyigeicrylLAQPPS 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3763 afyalqsqamRRELALNVRAVVfgGEALEPSRLQPWRERYPQAELVNMYGITETTVHVSFHrlsDEDLQSP--TSRIGSA 3840
Cdd:cd05939    214 ----------EEEQKHNVRLAV--GNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNI---DNHVGACgfNSRILPS 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3841 L-PDLAVHVLDAAGQPV--PLGVV--------GELV---VEGDGVAQ--GYWQRPElTAE---RFVERGGQRFYRSGDLG 3901
Cdd:cd05939    279 VyPIRLIKVDEDTGELIrdSDGLCipcqpgepGLLVgkiIQNDPLRRfdGYVNEGA-TNKkiaRDVFKKGDSAFLSGDVL 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3902 RYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV-TVE-GQGEGAWLMAyAVAADGAEPDPQSLREALR 3979
Cdd:cd05939    358 VMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVyGVEvPGVEGRAGMA-AIVDPERKVDLDRFSAVLA 436
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1246793773 3980 ALLPDYMLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:cd05939    437 KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
2176-2523 2.28e-13

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: 75.59  E-value: 2.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLP-VLDLGEDASLATLstvaADLGFTALFGALL-----SGRRVRLL 2249
Cdd:cd05958     96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVnVLRLREDDRFVGS----PPLAFTFGLGGVLlfpfgVGASGVLL 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 PAELAFDaqALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLP--REClVTGGEALTGALVQQVRAlAPTLRIVNHYGP 2327
Cdd:cd05958    172 EEATPDL--LLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSslRKC-VSAGEALPAALHRAWKE-ATGIPIIDGIGS 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2328 TETTVGILTCTVPEEWPVEQGVPVghplAGNEAWVLDRFGLPAPVGVAGELYLGGgnlSLGYWQRAEQTAERFVAhplap 2407
Cdd:cd05958    248 TEMFHIFISARPGDARPGATGKPV----PGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQ----- 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2408 DRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI-----QGS 2482
Cdd:cd05958    316 GGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVvlrpgVIP 394
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773 2483 LEGVAEALAQRLPEYLCPSRW-RAVE---SMPRLGNGKIDRQALA 2523
Cdd:cd05958    395 GPVLARELQDHAKAHIAPYKYpRAIEfvtELPRTATGKLQRFALR 439
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1143-1327 3.06e-13

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: 75.03  E-value: 3.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1143 SPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASF-ERADGQWRQQVAAPGPapaiqaQDWR 1221
Cdd:cd19545      5 TPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESP------ISWT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1222 GAADLDSRVDAAfarMQEATPLAGPLVALTHAHCDDGER-LLICAHHLIVDAVSWRLLLGELfdgLAALARgeawTPSAR 1300
Cdd:cd19545     79 ESTSLDEYLEED---RAAPMGLGGPLVRLALVEDPDTERyFVWTIHHALYDGWSLPLILRQV---LAAYQG----EPVPQ 148
                          170       180
                   ....*....|....*....|....*..
gi 1246793773 1301 GASYADYVEALREADDAQRfdAGFWRE 1327
Cdd:cd19545    149 PPPFSRFVKYLRQLDDEAA--AEFWRS 173
PRK06164 PRK06164
acyl-CoA synthetase; Validated
529-1062 3.88e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 75.55  E-value: 3.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  529 PAPRTVGNVVDAIARAAdefPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRA 608
Cdd:PRK06164     7 PRADTLASLLDAHARAR---PDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  609 GLSVIPLDTEWPQARRAEVVAASGCD----------------------AVLTDAQGLAGF--------APSVAIAVDELK 658
Cdd:PRK06164    84 GATVIAVNTRYRSHEVAHILGRGRARwlvvwpgfkgidfaailaavppDALPPLRAIAVVddaadatpAPAPGARVQLFA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  659 L-DGAGENGSGENAAPNQLAYILY-TSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAA 736
Cdd:PRK06164   164 LpDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  737 WSRGACVVARPdeLLEPQRFLAFLSERAITVTdlapAYANELVR--ASVADDWRDLALRCLVVGGDVLPvalaqRWFEL- 813
Cdd:PRK06164   244 LAGGAPLVCEP--VFDAARTARALRRHRVTHT----FGNDEMLRriLDTAGERADFPSARLFGFASFAP-----ALGELa 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  814 --GLDRRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLL--PGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYR 889
Cdd:PRK06164   313 alARARGVPLTGLYGSSEVQALVALQPATDPVSVRIEGGGRPAspEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYL 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  890 GDAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGE 969
Cdd:PRK06164   393 DNPDATARALT----DDG----YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  970 GAAQRLVAWVEcagedgfgqadlnQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASG---KIDRRALPAppv 1046
Cdd:PRK06164   465 DGKTVPVAFVI-------------PTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE--- 528
                          570
                   ....*....|....*.
gi 1246793773 1047 LAQAertppRTAEESA 1062
Cdd:PRK06164   529 MAQA-----RLAAERA 539
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
2084-2426 4.73e-13

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 75.54  E-value: 4.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2084 QPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL-DPQHPD--ARQIAVLDDSGARIVIGWGAAPAWVPASVRWLDA---- 2156
Cdd:PRK07769    77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGhvGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAkerp 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2157 -----ESVLDVVSAYEEPPrvDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADL 2231
Cdd:PRK07769   157 rviavDAVPDEVGATWVPP--EANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDM 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2232 GF-TALFGALLSGRRVRLLPA-----------ELAFDAQALAAHLQAHPvdclKIVPSHLAGLLaaaggtavLPRE---- 2295
Cdd:PRK07769   235 GLiTVLLPALLGHYITFMSPAafvrrpgrwirELARKPGGTGGTFSAAP----NFAFEHAAARG--------LPKDgepp 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2296 -------CLVTGGEALTGALVQQV-RALAP-TLR---IVNHYGPTETTVGILTCTVPEE----------------WPVEQ 2347
Cdd:PRK07769   303 ldlsnvkGLLNGSEPVSPASMRKFnEAFAPyGLPptaIKPSYGMAEATLFVSTTPMDEEptviyvdrdelnagrfVEVPA 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVP--VGHPLAGNEA---W---VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERF---VAHPLAP--------D 2408
Cdd:PRK07769   383 DAPnaVAQVSAGKVGvseWaviVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdD 462
                          410       420
                   ....*....|....*....|...
gi 1246793773 2409 RLLYRSGDL-ARLDGE----GRI 2426
Cdd:PRK07769   463 ALWVRTGDYgVYFDGElyitGRV 485
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
2136-2530 5.10e-13

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: 75.43  E-value: 5.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2136 IVIGWGAAPAWVPASVRWLDAESVLdvvSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLA---NY------- 2205
Cdd:cd05967    192 LVLNRPQVPADLTKPGRDLDWSELL---AKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAvalNWsmrniyg 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2206 ---------------------------VAGVLPVLDLGE-----DASlaTLSTVAADLGFTALFGALLSGRRVRLLPAEL 2253
Cdd:cd05967    269 ikpgdvwwaasdvgwvvghsyivygplLHGATTVLYEGKpvgtpDPG--AFWRVIEKYQVNALFTAPTAIRAIRKEDPDG 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2254 AFdaqalaahLQAHPVDCLKIvpshlagllaaaggtavlprecLVTGGEALTGALVQQVRALAPTLrIVNHYGPTETTVG 2333
Cdd:cd05967    347 KY--------IKKYDLSSLRT----------------------LFLAGERLDPPTLEWAENTLGVP-VIDHWWQTETGWP 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2334 ILT-CTVPEEWPVEQGVPvGHPLAGNEAWVLDRFGLPAPVGVAGELYLGG----GNLsLGYWQraeqTAERFVAHPLAPD 2408
Cdd:cd05967    396 ITAnPVGLEPLPIKAGSP-GKPVPGYQVQVLDEDGEPVGPNELGNIVIKLplppGCL-LTLWK----NDERFKKLYLSKF 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2409 RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGA-NGVLQLGACI-QGSLEGV 2486
Cdd:cd05967    470 PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGLVVlKEGVKIT 549
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2487 AEALAQRLPEYL--------CPSRWRAVESMPRLGNGKIDRQALADLLQQDD 2530
Cdd:cd05967    550 AEELEKELVALVreqigpvaAFRLVIFVKRLPKTRSGKILRRTLRKIADGED 601
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
539-1038 5.25e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 75.19  E-value: 5.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  539 DAIARAADEFPERAAL---ETAQgRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPL 615
Cdd:PRK12583    22 DAFDATVARFPDREALvvrHQAL-RYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  616 DtewPQARRAEVVAA---SGCDAVLTdaqgLAGFAPSVAIA-----VDELKLDGAGENGS------------GENAAPNQ 675
Cdd:PRK12583   101 N---PAYRASELEYAlgqSGVRWVIC----ADAFKTSDYHAmlqelLPGLAEGQPGALACerlpelrgvvslAPAPPPGF 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  676 LAY-----------------------------ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------H 720
Cdd:PRK12583   174 LAWhelqargetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvpvplyH 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  721 VAGLAVDTtleqiLAAWSRGACVVArPDELLEPQRFL-AFLSERAITVTDLAPAYANELVRASVADdwRDL-ALRCLVVG 798
Cdd:PRK12583   254 CFGMVLAN-----LGCMTVGACLVY-PNEAFDPLATLqAVEEERCTALYGVPTMFIAELDHPQRGN--FDLsSLRTGIMA 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  799 GDVLPVALAQRWFElglDRRCALIN-AYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGEL 877
Cdd:PRK12583   326 GAPCPIEVMRRVMD---EMHMAEVQiAYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGEL 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  878 ALGGIGLAEGYRGDAAASerrfaplRLPSGESLRMYrSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLP 957
Cdd:PRK12583   403 CTRGYSVMKGYWNNPEAT-------AESIDEDGWMH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHP 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  958 QVRAAAA-GVVGEGAAQRLVAWVECAGedgfGQAdlnqtdSDQTESERWHRAlceRLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:PRK12583   475 AVADVQVfGVPDEKYGEEIVAWVRLHP----GHA------ASEEELREFCKA---RIAHFKVPRYFRFVDEFPMTVTGKV 541

                   ..
gi 1246793773 1037 DR 1038
Cdd:PRK12583   542 QK 543
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
677-1041 5.99e-13

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: 74.31  E-value: 5.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  677 AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQILAAWSrgACVVARPDEl 750
Cdd:cd05912     80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLcalplfHISGLSI--LMRSVIYGMT--VYLVDKFDA- 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  751 lepQRFLAFLSERAITVTDLAPAYANELvrASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPTE- 829
Cdd:cd05912    155 ---EQVLHLINSGKVTIISVVPTMLQRL--LEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGI----PVYQSYGMTEt 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  830 ----ATISSHYHRVQAIDASRPVPLGQLlpgRIAavldaHGRIVPRGVcGELALGGIGLAEGYRGDAAASERRFAplrlp 905
Cdd:cd05912    226 csqiVTLSPEDALNKIGSAGKPLFPVEL---KIE-----DDGQPPYEV-GEILLKGPNVTKGYLNRPDATEESFE----- 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  906 SGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAA---QRLVAWVECA 982
Cdd:cd05912    292 NG----WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI--KEAGVVGIPDDkwgQVPVAFVVSE 365
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  983 GEdgFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05912    366 RP--ISEEEL--------------IAYCsEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
3655-3976 6.53e-13

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: 74.94  E-value: 6.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3655 PEVPT-EAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAA--TQTGRFSFDEHDVWSLF--HSHAFDFAVweLWGAWLYGG 3729
Cdd:cd05927    108 PPPPKpEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkILEILNKINPTDVYISYlpLAHIFERVV--EALFLYHGA 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3730 R---------------AVLVPEAVCRQPDAFLDLLAEYGVTVLNQTP-----------SAFYALQSQAMRRE-------- 3775
Cdd:cd05927    186 KigfysgdirlllddiKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPlkrklfnfalnYKLAELRSGVVRASpfwdklvf 265
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3776 ------LALNVRAVVFGGEALEPSRLQPWRErYPQAELVNMYGITETTVHVSFHRLSDEDlqspTSRIGSALPDLAVHVL 3849
Cdd:cd05927    266 nkikqaLGGNVRLMLTGSAPLSPEVLEFLRV-ALGCPVLEGYGQTECTAGATLTLPGDTS----VGHVGGPLPCAEVKLV 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3850 DA------AGQPVPlgvVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-R 3922
Cdd:cd05927    341 DVpemnydAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEALDEDG---WLHTGDIGEWLPNGTLKIIDRKKNIFKLsQ 414
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 3923 GYRIEPGEIAAKIASLPQVSDaaVTVEGQGEGAWLMAYAVaadgaePDPQSLRE 3976
Cdd:cd05927    415 GEYVAPEKIENIYARSPFVAQ--IFVYGDSLKSFLVAIVV------PDPDVLKE 460
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
2053-2517 8.60e-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: 74.26  E-value: 8.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2053 VAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHpDARQIAV-LDD 2131
Cdd:cd12118     21 TSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL-DAEEIAFiLRH 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgaapawvpasvrwldaesvLDVVSAYEE---------PPRVDVDADTPAYLIYTSGSTGTPKGVVVSqgNL 2202
Cdd:cd12118    100 SEAKVLF---------------------VDREFEYEDllaegdpdfEWIPPADEWDPIALNYTSGTTGRPKGVVYH--HR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 ANYVAGVLPVLDLGEDASLATLSTV----AADLGF----TALFGALLSGRRVRllpAELAFDAQALAAhlqahpVDCLKI 2274
Cdd:cd12118    157 GAYLNALANILEWEMKQHPVYLWTLpmfhCNGWCFpwtvAAVGGTNVCLRKVD---AKAIYDLIEKHK------VTHFCG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2275 VPS-HLAGLLAAAGGTAVLPRECLV-TGGEALTGALVQQVRALAptLRIVNHYGPTETTVGILTCTVPEEW---PVE--- 2346
Cdd:cd12118    228 APTvLNMLANAPPSDARPLPHRVHVmTAGAPPPAAVLAKMEELG--FDVTHVYGLTETYGPATVCAWKPEWdelPTEera 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2347 -----QGVPVghpLAGNEAWVLDRFGL---PAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLA 2418
Cdd:cd12118    306 rlkarQGVRY---VGLEEVDVLDPETMkpvPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAFRGG-------WFHSGDLA 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIvylgrgdhQVKIR--------GYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIQGs 2482
Cdd:cd12118    376 VIHPDGYI--------EIKDRskdiiisgGENISSVEVEGVLYKHPAVLEAAVVARPDekwgevpcAFVELKEGAKVTE- 446
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1246793773 2483 lEGVAEALAQRLPEYLCPsrwRAVE--SMPRLGNGKI 2517
Cdd:cd12118    447 -EEIIAFCREHLAGFMVP---KTVVfgELPKTSTGKI 479
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
3930-4004 9.29e-13

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: 66.03  E-value: 9.29e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3930 EIAAKIASLPQVSDAAVT-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGK 4004
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVgVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
602-1036 9.43e-13

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 74.43  E-value: 9.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  602 LLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQgLAGFAPSVAIAVDELKL----DGAGENGS-------GEN 670
Cdd:PRK07786    84 VLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA-LAPVATAVRDIVPLLSTvvvaGGSSDDSVlgyedllAEA 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  671 AAPNQL--------AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRV-------LHVAGLAvdttleQILA 735
Cdd:PRK07786   163 GPAHAPvdipndspALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgfvgvplFHIAGIG------SMLP 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  736 AWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDLALRCLVVGGDVLPVALAQRWFELGL 815
Cdd:PRK07786   237 GLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTLLRQMAATFP 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  816 DrrCALINAYGPTEatISSHYHRVQAIDASRPV-PLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAA 894
Cdd:PRK07786   316 E--AQILAAFGQTE--MSPVTCMLLGEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEA 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  895 SERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQr 974
Cdd:PRK07786   392 TAEAFA-----GG----WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVA--VIGRADEK- 459
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773  975 lvaWvecaGEDGFGQADLNQTDSDQT--ESERWhraLCERLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:PRK07786   460 ---W----GEVPVAVAAVRNDDAALTleDLAEF---LTDRLARYKHPKALEIVDALPRNPAGKV 513
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
87-294 1.13e-12

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: 73.44  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   87 PAPLSLGQErlWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLD-RCIQGEDSV------AAGGGAAV 159
Cdd:cd19534      1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRmRFRREDGGWqqrirgDVEELFRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  160 ESADLRGRGQDE-IDALVEGFRlRPFELQRQRPLRMQLLRLDGQGDgpvRHWLqvVVHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19534     79 EVVDLSSLAQAAaIEALAAEAQ-SSLDLEEGPLLAAALFDGTDGGD---RLLL--VIHHLVVDGVSWRILLEDLEAAYE- 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  239 ecGLAAEPAPPLP--CQYGDYARWQRD--TLDRLDASLRHHVEALsgAPHLHELPLDHER 294
Cdd:cd19534    152 --QALAGEPIPLPskTSFQTWAELLAEyaQSPALLEELAYWRELP--AADYWGLPKDPEQ 207
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
679-1038 1.16e-12

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: 72.68  E-value: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTtleqILAAWSR------GACVVARpdELLE 752
Cdd:cd17635      6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHI----GGLWWILtclihgGLCVTGG--ENTT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  753 PQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDvLPVALAQRWFELGLDRRCAliNAYGPTEATI 832
Cdd:cd17635     80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS-RAIAADVRFIEATGLTNTA--QVYGLSETGT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  833 SS--HYHRvQAIDASrpvPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDaaaserrfaPLRLPSGESL 910
Cdd:cd17635    157 ALclPTDD-DSIEIN---AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNN---------PERTAEVLID 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  911 RMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDgfgq 989
Cdd:cd17635    224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQeCACYEISDEEFGELVGLAVVASAEL---- 299
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773  990 aDLNQTdSDQTESERwhralcERLPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd17635    300 -DENAI-RALKHTIR------RELEPYARPSTIVIVTDIPRTQSGKVKR 340
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
3646-3946 1.47e-12

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: 73.61  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 LDAVEPG----ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVerlftAATQTGRFSFDEHdvwslfhsHAFDFAVWEL 3721
Cdd:cd17641    140 LDRRDPGlyerEVAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNF-----LGHCAAYLAADPL--------GPGDEYVSVL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3722 WGAW-----------LYGGRAVLVPEAVCR--------QPDAFL----------------------------DLLAEYGV 3754
Cdd:cd17641    207 PLPWigeqmysvgqaLVCGFIVNFPEEPETmmedlreiGPTFVLlpprvwegiaadvrarmmdatpfkrfmfELGMKLGL 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3755 TVLNQTPSA-------------FYALQSQAMRRELAL-NVRAVVFGGEALEPSRLqpwreRYPQAELVNM---YGITETT 3817
Cdd:cd17641    287 RALDRGKRGrpvslwlrlaswlADALLFRPLRDRLGFsRLRSAATGGAALGPDTF-----RFFHAIGVPLkqlYGQTELA 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3818 VHVSFHRLSDEDLQSptsrIGSALPDLAVHVLDaagqpvplgvVGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRS 3897
Cdd:cd17641    362 GAYTVHRDGDVDPDT----VGVPFPGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDG---WLHT 424
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3898 GDLGRYRADGSLEYRGRGDDQVKL-RGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:cd17641    425 GDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVV 474
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
3663-3931 1.57e-12

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: 73.29  E-value: 1.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKGVVVTHRN-VERLFTAATQTGRFSFDEHDVWsLFHSHAFDFAVWELwgAWLYGG-RAVLVPEAV-C 3739
Cdd:cd05908    109 AFIQFSSGSTGDPKGVMLTHENlVHNMFAILNSTEWKTKDRILSW-MPLTHDMGLIAFHL--APLIAGmNQYLMPTRLfI 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3740 RQPDAFLDLLAEYGVTVLNqTPSAFYALQSQAMRRELALN-----VRAVVFGGEALEP-------SRLQPWRERypQAEL 3807
Cdd:cd05908    186 RRPILWLKKASEHKATIVS-SPNFGYKYFLKTLKPEKANDwdlssIRMILNGAEPIDYelcheflDHMSKYGLK--RNAI 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3808 VNMYGITETTVHVSFHRLsDEDLQSPT-------------------------SRIGSALPDLAVHVLDAAGQPVPLGVVG 3862
Cdd:cd05908    263 LPVYGLAEASVGASLPKA-QSPFKTITlgrrhvthgepepevdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIG 341
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3863 ELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRaDGSLEYRGRGDDQVKLRGYRIEPGEI 3931
Cdd:cd05908    342 HIQIRGKNVTPGYYNNPEATAKVFTDDG---WLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDI 406
PRK06188 PRK06188
acyl-CoA synthetase; Validated
535-1045 1.79e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 73.48  E-value: 1.79e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  535 GNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIP 614
Cdd:PRK06188    12 ATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  615 LDTEWPQARRAEVVAASGCDAVLTD-------AQGLAGFAPS---------VAIAVDELKLDGAGENGSGENAA-PNQLA 677
Cdd:PRK06188    92 LHPLGSLDDHAYVLEDAGISTLIVDpapfverALALLARVPSlkhvltlgpVPDGVDLLAAAAKFGPAPLVAAAlPPDIA 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  678 YILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLeqilaawSRGACVVARPDelL 751
Cdd:PRK06188   172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLmctplsHAGGAFFLPTL-------LRGGTVIVLAK--F 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  752 EPQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDL-ALRCLVVGGD-VLPVALAQrwfelGLDR-RCALINAYGPT 828
Cdd:PRK06188   243 DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT-RDLsSLETVYYGASpMSPVRLAE-----AIERfGPIFAQYYGQT 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  829 EATISSHYHRVQAIDASRPVPL---GQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPLRLp 905
Cdd:PRK06188   317 EAPMVITYLRKRDHDPDDPKRLtscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWL- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  906 sgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGegaaqrlvawvecAGED 985
Cdd:PRK06188   396 --------HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV--AQVAVIG-------------VPDE 452
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773  986 GFGQA----DLNQTDSDQTESErWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRALPAPP 1045
Cdd:PRK06188   453 KWGEAvtavVVLRPGAAVDAAE-LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
2061-2524 2.04e-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: 72.85  E-value: 2.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIg 2139
Cdd:cd05937      5 TWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 wgaapawvpasvrwldaesvldvvsayeepprvdVDADTPAYLIYTSGSTGTPKGVVVSqgNLANYVAGVLPVLDLGEDA 2219
Cdd:cd05937     84 ----------------------------------VDPDDPAILIYTSGTTGLPKAAAIS--WRRTLVTSNLLSHDLNLKN 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLSTVA---ADLGFTALFGALLSGRRVRLLPaelafdaqalaahlqahpvdclKIVPSHLAGLLAAAGGTAVL---- 2292
Cdd:cd05937    128 GDRTYTCMPlyhGTAAFLGACNCLMSGGTLALSR----------------------KFSASQFWKDVRDSGATIIQyvge 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 --------PRE-------CLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGILTCTVPE-------------EWP 2344
Cdd:cd05937    186 lcryllstPPSpydrdhkVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVGDfgagaighhglirRWK 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2345 VE-QGVPVGHPLAGNEAWVLDR--FGLPAPVGVAGELY--LGGGNLSL--GYWQRAEQTAERFVAHPLAPDRLLYRSGDL 2417
Cdd:cd05937    266 FEnQVVLVKMDPETDDPIRDPKtgFCVRAPVGEPGEMLgrVPFKNREAfqGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2418 ARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAV--LALPGANGVLQLGACI--QGSLEGVAEALA-- 2491
Cdd:cd05937    346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITleESSAVPTEFTKSll 425
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1246793773 2492 -----QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:cd05937    426 aslarKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
PRK07638 PRK07638
acyl-CoA synthetase; Validated
537-1041 2.77e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 72.50  E-value: 2.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  537 VVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARsVALCLPRGLDWYCLLLGAWRAGLSVIPLD 616
Cdd:PRK07638     3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  617 TEWPQARRAEVVAASGCDAVLTDAQGLAGF--APSVAIAVDELK--LDGAGENGSGENAAPNQLAYILYTSGSTGIPKGV 692
Cdd:PRK07638    82 IKWKQDELKERLAISNADMIVTERYKLNDLpdEEGRVIEIDEWKrmIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  693 EVGHAALAAHIDAAAEALALSADDRVLhVAGLAVDTT-LEQILAAWSRGACVVARPDelLEPQRFLAFLSERAITVTDLA 771
Cdd:PRK07638   162 LRAQQSWLHSFDCNVHDFHMKREDSVL-IAGTLVHSLfLYGAISTLYVGQTVHLMRK--FIPNQVLDKLETENISVMYTV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  772 PAYANELVRasvADDWRDLALRCLVVGGDVLPVA---LAQRWFELgldrrcALINAYGPTEATISSHYHRVQAidASRPV 848
Cdd:PRK07638   239 PTMLESLYK---ENRVIENKMKIISSGAKWEAEAkekIKNIFPYA------KLYEFYGASELSFVTALVDEES--ERRPN 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  849 PLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAaserrfAPLRLPSGESLRMYRSG--DRvrlldDGE 926
Cdd:PRK07638   308 SVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGV------LARELNADGWMTVRDVGyeDE-----EGF 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  927 LQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVEcagedgfGQADLNQTdsdqteserw 1005
Cdd:PRK07638   377 IYIVGREKNMILFGGINIFPEEIESVLHEHPAVdEIVVIGVPDSYWGEKPVAIIK-------GSATKQQL---------- 439
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1246793773 1006 hRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK07638   440 -KSFClQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1170-1327 2.89e-12

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: 72.14  E-value: 2.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1170 QPLDAQHLAQVWDALWRRHDLLRASFErADGQwrQQVAAPGPAPAIQAQDWRGAADLDsrVDAAFARMQEAT------PL 1243
Cdd:cd19535     35 EDLDPDRLERAWNKLIARHPMLRAVFL-DDGT--QQILPEVPWYGITVHDLRGLSEEE--AEAALEELRERLshrvldVE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1244 AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGElfdgLAALARGEAWTPSARGASYADYVEALREADDAQR-FD 1321
Cdd:cd19535    110 RGPLFDIRLSLLPEGRtRLHLSIDLLVADALSLQILLRE----LAALYEDPGEPLPPLELSFRDYLLAEQALRETAYeRA 185

                   ....*.
gi 1246793773 1322 AGFWRE 1327
Cdd:cd19535    186 RAYWQE 191
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2168-2536 3.44e-12

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 73.08  E-value: 3.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2168 EPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGedaslatlstvAADLGFTAL-----FG---- 2238
Cdd:PRK06814   784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFS-----------PEDKVFNALpvfhsFGltgg 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2239 ---ALLSGRRVRLLPAELAFdaqalaahlqahpvdclKIVPShlagLLAAAGGTAVLPRECLVT---------------- 2299
Cdd:PRK06814   853 lvlPLLSGVKVFLYPSPLHY-----------------RIIPE----LIYDTNATILFGTDTFLNgyaryahpydfrslry 911
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2300 ---GGEALTGAlVQQVRALAPTLRIVNHYGPTETTvGILTCTVPEEWPVEQgvpVGHPLAGNEaWVLDrfglPAPvGV-- 2374
Cdd:PRK06814   912 vfaGAEKVKEE-TRQTWMEKFGIRILEGYGVTETA-PVIALNTPMHNKAGT---VGRLLPGIE-YRLE----PVP-GIde 980
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2375 AGELYLGGGNLSLGYWqRAEQTAerfVAHPLAPDrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQ 2454
Cdd:PRK06814   981 GGRLFVRGPNVMLGYL-RAENPG---VLEPPADG--WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAE 1054
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2455 L-PGVEVAAVlALP----GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK06814  1055 LwPDALHAAV-SIPdarkGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEA 1133

                   ....*..
gi 1246793773 2530 DADSSAE 2536
Cdd:PRK06814  1134 AAKPEAA 1140
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
604-1040 3.47e-12

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 72.34  E-value: 3.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  604 GAWRAGLSVIPLDTEWPQ---ARRAE----VVAASGCDAVLTDA--QGLAGFAPSVAIAVDELKLDGAGENGSGENAAPN 674
Cdd:PRK07768    73 GLWMRGASLTMLHQPTPRtdlAVWAEdtlrVIGMIGAKAVVVGEpfLAAAPVLEEKGIRVLTVADLLAADPIDPVETGED 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL-------H----VAGLAVDTTleqilaawsRGACV 743
Cdd:PRK07768   153 DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMvswlplfHdmgmVGFLTVPMY---------FGAEL 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  744 V-ARPDELL-EPQRFLAFLSERAITVTdLAPAYANELVR---ASVADDWR-DL-ALRCLVVGGDVLPVALAQRWFE---- 812
Cdd:PRK07768   224 VkVTPMDFLrDPLLWAELISKYRGTMT-AAPNFAYALLArrlRRQAKPGAfDLsSLRFALNGAEPIDPADVEDLLDagar 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  813 LGLdRRCALINAYGPTEATISSHYH------RVQAIDA-----------------SRPVPLGQLLPGRIAAVLDAHGRIV 869
Cdd:PRK07768   303 FGL-RPEAILPAYGMAEATLAVSFSpcgaglVVDEVDAdllaalrravpatkgntRRLATLGPPLPGLEVRVVDEDGQVL 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  870 P-RGVcGELALGGIGLAEGYRGDAAaserrFAPLRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEE 948
Cdd:PRK07768   382 PpRGV-GVIELRGESVTPGYLTMDG-----FIPAQDADG----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTD 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  949 IEHCLGQLPQVRAAAAGVVGEGAAQRlvawvecagEDGFGQADLNQTDSDQTESERWHRALCERLPAY--MVPTQFVALP 1026
Cdd:PRK07768   452 IERAAARVEGVRPGNAVAVRLDAGHS---------REGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLG 522
                          490
                   ....*....|....*.
gi 1246793773 1027 --RLPRNASGKIDRRA 1040
Cdd:PRK07768   523 pgSIPKTPSGKLRRAN 538
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
636-1041 3.64e-12

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: 72.28  E-value: 3.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  636 VLTDAQGLAGFAPSVAIAVDELKLDGAGENG---SGENAApnqlAYILYTSGSTGIPKGVEVGHAALaahidaaaealal 712
Cdd:cd12119    126 VMTDDAAMPEPAGVGVLAYEELLAAESPEYDwpdFDENTA----AAICYTSGTTGNPKGVVYSHRSL------------- 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  713 saddrVLH-VAGLAVDTT-LEQ-------------------ILAAWSrGACVVArPDELLEPQRFLAFLSERAITVTDLA 771
Cdd:cd12119    189 -----VLHaMAALLTDGLgLSEsdvvlpvvpmfhvnawglpYAAAMV-GAKLVL-PGPYLDPASLAELIEREGVTFAAGV 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  772 PAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDrrcaLINAYGPTE----ATISSHYHRVQAIDASRP 847
Cdd:cd12119    262 PTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR----VIHAWGMTEtsplGTVARPPSEHSNLSEDEQ 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  848 VPL----GQLLPGRIAAVLDAHGRIVPR--GVCGELALGGIGLAEGYRGDAAASERRFAPLRLpsgeslrmyRSGDRVRL 921
Cdd:cd12119    338 LALrakqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL---------RTGDVATI 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  922 LDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVECAGEDGFGQADLNQTdsd 998
Cdd:cd12119    409 DEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAA--VIGvphPKWGERPLAVVVLKEGATVTAEELLEF--- 483
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1246793773  999 qteserwhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd12119    484 ----------LADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
2299-2525 4.07e-12

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 72.16  E-value: 4.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2299 TGGEALTGALVQQVRALApTLRIVNHYGPTETTVgiLTCTVPEEWPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGEL 2378
Cdd:PRK12492   340 SGGTALVKATAERWEQLT-GCTIVEGYGLTETSP--VASTNPYGELARLGT-VGIPVPGTALKVIDDDGNELPLGERGEL 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2379 YLGGGNLSLGYWQRAEQTAERFVAHPlapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV 2458
Cdd:PRK12492   416 CIKGPQVMKGYWQQPEATAEALDAEG------WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2459 EVAAVLALP----GANGVLQLGACIQG-SLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK12492   490 ANCAAIGVPdersGEAVKLFVVARDPGlSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
89-385 4.64e-12

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: 71.57  E-value: 4.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   89 PLSLGQERLWFLEQFEPGGHAYHLAALFELRGELDAAALERAVHGLLIRHEVLDRCIQGEDS------VAAGGGAAVESA 162
Cdd:cd19547      3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRaeplqyVRDDLAPPWALL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  163 DLRGRGQDEIDALVEGF----RLRPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRv 238
Cdd:cd19547     83 DWSGEDPDRRAELLERLladdRAAGLSLADCPLYRLTLVRLGGG-----RHYLLWSHHHILLDGWCLSLIWGDVFRVYE- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  239 ecGLAAEPAPPL-PCQ-YGDYARWQRDTLDRLDAS---LRHHVEALSGAPhLHELPLDHErpavlGQSGAKLRlAFPPGL 313
Cdd:cd19547    157 --ELAHGREPQLsPCRpYRDYVRWIRARTAQSEESerfWREYLRDLTPSP-FSTAPADRE-----GEFDTVVH-EFPEQL 227
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773  314 SERVAAYAQASRATAFHVLQAAFAALLARCGAGDDLLIGTPVAGRvRPELDS---LVGLFVNTVVLRTQLhdDPD 385
Cdd:cd19547    228 TRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR-PPELEGsehMVGIFINTIPLRIRL--DPD 299
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
2063-2519 4.97e-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: 71.70  E-value: 4.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDARQiAVLDDSgarivigwg 2141
Cdd:cd05914      9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEfTADEVH-HILNHS--------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 aapawvpasvrwldaESVLDVVSayeepprvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DAS 2220
Cdd:cd05914     79 ---------------EAKAIFVS----------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKgDKI 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAA-DLGFTALFGALLSGRRVRL--LPAELAFDAQALAAHLQA---HPVDCLKI-----VPSHLAGLLAAAGGT 2289
Cdd:cd05914    134 LSILPLHHIyPLTFTLLLPLLNGAHVVFLdkIPSAKIIALAFAQVTPTLgvpVPLVIEKIfkmdiIPKLTLKKFKFKLAK 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2290 AVLPRECL------------------VTGGEALTGALVQQVRALAPTLRIvnHYGPTETTvGILTCTVPEEwpvEQGVPV 2351
Cdd:cd05914    214 KINNRKIRklafkkvheafggnikefVIGGAKINPDVEEFLRTIGFPYTI--GYGMTETA-PIISYSPPNR---IRLGSA 287
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGNEAWVLDrfglPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVahplaPDRLLyRSGDLARLDGEGRIVYLGR 2431
Cdd:cd05914    288 GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFD-----KDGWF-HTGDLGKIDAEGYLYIRGR 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2432 GDHQ-VKIRGYRVELGEVEQVLAQLPGV-----------EVAAVLALPGANGVLQLG--ACIQGSLEGVAEALAQRLPEY 2497
Cdd:cd05914    358 KKEMiVLSSGKNIYPEEIEAKINNMPFVleslvvvqekkLVALAYIDPDFLDVKALKqrNIIDAIKWEVRDKVNQKVPNY 437
                          490       500
                   ....*....|....*....|...
gi 1246793773 2498 LCPSRWRAV-ESMPRLGNGKIDR 2519
Cdd:cd05914    438 KKISKVKIVkEEFEKTPKGKIKR 460
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
529-1041 5.01e-12

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 71.84  E-value: 5.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  529 PAPRTVG-NVVDAIARAADEFPERAALETAQGR--LSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGA 605
Cdd:PRK05852     9 PMASDFGpRIADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  606 WRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAP--------SVAIAVDELKLDGAGENGSGENAAPNQL- 676
Cdd:PRK05852    89 SRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEpttrwwplTVNVGGDSGPSGGTLSVHLDAATEPTPAt 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  677 ----------AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTL-EQILAAWSRGACVVA 745
Cdd:PRK05852   169 stpeglrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAVLL 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 RPDELLEPQRFLAFLSERAITVTDLAPAYANELV-RASVADDWRD-LALRCLVVGGDVLPVALAQrwfelGLDRRCA--L 821
Cdd:PRK05852   249 PARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLeRAATEPSGRKpAALRFIRSCSAPLTAETAQ-----ALQTEFAapV 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  822 INAYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAA----VLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASER 897
Cdd:PRK05852   324 VCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTGaqirIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  898 RFAPLRLpsgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEGAA 972
Cdd:PRK05852   404 NFTDGWL---------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfgvpdQLYGEAVA 474
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  973 QRLVAwvecagedgfgQADLNQTDSDQTESERwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK05852   475 AVIVP-----------RESAPPTAEELVQFCR------ERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
2169-2522 5.08e-12

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: 71.79  E-value: 5.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2169 PPRVDVDADTpAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDASLATLSTVAADLGF--TALFGALLSGRR 2245
Cdd:cd17642    177 PPSFDRDEQV-ALIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTAILTVIPFHHGFgmFTTLGYLICGFR 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2246 VRLLPAelaFDAQALAAHLQAHPVDCLKIVPShlagllaaagGTAVLPRECLV------------TGGEALTGALVQQV- 2312
Cdd:cd17642    256 VVLMYK---FEEELFLRSLQDYKVQSALLVPT----------LFAFFAKSTLVdkydlsnlheiaSGGAPLSKEVGEAVa 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2313 -RALAPTLRivNHYGPTETTVGILTctVPEEWpVEQGVpVGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYW 2390
Cdd:cd17642    323 kRFKLPGIR--QGYGLTETTSAILI--TPEGD-DKPGA-VGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYV 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2391 QRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA----- 2465
Cdd:cd17642    397 NNPEATKALIDK-----DGWL-HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGipded 470
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2466 ---LPGANGVLQLGACIqgslegVAEALAQRLPEYLCPSRW-----RAVESMPRLGNGKIDRQAL 2522
Cdd:cd17642    471 ageLPAAVVVLEAGKTM------TEKEVMDYVASQVSTAKRlrggvKFVDEVPKGLTGKIDRRKI 529
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
588-970 5.11e-12

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: 71.47  E-value: 5.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAqglagfapsvaiavdelkldgagengs 667
Cdd:cd05907     33 VAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED--------------------------- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 genaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAvdTTLEQILAAW---SRGACVV 744
Cdd:cd05907     86 -----PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLA--HVFERRAGLYvplLAGARIY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  745 -ARPDELL-------EPQRFLAFLS--ER--AITVTDLAPAYANELVRASVADDwrdlaLRCLVVGGDVLPVALAQRWFE 812
Cdd:cd05907    159 fASSAETLlddlsevRPTVFLAVPRvwEKvyAAIKVKAVPGLKRKLFDLAVGGR-----LRFAASGGAPLPAELLHFFRA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  813 LGLDrrcaLINAYGPTEATISSHYHRVQAIDASRPvplGQLLPGriaavldAHGRIVPRgvcGELALGGIGLAEGYRGDA 892
Cdd:cd05907    234 LGIP----VYEGYGLTETSAVVTLNPPGDNRIGTV---GKPLPG-------VEVRIADD---GEILVRGPNVMLGYYKNP 296
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  893 AASERRFaplrLPSGEslrmYRSGDRVRLLDDGELQFLGRA-DFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEG 970
Cdd:cd05907    297 EATAEAL----DADGW----LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAV--VIGDG 365
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
3547-4010 5.38e-12

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 71.71  E-value: 5.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3547 YATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL---EDSGVCLSVS- 3622
Cdd:PRK06018    42 YAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIInhaEDRVVITDLTf 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3623 ---QRALAVELPGT-------------------ALCLDDPFTRAQLDaVEPGELPEvptEAPAYLIYTSGSTGTPKGVVV 3680
Cdd:PRK06018   122 vpiLEKIADKLPSVeryvvltdaahmpqttlknAVAYEEWIAEADGD-FAWKTFDE---NTAAGMCYTSGTTGDPKGVLY 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3681 THR-NVerLFT-AATQTGRFSFDEHD----VWSLFHSHAFDFAvwelWGAWLYGGRAVLvpeavcrqPDAFLD------L 3748
Cdd:PRK06018   198 SHRsNV--LHAlMANNGDALGTSAADtmlpVVPLFHANSWGIA----FSAPSMGTKLVM--------PGAKLDgasvyeL 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3749 LAEYGVTVLNQTPSAFYALQsQAMRRE-LAL-NVRAVVFGGEALEPSRLQPWRERypQAELVNMYGITETTVHVSFHRLS 3826
Cdd:PRK06018   264 LDTEKVTFTAGVPTVWLMLL-QYMEKEgLKLpHLKMVVCGGSAMPRSMIKAFEDM--GVEVRHAWGMTEMSPLGTLAALK 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3827 DEDLQSPtsrigsalPDLAVHVLDAAGQPvPLGV------------------VGELVVEGDGVAQGYWQrpeLTAERFVE 3888
Cdd:PRK06018   341 PPFSKLP--------GDARLDVLQKQGYP-PFGVemkitddagkelpwdgktFGRLKVRGPAVAAAYYR---VDGEILDD 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3889 RGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTveGQGEGAW---LMAYAVAAD 3965
Cdd:PRK06018   409 DG---FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI--GVYHPKWderPLLIVQLKP 483
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773 3966 GAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK06018   484 GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
2052-2524 6.24e-12

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 71.47  E-value: 6.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDpQHPDARQIA-VLD 2130
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPIN-WHLTAAEIAyIVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2131 DSGARIVIGWGA-------APAWVP--ASVRWLDAESVlDVVSAYEEppRVDVDADTP-------AYLIYTSGSTGTPKG 2194
Cdd:PRK08276    81 DSGAKVLIVSAAladtaaeLAAELPagVPLLLVVAGPV-PGFRSYEE--ALAAQPDTPiadetagADMLYSSGTTGRPKG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2195 VVVSQGNLANYVAG----VLPVLDLGEDASLATLSTV----AADLGFTAlfGALLSGRRVRLLPaelAFDAQALAAHLQA 2266
Cdd:PRK08276   158 IKRPLPGLDPDEAPgmmlALLGFGMYGGPDSVYLSPAplyhTAPLRFGM--SALALGGTVVVME---KFDAEEALALIER 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2267 HPVDCLKIVPSHLAGLLAaaggtavLPREclvtggealtgalvqqVRAL--APTLRIVNH-------------------- 2324
Cdd:PRK08276   233 YRVTHSQLVPTMFVRMLK-------LPEE----------------VRARydVSSLRVAIHaaapcpvevkramidwwgpi 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 ----YGPTETtvGILTCTVPEEWPVEQGvPVGHPLAGnEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERF 2400
Cdd:PRK08276   290 iheyYASSEG--GGVTVITSEDWLAHPG-SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAAR 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2401 VAHPLAPdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAN------GVLQ 2474
Cdd:PRK08276   366 NPHGWVT------VGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEmgervkAVVQ 439
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2475 LGACIQGSLEGVAEALA---QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK08276   440 PADGADAGDALAAELIAwlrGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
679-1038 6.61e-12

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: 70.38  E-value: 6.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRV------LHVAGLAVDttleqILAAWSRGACVVArPDELLE 752
Cdd:cd05917      7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCFGSVLG-----VLACLTHGATMVF-PSPSFD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  753 PQRFLAFLSERAITVTDLAPA-YANELVRASVADDwrDLA-LRCLVVGGDVLPVALAQRWFE-LGLDrrcALINAYGPTE 829
Cdd:cd05917     81 PLAVLEAIEKEKCTALHGVPTmFIAELEHPDFDKF--DLSsLRTGIMAGAPCPPELMKRVIEvMNMK---DVTIAYGMTE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  830 ATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVP-RGVCGELALGGIGLAEGYRGDAAASERRFaplrlpSGE 908
Cdd:cd05917    156 TSPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAI------DGD 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  909 slRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVecAGEDGf 987
Cdd:cd05917    230 --GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSdVQVVGVPDERYGEEVCAWI--RLKEG- 304
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773  988 gqadlnqtdSDQTESERwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd05917    305 ---------AELTEEDI--KAYCkGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
584-1041 8.34e-12

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: 70.87  E-value: 8.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  584 QARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPqaRRAEVVAASGCDAVLTDAQGLAGFAPSvAIAVDELKLDGAG 663
Cdd:cd05929     41 IADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP--RAEACAIIEIKAAALVCGLFTGGGALD-GLEDYEAAEGGSP 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  664 ENGSGENAAPNqlaYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALAL---SADDRVLHVAGLAVDTTLEQILAAWSRG 740
Cdd:cd05929    118 ETPIEDEAAGW---KMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGfgpGADSVYLSPAPLYHAAPFRWSMTALFMG 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  741 ACVVARpdELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWR-DLA-LRCLVVGGDVLPVALAQRWFELGLDRr 818
Cdd:cd05929    195 GTLVLM--EKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAyDLSsLKRVIHAAAPCPPWVKEQWIDWGGPI- 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  819 caLINAYGPTEATISShyhrvqAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGVCGELalggiglaegYRGDAAA 894
Cdd:cd05929    272 --IWEYYGGTEGQGLT------IINGeewlTHPGSVGRAVLGKV-HILDEDGNEVPPGEIGEV----------YFANGPG 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  895 SERRFAPLRLPSGESLRMYRS-GDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAA 972
Cdd:cd05929    333 FEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvGVPDEELG 412
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  973 QRLVAWVECAGEDGFGQADLNQTdsdqteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05929    413 QRVHAVVQPAPGADAGTALAEEL-----------IAFLrDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2545-2602 1.03e-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: 62.58  E-value: 1.03e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2545 EVLRELWQKLLGREH--IGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLA 2602
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
2052-2523 1.04e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 70.80  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASwtYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK13383    53 AIIDDDGALS--YRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRA 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIgwgAAPAWVPASVRWLDAESVLD--VVSAYEEPPRVDVDADTPAYLIyTSGSTGTPKGVVvSQGNLANYVAGV 2209
Cdd:PRK13383   131 HHISTVV---ADNEFAERIAGADDAVAVIDpaTAGAEESGGRPAVAAPGRIVLL-TSGTTGKPKGVP-RAPQLRSAVGVW 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 LPVLD-----LGEDASLATLSTVAADLGF----TALFGALLSGRRvrllpaelaFDAQALAAHLQAHPVDCLKIVPSHLA 2280
Cdd:PRK13383   206 VTILDrtrlrTGSRISVAMPMFHGLGLGMlmltIALGGTVLTHRH---------FDAEAALAQASLHRADAFTAVPVVLA 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2281 GLLAAAGGT-AVLPRECL---VTGGEALTGALVQQVRALAPTLrIVNHYGPTETTVGIL-TCTVPEEWPVEqgvpVGHPL 2355
Cdd:PRK13383   277 RILELPPRVrARNPLPQLrvvMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALaTPADLRDAPET----VGKPV 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2356 AGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYwqraEQTAERFVAHPLApdrllyRSGDLARLDGEGRIVYLGRGDHQ 2435
Cdd:PRK13383   352 AGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY----TDGGGKAVVDGMT------STGDMGYLDNAGRLFIVGREDDM 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2436 VKIRGYRVELGEVEQVLAQLPGVEVAAVLALP--------GANGVLQLGACIQGslEGVAEALAQRLPEYLCPSRWRAVE 2507
Cdd:PRK13383   422 IISGGENVYPRAVENALAAHPAVADNAVIGVPderfghrlAAFVVLHPGSGVDA--AQLRDYLKDRVSRFEQPRDINIVS 499
                          490
                   ....*....|....*.
gi 1246793773 2508 SMPRLGNGKIDRQALA 2523
Cdd:PRK13383   500 SIPRNPTGKVLRKELP 515
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
3498-4005 1.06e-11

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 70.89  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3498 PLLPSQTRSAAwtsrERYACTGNLVSRFAE-IARRYpariavsaedgelDYATLDRRSSQLATLLIRQGAGPGQRVGLCL 3576
Cdd:PRK07008     9 PLLISSLIAHA----ARHAGDTEIVSRRVEgDIHRY-------------TYRDCERRAKQLAQALAALGVEPGDRVGTLA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3577 PRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFIL---EDSGVCLSVS----QRALAVELPGT----ALCLDDPFTRAQ 3645
Cdd:PRK07008    72 WNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVnhaEDRYVLFDLTflplVDALAPQCPNVkgwvAMTDAAHLPAGS 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3646 LD--------AVEPG--ELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHD----VWSLFHS 3711
Cdd:PRK07008   152 TPllcyetlvGAQDGdyDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSARDavlpVVPMFHV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3712 HAfdfavWEL-WGAWLYGGRAVLvpeavcrqPDAFLD------LLAEYGVTVLNQTPSAFYALQSQAMRRELALN-VRAV 3783
Cdd:PRK07008   232 NA-----WGLpYSAPLTGAKLVL--------PGPDLDgkslyeLIEAERVTFSAGVPTVWLGLLNHMREAGLRFStLRRT 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3784 VFGGEALEPSRLQPWRERYpQAELVNMYGITE-------TTVHVSFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPV 3856
Cdd:PRK07008   299 VIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEmsplgtlCKLKWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGREL 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3857 PL-GVV-GELVVEGDGVAQGYWQRpelTAERFVerggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAK 3934
Cdd:PRK07008   378 PWdGKAfGDLQVRGPWVIDRYFRG---DASPLV----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENV 450
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 3935 IASLPQVSDAAVTveGQGEGAW----LMAyAVAADGAEpdpqSLREALRAL----LPDYMLPRLIQLLPALPLTANGKL 4005
Cdd:PRK07008   451 AVAHPAVAEAACI--ACAHPKWderpLLV-VVKRPGAE----VTREELLAFyegkVAKWWIPDDVVFVDAIPHTATGKL 522
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
3637-3982 1.15e-11

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 70.18  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3637 LDD----PFTRAQ-LDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVT-------HRNVERLFTAAtqtGrfsFDEHD 3704
Cdd:COG1541     55 LEDlaklPFTTKEdLRDNYPFGLFAVPLEEIVRIHASSGTTGKPTVVGYTrkdldrwAELFARSLRAA---G---VRPGD 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VwslFHsHAFDFAVWelWGAWL--YGGRAV---LVPEAVcRQPDAFLDLLAEYGVTVLNQTPSafYALQ-SQAMRRE--- 3775
Cdd:COG1541    129 R---VQ-NAFGYGLF--TGGLGlhYGAERLgatVIPAGG-GNTERQLRLMQDFGPTVLVGTPS--YLLYlAEVAEEEgid 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3776 -LALNVRAVVFGGEALEPSrlqpWRERYPQ---AELVNMYGITETTVHVSFhrlsdedlQSPTSRiGSALPDLAVHV--L 3849
Cdd:COG1541    200 pRDLSLKKGIFGGEPWSEE----MRKEIEErwgIKAYDIYGLTEVGPGVAY--------ECEAQD-GLHIWEDHFLVeiI 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3850 D-AAGQPVPLGVVGELVVEGdgvaqgywqrpeLTAE-----RfverggqrfYRSGDLGRYRADGS--------LEY-RGR 3914
Cdd:COG1541    267 DpETGEPVPEGEEGELVVTT------------LTKEampliR---------YRTGDLTRLLPEPCpcgrthprIGRiLGR 325
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 3915 GDDQVKLRGYRIEPGEIAAKIASLPQVSDAA-VTVEGQGEGAWLMAYAVAADGAEPDP--QSLREALRALL 3982
Cdd:COG1541    326 ADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYqIVVDREGGLDELTVRVELAPGASLEAlaEAIAAALKAVL 396
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1181-1723 1.19e-11

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 71.44  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1181 WDALW-----RRHDLLRASFEradgqwRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHAHC 1255
Cdd:COG3321    849 WSALYpgrgrRRVPLPTYPFQ------REDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALA 922
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1256 DDGERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGAsyadyveALREADDAQRFDAGFWRELAAQPMQA 1335
Cdd:COG3321    923 AAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAA-------AAAAAAAAAAAAAAAAAAAAAAAAAA 995
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1336 LPQDRPVALADARQSNVGRIVQTLDAGLTADLLERAGEAYRCRTDEVLLIALARALATRTGRNRLWLDRERHGRDVLDGR 1415
Cdd:COG3321    996 LAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALA 1075
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1416 DWSSVLGWYTAVHPLPLDLGVADGPAQIGALKEQIRALARRGLDYMPLVASARIPALPAGQLLFNYHGVVDAGAHPAFEV 1495
Cdd:COG3321   1076 ELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAA 1155
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1496 EPRTLASGNGADNPPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAHCLQPGSGALTASDLPQA 1575
Cdd:COG3321   1156 AAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALAL 1235
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1576 RLQADEFALLAAREDARAIEHAFPLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAI 1655
Cdd:COG3321   1236 LALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAA 1315
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1656 VWEGLSVPHQIVLADAAAPWQTLDWSALDDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGR 1723
Cdd:COG3321   1316 AAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
3653-4017 1.23e-11

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 71.28  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3653 ELPEVPTEApAYLIYTSGSTGTPKGVVVTHR----NVERLFTAATQTGRFSFdeHDVWSLFHshAFDFAVwELWGAWLYG 3728
Cdd:PRK08043   359 QVKQQPEDA-ALILFTSGSEGHPKGVVHSHKsllaNVEQIKTIADFTPNDRF--MSALPLFH--SFGLTV-GLFTPLLTG 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3729 GRAVL---------VPEavcrqpdafldLLAEYGVTVLNQTpSAF---YAlqSQAMRRELAlNVRAVVFGGEALEPSRLQ 3796
Cdd:PRK08043   433 AEVFLypsplhyriVPE-----------LVYDRNCTVLFGT-STFlgnYA--RFANPYDFA-RLRYVVAGAEKLQESTKQ 497
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3797 PWRERYpQAELVNMYGITETTVHVSFhrlsDEDLQSPTSRIGSALPDLAVHVLdaagqPVPlGVV--GELVVEGDGVAQG 3874
Cdd:PRK08043   498 LWQDKF-GLRILEGYGVTECAPVVSI----NVPMAAKPGTVGRILPGMDARLL-----SVP-GIEqgGRLQLKGPNIMNG 566
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3875 YW--QRP-ELTAERFVERGGQR---FYRSGDLGRYRADGSLEYRGRGDDQVKlrgyriepgeIAAKIASLPQVSDAAVTV 3948
Cdd:PRK08043   567 YLrvEKPgVLEVPTAENARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAK----------IAGEMVSLEMVEQLALGV 636
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3949 EGQGEgawlMAYAVAADGAE--------PDPQSLREALRAL-----LPDYMLPRLIQLLPALPLTANGKLD----RKALP 4011
Cdd:PRK08043   637 SPDKQ----HATAIKSDASKgealvlftTDSELTREKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDfvtlKSMVD 712

                   ....*.
gi 1246793773 4012 KPETQD 4017
Cdd:PRK08043   713 EPEQHD 718
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
643-1039 1.43e-11

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 70.41  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  643 LAGFAPSvAIAVDELKLDGAGENGSGEN---AAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE--ALALSADDR 717
Cdd:PRK05605   186 LTGPAPG-TVPWETLVDAAIGGDGSDVShprPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvPGLGDGPER 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  718 VL------HVAGLAVDTTLeqilaAWSRGACVVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLA 791
Cdd:PRK05605   265 VLaalpmfHAYGLTLCLTL-----AVSIGGELVLLPA--PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSG 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  792 LRCLVVGGDVLPVALAQRWFEL--GLdrrcaLINAYGPTEAT-------ISSHyhrvqaidaSRPVPLGQLLPGRIAAVL 862
Cdd:PRK05605   338 VRNAFSGAMALPVSTVELWEKLtgGL-----LVEGYGLTETSpiivgnpMSDD---------RRPGYVGVPFPDTEVRIV 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  863 DAH--GRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLDDGELQFLGRADFQVKLR 940
Cdd:PRK05605   404 DPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLD---------GWFRTGDVVVMEEDGFIRIVDRIKELIITG 474
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  941 GYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMV 1018
Cdd:PRK05605   475 GFNVYPAEVEEVLREHPGVEdAAVVGLPREDGSEEVVAAVVLEPGAALDPEGL--------------RAYCrEHLTRYKV 540
                          410       420
                   ....*....|....*....|.
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRR 1039
Cdd:PRK05605   541 PRRFYHVDELPRDQLGKVRRR 561
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
677-1041 1.54e-11

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 70.48  E-value: 1.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  677 AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHV-AGLAVDTTLEQILAAWSRGACVVarpdeLLEPQR 755
Cdd:PRK08008   176 AEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVmPAFHIDCQCTAAMAAFSAGATFV-----LLEKYS 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  756 FLAFLSE----RAiTVTDLAPAYANELVRASVADDWRDLALRclvvggDV---LPVALAQRW-FELGLDRRcaLINAYGP 827
Cdd:PRK08008   251 ARAFWGQvckyRA-TITECIPMMIRTLMVQPPSANDRQHCLR------EVmfyLNLSDQEKDaFEERFGVR--LLTSYGM 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  828 TEaTIsshyhrVQAI-----DASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGI---GLAEGYRGDAAASERRF 899
Cdd:PRK08008   322 TE-TI------VGIIgdrpgDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVL 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  900 AplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG------EGAAQ 973
Cdd:PRK08008   395 E----ADG----WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIV--VVGikdsirDEAIK 464
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  974 RLVAWVEcaGEdgfgqadlnqtdsdqTESERWHRALCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK08008   465 AFVVLNE--GE---------------TLSEEEFFAFCEqNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
3638-4010 1.60e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 69.30  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3638 DDPFTRAQLDAVEPGElpevPTEAP-AYLIYTSGSTGTPKGVVVTHRNverLFTAATQTGRFSFDEHDvW--SLFHSHAF 3714
Cdd:PRK07824    16 DERRAALLRDALRVGE----PIDDDvALVVATSGTTGTPKGAMLTAAA---LTASADATHDRLGGPGQ-WllALPAHHIA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3715 DFAVweLWGAWLYGGRAVLVPEAVCRQPDAFLDLLAE------YGVTVLNQTPSAFYALQSQAMRRELAlnvrAVVFGGE 3788
Cdd:PRK07824    88 GLQV--LVRSVIAGSEPVELDVSAGFDPTALPRAVAElgggrrYTSLVPMQLAKALDDPAATAALAELD----AVLVGGG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3789 ALEPsrlqPWRERYPQA--ELVNMYGITETTVHVSFHrlsdedlqsptsriGSALPDLAVHVLDaagqpvplgvvGELVV 3866
Cdd:PRK07824   162 PAPA----PVLDAAAAAgiNVVRTYGMSETSGGCVYD--------------GVPLDGVRVRVED-----------GRIAL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3867 EGDGVAQGYWQRPELTAerFVERGgqrFYRSGDLGRYrADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAV 3946
Cdd:PRK07824   213 GGPTLAKGYRNPVDPDP--FAEPG---WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAV 286
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 3947 T-VEGQGEGAWLMAYAVAADGAEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRKAL 4010
Cdd:PRK07824   287 FgLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
677-1041 1.77e-11

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: 69.80  E-value: 1.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  677 AYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLhvAGLAVDTTLEQILAAWSRGACVVARPDELLEPQRF 756
Cdd:cd05910     88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL--ATFPLFALFGPALGLTSVIPDMDPTRPARADPQKL 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  757 LAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRwFELGLDRRCALINAYGPTEA----TI 832
Cdd:cd05910    166 VGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAAR-LRKMLSDEAEILTPYGATEAlpvsSI 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  833 SSH---YHRVQAIDASRPVPLGQLLPG---RIAAVLDA------HGRIVPRGVCGELALGGIGLAEGYRGDAAASerRFA 900
Cdd:cd05910    245 GSRellATTTAATSGGAGTCVGRPIPGvrvRIIEIDDEpiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVAT--ALA 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  901 PLRLPSGESLrmYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVVGEGAAQRLVAWVE 980
Cdd:cd05910    323 KIDDNSEGFW--HRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVE 400
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773  981 cagedgfgqaDLNQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLP----RNAsgKIDRRAL 1041
Cdd:cd05910    401 ----------PLPGTITPRARLEQELRALAKDYPHTQRIGRFLIHPSFPvdirHNA--KIFREKL 453
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
2298-2524 2.02e-11

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 70.18  E-value: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2298 VTGGEALTGALVQQVRALApTLRIVNHYGPTETTvgiltctvpeewPVEQGVPVGH--------PLAGNEAWVLDRFGLP 2369
Cdd:PRK05677   332 LSGGMALQLATAERWKEVT-GCAICEGYGMTETS------------PVVSVNPSQAiqvgtigiPVPSTLCKVIDDDGNE 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:PRK05677   399 LPLGEVGELCVKGPQVMKGYWQRPEATDEILDS-----DGWL-KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2450 QVLAQLPGVEVAAVLALPGANG--------VLQLGACIqgSLEGVAEALAQRLPEYLCPsrwRAVE---SMPRLGNGKID 2518
Cdd:PRK05677   473 DVLAALPGVLQCAAIGVPDEKSgeaikvfvVVKPGETL--TKEQVMEHMRANLTGYKVP---KAVEfrdELPTTNVGKIL 547

                   ....*.
gi 1246793773 2519 RQALAD 2524
Cdd:PRK05677   548 RRELRD 553
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
2063-2493 2.40e-11

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: 69.31  E-value: 2.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCL---PR-TFAQLAAMAAvwhrGAAWLPLDPQHP--DARQIavLDDSGARI 2136
Cdd:cd17640      7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFAdnsPRwLIADQGIMAL----GAVDVVRGSDSSveELLYI--LNHSESVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2137 VIgwgaapawvpasvrwldaesvldvvsayeepprVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG 2216
Cdd:cd17640     81 LV---------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2217 E-DASLATL----------STVAADLGFTALFGAllsgrrVRLLPAELAfdaqalaahlqAHPVDCLKIVP--------- 2276
Cdd:cd17640    128 PgDRFLSILpiwhsyersaEYFIFACGCSQAYTS------IRTLKDDLK-----------RVKPHYIVSVPrlweslysg 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2277 -----SHLAGLLAAAGGTAVLPRE--CLVTGGealtGALVQQVRAL--APTLRIVNHYGPTETTvGILTCTVPeeWPVEQ 2347
Cdd:cd17640    191 iqkqvSKSSPIKQFLFLFFLSGGIfkFGISGG----GALPPHVDTFfeAIGIEVLNGYGLTETS-PVVSARRL--KCNVR 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVpVGHPLAGNEAWVLDRFG-LPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfvahPLAPDRLLyRSGDLARLDGEGRI 2426
Cdd:cd17640    264 GS-VGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK-----VLDSDGWF-NTGDLGWLTCGGEL 336
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2427 VYLGRG-DHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLalpganGVLQ--LGACIQGSLEGVAEALAQR 2493
Cdd:cd17640    337 VLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV------GQDQkrLGALIVPNFEELEKWAKES 400
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3662-4012 2.68e-11

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. 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, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 69.38  E-value: 2.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3662 PAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVW----SLFHSHAFDFavweLWGAWLYGGRAVLVPEA 3737
Cdd:cd05915    155 ACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVlpvvPMFHVNAWCL----PYAATLVGAKQVLPGPR 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3738 vcRQPDAFLDLLAEYGVTVLNQTPSAFYALQS--QAMRRELALNVRaVVFGGEAlePSRLQPWRERYPQAELVNMYGITE 3815
Cdd:cd05915    231 --LDPASLVELFDGEGVTFTAGVPTVWLALADylESTGHRLKTLRR-LVVGGSA--APRSLIARFERMGVEVRQGYGLTE 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3816 T----TVHV---SFHRLSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLG--VVGELVVEGDGVAQGYWQRPELTaERF 3886
Cdd:cd05915    306 TspvvVQNFvksHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDgkALGEVQLKGPWITGGYYGNEEAT-RSA 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 VERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVT---VEGQGEGawlMAYAVA 3963
Cdd:cd05915    385 LTPDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVaipHPKWQER---PLAVVV 459
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3964 ADGAEPDPQSLREALRALLPDY-MLPRLIQLLPALPLTANGKLDRKALPK 4012
Cdd:cd05915    460 PRGEKPTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALRE 509
PLN03102 PLN03102
acyl-activating enzyme; Provisional
2175-2550 2.93e-11

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 69.66  E-value: 2.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2175 DADTPAYLIYTSGSTGTPKGVVVSQ--------GNLANYVAGVLPVLdlgedasLATLSTVAADlGFTALFGALLSGRRV 2246
Cdd:PLN03102   184 DEHDPISLNYTSGTTADPKGVVISHrgaylstlSAIIGWEMGTCPVY-------LWTLPMFHCN-GWTFTWGTAARGGTS 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2247 RLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLvTGGEALTGALVQQVRALAptLRIVNHYG 2326
Cdd:PLN03102   256 VCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVL-TGGSPPPAALVKKVQRLG--FQVMHAYG 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2327 PTETTVGILTCTVPEEW-----------PVEQGVPVghpLAGNEAWVLDRFGL---PAPVGVAGELYLGGGNLSLGYWQR 2392
Cdd:PLN03102   333 LTEATGPVLFCEWQDEWnrlpenqqmelKARQGVSI---LGLADVDVKNKETQesvPRDGKTMGEIVIKGSSIMKGYLKN 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFVAHPLapdrllyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP----- 2467
Cdd:PLN03102   410 PKATSEAFKHGWL-------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwg 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2468 -----------GANGVLQLGACIQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADL---LQQDDADS 2533
Cdd:PLN03102   483 etpcafvvlekGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIakgLVVEDEDN 562
                          410
                   ....*....|....*..
gi 1246793773 2534 SAEAIDETPVNEVLREL 2550
Cdd:PLN03102   563 VIKKVHQRPVEHFSSRL 579
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
3655-4012 3.20e-11

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 69.76  E-value: 3.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3655 PEVPTEAP-AYLIYTSGSTGTPKGVVVTHRNVerLFT-AATQTGRFSFDEHDVW--SLFHSHAFDFA----VWELWGAWL 3726
Cdd:PLN02387   244 PDLPSPNDiAVIMYTSGSTGLPKGVMMTHGNI--VATvAGVMTVVPKLGKNDVYlaYLPLAHILELAaesvMAAVGAAIG 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3727 YG-----------------GRA-VLVP--------------EAVCRQPDA-------FLDLLAEYGVTVLNQTPSAFYAL 3767
Cdd:PLN02387   322 YGspltltdtsnkikkgtkGDAsALKPtlmtavpaildrvrDGVRKKVDAkgglakkLFDIAYKRRLAAIEGSWFGAWGL 401
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3768 QS--------QAMRRELALNVRAVVFGGEALEPSRlqpwrERYPQ----AELVNMYGITETTVHVSFHRLSDedlqSPTS 3835
Cdd:PLN02387   402 EKllwdalvfKKIRAVLGGRIRFMLSGGAPLSGDT-----QRFINiclgAPIGQGYGLTETCAGATFSEWDD----TSVG 472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3836 RIGSALPDLAVHVLD-------AAGQPVPLGvvgELVVEGDGVAQGYWQRPELTAERF-VERGGQRFYRSGDLGRYRADG 3907
Cdd:PLN02387   473 RVGPPLPCCYVKLVSweeggylISDKPMPRG---EIVIGGPSVTLGYFKNQEKTDEVYkVDERGMRWFYTGDIGQFHPDG 549
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3908 SLEYRGRGDDQVKLR-GYRIEPGEIAAKIASLPQVSD-------------AAVTVEGQGEGAWLMAYAVA-ADGAE--PD 3970
Cdd:PLN02387   550 CLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNimvhadpfhsycvALVVPSQQALEKWAKKAGIDySNFAElcEK 629
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 3971 PQSLREALRAL--------LPDYMLPRLIQLLPAL--P----LTANGKLDRKALPK 4012
Cdd:PLN02387   630 EEAVKEVQQSLskaakaarLEKFEIPAKIKLLPEPwtPesglVTAALKLKREQIRK 685
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
2050-2524 3.44e-11

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 69.24  E-value: 3.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2050 AQAVAVEEGAA--SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT----FAQLAAMAAvwhrGAAWLPLDP----- 2118
Cdd:PLN02330    42 ADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVaeygIVALGIMAA----GGVFSGANPtales 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2119 ------QHPDARQIaVLDDSGARIVIGWGAaPAWV------PASVRW---LDAESVLDVVSAYEEPPRVDVDAdtpayLI 2183
Cdd:PLN02330   118 eikkqaEAAGAKLI-VTNDTNYGKVKGLGL-PVIVlgeekiEGAVNWkelLEAADRAGDTSDNEEILQTDLCA-----LP 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2184 YTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLD--LGEDASLATLSTVAAdLGFTALFGALL--SGRRVrllpAELAFDAQ 2258
Cdd:PLN02330   191 FSSGTTGISKGVMLTHRNLvANLCSSLFSVGPemIGQVVTLGLIPFFHI-YGITGICCATLrnKGKVV----VMSRFELR 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2259 ALAAHLQAHPVDCLKIVP----SHLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAPTLRIVNHYGPTETTVGI 2334
Cdd:PLN02330   266 TFLNALITQEVSFAPIVPpiilNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCIT 345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwpvEQGVP----VGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAhplapDR 2409
Cdd:PLN02330   346 LTHGDPEK---GHGIAkknsVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDE-----DG 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2410 LLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACI------QGSL 2483
Cdd:PLN02330   418 WLH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVvinpkaKESE 496
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1246793773 2484 EGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PLN02330   497 EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
2079-2467 3.54e-11

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: 69.03  E-value: 3.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2079 DAVGVQPGAHVALCLPRT----FAQLAAMAAvwhrGAAWLPLDPQHPDARQIAVLDDSGAR-IVIGWGAAPA-------- 2145
Cdd:cd05928     60 GACGLQRGDRVAVILPRVpewwLVNVACIRT----GLVFIPGTIQLTAKDILYRLQASKAKcIVTSDELAPEvdsvasec 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2146 -------WVPASVR--WLDAESVLDvvSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLA-NYVAGVLPVLDL 2215
Cdd:cd05928    136 pslktklLVSEKSRdgWLNFKELLN--EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGlGLKVNGRYWLDL 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2216 GE-DASLATLSTVAADLGFTALFGALLSGRRV--RLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVL 2292
Cdd:cd05928    214 TAsDIMWNTSDTGWIKSAWSSLFEPWIQGACVfvHHLPR---FDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKF 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 P--RECLvTGGEALTGALVQQVRALApTLRIVNHYGPTETtvgILTCTVPEEWPVEQGvPVGHPLAGNEAWVLDRFGLPA 2370
Cdd:cd05928    291 PslQHCV-TGGEPLNPEVLEKWKAQT-GLDIYEGYGQTET---GLICANFKGMKIKPG-SMGKASPPYDVQIIDDNGNVL 364
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2371 PVGVAGELYLGGG-----NLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVEL 2445
Cdd:cd05928    365 PPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGP 437
                          410       420
                   ....*....|....*....|..
gi 1246793773 2446 GEVEQVLAQLPGVEVAAVLALP 2467
Cdd:cd05928    438 FEVESALIEHPAVVESAVVSSP 459
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
2061-2467 3.64e-11

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 69.15  E-value: 3.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPL----DPQHPDARqiavLDDSGARI 2136
Cdd:PRK04319    73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDR----LEDSEAKV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2137 VIGWGAAPAWVPA----SVRWL-----DAESVLDVVS-------AYEEPPRVDVDADTPAYLIYTSGSTGTPKGVV-VSQ 2199
Cdd:PRK04319   149 LITTPALLERKPAddlpSLKHVllvgeDVEEGPGTLDfnalmeqASDEFDIEWTDREDGAILHYTSGSTGKPKGVLhVHN 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2200 GNLANYVAGVLpVLDLGEDaslaTLSTVAADLGFTA-----LFGALLSGrrVRLLPAELAFDAQALAAHLQAHPVDCLKI 2274
Cdd:PRK04319   229 AMLQHYQTGKY-VLDLHED----DVYWCTADPGWVTgtsygIFAPWLNG--ATNVIDGGRFSPERWYRILEDYKVTVWYT 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2275 VPshlagllaaaggTAV---------------LPRECLVTG-GEALTG-ALVQQVRALAptLRIVNHYGPTETTvGILTC 2337
Cdd:PRK04319   302 AP------------TAIrmlmgagddlvkkydLSSLRHILSvGEPLNPeVVRWGMKVFG--LPIHDNWWMTETG-GIMIA 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2338 TVPEEwPVEQGvPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSL--GYWQRAEQTAERFvahplAPDrlLYRSG 2415
Cdd:PRK04319   367 NYPAM-DIKPG-SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMmrGIWNNPEKYESYF-----AGD--WYVSG 437
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2416 DLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:PRK04319   438 DSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
531-1041 5.50e-11

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 68.45  E-value: 5.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  531 PRTvgNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQA--RsVALCLPRGLDWYCLLLGAWRA 608
Cdd:PRK08314     8 PET--SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKgdR-VLLYMQNSPQFVIAYYAILRA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  609 GLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPS----------VAIAVDELKLDG----------------- 661
Cdd:PRK08314    85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAvgnlrlrhviVAQYSDYLPAEPeiavpawlraepplqal 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  662 -------------AGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVA 722
Cdd:PRK08314   165 apggvvawkealaAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLavlplfHVT 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  723 G--------LAVDTTLeQILAAWSRGAcvvARpdELLEPQRflaflseraITVTDLAPAYANELVrASVADDWRDLA-LR 793
Cdd:PRK08314   245 GmvhsmnapIYAGATV-VLMPRWDREA---AA--RLIERYR---------VTHWTNIPTMVVDFL-ASPGLAERDLSsLR 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  794 CLVVGGDVLPVALAQRWFEL-GLDrrcaLINAYGPTEaTIS-SHyhrVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVP 870
Cdd:PRK08314   309 YIGGGGAAMPEAVAERLKELtGLD----YVEGYGLTE-TMAqTH---SNPPDRPKLQCLGIPTFGVDARVIDpETLEELP 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  871 RGVCGELALGGIGLAEGYRGDAAASERRFAPLrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIE 950
Cdd:PRK08314   381 PGEVGEIVVHGPQVFKGYWNRPEATAEAFIEI-----DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  951 HCLGQLPQVRAAAagVVGEGAAQRlvawvecaGEDGFGQADLNQTDSDQTESER---WHRalcERLPAYMVP--TQFVAl 1025
Cdd:PRK08314   456 NLLYKHPAIQEAC--VIATPDPRR--------GETVKAVVVLRPEARGKTTEEEiiaWAR---EHMAAYKYPriVEFVD- 521
                          570
                   ....*....|....*.
gi 1246793773 1026 pRLPRNASGKIDRRAL 1041
Cdd:PRK08314   522 -SLPKSGSGKILWRQL 536
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
2052-2524 5.85e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 68.56  E-value: 5.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK13391    15 AVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGA-------APAWVPASVRWL--DAESVLDVVSAYEE-----PPRVDVDADTPAYLIYTSGSTGTPKGVVV 2197
Cdd:PRK13391    95 SGARALITSAAkldvaraLLKQCPGVRHRLvlDGDGELEGFVGYAEavaglPATPIADESLGTDMLYSSGTTGRPKGIKR 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2198 SQGNLAnyVAGVLPVLDLGE-----DASLATLSTV----AADLGFTALFGALlsGRRVRLLPAelaFDAQALAAHLQAHP 2268
Cdd:PRK13391   175 PLPEQP--PDTPLPLTAFLQrlwgfRSDMVYLSPAplyhSAPQRAVMLVIRL--GGTVIVMEH---FDAEQYLALIEEYG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2269 VDCLKIVPSHLAGLLAaaggtavLPREclvtggealtgalvQQVRALAPTLRIVNH------------------------ 2324
Cdd:PRK13391   248 VTHTQLVPTMFSRMLK-------LPEE--------------VRDKYDLSSLEVAIHaaapcppqvkeqmidwwgpiihey 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETtVGILTCTvPEEWPVEQGVpVGHPLAGnEAWVLDRFGLPAPVGVAGELYLGGGnLSLGYWQRAEQTAErfvAHp 2404
Cdd:PRK13391   307 YAATEG-LGFTACD-SEEWLAHPGT-VGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG-RPFEYLNDPAKTAE---AR- 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2405 lAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG------ANGVLQLGAC 2478
Cdd:PRK13391   378 -HPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNedlgeeVKAVVQPVDG 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1246793773 2479 IQGSLEGVAEALA---QRLPEYLCPSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK13391   457 VDPGPALAAELIAfcrQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
2052-2517 6.24e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 68.50  E-value: 6.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2052 AVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDD 2131
Cdd:PRK13390    15 AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVIGWGA-----APAWVPASVRwLDAESVLDVVSAYEEP-----PRVdvdADTP--AYLIYTSGSTGTPKGV---- 2195
Cdd:PRK13390    95 SGARVLVASAAldglaAKVGADLPLR-LSFGGEIDGFGSFEAAlagagPRL---TEQPcgAVMLYSSGTTGFPKGIqpdl 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2196 ----VVSQGNLANYVAGVLpvLDLGEDASLATLSTV--AADLGFTALFGALlsGRRVRLLPAelaFDAQALAAHLQAHPV 2269
Cdd:PRK13390   171 pgrdVDAPGDPIVAIARAF--YDISESDIYYSSAPIyhAAPLRWCSMVHAL--GGTVVLAKR---FDAQATLGHVERYRI 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2270 DCLKIVPSHLAGLLAAAGGTAV---LPRECLVTGGEALTGALVQQ--VRALAPTlrIVNHYGPTEttVGILTCTVPEEWP 2344
Cdd:PRK13390   244 TVTQMVPTMFVRLLKLDADVRTrydVSSLRAVIHAAAPCPVDVKHamIDWLGPI--VYEYYSSTE--AHGMTFIDSPDWL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2345 VEQGvPVGHPLAGNeAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfVAHPLAPdrLLYRSGDLARLDGEG 2424
Cdd:PRK13390   320 AHPG-SVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP--FWTTVGDLGSVDEDG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2425 RIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG------ANGVLQLGACIQGSLEGVAEAL---AQRLP 2495
Cdd:PRK13390   394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpemgeqVKAVIQLVEGIRGSDELARELIdytRSRIA 473
                          490       500
                   ....*....|....*....|..
gi 1246793773 2496 EYLCPSRWRAVESMPRLGNGKI 2517
Cdd:PRK13390   474 HYKAPRSVEFVDELPRTPTGKL 495
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2636-3043 6.63e-11

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: 67.79  E-value: 6.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2636 WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRFAHREADAG---- 2711
Cdd:cd19539     12 WFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPdsdr 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2712 -QREDLLAQWQAGLSFDGA---LLRVLALPDPQDgDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRS---PALAA 2784
Cdd:cd19539     92 eRRLEELLRERESRGFDLDeepPIRAVLGRFDPD-DHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAaplPELRQ 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2785 EACGFGAWQAalRQLSAATLDGWRSYWRAQAADAEAIALPWQD--SDNRYADTVHLHDRFERDWTERlLTQTARAYGNEP 2862
Cdd:cd19539    171 QYKEYAAWQR--EALAAPRAAELLDFWRRRLRGAEPTALPTDRprPAGFPYPGADLRFELDAELVAA-LRELAKRARSSL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2863 QEVLLtalalalrdggdAATLWVEMEGHGRDDLGAGL--------DLSRTVGWFTARYPLALHLPAGEDLGAALRSTkdr 2934
Cdd:cd19539    248 FMVLL------------AAYCVLLRRYTGQTDIVVGTpvagrnhpRFESTVGFFVNLLPLRVDVSDCATFRDLIARV--- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2935 MRAVPDrglgfgvlRYLHGEL------AELPVP---------QVCFNYLgQLRAGERDGWALCEEPDGGGRAGGNrrrhL 2999
Cdd:cd19539    313 RKALVD--------AQRHQELpfqqlvAELPVDrdagrhplvQIVFQVT-NAPAGELELAGGLSYTEGSDIPDGA----K 379
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773 3000 LDVNAMLVD--GELRLDWAWPQDAASREAMQALSRRYLAVLRELIA 3043
Cdd:cd19539    380 FDLNLTVTEegTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLA 425
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
670-1041 8.77e-11

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 67.85  E-value: 8.77e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  670 NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTT-LEQILAAWSRGACVVARpd 748
Cdd:PRK06087   183 TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLL-- 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  749 ELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPT 828
Cdd:PRK06087   261 DIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQRGI----KLLSVYGST 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  829 EatisSHYHRVQAIDasRPVPL-----GQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplr 903
Cdd:PRK06087   337 E----SSPHAVVNLD--DPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL---- 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  904 lpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVE 980
Cdd:PRK06087   407 ----DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDAC--VVAmpdERLGERSCAYVV 480
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773  981 CAGEdgfgqaDLNQTDSDQTESerwhraLCE-RLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06087   481 LKAP------HHSLTLEEVVAF------FSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
675-1041 1.00e-10

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: 67.94  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE---ALALSADDRVLHVA----GLAVDTTLEQILAawsrGACVVARP 747
Cdd:cd17642    185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQIIPDTAILTVIpfhhGFGMFTTLGYLIC----GFRVVLMY 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  748 DelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWrDLA-LRCLVVGGDVLPV----ALAQRwFELGLDRRcali 822
Cdd:cd17642    261 K--FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKY-DLSnLHEIASGGAPLSKevgeAVAKR-FKLPGIRQ---- 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  823 nAYGPTEATISShyhRVQAIDASRPVPLGQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASErrfaP 901
Cdd:cd17642    333 -GYGLTETTSAI---LITPEGDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATK----A 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  902 LRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVE 980
Cdd:cd17642    405 LIDKDG----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFdAGVAGIPDEDAGELPAAVVV 480
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  981 CAGEDGFGQADLNQTDSDQTESERWHRAlcerlpaymvPTQFValPRLPRNASGKIDRRAL 1041
Cdd:cd17642    481 LEAGKTMTEKEVMDYVASQVSTAKRLRG----------GVKFV--DEVPKGLTGKIDRRKI 529
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1142-1349 1.04e-10

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: 67.09  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQP--DRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQD 1219
Cdd:cd19536      4 LSSLQEGMLFHSLLNPggSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTELD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1220 WRGAADLDSRVDAAFAR-MQEATPLAG-PLVALTHAHCDDGER--LLICAHHLIVDAVSWRLLLGELFDGLAALARGEAW 1295
Cdd:cd19536     84 LTPLEEQLDPLRAYKEEtKIRRFDLGRaPLVRAALVRKDERERflLVISDHHSILDGWSLYLLVKEILAVYNQLLEYKPL 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 1296 TPSARgASYADYVeALREADDAQRFDAGFWRE-LAAQPMQALPQDRPVALADARQ 1349
Cdd:cd19536    164 SLPPA-QPYRDFV-AHERASIQQAASERYWREyLAGATLATLPALSEAVGGGPEQ 216
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
2307-2529 1.05e-10

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 67.33  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2307 ALVQQVRA----LAPTlrivnhYGPTETTVGILTCTvPEEWpveqgvpvghpLAGNeawvlDRFGLPAP-------VGVA 2375
Cdd:PRK07445   245 SLLEQARQlqlrLAPT------YGMTETASQIATLK-PDDF-----------LAGN-----NSSGQVLPhaqitipANQT 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2376 GELYLGGGNLSLGYWQRAEQTAERFVahplapdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL 2455
Cdd:PRK07445   302 GNITIQAQSLALGYYPQILDSQGIFE------------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2456 PGVEVAAVLALPGANGVLQLGACI-----QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQD 2529
Cdd:PRK07445   370 GLVQDVCVLGLPDPHWGEVVTAIYvpkdpSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQR 448
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
2171-2463 1.56e-10

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 67.39  E-value: 1.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2171 RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL------ANYVAG------------VLPV-------------LDLGEDA 2219
Cdd:PRK08974   200 KPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlanleqAKAAYGpllhpgkelvvtALPLyhifaltvncllfIELGGQN 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLAT----LSTVAADLG---FTA------LFGALLSGRRVRllpaELAFDAqalaahlqahpvdcLKIVpshlagllaaa 2286
Cdd:PRK08974   280 LLITnprdIPGFVKELKkypFTAitgvntLFNALLNNEEFQ----ELDFSS--------------LKLS----------- 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2287 ggtavlpreclVTGGEALTGALVQQVRALAPTlRIVNHYGPTETTvGILTCTvPEEWPVEQGvPVGHPLAGNEAWVLDRF 2366
Cdd:PRK08974   331 -----------VGGGMAVQQAVAERWVKLTGQ-YLLEGYGLTECS-PLVSVN-PYDLDYYSG-SIGLPVPSTEIKLVDDD 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2367 GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLApdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELG 2446
Cdd:PRK08974   396 GNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPN 468
                          330
                   ....*....|....*...
gi 1246793773 2447 EVEQVLAQLPGV-EVAAV 2463
Cdd:PRK08974   469 EIEDVVMLHPKVlEVAAV 486
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
735-975 1.58e-10

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: 66.82  E-value: 1.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  735 AAWSRGACVVARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADdwRDLALRCLVVGGDVL-PVALAQRWFEL 813
Cdd:cd05974    147 APWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLAS--FDVKLREVVGAGEPLnPEVIEQVRRAW 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  814 GLDRRcaliNAYGPTEATISSHYHRVQAIdasRPVPLGQLLPGRIAAVLDAHGRIVPRG-VCGEL-ALGGIGLAEGYRGD 891
Cdd:cd05974    225 GLTIR----DGYGQTETTALVGNSPGQPV---KAGSMGRPLPGYRVALLDPDGAPATEGeVALDLgDTRPVGLMKGYAGD 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  892 aaaserrfaPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGA 971
Cdd:cd05974    298 ---------PDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAV--AEAAVVPSPD 366

                   ....
gi 1246793773  972 AQRL 975
Cdd:cd05974    367 PVRL 370
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2539-2610 1.85e-10

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: 59.87  E-value: 1.85e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2539 DETPVNEVLRELWQKLLG--REHIGAHDNFFA-LGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQA 2610
Cdd:COG0236      2 PREELEERLAEIIAEVLGvdPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEE 77
PRK07867 PRK07867
acyl-CoA synthetase; Validated
601-1059 1.87e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 67.01  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  601 LLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD---AQGLAGFAPSVAI------AVDELKLDGAGENGSGENA 671
Cdd:PRK07867    70 LLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTEsahAELLDGLDPGVRVinvdspAWADELAAHRDAEPPFRVA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGlavdttleqILAAWSRGACVVA 745
Cdd:PRK07867   150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYvsmplfHSNA---------VMAGWAVALAAGA 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 rpdELLEPQRFLA--FLSE-RAITVTdlapaYANELVRA--------SVADDwRDLALRcLVVGGDVLPVALAQrwFElg 814
Cdd:PRK07867   221 ---SIALRRKFSAsgFLPDvRRYGAT-----YANYVGKPlsyvlatpERPDD-ADNPLR-IVYGNEGAPGDIAR--FA-- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  815 ldRR--CALINAYGPTEATISshyhrVQAIDASRPVPLGQLLPG-RI----------AAVLDAHGRIVPRGVCGELA-LG 880
Cdd:PRK07867   287 --RRfgCVVVDGFGSTEGGVA-----ITRTPDTPPGALGPLPPGvAIvdpdtgtecpPAEDADGRLLNADEAIGELVnTA 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  881 GIGLAEGYRGDAAASERRfaplrlpsgesLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ 958
Cdd:PRK07867   360 GPGGFEGYYNDPEADAER-----------MRggVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPD 428
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  959 VRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTEserwhralcerLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:PRK07867   429 ATEVAVyAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQPD-----------LGPKQWPSYVRVCAELPRTATFKVL 497
                          490       500
                   ....*....|....*....|....*...
gi 1246793773 1038 RRALPA------PPVLAQAERTPPRTAE 1059
Cdd:PRK07867   498 KRQLSAegvdcaDPVWWIRRLTPSDYAA 525
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
2141-2523 1.91e-10

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 65.84  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 GAAPAWVPASVRWLD-AESVLDVVSAYEEpprvdVDADTpAYLIYTSGSTGTPKGVVVSQGNLA---------------- 2203
Cdd:PRK07824     4 GRAPALLPVPAQDERrAALLRDALRVGEP-----IDDDV-ALVVATSGTTGTPKGAMLTAAALTasadathdrlggpgqw 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2204 -----------------NYVAGVLPV-LDLGEDASLATLSTVAADLGftalfgallSGRR-VRLLPAEL--AFDaqalaa 2262
Cdd:PRK07824    78 llalpahhiaglqvlvrSVIAGSEPVeLDVSAGFDPTALPRAVAELG---------GGRRyTSLVPMQLakALD------ 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2263 hlqahpvdclkivpsHLAGLLAAAGGTAVLpreclvTGGEALTGALVQQVRALAptLRIVNHYGPTETTVGiltCtvpee 2342
Cdd:PRK07824   143 ---------------DPAATAALAELDAVL------VGGGPAPAPVLDAAAAAG--INVVRTYGMSETSGG---C----- 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2343 wpVEQGVpvghPLAGNEAWVLDrfglpapvgvaGELYLGGGNLSLGYwqraeqtaERFVAHPLAPDRLLYRSGDLARLDg 2422
Cdd:PRK07824   192 --VYDGV----PLDGVRVRVED-----------GRIALGGPTLAKGY--------RNPVDPDPFAEPGWFRTDDLGALD- 245
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2423 EGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGS------LEGVAEALAQRLPE 2496
Cdd:PRK07824   246 DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDggpaptLEALRAHVARTLDR 325
                          410       420
                   ....*....|....*....|....*..
gi 1246793773 2497 YLCPSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:PRK07824   326 TAAPRELHVVDELPRRGIGKVDRRALV 352
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
673-1041 2.01e-10

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: 65.96  E-value: 2.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRGACVV-A 745
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLcglplfHVNGSVV-----TLLTPLASGAHVVlA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 RPDELLEPQRFLAF--LSE--RAITVTDLAPAYAnelVRASVADDwRDL-ALRCLVVGGDVLPVALAQRwFE--LGLdrr 818
Cdd:cd05944     76 GPAGYRNPGLFDNFwkLVEryRITSLSTVPTVYA---ALLQVPVN-ADIsSLRFAMSGAAPLPVELRAR-FEdaTGL--- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  819 cALINAYGPTEATISSHyhRVQAIDASRPVPLGQLLP---GRIAaVLDAHGRIVPR---GVCGELALGGIGLAEGYRGDA 892
Cdd:cd05944    148 -PVVEGYGLTEATCLVA--VNPPDGPKRPGSVGLRLPyarVRIK-VLDGVGRLLRDcapDEVGEICVAGPGVFGGYLYTE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  893 AASERRFAPLRLpsgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAA 972
Cdd:cd05944    224 GNKNAFVADGWL---------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV--AFAGAVGQPDA 292
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  973 QrlvawvecAGEDGFGQADLNQ-TDSDQTESERWHRalcERLPAY-MVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05944    293 H--------AGELPVAYVQLKPgAVVEEEELLAWAR---DHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
2180-2532 2.61e-10

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 66.60  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2180 AYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDL--GEDASLATLSTVAAdLGFTALFG-ALLSGRRVRLLPaelAF 2255
Cdd:PRK06710   209 ALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCkeGEEVVLGVLPFFHV-YGMTAVMNlSIMQGYKMVLIP---KF 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2256 DAQALAAHLQAHPVDCLKIVPShlagLLAAAGGTAVLP-------RECLvtGGEALTGALVQQVRALAPTLRIVNHYGPT 2328
Cdd:PRK06710   285 DMKMVFEAIKKHKVTLFPGAPT----IYIALLNSPLLKeydissiRACI--SGSAPLPVEVQEKFETVTGGKLVEGYGLT 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2329 ETTVgiltcTVPEEWPVEQGVP--VGHPLAGNEAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAerfvahPL 2405
Cdd:PRK06710   359 ESSP-----VTHSNFLWEKRVPgsIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA------AV 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2406 APDRLLYrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGA 2477
Cdd:PRK06710   428 LQDGWLH-TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDpyrgetvkAFVVLKEGT 506
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2478 -CIQGSLEGVAEalaQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDAD 2532
Cdd:PRK06710   507 eCSEEELNQFAR---KYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNED 559
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2352-2528 3.18e-10

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 66.17  E-value: 3.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2352 GHPLAGN-EAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHPLapdrllYRSGDLARLDGEGRIVYLG 2430
Cdd:PRK10946   356 GRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------YCSGDLVSIDPDGYITVVG 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2431 RGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGAngvlQLG----ACI--QGSLEGVA---EALAQRLPEYLCPS 2501
Cdd:PRK10946   430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDE----LMGekscAFLvvKEPLKAVQlrrFLREQGIAEFKLPD 505
                          170       180
                   ....*....|....*....|....*..
gi 1246793773 2502 RWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK10946   506 RVECVDSLPLTAVGKVDKKQLRQWLAS 532
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1598-1828 4.22e-10

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: 65.35  E-value: 4.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1598 FPLTPLQRgvLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSvpHQIVLADAAAPWQT 1677
Cdd:cd19534      2 VPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGG--WQQRIRGDVEELFR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1678 LDWSALDDAAQDAQLQRwLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG 1757
Cdd:cd19534     78 LEVVDLSSLAQAAAIEA-LAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 1758 ATLRLPPAPGFQaylDWRERQ-------DLARQRGWWRERLSGYAGTAALPAPVAAAHhpvqREECERRLSAHDSERL 1828
Cdd:cd19534    157 EPIPLPSKTSFQ---TWAELLaeyaqspALLEELAYWRELPAADYWGLPKDPEQTYGD----ARTVSFTLDEEETEAL 227
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
3540-3946 6.38e-10

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: 65.45  E-value: 6.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3540 AEDGELDYATLDRRSSQLA-TLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVC 3618
Cdd:cd05905     10 KEATTLTWGKLLSRAEKIAaVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3619 LSVSQRALAVELP------GTALCLDDP--------------FTRAQLDAVEPGELPEVPTEapAYLIYTSGSTGTPKGV 3678
Cdd:cd05905     90 VALTVEACLKGLPkkllksKTAAEIAKKkgwpkildfvkipkSKRSKLKKWGPHPPTRDGDT--AYIEYSFSSDGSLSGV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3679 VVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLyGGRAVLVPEA-VCRQPDAFLDLLAEYGVTVL 3757
Cdd:cd05905    168 AVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYS-GHHTILIPPElMKTNPLLWLQTLSQYKVRDA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3758 NQTPSAFYALQSQAMRRELALNVRAVVFGG------EALEP---SRLQPWRERY-------------------PQAELVN 3809
Cdd:cd05905    247 YVKLRTLHWCLKDLSSTLASLKNRDVNLSSlrmcmvPCENRpriSSCDSFLKLFqtlglspravstefgtrvnPFICWQG 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3810 MYGITETTVHVSFHRLSdEDLQSPTSR----------IGSALPDLAVHVLDAAGQPvPLGV--VGELVVEGDGVAQGYWQ 3877
Cdd:cd05905    327 TSGPEPSRVYLDMRALR-HGVVRLDERdkpnslplqdSGKVLPGAQVAIVNPETKG-LCKDgeIGEIWVNSPANASGYFL 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3878 RPELTAERFVER---------GGQRFYRSGDLGRYR---------ADGSLEYR-GRGDDQVKLRGYRIEPGEIAAKI-AS 3937
Cdd:cd05905    405 LDGETNDTFKVFpstrlstgiTNNSYARTGLLGFLRptkctdlnvEEHDLLFVvGSIDETLEVRGLRHHPSDIEATVmRV 484

                   ....*....
gi 1246793773 3938 LPQVSDAAV 3946
Cdd:cd05905    485 HPYRGRCAV 493
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
615-1041 8.70e-10

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 64.69  E-value: 8.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  615 LDTEWPQARRAEVVAASGCDavltdaqglaGFAPSVAIAVDELKLDgAGENGSGENAAPNQLAYILYTSGSTGIPKGVEV 694
Cdd:PRK13295   149 LRPELPALRHVVVVGGDGAD----------SFEALLITPAWEQEPD-APAILARLRPGPDDVTQLIYTSGTTGEPKGVMH 217
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  695 GHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQILaawsrGACVVARpdELLEPQRFLAFLSERAITVT 768
Cdd:PRK13295   218 TANTLMANIVPYAERLGLGADDVILmaspmaHQTGFMYGLMMPVML-----GATAVLQ--DIWDPARAAELIRTEGVTFT 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  769 DLAPAYANELVRAsVADDWRDLA-LRCLVVGGDVLPVALAQR-WFELGLdrrcALINAYGPTE---ATISSHYHRVQAID 843
Cdd:PRK13295   291 MASTPFLTDLTRA-VKESGRPVSsLRTFLCAGAPIPGALVERaRAALGA----KIVSAWGMTEngaVTLTKLDDPDERAS 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  844 ASRPVPlgqlLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYrgdaaaserrFAPLRLPSGESLRMYRSGDRVRLLD 923
Cdd:PRK13295   366 TTDGCP----LPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGY----------LKRPQLNGTDADGWFDTGDLARIDA 431
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  924 DGELQFLGRADfQVKLRG-YRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVECAGEDGFGQADLnqtdsdq 999
Cdd:PRK13295   432 DGYIRISGRSK-DVIIRGgENIPVVEIEALLYRHPAIAQVA--IVAypdERLGERACAFVVPRPGQSLDFEEM------- 501
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1246793773 1000 tesERWHRAlcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK13295   502 ---VEFLKA--QKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
785-1041 8.80e-10

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 64.78  E-value: 8.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  785 DDWRDL---ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEAtisSHYHRVQAIDASRPVPLGQLLPGRIAAV 861
Cdd:PRK05677   318 EAFRKLdfsALKLTLSGGMALQLATAERWKEV---TGCAICEGYGMTET---SPVVSVNPSQAIQVGTIGIPVPSTLCKV 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  862 LDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRG 941
Cdd:PRK05677   392 IDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL--------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSG 463
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  942 YRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVecagedgfgqadLNQTDSDQTESE--RWHRAlceRLPAYMV 1018
Cdd:PRK05677   464 FNVYPNELEDVLAALPGVlQCAAIGVPDEKSGEAIKVFV------------VVKPGETLTKEQvmEHMRA---NLTGYKV 528
                          250       260
                   ....*....|....*....|...
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK05677   529 PKAVEFRDELPTTNVGKILRREL 551
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
549-1041 9.56e-10

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 64.60  E-value: 9.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVV 628
Cdd:PRK03640    16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  629 AASGCDAVLTDAQGLAGFAPSVAIAVDELkldgagENGSGENAAP------NQLAYILYTSGSTGIPKGVEVGHAALAAH 702
Cdd:PRK03640    96 DDAEVKCLITDDDFEAKLIPGISVKFAEL------MNGPKEEAEIqeefdlDEVATIMYTSGTTGKPKGVIQTYGNHWWS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  703 IDAAAEALALSADDRVL------HVAGLAVdtTLEQILaawsRGACVVARpdELLEPQRFLAFLSERAITVTDLAPAYAN 776
Cdd:PRK03640   170 AVGSALNLGLTEDDCWLaavpifHISGLSI--LMRSVI----YGMRVVLV--EKFDAEKINKLLQTGGVTIISVVSTMLQ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  777 ELVrASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrrcALINAYGPTE-----ATISSHYHRVQAIDASRPvplg 851
Cdd:PRK03640   242 RLL-ERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKGI----PVYQSYGMTEtasqiVTLSPEDALTKLGSAGKP---- 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  852 qLLPGRIAAVLDahGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLG 931
Cdd:PRK03640   313 -LFPCELKIEKD--GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-----DG----WFKTGDIGYLDEEGFLYVLD 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  932 RADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAA---QRLVAWVECAGEdgFGQADLnqtdsdqteserwhRA 1008
Cdd:PRK03640   381 RRSDLIISGGENIYPAEIEEVLLSHPGV--AEAGVVGVPDDkwgQVPVAFVVKSGE--VTEEEL--------------RH 442
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1246793773 1009 LC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK03640   443 FCeEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
3779-4018 1.04e-09

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 64.25  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEALEPSRLQpwRERYPQAELVNMYGITETTvhvsfhrlsdedlqsptSRIGSALPDLAVHVLDAAGQPVP- 3857
Cdd:PRK07445   231 QFRTILLGGAPAWPSLLE--QARQLQLRLAPTYGMTETA-----------------SQIATLKPDDFLAGNNSSGQVLPh 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3858 ------LGVVGELVVEGDGVAQGYWqrPELTAErfverggQRFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEI 3931
Cdd:PRK07445   292 aqitipANQTGNITIQAQSLALGYY--PQILDS-------QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEV 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3932 AAKIASLPQVSDaaVTVEGQGEGAW---LMAYAVAADGaEPDPQSLREALRALLPDYMLPRLIQLLPALPLTANGKLDRK 4008
Cdd:PRK07445   363 EAAILATGLVQD--VCVLGLPDPHWgevVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQ 439
                          250
                   ....*....|
gi 1246793773 4009 ALPKPETQDR 4018
Cdd:PRK07445   440 QLQQIAVQRL 449
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
3654-4007 1.24e-09

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 64.40  E-value: 1.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3654 LPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVERLFTAATQtgRFSFDE-HDV---W-SLFHSHAFDFAVWELWGawlyG 3728
Cdd:PRK05851   146 LTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNA--RVGLDAaTDVgcsWlPLYHDMGLAFLLTAALA----G 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3729 GRAVLVPE-AVCRQPDAFLDLLAEYGVTvLNQTPSAFYALQSQAMRR--ELAL-NVRAVVFGGE------------ALEP 3792
Cdd:PRK05851   220 APLWLAPTtAFSASPFRWLSWLSDSRAT-LTAAPNFAYNLIGKYARRvsDVDLgALRVALNGGEpvdcdgferfatAMAP 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3793 SRLQPwrerypqAELVNMYGITETTVHVS---------FHRLSDEDLQSPT--SRIGSALPDLAVHVlDAAGQPVPLGV- 3860
Cdd:PRK05851   299 FGFDA-------GAAAPSYGLAESTCAVTvpvpgiglrVDEVTTDDGSGARrhAVLGNPIPGMEVRI-SPGDGAAGVAGr 370
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3861 -VGELVVEGDGVAQGYWQRPELTAerfverggQRFYRSGDLGrYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLP 3939
Cdd:PRK05851   371 eIGEIEIRGASMMSGYLGQAPIDP--------DDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVR 441
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 3940 QVSDAAVTVEGQGEGAWLMAYAVAADGAEPDPQSLREAL--RALLPDYMLPRLIQLLP--ALPLTANGKLDR 4007
Cdd:PRK05851   442 GVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSEVvqRVASECGVVPSDVVFVApgSLPRTSSGKLRR 513
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
678-1038 1.95e-09

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: 62.42  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  678 YILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVArpDELLEPQRFL 757
Cdd:cd17633      4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG--QRKFNPKSWI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  758 AFLSERAITVTDLAPAYANELVRASVAddwrDLALRCLVVGGDVLPVALAQ---RWFElgldrRCALINAYGPTEATISS 834
Cdd:cd17633     82 RKINQYNATVIYLVPTMLQALARTLEP----ESKIKSIFSSGQKLFESTKKklkNIFP-----KANLIEFYGTSELSFIT 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  835 hYHRVQaiDASRPVPLGQLLPGRIAAVLDAHGRIVPR-GVCGELALGGIGLAEGYRGDAaaserrfaplrlpsgeslrMY 913
Cdd:cd17633    153 -YNFNQ--ESRPPNSVGRPFPNVEIEIRNADGGEIGKiFVKSEMVFSGYVRGGFSNPDG-------------------WM 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  914 RSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRaaAAGVVGEGAAqrlvawvecagedGFGQADLN 993
Cdd:cd17633    211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIE--EAIVVGIPDA-------------RFGEIAVA 275
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773  994 QTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDR 1038
Cdd:cd17633    276 LYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1160-1370 1.95e-09

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: 63.10  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1160 YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPaPAIQAQDwrgAADLDSRVDAAFARMQE 1239
Cdd:cd20484     24 YNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKP-LSFQEED---ISSLKESEIIAYLREKA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1240 ATPLA---GPLVALTHAHCDDGER-LLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVE----AL 1311
Cdd:cd20484    100 KEPFVlenGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPASYYDFVAweqdML 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1312 READDAQRFdaGFWREL--AAQPMQALPQDRPVALAdarQSNVGrivQTLDAGLTADLLER 1370
Cdd:cd20484    180 AGAEGEEHR--AYWKQQlsGTLPILELPADRPRSSA---PSFEG---QTYTRRLPSELSNQ 232
PRK08316 PRK08316
acyl-CoA synthetase; Validated
533-1041 2.08e-09

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 63.41  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  533 TVGnvvDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALcLPRGLDWYCLL-LGAWRAGLS 611
Cdd:PRK08316    12 TIG---DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAA-LGHNSDAYALLwLACARAGAV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  612 VIPLDTEWPQARRAEVVAASGCDAVLTDaqglAGFAPSVAIAVDELK-------------------LDGAGENGSGENAA 672
Cdd:PRK08316    88 HVPVNFMLTGEELAYILDHSGARAFLVD----PALAPTAEAALALLPvdtlilslvlggreapggwLDFADWAEAGSVAE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  673 P------NQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGL----AVDTTLEQILAAWSRGAc 742
Cdd:PRK08316   164 PdveladDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLyhcaQLDVFLGPYLYVGATNV- 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  743 VVARPDellePQRFLAFLSERAITVTDLAPAYANELVRASVADDwRDL-ALRCLVVGGDVLPVALAQRwfelgLDRR--- 818
Cdd:PRK08316   243 ILDAPD----PELILRTIEAERITSFFAPPTVWISLLRHPDFDT-RDLsSLRKGYYGASIMPVEVLKE-----LRERlpg 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  819 CALINAYGPTE----ATI-SSHYHRVQAIDASRPVPLGQllpgriAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAA 893
Cdd:PRK08316   313 LRFYNCYGQTEiaplATVlGPEEHLRRPGSAGRPVLNVE------TRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPE 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  894 ASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVGEGAAQ 973
Cdd:PRK08316   387 KTAEAFR-----GG----WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA--VIGLPDPK 455
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  974 rlvaWVEC--------AGEdgfgqadlnqtdsDQTESERWhrALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK08316   456 ----WIEAvtavvvpkAGA-------------TVTEDELI--AHCrARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
PRK08315 PRK08315
AMP-binding domain protein; Validated
2325-2531 2.21e-09

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 63.29  E-value: 2.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2325 YGPTETTVGIlTCTVPEEwPVEQGV-PVGHPLAGNEAWVLDRF-GLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErfva 2402
Cdd:PRK08315   348 YGMTETSPVS-TQTRTDD-PLEKRVtTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE---- 421
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2403 hPLAPDRLLyRSGDLARLDGEG--RIVylGRgdhqVK---IRG----Y-RvelgEVEQVLAQLPGVEVAAVLALPGANGV 2472
Cdd:PRK08315   422 -AIDADGWM-HTGDLAVMDEEGyvNIV--GR----IKdmiIRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYG 489
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2473 LQLGACI------QGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKID----RQALADLLQQDDA 2531
Cdd:PRK08315   490 EEVCAWIilrpgaTLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQkfkmREMMIEELGLQAA 558
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
672-1036 2.29e-09

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: 63.36  E-value: 2.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGV-EVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQIL-AAWSRGACVV---AR 746
Cdd:cd17634    230 NAEDPLFILYTSGTTGKPKGVlHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLyGPLACGATTLlyeGV 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  747 PDELlEPQRFLAFLSERAITVTDLAPAYANELVRASvaDDW---RDLA-LRCLVVGGDVL-PVALAQRWFELGlDRRCAL 821
Cdd:cd17634    310 PNWP-TPARMWQVVDKHGVNILYTAPTAIRALMAAG--DDAiegTDRSsLRILGSVGEPInPEAYEWYWKKIG-KEKCPV 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  822 INAYGPTEA-----TISSHYHRVQAIDASRPVPlgqllpGRIAAVLDAHGRIVPRGVCGELALGgIGLAEGYRGDAAASE 896
Cdd:cd17634    386 VDTWWQTETggfmiTPLPGAIELKAGSATRPVF------GVQPAVVDNEGHPQPGGTEGNLVIT-DPWPGQTRTLFGDHE 458
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  897 RRFAP-LRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVGEGAAQR 974
Cdd:cd17634    459 RFEQTyFSTFKG----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVaEAAVVGIPHAIKGQA 534
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  975 LVAWVEC-AGEdgfgqadlnqTDSDQTESERWHRaLCERLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:cd17634    535 PYAYVVLnHGV----------EPSPELYAELRNW-VRKEIGPLATPDVVHWVDSLPKTRSGKI 586
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1142-1337 2.44e-09

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: 62.86  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASF--ERADGQWRQQVAAPgPAPAIQA 1217
Cdd:cd19532      4 MSFGQSrfWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLAS-SPLRLEH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRGAADldsrVDAAFARMQEAT--PLAGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGElfdgLAALARGEA 1294
Cdd:cd19532     83 VQISDEAE----VEEEFERLKNHVydLESGETMRIVLLSLSPTEhYLIFGYHHIAMDGVSFQIFLRD----LERAYNGQP 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773 1295 WTPSARgaSYADYVEALREADDAQRFDAG--FWRELAAQPMQALP 1337
Cdd:cd19532    155 LLPPPL--QYLDFAARQRQDYESGALDEDlaYWKSEFSTLPEPLP 197
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1141-1347 2.45e-09

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: 62.77  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1141 GLSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPaIQAQ 1218
Cdd:cd19533      3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVP-IRHI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1219 DWRGAADLDSrvdAAFARMQEAT----PLAG-PLVALTHAHCDDGERLL-ICAHHLIVDAVSWRLLLGELFDGLAALARG 1292
Cdd:cd19533     82 DLSGDPDPEG---AAQQWMQEDLrkplPLDNdPLFRHALFTLGDNRHFWyQRVHHIVMDGFSFALFGQRVAEIYTALLKG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1293 EAWTPSARGaSYADYVEALREADDAQRF--DAGFWRELAAQPMQalpqdrPVALADA 1347
Cdd:cd19533    159 RPAPPAPFG-SFLDLVEEEQAYRQSERFerDRAFWTEQFEDLPE------PVSLARR 208
PRK08308 PRK08308
acyl-CoA synthetase; Validated
2413-2522 2.62e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 62.75  E-value: 2.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2413 RSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVL----ALPGANGVLQLGACIQGSLEGVAE 2488
Cdd:PRK08308   294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEIDPVQLRE 373
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK08308   374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
602-1038 3.50e-09

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 62.86  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  602 LLGAWRAG--LSVIP------LDTEWPQARrAEVVAASGCDAVLTDAQGLAGFAPSV-AIAVDELKLDG-AGENGSGENA 671
Cdd:PRK05851    71 IQGAWLAGaaVSILPgpvrgaDDGRWADAT-LTRFAGIGVRTVLSHGSHLERLRAVDsSVTVHDLATAAhTNRSASLTPP 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSAD-DRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL 750
Cdd:PRK05851   150 DSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  751 LE--PQRFLAFLSERAITVTDlAPAYANELV--RASVADDWRDLALRCLVVGGDVLPVALAQRWFE----LGLDRRcALI 822
Cdd:PRK05851   230 FSasPFRWLSWLSDSRATLTA-APNFAYNLIgkYARRVSDVDLGALRVALNGGEPVDCDGFERFATamapFGFDAG-AAA 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  823 NAYGPTEAT---------ISSHYHRVQAIDAS---RPVPLGQLLPG---RIAAVlDAHGRIVPRGVcGELALGGIGLAEG 887
Cdd:PRK05851   308 PSYGLAESTcavtvpvpgIGLRVDEVTTDDGSgarRHAVLGNPIPGmevRISPG-DGAAGVAGREI-GEIEIRGASMMSG 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  888 YRGDAaaserrfaPLRlpSGEslrMYRSGDRVRLLDDGeLQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV 967
Cdd:PRK05851   386 YLGQA--------PID--PDD---WFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV 451
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773  968 G--EGAA-QRLVAWVECAGedgfgqadlnqTDSDQTESERWHR--ALCERLPAYMVptqFVALPRLPRNASGKIDR 1038
Cdd:PRK05851   452 GtgEGSArPGLVIAAEFRG-----------PDEAGARSEVVQRvaSECGVVPSDVV---FVAPGSLPRTSSGKLRR 513
PRK05857 PRK05857
fatty acid--CoA ligase;
2051-2523 5.08e-09

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 62.33  E-value: 5.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVE--EGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCL---PRTFAQLAAMAAVwhrGAAWLPLDPQHPDA-- 2123
Cdd:PRK05857    29 EAIALRrcDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISdngPETYLSVLACAKL---GAIAVMADGNLPIAai 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2124 -RQIAVLDDSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVD---------ADTPAYLIYTSGSTGTPK 2193
Cdd:PRK05857   106 eRFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAAslagnadqgSEDPLAMIFTSGTTGEPK 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2194 GVVvsqgnLANYVAGVLPvlDLGEDASLATLSTVAADLGFTAL----FGAL---LSGrrvrLLPAELAFDAQALAAHLQA 2266
Cdd:PRK05857   186 AVL-----LANRTFFAVP--DILQKEGLNWVTWVVGETTYSPLpathIGGLwwiLTC----LMHGGLCVTGGENTTSLLE 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2267 HPVD------CLkiVPS--HLAGLLAAAGGTAVLPRECLVTGGEALTGALVQQVRALAptLRIVNHYGPTETTVGILTCT 2338
Cdd:PRK05857   255 ILTTnavattCL--VPTllSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEATG--VRTAQVYGLSETGCTALCLP 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2339 VPEE--WPVEQGVpVGHPLAGNEAWVLDRFG------LPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrl 2410
Cdd:PRK05857   331 TDDGsiVKIEAGA-VGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG------- 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2411 LYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLE---GVA 2487
Cdd:PRK05857   403 WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEldeSAA 482
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1246793773 2488 EALAQRL-------PEYLC-PSRWRAVESMPRLGNGKIDRQALA 2523
Cdd:PRK05857   483 RALKHTIaarfrreSEPMArPSTIVIVTDIPRTQSGKVMRASLA 526
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
3637-3942 7.15e-09

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: 61.49  E-value: 7.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3637 LDD----PFTRAQ-LDAVEPGELPEVPTEAPAYLIYTSGSTGTPKGVVVTHRNVE-------RLFTAATQTGrfsfdeHD 3704
Cdd:cd05913     50 LDDlrklPFTTKEdLRDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDvwaelvaRCLDAAGVTP------GD 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3705 VWSLFHSHAFDFAVWEL-WGAWLYGgraVLVPEAVCRQPDAFLDLLAEYGVTVLNQTPSafYALQ--SQAMRREL---AL 3778
Cdd:cd05913    124 RVQNAYGYGLFTGGLGFhYGAERLG---ALVIPAGGGNTERQLQLIKDFGPTVLCCTPS--YALYlaEEAEEEGIdprEL 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3779 NVRAVVFGGEA-LEPSRLQpwRERYPQAELVNMYGITE---------TTVHVSFHRLSDEdlqsptsrigsalpdLAVHV 3848
Cdd:cd05913    199 SLKVGIFGAEPwTEEMRKR--IERRLGIKAYDIYGLTEiigpgvafeCEEKDGLHIWEDH---------------FIPEI 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3849 LD-AAGQPVPLGVVGELVVEgdgvaqgywqrpELTaerfVERGGQRFYRSGDLGRYRADGSLEYR---------GRGDDQ 3918
Cdd:cd05913    262 IDpETGEPVPPGEVGELVFT------------TLT----KEAMPLIRYRTRDITRLLPGPCPCGRthrridritGRSDDM 325
                          330       340
                   ....*....|....*....|....
gi 1246793773 3919 VKLRGYRIEPGEIAAKIASLPQVS 3942
Cdd:cd05913    326 LIIRGVNVFPSQIEDVLLKIPGLG 349
PRK07638 PRK07638
acyl-CoA synthetase; Validated
2108-2522 8.84e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 61.33  E-value: 8.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2108 HRGAAWLPLDPQHPDARQIaVLDDSGARIVIGWGAAPA-W--VPASVRWLDAE-------SVLDVV--SAY-------EE 2168
Cdd:PRK07638    37 CKVANWLNEKESKNKTIAI-LLENRIEFLQLFAGAAMAgWtcVPLDIKWKQDElkerlaiSNADMIvtERYklndlpdEE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2169 PPRVDVD---------ADTPA----------YLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAA 2229
Cdd:PRK07638   116 GRVIEIDewkrmiekyLPTYApienvqnapfYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVH 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2230 DLgFtaLFGA---LLSGRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPShlaGLLAAAGGTAVLPRECLVTGGEALTG 2306
Cdd:PRK07638   196 SL-F--LYGAistLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVPT---MLESLYKENRVIENKMKIISSGAKWE 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2307 AL-VQQVRALAPTLRIVNHYGPTEttVGILTCTVPEEwPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNL 2385
Cdd:PRK07638   267 AEaKEKIKNIFPYAKLYEFYGASE--LSFVTALVDEE-SERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQF 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2386 SLGYWQRAEQTAErfvahplAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA 2465
Cdd:PRK07638   344 FMGYIIGGVLARE-------LNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG 416
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2466 LPGANGVLQLGACIQGS--LEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK07638   417 VPDSYWGEKPVAIIKGSatKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PLN02574 PLN02574
4-coumarate--CoA ligase-like
2170-2526 1.04e-08

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 61.40  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2170 PRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAgvlpvLDLGEDASL----ATLSTVAADLGFTALFG------A 2239
Cdd:PLN02574   191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVE-----LFVRFEASQyeypGSDNVYLAALPMFHIYGlslfvvG 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2240 LLS-GRRVRLLPAelaFDAQALAAHLQAHPVDCLKIVPSHLAGLLAAAGGTAVLPRECLV---TGGEALTGALVQQVRAL 2315
Cdd:PLN02574   266 LLSlGSTIVVMRR---FDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKqvsCGAAPLSGKFIQDFVQT 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETT-VGILTCTVPEewpVEQGVPVGHpLAGN-EAWVLD-RFGLPAPVGVAGELYLGGGNLSLGYWQR 2392
Cdd:PLN02574   343 LPHVDFIQGYGMTESTaVGTRGFNTEK---LSKYSSVGL-LAPNmQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNN 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLA------- 2465
Cdd:PLN02574   419 PKATQSTIDK-----DGWL-RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAvpdkecg 492
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 2466 -LPGANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLL 2526
Cdd:PLN02574   493 eIPVAFVVRRQGSTL--SQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
2062-2497 1.68e-08

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: 60.56  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALcLPRTFAQ-LAAMAAVWHRGAAWLPLDPQ-HPD-ARQIavLDDSGARIVI 2138
Cdd:cd05932      7 FTWGEVADKARRLAAALRALGLEPGSKIAL-ISKNCAEwFITDLAIWMAGHISVPLYPTlNPDtIRYV--LEHSESKALF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 -----GWGAAPAWVPASV--RWLDAESVL-------DVVSAY----EEPPRvdvDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05932     84 vgkldDWKAMAPGVPEGLisISLPPPSAAncqyqwdDLIAQHppleERPTR---FPEQLATLIYTSGTTGQPKGVMLTFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2201 NLANYVAGVLPVLDLGEDASLATLSTVAADLGFTALF-GALLSGRRV--------------RLLPAeLAFDAQALAAHLQ 2265
Cdd:cd05932    161 SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVafaesldtfvedvqRARPT-LFFSVPRLWTKFQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2266 AHPVDclKIVPSHLAGLLAAAGGTAVLPR---------ECLVTGGEA--LTGALVQQVRALAptLRIVNHYGPTEtTVGI 2334
Cdd:cd05932    240 QGVQD--KIPQQKLNLLLKIPVVNSLVKRkvlkglgldQCRLAGCGSapVPPALLEWYRSLG--LNILEAYGMTE-NFAY 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2335 LTCTVPEEwpvEQGVPVGHPLAGNEAWVLDRfglpapvgvaGELYLGGGNLSLGYWQRAEQTAERFVAhplapDRLLyRS 2414
Cdd:cd05932    315 SHLNYPGR---DKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTA-----DGFL-RT 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2415 GDLARLDGEGRIVYLGRGDHQVKI-RGYRVELGEVEQVLAQLPGVEVAAVLA--LPGANGVLQLGAciqgslEGVAEALA 2491
Cdd:cd05932    376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGsgLPAPLALVVLSE------EARLRADA 449

                   ....*.
gi 1246793773 2492 QRLPEY 2497
Cdd:cd05932    450 FARAEL 455
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
2173-2525 1.80e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 60.60  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2173 DVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGE-DASLATLSTVAAdLGFT--ALFgALLSGrrvrlL 2249
Cdd:PRK06334   179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEdDVMMSFLPPFHA-YGFNscTLF-PLLSG-----V 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2250 PAELAFDaqalaahlqahPVDCLKIVPSHLAGLLAAAGGTAVL----------PRECL------VTGGEALTGALVQQVR 2313
Cdd:PRK06334   252 PVVFAYN-----------PLYPKKIVEMIDEAKVTFLGSTPVFfdyilktakkQESCLpslrfvVIGGDAFKDSLYQEAL 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2314 ALAPTLRIVNHYGPTETTVGILTCTvpEEWPVEQGVpVGHPLAGNEAWVL-DRFGLPAPVGVAGELYLGGGNLSLGYWqr 2392
Cdd:PRK06334   321 KTFPHIQLRQGYGTTECSPVITINT--VNSPKHESC-VGMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYL-- 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2393 AEQTAERFVAhpLAPDrLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLA------QLPGVEVAAVLAL 2466
Cdd:PRK06334   396 GEDFGQGFVE--LGGE-TWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMegfgqnAADHAGPLVVCGL 472
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2467 PGANGVLQLGACIQGSLEGVAEALAQ-RLPEYLCPSRWRAVESMPRLGNGKIDRQALADL 2525
Cdd:PRK06334   473 PGEKVRLCLFTTFPTSISEVNDILKNsKTSSILKISYHHQVESIPMLGTGKPDYCSLNAL 532
PRK13382 PRK13382
bile acid CoA ligase;
2321-2522 2.33e-08

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 60.16  E-value: 2.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2321 IVNHYGPTEttVGILTCTVPEEWpveQGVP--VGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQ-RAEQTA 2397
Cdd:PRK13382   340 IYNNYNATE--AGMIATATPADL---RAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSgSTKDFH 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2398 ERFVAhplapdrllyrSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGA 2477
Cdd:PRK13382   415 DGFMA-----------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2478 CI--QGSLEGVAEALAQ----RLPEYLCPSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK13382   484 FVvlKPGASATPETLKQhvrdNLANYKVPRDIVVLDELPRGATGKILRREL 534
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1061-1118 2.46e-08

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: 52.95  E-value: 2.46e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 1061 SALCEVWAEVLQC---EVGIHDSFFRLGGDSIRSLQVVARLRER-GYAVTPKLMYQYQSAAE 1118
Cdd:pfam00550    1 ERLRELLAEVLGVpaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
2173-2490 2.69e-08

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: 59.92  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2173 DVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLD--LGEDASLATLSTVAADLGFTALFGALLSGRR----- 2245
Cdd:cd17639     84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAHIFELAAENVCLYRGGTigygs 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2246 VRLL----------------PAELA-----FDAQALAAHLQAHPVDCLK-----IVPSHLAGLLAAAGGTAVL------- 2292
Cdd:cd17639    164 PRTLtdkskrgckgdltefkPTLMVgvpaiWDTIRKGVLAKLNPMGGLKrtlfwTAYQSKLKALKEGPGTPLLdelvfkk 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2293 PREclVTGGealtgalvqQVRAL--------APTLR--------IVNHYGPTETtVGILTCTVPEEWpvEQGVpVGHPLA 2356
Cdd:cd17639    244 VRA--ALGG---------RLRYMlsggaplsADTQEflnivlcpVIQGYGLTET-CAGGTVQDPGDL--ETGR-VGPPLP 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2357 GNEAWVLD--RFG----LPAPvgvAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLLyRSGDLARLDGEGRIVYLG 2430
Cdd:cd17639    309 CCEIKLVDweEGGystdKPPP---RGEILIRGPNVFKGYYKNPEKTKEAF-----DGDGWF-HTGDIGEFHPDGTLKIID 379
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 2431 RGDHQVKIR-GYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQGSLEGVAEAL 2490
Cdd:cd17639    380 RKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKH 440
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
3657-3941 2.97e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 60.14  E-value: 2.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEA--PAYLIYTSGSTGTPKGVV----------------VTHRNVERLFTAATQTGrfsfdehdvWSLFHSHafdfav 3718
Cdd:PTZ00237   249 VPVESshPLYILYTSGTTGNSKAVVrsngphlvglkyywrsIIEKDIPTVVFSHSSIG---------WVSFHGF------ 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3719 weLWGAWLYGGRAVLVPEAVCRQP---DAFLDLLAEYGVTVLNQTPSAFYAL-----QSQAMRRELAL-NVRAVVFGGEA 3789
Cdd:PTZ00237   314 --LYGSLSLGNTFVMFEGGIIKNKhieDDLWNTIEKHKVTHTLTLPKTIRYLiktdpEATIIRSKYDLsNLKEIWCGGEV 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3790 LEPSrLQPWRERYPQAELVNMYGITET--TVHVSFHRLSdedlqSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVE 3867
Cdd:PTZ00237   392 IEES-IPEYIENKLKIKSSRGYGQTEIgiTYLYCYGHIN-----IPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK 465
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 3868 ---GDGVAQGYWQRPELTAERFVERGGqrFYRSGDLGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQV 3941
Cdd:PTZ00237   466 lpmPPSFATTFYKNDEKFKQLFSKFPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2676-2810 3.48e-08

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: 59.14  E-value: 3.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2676 HPMLRARFQRDAAGQWQQ------TLGDWQADRfahREADAGQREDLLAQWQAG---LSFD---GALLRVLALPDPqDGD 2743
Cdd:cd19543     52 HPILRTSFVWEGLGEPLQvvlkdrKLPWRELDL---SHLSEAEQEAELEALAEEdreRGFDlarAPLMRLTLIRLG-DDR 127
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2744 TRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEAcGFGAWQAAL-RQLSAATLDGWRSY 2810
Cdd:cd19543    128 YRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLPPVR-PYRDYIAWLqRQDKEAAEAYWREY 194
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
2321-2463 3.65e-08

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 59.65  E-value: 3.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2321 IVNHYGPTETTvGILTCTvPEEWPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAErf 2400
Cdd:PRK07059   355 ITEGYGLSETS-PVATCN-PVDATEFSGT-IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAK-- 429
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773 2401 vahPLAPDRlLYRSGDLARLDGEG--RIVylGRGDHQVKIRGYRVELGEVEQVLAQLPGV-EVAAV 2463
Cdd:PRK07059   430 ---VMTADG-FFRTGDVGVMDERGytKIV--DRKKDMILVSGFNVYPNEIEEVVASHPGVlEVAAV 489
PRK05850 PRK05850
acyl-CoA synthetase; Validated
588-696 3.77e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 59.57  E-value: 3.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTewPQA-----RRAEVVAASGCDAVLT------------DAQGLAGfAPSV 650
Cdd:PRK05850    62 AVILAPQGLEYIVAFLGALQAGLIAVPLSV--PQGgahdeRVSAVLRDTSPSVVLTtsavvddvteyvAPQPGQS-APPV 138
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773  651 aIAVDELKLDGAGENGSGENAAPNqLAYILYTSGSTGIPKGVEVGH 696
Cdd:PRK05850   139 -IEVDLLDLDSPRGSDARPRDLPS-TAYLQYTSGSTRTPAGVMVSH 182
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1599-1919 4.07e-08

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: 59.03  E-value: 4.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1599 PLTPLQRGVLLESLRGDGADPYFQQTVAELDGEIDAAALAQAWQQTVRRQPMLRTAIVWEGLSVPHQIVLADAAAPWQTL 1678
Cdd:cd19546      6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1679 dwsaldDAAQDAQLQRWLADDAAQGVDFAHAPLARMSLIGRGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGAQG- 1757
Cdd:cd19546     86 ------VPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGr 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1758 ATLRLPPAPGFQAYLDW--------RERQDLA-RQRGWWRERLSGYAGTAALPAPVAAAHHPVQRE-ECERRLSAHDSER 1827
Cdd:cd19546    160 APERAPLPLQFADYALWerellageDDRDSLIgDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAgAVPLRLDAEVHAR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1828 LRAFCRERGCTLSDLIAMVWGLANARYGNHDDVVLGaTRSGRPPELAGVESMVGVFINTLPLRLRIDAGQPALDLLSALR 1907
Cdd:cd19546    240 LMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVR 318
                          330
                   ....*....|..
gi 1246793773 1908 SQSLEVAENEAV 1919
Cdd:cd19546    319 EAVREARRHQDV 330
PRK07867 PRK07867
acyl-CoA synthetase; Validated
2109-2524 4.73e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 58.92  E-value: 4.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2109 RGAAwLPLDPQHPDArQIAVLDDSGARIVIGwgaapawVPASVRWLDAESVL--DVVSAY--EEPPRVDVDADTPAYLIY 2184
Cdd:PRK07867    89 RGAA-LARDIAHADC-QLVLTESAHAELLDG-------LDPGVRVINVDSPAwaDELAAHrdAEPPFRVADPDDLFMLIF 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2185 TSGSTGTPKGVVVSQGNLAnyVAGVLPVLDLG---EDASLATL-----STVAADLGFTALFGALLSGRR----VRLLPAE 2252
Cdd:PRK07867   160 TSGTSGDPKAVRCTHRKVA--SAGVMLAQRFGlgpDDVCYVSMplfhsNAVMAGWAVALAAGASIALRRkfsaSGFLPDV 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2253 LAFDAQALaahlqahpvdclkivpSHLAGLLAAAGGTAVLPREC-----LVTGGEALTGALVQQVRALAptLRIVNHYGP 2327
Cdd:PRK07867   238 RRYGATYA----------------NYVGKPLSYVLATPERPDDAdnplrIVYGNEGAPGDIARFARRFG--CVVVDGFGS 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2328 TETTVGIL-TCTVPEE--WPVEQGVPVGHPLAGNE--AWVLDRFGLPAPVGVAGELY-LGGGNLSLGYWQRAEQTAERFV 2401
Cdd:PRK07867   300 TEGGVAITrTPDTPPGalGPLPPGVAIVDPDTGTEcpPAEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMR 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2402 AHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALPGANGVLQLGACIQg 2481
Cdd:PRK07867   380 GG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALV- 451
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2482 sLEGVAEALAQRLPEYLC----------PSRWRAVESMPRLGNGKIDRQALAD 2524
Cdd:PRK07867   452 -LAPGAKFDPDAFAEFLAaqpdlgpkqwPSYVRVCAELPRTATFKVLKRQLSA 503
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
672-1038 5.17e-08

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 59.04  E-value: 5.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPdell 751
Cdd:PLN02860   170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLP---- 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  752 epqRFLAFLSERAIT---VTDL--APAYANELV---RASVADDWRDlALRCLVVGGDVLPVALAQRWFELGldRRCALIN 823
Cdd:PLN02860   246 ---KFDAKAALQAIKqhnVTSMitVPAMMADLIsltRKSMTWKVFP-SVRKILNGGGSLSSRLLPDAKKLF--PNAKLFS 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  824 AYGPTEA--------------------------TISSHYHRVQAIDASRPVPLGQLlpgRIAAVLDAH-GRIVPRGVcge 876
Cdd:PLN02860   320 AYGMTEAcssltfmtlhdptlespkqtlqtvnqTKSSSVHQPQGVCVGKPAPHVEL---KIGLDESSRvGRILTRGP--- 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  877 lalggiGLAEGYRGD-AAASERRFAPLRLPSGEslrmyrsgdrVRLLDD-GELQFLGRADFQVKLRGYRIELEEIEHCLG 954
Cdd:PLN02860   394 ------HVMLGYWGQnSETASVLSNDGWLDTGD----------IGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  955 QLPQV-RAAAAGVVGEGAAQRLVAWVECagEDGFGQADlnqtdsDQTESERWHRALCE----------RLPAYMVPTQFV 1023
Cdd:PLN02860   458 QHPGVaSVVVVGVPDSRLTEMVVACVRL--RDGWIWSD------NEKENAKKNLTLSSetlrhhcrekNLSRFKIPKLFV 529
                          410
                   ....*....|....*.
gi 1246793773 1024 ALPR-LPRNASGKIDR 1038
Cdd:PLN02860   530 QWRKpFPLTTTGKIRR 545
PRK07529 PRK07529
AMP-binding domain protein; Validated
667-1080 6.03e-08

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 58.81  E-value: 6.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  667 SGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdttleQILAAWSRG 740
Cdd:PRK07529   206 SGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFcglplfHVNALLV-----TGLAPLARG 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  741 ACVV------ARPDELLepQRFLAFLSERAITVTDLAP-AYAnelVRASVADDWRDL-ALRCLVVGGDVLPVALAQRwFE 812
Cdd:PRK07529   281 AHVVlatpqgYRGPGVI--ANFWKIVERYRINFLSGVPtVYA---ALLQVPVDGHDIsSLRYALCGAAPLPVEVFRR-FE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  813 --LGLdrrcALINAYGPTEATISShyhRVQAID-ASRPVPLGQLLPG---RIaAVLDAHGRIV---PRGVCGELALGGIG 883
Cdd:PRK07529   355 aaTGV----RIVEGYGLTEATCVS---SVNPPDgERRIGSVGLRLPYqrvRV-VILDDAGRYLrdcAVDEVGVLCIAGPN 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  884 LAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAA 963
Cdd:PRK07529   427 VFSGYLEAAHNKGLWLED---------GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAV--AL 495
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  964 AGVVGEG---AAQRLVAWVECAGEDGFGQADLNQTDSDQTeSERwhralcerlpaYMVPTQFVALPRLPRNASGKIDRRA 1040
Cdd:PRK07529   496 AAAVGRPdahAGELPVAYVQLKPGASATEAELLAFARDHI-AER-----------AAVPKHVRILDALPKTAVGKIFKPA 563
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1246793773 1041 LpappvlaqaERTPPRTAEESALCEVWAEVLQCEVGIHDS 1080
Cdd:PRK07529   564 L---------RRDAIRRVLRAALRDAGVEAEVVDVVEDGR 594
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
668-1041 6.14e-08

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 59.17  E-value: 6.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 GENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQILaawsrGA 741
Cdd:PRK08633   776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILsslpffHSFGLTVTLWLPLLE-----GI 850
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  742 CVVARPDELlepqrflaflseRAITVTDLAPAYanelvRASV-----------ADDWR----DLA-LRCLVVGGDVLPVA 805
Cdd:PRK08633   851 KVVYHPDPT------------DALGIAKLVAKH-----RATIllgtptflrlyLRNKKlhplMFAsLRLVVAGAEKLKPE 913
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  806 LAQRwFELGLDRRcaLINAYGPTE----ATISSHYHRVQAID---ASRPVPLGQLLPGRIAAVLDAH-GRIVPRGVCGEL 877
Cdd:PRK08633   914 VADA-FEEKFGIR--ILEGYGATEtspvASVNLPDVLAADFKrqtGSKEGSVGMPLPGVAVRIVDPEtFEELPPGEDGLI 990
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  878 ALGGIGLAEGYRGDAaasERRFAPLRLPSGesLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQL- 956
Cdd:PRK08633   991 LIGGPQVMKGYLGDP---EKTAEVIKDIDG--IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAl 1065
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  957 --PQVRAAAAGVVGEGAAQRLVAWVECAGEDGfgqadlnqtdsdqtesERWHRALCE-RLPAYMVPTQFVALPRLPRNAS 1033
Cdd:PRK08633  1066 ggEEVVFAVTAVPDEKKGEKLVVLHTCGAEDV----------------EELKRAIKEsGLPNLWKPSRYFKVEALPLLGS 1129

                   ....*...
gi 1246793773 1034 GKIDRRAL 1041
Cdd:PRK08633  1130 GKLDLKGL 1137
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
588-1040 6.32e-08

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 58.98  E-value: 6.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPL-DTEWP-QARRAEVVAAsgcDA----VLTD---AQGLAGF--------APSV 650
Cdd:PRK12476    95 VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPgHAERLDTALR---DAeptvVLTTtaaAEAVEGFlrnlprlrRPRV 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  651 aIAVDELKlDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSadDRVLHVAG---LAVD 727
Cdd:PRK12476   172 -IAIDAIP-DSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLL--DRNTHGVSwlpLYHD 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  728 TTLEQI-LAAWSRGACVVARPDELL-EPQRFLAFLSE--RAITVTDLAPAYANELVRA-SVADDWRDLALR--CLVVGGD 800
Cdd:PRK12476   248 MGLSMIgFPAVYGGHSTLMSPTAFVrRPQRWIKALSEgsRTGRVVTAAPNFAYEWAAQrGLPAEGDDIDLSnvVLIIGSE 327
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  801 vlPVALAQ-RWFE-----LGLdRRCALINAYGPTEATIS------------SHYHRVQ------------AIDASRPVPL 850
Cdd:PRK12476   328 --PVSIDAvTTFNkafapYGL-PRTAFKPSYGIAEATLFvatiapdaepsvVYLDREQlgagravrvaadAPNAVAHVSC 404
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  851 GQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASERRF-APL--RLPSG-------ESLRMYRSGDRV 919
Cdd:PRK12476   405 GQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgAKLqsRLAEGshadgaaDDGTWLRTGDLG 484
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  920 RLLdDGELQFLGRADFQVKLRGYRIELEEIEHCLGQL-PQVRA---AAAGVVGEGaAQRLVAWVECAGedGFGQADlnqt 995
Cdd:PRK12476   485 VYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRgyvTAFTVPAED-NERLVIVAERAA--GTSRAD---- 556
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773  996 dsDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKIDRRA 1040
Cdd:PRK12476   557 --PAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRA 599
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1142-1365 7.74e-08

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: 58.04  E-value: 7.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAapgPAPAIQ--A 1217
Cdd:cd20483      4 MSTFQRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVL---DDPSFHliV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1218 QDWRGAADLDSRVDaAFARMQEATPL---AGPLVALTHAHCDDGE-RLLICAHHLIVDAVSWRLLLGE---LFDGLaaLA 1290
Cdd:cd20483     81 IDLSEAADPEAALD-QLVRNLRRQELdieEGEVIRGWLVKLPDEEfALVLASHHIAWDRGSSKSIFEQftaLYDAL--RA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1291 RGEAWTPSARGASYADYV---EALREADDAQRfDAGFWREL---AAQPMQALP---QDRPValadARQSNVGRIVQTLDA 1361
Cdd:cd20483    158 GRDLATVPPPPVQYIDFTlwhNALLQSPLVQP-LLDFWKEKlegIPDASKLLPfakAERPP----VKDYERSTVEATLDK 232

                   ....
gi 1246793773 1362 GLTA 1365
Cdd:cd20483    233 ELLA 236
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
2078-2467 7.95e-08

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 58.47  E-value: 7.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVGVQPGAHVALclprtfaqLAAMA--------AVWHRGAAWLPLdpQHPDAR---------QIAVLDDSGARIVIGw 2140
Cdd:PRK07768    46 LAAAGVGPGDAVAV--------LAGAPveiaptaqGLWMRGASLTML--HQPTPRtdlavwaedTLRVIGMIGAKAVVV- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2141 gAAPAWVPASVRWLDAESVLDVVSAYEEPP--RVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV--------- 2209
Cdd:PRK07768   115 -GEPFLAAAPVLEEKGIRVLTVADLLAADPidPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMfvaaefdve 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2210 -------LPVL-DLGEDASLATLSTVAAD---------LGFTALFGALLS-----------------GRRVRLLPAELAF 2255
Cdd:PRK07768   194 tdvmvswLPLFhDMGMVGFLTVPMYFGAElvkvtpmdfLRDPLLWAELISkyrgtmtaapnfayallARRLRRQAKPGAF 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2256 DaqalaahlqahpVDCLKIVpshlagllaaaggtavlpreclVTGGEALTGALVQQ-VRALAP-TLR---IVNHYGPTET 2330
Cdd:PRK07768   274 D------------LSSLRFA----------------------LNGAEPIDPADVEDlLDAGARfGLRpeaILPAYGMAEA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2331 TV---------GILTCTV-------------PEEWPVEQGVPVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLG 2388
Cdd:PRK07768   320 TLavsfspcgaGLVVDEVdadllaalrravpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG 399
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2389 YwqraeQTAERFVahPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:PRK07768   400 Y-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVR 471
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
846-1043 8.45e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 58.37  E-value: 8.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  846 RPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELAL--GGIGLAEGYRGDAAASERRFAPlrlpsgeslRMYRSGDRVRLLD 923
Cdd:PRK04319   374 KPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAG---------DWYVSGDSAYMDE 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  924 DGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVG---EGAAQRLVAWVecAGEDGFgqadlNQTDSDQT 1000
Cdd:PRK04319   445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV--AEAGVIGkpdPVRGEIIKAFV--ALRPGY-----EPSEELKE 515
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 1001 ESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK04319   516 EIRGFVK---KGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
2123-2431 1.38e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 57.75  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIVIGWGAAPAwvPASVRWldAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL 2202
Cdd:PRK12582   170 ARALAALDLLDVTVVHVTGPGEG--IASIAF--ADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMM 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2203 ANYVAGVLPVLDLGEDASLATL-------STVAADLGFTALF--GALLSGRRVRLLPAELAfdaQALAAHLQAHPVDCLK 2273
Cdd:PRK12582   246 CANIAMQEQLRPREPDPPPPVSldwmpwnHTMGGNANFNGLLwgGGTLYIDDGKPLPGMFE---ETIRNLREISPTVYGN 322
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2274 iVPSHLAGLLAAAGGTAVLPR------ECLVTGGEALTGALVQQVRALAptLRIVNH-------YGPTETTvGILTCTvp 2340
Cdd:PRK12582   323 -VPAGYAMLAEAMEKDDALRRsffknlRLMAYGGATLSDDLYERMQALA--VRTTGHripfytgYGATETA-PTTTGT-- 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2341 eEWPVEQGVPVGHPLAGNEAWVldrfglpAPVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplaPDRLLYRSGDLARL 2420
Cdd:PRK12582   397 -HWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAF------DEEGFYRLGDAARF 462
                          330
                   ....*....|....*
gi 1246793773 2421 ----DGEGRIVYLGR 2431
Cdd:PRK12582   463 vdpdDPEKGLIFDGR 477
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
2176-2531 1.42e-07

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 57.80  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDL-GEDASLATLSTVAAdLGFT-ALFGALLSGRRVRLLPAEL 2253
Cdd:PRK08043   364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFtPNDRFMSALPLFHS-FGLTvGLFTPLLTGAEVFLYPSPL 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2254 AFdaqalaahlqahpvdclKIVPShlagllaaaggtAVLPRECLVTGGEA---------------------LTGA--LVQ 2310
Cdd:PRK08043   443 HY-----------------RIVPE------------LVYDRNCTVLFGTStflgnyarfanpydfarlryvVAGAekLQE 493
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2311 QVRALAPT---LRIVNHYGPTETT--VGIltcTVPEEWPVEQgvpVGHPLAGNEAWVLdrfglPAPvGVA--GELYLGGG 2383
Cdd:PRK08043   494 STKQLWQDkfgLRILEGYGVTECApvVSI---NVPMAAKPGT---VGRILPGMDARLL-----SVP-GIEqgGRLQLKGP 561
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2384 NLSLGYWqRAEQTAErfVAHPLAPD------RLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQL-P 2456
Cdd:PRK08043   562 NIMNGYL-RVEKPGV--LEVPTAENargemeRGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVsP 638
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2457 GVEVAAVLALPGANG---VL-----QLGaciQGSLEGVAEALAqrLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQ 2528
Cdd:PRK08043   639 DKQHATAIKSDASKGealVLfttdsELT---REKLQQYAREHG--VPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713

                   ...
gi 1246793773 2529 DDA 2531
Cdd:PRK08043   714 PEQ 716
PRK07788 PRK07788
acyl-CoA synthetase; Validated
2183-2467 1.62e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 57.24  E-value: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2183 IYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTAL-----FGALLSGRRVrllpaelaFDA 2257
Cdd:PRK07788   213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLtlamaLGSTVVLRRR--------FDP 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2258 QALAAHLQAHPVDCLKIVPSHLAGLLAAAGgtAVLPR------ECLVTGGEALTGALVQQV-RALAPTLriVNHYGPTEt 2330
Cdd:PRK07788   285 EATLEDIAKHKATALVVVPVMLSRILDLGP--EVLAKydtsslKIIFVSGSALSPELATRAlEAFGPVL--YNLYGSTE- 359
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2331 tVGILTCTVPEEWPVEQGVpVGHPLAGNEAWVLDRFGLPAPVGVAGELYLGGGNLSLGYwqraeqTAERfvaHPLAPDRL 2410
Cdd:PRK07788   360 -VAFATIATPEDLAEAPGT-VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDGL 428
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 2411 LyRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEVAAVLALP 2467
Cdd:PRK07788   429 L-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVD 484
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
669-957 1.82e-07

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: 56.98  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  669 ENAaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGL--AVDTTLEQILAAWSrGAC---- 742
Cdd:cd17640     84 END-SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIwhSYERSAEYFIFACG-CSQayts 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  743 VVARPDEL--LEPQRFLAF------LSERAITVTDLAPAYANELVRASVADDwrdlALRCLVVGGDVLPVALaQRWFE-L 813
Cdd:cd17640    162 IRTLKDDLkrVKPHYIVSVprlwesLYSGIQKQVSKSSPIKQFLFLFFLSGG----IFKFGISGGGALPPHV-DTFFEaI 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  814 GLDrrcaLINAYGPTEATISSHYHRVqaidaSRPV--PLGQLLPGRIAAVLDAHGR-IVPRGVCGELALGGIGLAEGYRG 890
Cdd:cd17640    237 GIE----VLNGYGLTETSPVVSARRL-----KCNVrgSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYK 307
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  891 DAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRA-DFQVKLRGYRIELEEIEHCLGQLP 957
Cdd:cd17640    308 NPEATSKVLD----SDG----WFNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSP 367
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1055-1120 1.89e-07

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: 51.01  E-value: 1.89e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1055 PRTAEESALCEVWAEVLQC---EVGIHDSFFR-LGGDSIRSLQVVARLRER-GYAVTPKLMYQYQSAAELA 1120
Cdd:COG0236      2 PREELEERLAEIIAEVLGVdpeEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLA 72
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
791-1041 2.45e-07

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 56.75  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  791 ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEAT--ISSHYHRVQAidasRPVPLGQLLPGRIAAVLDAHGRI 868
Cdd:PRK12492   334 ALKLTNSGGTALVKATAERWEQL---TGCTIVEGYGLTETSpvASTNPYGELA----RLGTVGIPVPGTALKVIDDDGNE 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  869 VPRGVCGELALGGIGLAEGYRGDAAASErrfaplrlpsgESLRM---YRSGDRVRLLDDGELQFLGRADFQVKLRGYRIE 945
Cdd:PRK12492   407 LPLGERGELCIKGPQVMKGYWQQPEATA-----------EALDAegwFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  946 LEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVeCAGEDGFGQADLnqtdsdqteserwhRALC-ERLPAYMVPTQFV 1023
Cdd:PRK12492   476 PNEIEDVVMAHPKVANCAAiGVPDERSGEAVKLFV-VARDPGLSVEEL--------------KAYCkENFTGYKVPKHIV 540
                          250
                   ....*....|....*...
gi 1246793773 1024 ALPRLPRNASGKIDRRAL 1041
Cdd:PRK12492   541 LRDSLPMTPVGKILRREL 558
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
875-1041 2.47e-07

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 56.21  E-value: 2.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  875 GELALGGIGLAEGYRG----DAAASERRFAPlrlpsgeslrmyrsgDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIE 950
Cdd:PRK07824   208 GRIALGGPTLAKGYRNpvdpDPFAEPGWFRT---------------DDLGALDDGVLTVLGRADDAISTGGLTVLPQVVE 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  951 HCLGQLPQVRAAAA-GVVGEGAAQRLVAWVECAGEDGFGQADLnqtdsdqteseRWHRAlcERLPAYMVPTQFVALPRLP 1029
Cdd:PRK07824   273 AALATHPAVADCAVfGLPDDRLGQRVVAAVVGDGGPAPTLEAL-----------RAHVA--RTLDRTAAPRELHVVDELP 339
                          170
                   ....*....|..
gi 1246793773 1030 RNASGKIDRRAL 1041
Cdd:PRK07824   340 RRGIGKVDRRAL 351
PLN02246 PLN02246
4-coumarate--CoA ligase
2060-2207 2.56e-07

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 56.91  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2060 ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT--FAqLAAMAAVwHRGAAWL---PLDPQHPDARQIAVlddSGA 2134
Cdd:PLN02246    49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCpeFV-LAFLGAS-RRGAVTTtanPFYTPAEIAKQAKA---SGA 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2135 RIVIgwgAAPAWVPaSVRWLDAESVLDVV-----------------SAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVV 2197
Cdd:PLN02246   124 KLII---TQSCYVD-KLKGLAEDDGVTVVtiddppegclhfseltqADENELPEVEISPDDVVALPYSSGTTGLPKGVML 199
                          170
                   ....*....|
gi 1246793773 2198 SQGNLANYVA 2207
Cdd:PLN02246   200 THKGLVTSVA 209
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
588-1041 2.70e-07

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 56.42  E-value: 2.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAqglAGFAPSVAIAVDELKLDGAGEngs 667
Cdd:PRK09029    56 VALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLE---GENTFSALTSLHLQLVEGAHA--- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 gENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAvdttleqILAAW-SRG 740
Cdd:PRK09029   130 -VAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLlslplfHVSGQG-------IVWRWlYAG 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  741 ACVVARPDELLEpqrflaflseRAITVTDLAPAYANELVRAsVADDWRDLALRCLVVGGDVLPVALAQRWFELGLdrRCA 820
Cdd:PRK09029   202 ATLVVRDKQPLE----------QALAGCTHASLVPTQLWRL-LDNRSEPLSLKAVLLGGAAIPVELTEQAEQQGI--RCW 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  821 LinAYGPTEA--TISshyhrVQAIDASRPVplGQLLPGRiaAVldahgrivpRGVCGELALGGIGLAEGYrgdaaaserr 898
Cdd:PRK09029   269 C--GYGLTEMasTVC-----AKRADGLAGV--GSPLPGR--EV---------KLVDGEIWLRGASLALGY---------- 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  899 faplrlpsgeslrmYRSGDRVRLLDD--------------GELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAa 964
Cdd:PRK09029   319 --------------WRQGQLVPLVNDegwfatrdrgewqnGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVF- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  965 gVV-------GegaaQRLVAWVECAgedgfgqadlnqTDSDQTESERWhraLCERLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:PRK09029   384 -VVpvadaefG----QRPVAVVESD------------SEAAVVNLAEW---LQDKLARFQQPVAYYLLPPELKNGGIKIS 443

                   ....
gi 1246793773 1038 RRAL 1041
Cdd:PRK09029   444 RQAL 447
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
101-290 3.24e-07

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: 55.96  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  101 EQFEPGG---HAYhlaalFELRGE-LDAAALERAVHGLLIRHEVLdRCIQGEDS----VAAGGGAAVESADLRGRGQDEI 172
Cdd:cd19535     17 DDQELGGvgcHAY-----LEFDGEdLDPDRLERAWNKLIARHPML-RAVFLDDGtqqiLPEVPWYGITVHDLRGLSEEEA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  173 DALVEGFR--L--RPFELQRQRPLRMQLLRLDGQgdgpvRHWLQVVVHHIACDGVSLGLLTQDLSRAYRVECglaaEPAP 248
Cdd:cd19535     91 EAALEELRerLshRVLDVERGPLFDIRLSLLPEG-----RTRLHLSIDLLVADALSLQILLRELAALYEDPG----EPLP 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773  249 PLPCQYGDY-ARWQRDTLDRLDASLRH---HVEALSGAPhlhELPL 290
Cdd:cd19535    162 PLELSFRDYlLAEQALRETAYERARAYwqeRLPTLPPAP---QLPL 204
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
3665-3944 3.70e-07

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: 56.21  E-value: 3.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3665 LIYTSGSTGTPKGVVVTHRNVERLFTAATQTGRFSFD----EHDVWSLFHSHA----FDfavweLWGAWLYGGravlvpe 3736
Cdd:cd05933    155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPAtvgqESVVSYLPLSHIaaqiLD-----IWLPIKVGG------- 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3737 AVC-RQPDA----FLDLLAEYGVTVLNQTPSAF---------YALQSQAMRRELALNVRAVVF-------GGEaLEPSRL 3795
Cdd:cd05933    223 QVYfAQPDAlkgtLVKTLREVRPTAFMGVPRVWekiqekmkaVGAKSGTLKRKIASWAKGVGLetnlklmGGE-SPSPLF 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3796 QPWRERY----------------------PQAE------------LVNMYGITETTvhvSFHRLSDEDLQSPTSrIGSAL 3841
Cdd:cd05933    302 YRLAKKLvfkkvrkalgldrcqkfftgaaPISRetlefflslnipIMELYGMSETS---GPHTISNPQAYRLLS-CGKAL 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3842 P--DLAVHVLDAAGQpvplgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQV 3919
Cdd:cd05933    378 PgcKTKIHNPDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDG---WLHSGDLGKLDEDGFLYITGRIKELI 447
                          330       340
                   ....*....|....*....|....*..
gi 1246793773 3920 KLR-GYRIEPGEIAAKI-ASLPQVSDA 3944
Cdd:cd05933    448 ITAgGENVPPVPIEDAVkKELPIISNA 474
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
679-1043 3.92e-07

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: 56.34  E-value: 3.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKG-VEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVV---ARPDeLLEPQ 754
Cdd:cd05968    241 IIYTSGTTGKPKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVlydGAPD-HPKAD 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  755 RFLAFLSERAITVTDLAPAyaneLVRASVA--DDWRD----LALRclVVGGDVLPVAL-AQRW-FELGLDRRCALINAYG 826
Cdd:cd05968    320 RLWRMVEDHEITHLGLSPT----LIRALKPrgDAPVNahdlSSLR--VLGSTGEPWNPePWNWlFETVGKGRNPIINYSG 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  827 PTEatISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVcGELALGG--IGLAEGYRGDaaasERRFAPL-- 902
Cdd:cd05968    394 GTE--ISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEV-GELVLLApwPGMTRGFWRD----EDRYLETyw 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  903 -RLPSgeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVe 980
Cdd:cd05968    467 sRFDN-----VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLeSAAIGVPHPVKGEAIVCFV- 540
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  981 cAGEDGFGQADLNQTDSDQTESERWHRALCerlpaymvPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:cd05968    541 -VLKPGVTPTEALAEELMERVADELGKPLS--------PERILFVKDLPKTRNAKVMRRVIRA 594
PRK05850 PRK05850
acyl-CoA synthetase; Validated
2098-2205 5.35e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 55.72  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2098 AQLAAMAAvwhrGAAWLPLDPQHP---DARQIAVLDDSGARIVIGWGAA-----------PAWVPASVRWLDAesvLDVV 2163
Cdd:PRK05850    75 AFLGALQA----GLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVvddvteyvapqPGQSAPPVIEVDL---LDLD 147
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 2164 SAYEEPPRVDvDADTPAYLIYTSGSTGTPKGVVVSQGNL-ANY 2205
Cdd:PRK05850   148 SPRGSDARPR-DLPSTAYLQYTSGSTRTPAGVMVSHRNViANF 189
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1142-1371 5.98e-07

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: 55.27  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFdsapaqpdryHQY------------VALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAap 1209
Cdd:cd19537      4 LSPIEREWW----------HKYqlstgtssfnvsFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYS-- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1210 gpAPAIQAQdWRGAADLDSRVDAAFARMQEaTPLagpLVALTHAHcddgerLLICAHHLIVDAVSWRLLLGElfdgLAAL 1289
Cdd:cd19537     72 --SSPPRVQ-RVDTLDVWKEINRPFDLERE-DPI---RVFISPDT------LLVVMSHIICDLTTLQLLLRE----VSAA 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1290 ARGEAWTPSARgaSYADYVEALREADDAQRFdagFWRE-LAAQPMQALPqdRPVALADARQSnvgRIVQTLDAGLTADLL 1368
Cdd:cd19537    135 YNGKLLPPVRR--EYLDSTAWSRPASPEDLD---FWSEyLSGLPLLNLP--RRTSSKSYRGT---SRVFQLPGSLYRSLL 204

                   ...
gi 1246793773 1369 ERA 1371
Cdd:cd19537    205 QFS 207
PRK03584 PRK03584
acetoacetate--CoA ligase;
3533-4005 6.77e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 55.57  E-value: 6.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3533 PARIAVSaEDG---ELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDP----HAPA 3605
Cdd:PRK03584   101 PAIIFRG-EDGprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPdfgvQGVL 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3606 ARRG------FILED----SGVCLSVSQ--RALAVELPG-TALC----LDDPFTRAQL-------DAVEPGELPE----- 3656
Cdd:PRK03584   180 DRFGqiepkvLIAVDgyryGGKAFDRRAkvAELRAALPSlEHVVvvpyLGPAAAAAALpgallweDFLAPAEAAElefep 259
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3657 VPTEAPAYLIYTSGSTGTPK-------GVVVTH----------RNVERLFTAATqTGrfsfdehdvwslfhshafdfavW 3719
Cdd:PRK03584   260 VPFDHPLWILYSSGTTGLPKcivhghgGILLEHlkelglhcdlGPGDRFFWYTT-CG----------------------W 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3720 ELWGaWLYGGRAV---LV--------PeavcrQPDAFLDLLAEYGVTVLNqTPSAFYALQSQA---MRRELAL-NVRAVV 3784
Cdd:PRK03584   317 MMWN-WLVSGLLVgatLVlydgspfyP-----DPNVLWDLAAEEGVTVFG-TSAKYLDACEKAglvPGETHDLsALRTIG 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3785 FGGEALEPSrLQPW--RERYPQAELVNMYGITettvhvsfhrlsdeDLQS------PTS-----RIGSALPDLAVHVLDA 3851
Cdd:PRK03584   390 STGSPLPPE-GFDWvyEHVKADVWLASISGGT--------------DICScfvggnPLLpvyrgEIQCRGLGMAVEAWDE 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3852 AGQPVpLGVVGELVVegdgvAQ-------GYWQRPeltaerfverGGQRfYRS------------GDLGRYRADGSLEYR 3912
Cdd:PRK03584   455 DGRPV-VGEVGELVC-----TKpfpsmplGFWNDP----------DGSR-YRDayfdtfpgvwrhGDWIEITEHGGVVIY 517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3913 GRGDDQVKLRGYRIEPGEIAAKIASLPQVSDA-AVTVEGQGEGAWLMAYAVAADGAEPDP---QSLREALRALLPDYMLP 3988
Cdd:PRK03584   518 GRSDATLNRGGVRIGTAEIYRQVEALPEVLDSlVIGQEWPDGDVRMPLFVVLAEGVTLDDalrARIRTTIRTNLSPRHVP 597
                          570
                   ....*....|....*..
gi 1246793773 3989 RLIQLLPALPLTANGKL 4005
Cdd:PRK03584   598 DKIIAVPDIPRTLSGKK 614
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
549-1036 6.81e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 55.40  E-value: 6.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  549 PERAALETAQG--RLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAE 626
Cdd:PRK13390    11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  627 VVAASGCDAVLTDAqGLAGFAPSVAiAVDELKL------DGAGENGSGENAAPNQL------AYILYTSGSTGIPKGVEv 694
Cdd:PRK13390    91 IVGDSGARVLVASA-ALDGLAAKVG-ADLPLRLsfggeiDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKGIQ- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  695 ghaalaahiDAAAEALALSADDRVLHVAGLAVDTTLEQIL--------AAWSR---------GACVVARPdelLEPQRFL 757
Cdd:PRK13390   168 ---------PDLPGRDVDAPGDPIVAIARAFYDISESDIYyssapiyhAAPLRwcsmvhalgGTVVLAKR---FDAQATL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  758 AFLSERAITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPValaqrwfelglDRRCALINAYGPT--EATIS 833
Cdd:PRK13390   236 GHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPV-----------DVKHAMIDWLGPIvyEYYSS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  834 SHYHRVQAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGD---AAASERRFAPLrlps 906
Cdd:PRK13390   305 TEAHGMTFIDSpdwlAHPGSVGRSVLGDL-HICDDDGNELPAGRIGTVYFERDRLPFRYLNDpekTAAAQHPAHPF---- 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  907 geslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVE-CAGE 984
Cdd:PRK13390   380 -----WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHdVAVIGVPDPEMGEQVKAVIQlVEGI 454
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1246793773  985 DgfGQADLNQTDSDQTESerwhralceRLPAYMVPTQFVALPRLPRNASGKI 1036
Cdd:PRK13390   455 R--GSDELARELIDYTRS---------RIAHYKAPRSVEFVDELPRTPTGKL 495
TubC_N pfam18563
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ...
21-68 7.60e-07

TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.


Pssm-ID: 436580 [Multi-domain]  Cd Length: 52  Bit Score: 48.67  E-value: 7.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773   21 LERARAAGVALHVEDGRLGYKATRAPLDAQLRADIVAQREALITLLSQ 68
Cdd:pfam18563    5 LAELYALGIKLWLEGGRLRFRAPKGVLTPELREKLKERKAEIIAFLQQ 52
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
740-1041 9.49e-07

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 55.00  E-value: 9.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  740 GACVVARPDEllEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRD-LA-LRCLVVGGDVLPVALAQRW-FELGld 816
Cdd:PRK10946   250 GGTVVLAPDP--SATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAqLAsLKLLQVGGARLSETLARRIpAELG-- 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  817 rrCALINAYGPTEATISshYHRVQAID------ASRPVPlgqllPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRG 890
Cdd:PRK10946   326 --CQLQQVFGMAEGLVN--YTRLDDSDerifttQGRPMS-----PDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  891 DAAASERRFaplrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagvvgeg 970
Cdd:PRK10946   397 SPQHNASAF--------DANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAA------- 461
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  971 aaqrLVAWVECA-GEDGFgqADLNQTDSDQTESERwhRALCERLPA-YMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK10946   462 ----LVSMEDELmGEKSC--AFLVVKEPLKAVQLR--RFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
2063-2207 9.62e-07

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: 54.95  E-value: 9.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAwlpldpqH--------PDARQIAVLDdSGA 2134
Cdd:TIGR02188   90 TYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAI-------HsvvfggfsAEALADRIND-AGA 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2135 RIVI----GW---------------------------------GAAPAWVPASVRWLdaESVLDVVSAYEEPPrvDVDAD 2177
Cdd:TIGR02188  162 KLVItadeGLrggkviplkaivdealekcpvsvehvlvvrrtgNPVVPWVEGRDVWW--HDLMAKASAYCEPE--PMDSE 237
                          170       180       190
                   ....*....|....*....|....*....|
gi 1246793773 2178 TPAYLIYTSGSTGTPKGVVVSQGNLANYVA 2207
Cdd:TIGR02188  238 DPLFILYTSGSTGKPKGVLHTTGGYLLYAA 267
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3162-3663 9.85e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 55.26  E-value: 9.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3162 DWSGLEPAQARSRLS--------ELQAQQCEAGFDLAAPPLMRLALLRRSADEH--WLVWTRHHLIVDGWSSALLLDEVW 3231
Cdd:COG3321    848 DWSALYPGRGRRRVPlptypfqrEDAAAALLAAALAAALAAAAALGALLLAALAaaLAAALLALAAAAAAALALAAAALA 927
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3232 RLYAALRESRTPQLPAAPPFRDYLHWLRGQDEAAARAFWREQLTGLEPAALPEATEPAEGYASSTRRFDLAAASAWAQSH 3311
Cdd:COG3321    928 ALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAA 1007
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3312 GLTASSLLQGALALVLQRYYGRDDFALGITIAGRPPELAGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRT 3391
Cdd:COG3321   1008 AALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALA 1087
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3392 HGYLPLAQIQRAGAADAVSPFDVLLVFENLPTESREERSGMRIEELDHRAHSNYPLMLTAIPDAGGLRIEAALDRSKLDG 3471
Cdd:COG3321   1088 AALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAAL 1167
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3472 WLVEQMLDDLDFVLQQVPALQRFDALPLLPSQTRSAAWTSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLD 3551
Cdd:COG3321   1168 LAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAA 1247
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3552 RRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELP 3631
Cdd:COG3321   1248 LAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLA 1327
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1246793773 3632 GTALCLDDPFTRAQLDAVEPGELPEVPTEAPA 3663
Cdd:COG3321   1328 AALAALAAAVAAALALAAAAAAAAAAAAAAAA 1359
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
3825-4085 1.18e-06

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 53.60  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3825 LSDEDLQSPTSRIGSALPDLAVHVLDAAGQPVPLGVVGELVVEGDGVAQGYWQRPELTAERFVE-----RGGQRFYRSGD 3899
Cdd:COG3433      4 ATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARApfipvPYPAQPGRQAD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3900 LGRYRADGSLEYRGRGDDQVKLRGYRIEPGEIAAKIASLPQVSDAAVTVEGQGEGAW---LMAYAVAADGAEPDPQSLRE 3976
Cdd:COG3433     84 DLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGvglLLIVGAVAALDGLAAAAALA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3977 ALRALLPDYMLPRLIQLLPALPLTANGKLDRKALPKPETQDRDEG------VLESASERRLAELWRQLLGGEL--PGRGA 4048
Cdd:COG3433    164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAaspapaLETALTEEELRADVAELLGVDPeeIDPDD 243
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1246793773 4049 HFFARGGHSLLVVRLAEAIRAEFaIAVPLKSLFEQPR 4085
Cdd:COG3433    244 NLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPT 279
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
526-970 1.30e-06

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 54.72  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  526 KREPAPRTVGNVVDAIARAADEFPERAALETAQG----RLSYRELLTaadaraaalrrrlgaQARSVAlclpRGL----- 596
Cdd:COG1022      2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAE---------------RVRALA----AGLlalgv 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  597 --------------DWYCLLLGAWRAGLSVIPLDtewPQARRAEV---VAASGCDAVLTDAQ------------------ 641
Cdd:COG1022     63 kpgdrvailsdnrpEWVIADLAILAAGAVTVPIY---PTSSAEEVayiLNDSGAKVLFVEDQeqldkllevrdelpslrh 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  642 -----GLAGFAPSVAIAVDELKLDGAGENGSGE------NAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEAL 710
Cdd:COG1022    140 ivvldPRGLRDDPRLLSLDELLALGREVADPAElearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  711 ALSADDRVL------HVAglavdttlEQIL--AAWSRGACV--VARPDELLE------PQRFLA---------------- 758
Cdd:COG1022    220 PLGPGDRTLsflplaHVF--------ERTVsyYALAAGATVafAESPDTLAEdlrevkPTFMLAvprvwekvyagiqaka 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  759 --------FLSERAItvtDLAPAYANEL-----------VRASVADD-----WRDL---ALRCLVVGGDVLPVALAqRWF 811
Cdd:COG1022    292 eeagglkrKLFRWAL---AVGRRYARARlagkspslllrLKHALADKlvfskLREAlggRLRFAVSGGAALGPELA-RFF 367
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  812 E-LGLDrrcaLINAYGPTEAT--ISshyhrVQAIDASRPVPLGQLLPG---RIAAvldahgrivprgvCGELALGGIGLA 885
Cdd:COG1022    368 RaLGIP----VLEGYGLTETSpvIT-----VNRPGDNRIGTVGPPLPGvevKIAE-------------DGEILVRGPNVM 425
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  886 EGYRGDAAASERRFAP---LrlpsgeslrmyRSGDRVRLLDDGELQFLGRADFQVKLR-GYRIELEEIEHCLGQLPQVRA 961
Cdd:COG1022    426 KGYYKNPEATAEAFDAdgwL-----------HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQ 494

                   ....*....
gi 1246793773  962 AAagVVGEG 970
Cdd:COG1022    495 AV--VVGDG 501
PLN02654 PLN02654
acetate-CoA ligase
2150-2466 1.34e-06

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 54.52  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2150 SVRWLDAESVL--DVVSAYEEPPRVD-VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAgvlPVLDLGEDASLATLST 2226
Cdd:PLN02654   245 DTKWQEGRDVWwqDVVPNYPTKCEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTA---TTFKYAFDYKPTDVYW 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2227 VAADLGFTA-----LFGALLSGRRVrllpaeLAFDaqalAAHLQAHPVDCLKIVPSHlaglLAAAGGTA-VLPRECLVTG 2300
Cdd:PLN02654   322 CTADCGWITghsyvTYGPMLNGATV------LVFE----GAPNYPDSGRCWDIVDKY----KVTIFYTApTLVRSLMRDG 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQQVRALAPTLRIVNhygPTE-----TTVGILTCTVPEE-WPVEQGVPVGHPLAGneAW-------VLDRFG 2367
Cdd:PLN02654   388 DEYVTRHSRKSLRVLGSVGEPIN---PSAwrwffNVVGDSRCPISDTwWQTETGGFMITPLPG--AWpqkpgsaTFPFFG 462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2368 L-PAPVGVAGELYLG--GGNLSL-GYWQRAEQTA----ERFVAHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIR 2439
Cdd:PLN02654   463 VqPVIVDEKGKEIEGecSGYLCVkKSWPGAFRTLygdhERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 542
                          330       340
                   ....*....|....*....|....*..
gi 1246793773 2440 GYRVELGEVEQVLAQLPGVEVAAVLAL 2466
Cdd:PLN02654   543 GHRIGTAEVESALVSHPQCAEAAVVGI 569
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
2176-2465 1.58e-06

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: 54.03  E-value: 1.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLATLSTVAADLGFTAL-FGALLSGRRVRLLPAELA 2254
Cdd:cd05908    105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNQYLMPTRLF 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2255 FdaqalaahlqAHPVDCLKIVPSHLAGLLAAA--GGTAVLPR--------------ECLVTGGEALTGALVQQ-VRALAP 2317
Cdd:cd05908    185 I----------RRPILWLKKASEHKATIVSSPnfGYKYFLKTlkpekandwdlssiRMILNGAEPIDYELCHEfLDHMSK 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2318 -TLR---IVNHYGPTETTVGI------------------LTCTVPEEWPVEQG------VPVGHPLAGNEAWVLDRFGLP 2369
Cdd:cd05908    255 yGLKrnaILPVYGLAEASVGAslpkaqspfktitlgrrhVTHGEPEPEVDKKDsecltfVEVGKPIDETDIRICDEDNKI 334
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2370 APVGVAGELYLGGGNLSLGYWQRAEQTAERFvahplAPDRLLyRSGDLArLDGEGRIVYLGRGDHQVKIRGYRVELGEVE 2449
Cdd:cd05908    335 LPDGYIGHIQIRGKNVTPGYYNNPEATAKVF-----TDDGWL-KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIE 407
                          330
                   ....*....|....*.
gi 1246793773 2450 QVLAQLPGVEVAAVLA 2465
Cdd:cd05908    408 RIAEELEGVELGRVVA 423
PRK09274 PRK09274
peptide synthase; Provisional
533-980 2.71e-06

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 53.36  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  533 TVGNVVDAIARAADEFPERAALETAQGR-----LSYRELLTAADARAAALRRRLGAQA------RSVALCLPrGLDWYCL 601
Cdd:PRK09274     4 SMANIARHLPRAAQERPDQLAVAVPGGRgadgkLAYDELSFAELDARSDAIAHGLNAAgigrgmRAVLMVTP-SLEFFAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  602 LLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD-----AQGLAGFA-PSVAIAV-------------DELKLDGA 662
Cdd:PRK09274    83 TFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIpkahlARRLFGWGkPSVRRLVtvggrllwggttlATLLRDGA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  663 GENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR--------VLHVAGLAVDTTLEQIL 734
Cdd:PRK09274   163 AAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIdlptfplfALFGPALGMTSVIPDMD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  735 AawSRGACVvarpdellEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELg 814
Cdd:PRK09274   243 P--TRPATV--------DPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAM- 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  815 LDRRCALINAYGPTEA----TISSHYH---RVQAIDASRPVPLGQLLPG---RIAAVLDA------HGRIVPRGVCGELA 878
Cdd:PRK09274   312 LPPDAEILTPYGATEAlpisSIESREIlfaTRAATDNGAGICVGRPVDGvevRIIAISDApipewdDALRLATGEIGEIV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  879 LGGIGLAEGYRGDAAASerRFAplRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ 958
Cdd:PRK09274   392 VAGPMVTRSYYNRPEAT--RLA--KIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPG 467
                          490       500
                   ....*....|....*....|..
gi 1246793773  959 VRAAAAGVVGEGAAQRLVAWVE 980
Cdd:PRK09274   468 VKRSALVGVGVPGAQRPVLCVE 489
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2636-2812 2.96e-06

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: 53.13  E-value: 2.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2636 WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARF--------QR-DAAGQWQQTLGDWQADRFAHR 2706
Cdd:cd19531     12 WFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFvevdgepvQViLPPLPLPLPVVDLSGLPEAER 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2707 EADAgqrEDLLAQwQAGLSFD---GALLRVLALpdpQDGDTR--VLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPA 2781
Cdd:cd19531     92 EAEA---QRLARE-EARRPFDlarGPLLRATLL---RLGEDEhvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSP 164
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1246793773 2782 LAAEACGFG---AWQAalRQLSAATLDGWRSYWR 2812
Cdd:cd19531    165 LPPLPIQYAdyaVWQR--EWLQGEVLERQLAYWR 196
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
2167-2420 3.32e-06

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: 53.20  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2167 EEPPRVDVDA-------DTPAYLIYTSGSTGTPKGVVVSQGNLAN---YVAGVLPVLDlGEDASLATLSTVAADLGFTAL 2236
Cdd:cd05921    148 ATPPTAAVDAafaavgpDTVAKFLFTSGSTGLPKAVINTQRMLCAnqaMLEQTYPFFG-EEPPVLVDWLPWNHTFGGNHN 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2237 FGALLSGrrvrllPAELAFDAQALAAHLQAHPVDCLK--------IVPSHLAGLLAAAGGTAVLPR------ECLVTGGE 2302
Cdd:cd05921    227 FNLVLYN------GGTLYIDDGKPMPGGFEETLRNLReisptvyfNVPAGWEMLVAALEKDEALRRrffkrlKLMFYAGA 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2303 ALTGALVQQVRALA-----PTLRIVNHYGPTETTVGILTCTvpeeWPVEQGVPVGHPLAGNEAWVldrfglpAPVGVAGE 2377
Cdd:cd05921    301 GLSQDVWDRLQALAvatvgERIPMMAGLGATETAPTATFTH----WPTERSGLIGLPAPGTELKL-------VPSGGKYE 369
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1246793773 2378 LYLGGGNLSLGYWQRAEQTAERFvahplaPDRLLYRSGDLARL 2420
Cdd:cd05921    370 VRVKGPNVTPGYWRQPELTAQAF------DEEGFYCLGDAAKL 406
PRK08308 PRK08308
acyl-CoA synthetase; Validated
924-1043 3.88e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 52.73  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  924 DGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEGAAQRLVAwvecagEDGFGQADLNQtdsd 998
Cdd:PRK08308   304 RGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVyrgkdPVAGERVKAKVIS------HEEIDPVQLRE---- 373
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1246793773  999 qteserWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRALPA 1043
Cdd:PRK08308   374 ------WCI---QHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
673-1038 4.04e-06

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: 52.88  E-value: 4.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLeqilaAWSRGACVVARPDELLE 752
Cdd:cd05908    105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGL-----IAFHLAPLIAGMNQYLM 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  753 PQR--------FLAFLSERAITVTDlAPAYANELV----RASVADDWRDLALRCLVVGGDVLPVALAQRWFE----LGLd 816
Cdd:cd05908    180 PTRlfirrpilWLKKASEHKATIVS-SPNFGYKYFlktlKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmskYGL- 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  817 RRCALINAYGPTEATIS-------------SHYHR-------VQAIDASRP-----VPLGQLLPGRIAAVLDAHGRIVPR 871
Cdd:cd05908    258 KRNAILPVYGLAEASVGaslpkaqspfktiTLGRRhvthgepEPEVDKKDSecltfVEVGKPIDETDIRICDEDNKILPD 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  872 GVCGELALGGIGLAEGYRGDAAASERRFAplrlPSGeslrMYRSGDrVRLLDDGELQFLGRADFQVKLRGYRIELEEIEH 951
Cdd:cd05908    338 GYIGHIQIRGKNVTPGYYNNPEATAKVFT----DDG----WLKTGD-LGFIRNGRLVITGREKDIIFVNGQNVYPHDIER 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  952 CLGQLPQV---RAAAAGVVGEGAAQ-RLVAWVECA-GEDGFgqADLNQ-TDSDQTESERWHraLCERLPaymvptqfvaL 1025
Cdd:cd05908    409 IAEELEGVelgRVVACGVNNSNTRNeEIFCFIEHRkSEDDF--YPLGKkIKKHLNKRGGWQ--INEVLP----------I 474
                          410
                   ....*....|...
gi 1246793773 1026 PRLPRNASGKIDR 1038
Cdd:cd05908    475 RRIPKTTSGKVKR 487
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
2362-2518 4.37e-06

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: 51.92  E-value: 4.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2362 VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFVAHplapdrlLYRSGDLARLDGEGRIVYLGRGDHQVKIRGY 2441
Cdd:cd17636    176 ILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGG-------WHHTNDLGRREPDGSLSFVGPKTRMIKSGAE 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2442 RVELGEVEQVLAQLPGVEVAAVLALPG--------ANGVLQLGACIqgSLEGVAEALAQRLPEYLCPSRWRAVESMPRLG 2513
Cdd:cd17636    249 NIYPAEVERCLRQHPAVADAAVIGVPDprwaqsvkAIVVLKPGASV--TEAELIEHCRARIASYKKPKSVEFADALPRTA 326

                   ....*
gi 1246793773 2514 NGKID 2518
Cdd:cd17636    327 GGADD 331
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
2098-2243 4.45e-06

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: 52.84  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2098 AQLAAMAAvwHRGAAWLPLDPQHPDARQIAVLDDSGARIVIGWGAAP----------------AWVPASVRWLDAESVLD 2161
Cdd:cd17632    130 AQLAPILA--ETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVVFDHRPevdahraalesarerlAAVGIPVTTLTLIAVRG 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2162 VVSAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLAT----LSTVAadlGFTALF 2237
Cdd:cd17632    208 RDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnfmpMSHIA---GRISLY 284

                   ....*.
gi 1246793773 2238 GALLSG 2243
Cdd:cd17632    285 GTLARG 290
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2609-3082 4.84e-06

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: 52.94  E-value: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2609 QASSPAPATIKPATEAEQSFGLTPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAA 2688
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2689 GQWQQTLGDWQA-------DRFAHREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWG 2761
Cdd:COG1020     81 RPVQVIQPVVAAplpvvvlLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2762 IIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQ-LSAATLDGWRSYWRAqAADAEAIALPWQDSDNRYADTVHLHD 2840
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREwLQGEELARQLAYWRQ-QLAGLPPLLELPTDRPRPAVQSYRGA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2841 RFERDWTERL---LTQTARAYGnepqevlltalalalrdggdaATLWVEMEG---------HGRDDLGAGL--------D 2900
Cdd:COG1020    240 RVSFRLPAELtaaLRALARRHG---------------------VTLFMVLLAafalllarySGQDDVVVGTpvagrprpE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2901 LSRTVGWFTARYPLALHLPAGEDLGAALRSTKDRMR-AVPDRGLGFGVLR---YLHGELAELPVPQVCFNYLGQ-LRAGE 2975
Cdd:COG1020    299 LEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLaAYAHQDLPFERLVeelQPERDLSRNPLFQVMFVLQNApADELE 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2976 RDGWALCEEPdgggrAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIacvqtAEPRPTLA 3055
Cdd:COG1020    379 LPGLTLEPLE-----LDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALA-----ADPDQPLG 448
                          490       500
                   ....*....|....*....|....*..
gi 1246793773 3056 DLPLagLDNAPLDALLSQHPQTQDVYP 3082
Cdd:COG1020    449 DLPL--LTAAERQQLLAEWNATAAPYP 473
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
588-1041 5.36e-06

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 52.21  E-value: 5.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQGLAGFAPSVA---IAVDELKLDGAGE 664
Cdd:PRK08276    39 VAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAELAAelpAGVPLLLVVAGPV 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  665 NG--SGENAAPNQLAY----------ILYTSGSTGIPKGVEV------GHAALAAHIDAAAEALALSADDRVLHVAGLAV 726
Cdd:PRK08276   119 PGfrSYEEALAAQPDTpiadetagadMLYSSGTTGRPKGIKRplpgldPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYH 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  727 DTTLEQILAAWSRGACVVArpDELLEPQRFLAFLSERAITVTDLAPAYANEL------VRASVaddwrDLA-LRCLVVGG 799
Cdd:PRK08276   199 TAPLRFGMSALALGGTVVV--MEKFDAEEALALIERYRVTHSQLVPTMFVRMlklpeeVRARY-----DVSsLRVAIHAA 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  800 DVLPVALAQrwfelgldrrcALINAYGPT--EATISSHYHRVQAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGV 873
Cdd:PRK08276   272 APCPVEVKR-----------AMIDWWGPIihEYYASSEGGGVTVITSedwlAHPGSVGKAVLGEV-RILDEDGNELPPGE 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  874 CGELALGGIGLAEGYRGDAAASERrfapLRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCL 953
Cdd:PRK08276   340 IGTVYFEMDGYPFEYHNDPEKTAA----ARNPHG----WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLL 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  954 GQLPQVR-AAAAGVVGEGAAQRLVAWVECAgeDGFgqadlnqTDSDQTESE--RWHRalcERLPAYMVPTQFVALPRLPR 1030
Cdd:PRK08276   412 VTHPKVAdVAVFGVPDEEMGERVKAVVQPA--DGA-------DAGDALAAEliAWLR---GRLAHYKCPRSIDFEDELPR 479
                          490
                   ....*....|.
gi 1246793773 1031 NASGKIDRRAL 1041
Cdd:PRK08276   480 TPTGKLYKRRL 490
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
526-1023 5.58e-06

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 52.57  E-value: 5.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  526 KREPAPRTVGnvvDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGA 605
Cdd:PRK08279    31 ITPDSKRSLG---DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGL 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  606 WRAGLSVIPLDTewpQARRA------------EVVAASGCDAVLTDAQGLAGFAPSVAIAVDELK--------LDGAGEN 665
Cdd:PRK08279   108 AKLGAVVALLNT---QQRGAvlahslnlvdakHLIVGEELVEAFEEARADLARPPRLWVAGGDTLddpegyedLAAAAAG 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  666 GSGENAA------PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQI 733
Cdd:PRK08279   185 APTTNPAsrsgvtAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYcclplyHNTGGTV--AWSSV 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  734 LAAwsrGACVVARPdellepqRFLA--FLSE-RAITVTdlAPAYANELVR----ASVADDWRDLALRClVVG----GDVL 802
Cdd:PRK08279   263 LAA---GATLALRR-------KFSAsrFWDDvRRYRAT--AFQYIGELCRyllnQPPKPTDRDHRLRL-MIGnglrPDIW 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  803 PvALAQRWfelGLDRRCALinaYGPTEATIS--SHYHRVQAIdasrpvplgqllpGRIAAVLDAHGRIV----------- 869
Cdd:PRK08279   330 D-EFQQRF---GIPRILEF---YAASEGNVGfiNVFNFDGTV-------------GRVPLWLAHPYAIVkydvdtgepvr 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  870 -PRGVCGELALGGIGLA----------EGYRgDAAASERR-----FAPlrlpsGEslRMYRSGDRVRLLDDGELQFLGRA 933
Cdd:PRK08279   390 dADGRCIKVKPGEVGLLigritdrgpfDGYT-DPEASEKKilrdvFKK-----GD--AWFNTGDLMRDDGFGHAQFVDRL 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  934 dfqvklrG--YRIELE-----EIEHCLGQLPQVraAAAGVVGegaaqrlvawVECAGEDG-FGQADLNQTDSDQTESERW 1005
Cdd:PRK08279   462 -------GdtFRWKGEnvattEVENALSGFPGV--EEAVVYG----------VEVPGTDGrAGMAAIVLADGAEFDLAAL 522
                          570
                   ....*....|....*...
gi 1246793773 1006 HRALCERLPAYMVPtQFV 1023
Cdd:PRK08279   523 AAHLYERLPAYAVP-LFV 539
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1138-1371 6.19e-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: 52.10  E-value: 6.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1138 GEVGLSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQV----AAPGP 1211
Cdd:cd19546      3 DEVPATAGQLrtWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldadAARPE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1212 APAIQAQDWRGAADLDSRVDAAFARMQEaTPLAGPLVALThahcDDGERLLICAHHLIVDAVSWRLLLGELFDGLAALAR 1291
Cdd:cd19546     83 LPVVPATEEELPALLADRAAHLFDLTRE-TPWRCTLFALS----DTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARRE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1292 GEAWTPSARGASYADYV----EALREADDAQRF---DAGFWRELAA--QPMQALPQDRPVALADARQSnvGRIVQTLDAG 1362
Cdd:cd19546    158 GRAPERAPLPLQFADYAlwerELLAGEDDRDSLigdQIAYWRDALAgaPDELELPTDRPRPVLPSRRA--GAVPLRLDAE 235

                   ....*....
gi 1246793773 1363 LTADLLERA 1371
Cdd:cd19546    236 VHARLMEAA 244
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
2062-2516 6.59e-06

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: 51.97  E-value: 6.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWhrgaawlpldpqhpdarqiavlddsgaRIvigwG 2141
Cdd:cd05940      4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLV---------------------------KI----G 52
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2142 AAPAWVPASVRWLDAESVLDVVSAYEepprVDVDadtPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPV-LDLGEDAS 2220
Cdd:cd05940     53 AVAALINYNLRGESLAHCLNVSSAKH----LVVD---AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSgGALPSDVL 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2221 LATLSTVAADLGFTALFGALLSGRRVRLLPaelafdaqalaahlqahpvdclKIVPSHLAGLLAAAGGTavlpreCLVTG 2300
Cdd:cd05940    126 YTCLPLYHSTALIVGWSACLASGATLVIRK----------------------KFSASNFWDDIRKYQAT------IFQYI 177
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2301 GEALTGALVQ---------QVRA-----LAPTL-----------RIVNHYGPTE------------TTVGILTCTVPEEW 2343
Cdd:cd05940    178 GELCRYLLNQppkpterkhKVRMifgngLRPDIweefkerfgvpRIAEFYAATEgnsgfinffgkpGAIGRNPSLLRKVA 257
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2344 P---VEQGVPVGHPLAGNEAwvldrFGLPAPVGVAGEL--YLGGGNLSLGYWQRAEQTaERFVAHPLAPDRLLYRSGDLA 2418
Cdd:cd05940    258 PlalVKYDLESGEPIRDAEG-----RCIKVPRGEPGLLisRINPLEPFDGYTDPAATE-KKILRDVFKKGDAWFNTGDLM 331
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2419 RLDGEGRIVYLGR-GDhQVKIRGYRVELGEVEQVLAQLPGVEVAAV--LALPGANG-------VLQLGACIQGSleGVAE 2488
Cdd:cd05940    332 RLDGEGFWYFVDRlGD-TFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGragmaaiVLQPNEEFDLS--ALAA 408
                          490       500
                   ....*....|....*....|....*...
gi 1246793773 2489 ALAQRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:cd05940    409 HLEKNLPGYARPLFLRLQPEMEITGTFK 436
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2300-2522 6.81e-06

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: 51.71  E-value: 6.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2300 GGEALTGALVQQVRAlAPTLRIVNHYGPTETTVGIlTCTVPE--EWPVEQGVPVghPLAGNEAWVLD---RFGLPAPVGV 2374
Cdd:cd05944    129 GAAPLPVELRARFED-ATGLPVVEGYGLTEATCLV-AVNPPDgpKRPGSVGLRL--PYARVRIKVLDgvgRLLRDCAPDE 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2375 AGELYLGGGNLSLGYWQrAEQTAERFVahplapDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQ 2454
Cdd:cd05944    205 VGEICVAGPGVFGGYLY-TEGNKNAFV------ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR 277
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2455 LPGVEVAAVLALPGAN------GVLQLGACIQGSLEGVAEALAQRLPEYLC-PSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:cd05944    278 HPAVAFAGAVGQPDAHagelpvAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL 352
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
2063-2200 7.54e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 52.07  E-value: 7.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAwlpldpqH--------PDA---RqiavLDD 2131
Cdd:PRK00174   100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV-------HsvvfggfsAEAladR----IID 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVI----GW-------------------------------GAAPAWVPASVRWLDaeSVLDVVSAYEEPprVDVDA 2176
Cdd:PRK00174   169 AGAKLVItadeGVrggkpiplkanvdealancpsvekvivvrrtGGDVDWVEGRDLWWH--ELVAGASDECEP--EPMDA 244
                          170       180
                   ....*....|....*....|....
gi 1246793773 2177 DTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:PRK00174   245 EDPLFILYTSGSTGKPKGVLHTTG 268
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
88-442 7.97e-06

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: 51.67  E-value: 7.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773   88 APLslgQERLWFLEQFEPGGHAYHLAALFEL--RGELDA--AALERAVHglliRHEVLDRCIQGEdsvaaGGGAAVE--- 160
Cdd:cd19544      5 APL---QEGILFHHLLAEEGDPYLLRSLLAFdsRARLDAflAALQQVID----RHDILRTAILWE-----GLSEPVQvvw 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  161 -SADLR------GRGQDEIDALVEGFRLRPFELQRQRP--LRMQLLRLDGQGdgpvRHWLQVVVHHIACDGVSLGLLTQD 231
Cdd:cd19544     73 rQAELPveeltlDPGDDALAQLRARFDPRRYRLDLRQAplLRAHVAEDPANG----RWLLLLLFHHLISDHTSLELLLEE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  232 LsRAYrvECGLAAEPAPPLPcqYGDY---ARWQRDTldrlDASLRHHVEALSG-----APH-LHELPLDherpavlGQSG 302
Cdd:cd19544    149 I-QAI--LAGRAAALPPPVP--YRNFvaqARLGASQ----AEHEAFFREMLGDvdeptAPFgLLDVQGD-------GSDI 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  303 AKLRLAFPPGLSERVAAYAQA---SRATAFH-----VLQaafaallaRCGAGDDLLIGTPVAGRVR--PELDSLVGLFVN 372
Cdd:cd19544    213 TEARLALDAELAQRLRAQARRlgvSPASLFHlawalVLA--------RCSGRDDVVFGTVLSGRMQggAGADRALGMFIN 284
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773  373 TVVLRTQLhDDPDFASLVARCRdHQLAAL---EHQALPLervietlqVERSSR---HAPLFQLMFALRHDADLALD 442
Cdd:cd19544    285 TLPLRVRL-GGRSVREAVRQTH-ARLAELlrhEHASLAL--------AQRCSGvpaPTPLFSALLNYRHSAAAAAA 350
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
844-1041 9.64e-06

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: 51.79  E-value: 9.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  844 ASRPvplgqlLPGRIAAVLDAHGRIVPRGVCGELAlggI-----GLAEGYRGDaaasERRFAPLRLP--SGeslrMYRSG 916
Cdd:cd05966    412 ATRP------FFGIEPAILDEEGNEVEGEVEGYLV---IkrpwpGMARTIYGD----HERYEDTYFSkfPG----YYFTG 474
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  917 DRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVG---EGAAQRLVAWVecAGEDGFgqadln 993
Cdd:cd05966    475 DGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAV--AEAAVVGrphDIKGEAIYAFV--TLKDGE------ 544
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1246793773  994 qTDSDQTESE--RWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:cd05966    545 -EPSDELRKElrKHVR---KEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
2174-2224 9.75e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 51.66  E-value: 9.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2174 VDADTP-----AYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVL-DLG-EDASLATL 2224
Cdd:PLN02387   242 VDPDLPspndiAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGkNDVYLAYL 299
PLN02736 PLN02736
long-chain acyl-CoA synthetase
3660-3975 1.01e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 51.64  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3660 EAPAYLIYTSGSTGTPKGVVVTHRNVerLFTAATQTGRFSFDEHDVW-----------------SLFHSHAFDFAVWELW 3722
Cdd:PLN02736   221 EDVATICYTSGTTGTPKGVVLTHGNL--IANVAGSSLSTKFYPSDVHisylplahiyervnqivMLHYGVAVGFYQGDNL 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3723 GawLYGGRAVLVPEAVCRQP-------DAFLDLLAEYGVtVLNQTPSAFYALQSQAM------------------RRELA 3777
Cdd:PLN02736   299 K--LMDDLAALRPTIFCSVPrlynriyDGITNAVKESGG-LKERLFNAAYNAKKQALengknpspmwdrlvfnkiKAKLG 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3778 LNVRAVVFGGEALEPSRLQPWRERYpQAELVNMYGITETTVHVSFHRLSDedlqSPTSRIGSALPDLAVHVLD------- 3850
Cdd:PLN02736   376 GRVRFMSSGASPLSPDVMEFLRICF-GGRVLEGYGMTETSCVISGMDEGD----NLSGHVGSPNPACEVKLVDvpemnyt 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3851 AAGQPVPLgvvGELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-RGYRIEPG 3929
Cdd:PLN02736   451 SEDQPYPR---GEICVRGPIIFKGYYKDEVQTREVIDEDG---WLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAPE 524
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773 3930 EIAAKIASLPQVSDAAVtvegqgEGAWLMAYAVAAdgAEPDPQSLR 3975
Cdd:PLN02736   525 KIENVYAKCKFVAQCFV------YGDSLNSSLVAV--VVVDPEVLK 562
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
2145-2207 1.11e-05

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: 51.41  E-value: 1.11e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 2145 AWVPASVRWLDaeSVLDVVSAYEEPprVDVDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVA 2207
Cdd:cd05966    203 PMTEGRDLWWH--DLMAKQSPECEP--EWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAA 261
PLN02574 PLN02574
4-coumarate--CoA ligase-like
821-1041 1.14e-05

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 51.38  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  821 LINAYGPTEATiSSHYHRVQAIDASRPVPLGQLLPGRIAAVLD-AHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF 899
Cdd:PLN02574   348 FIQGYGMTEST-AVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  900 aplrlpsgESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ-VRAAAAGVVGEGAAQRLVAW 978
Cdd:PLN02574   427 --------DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEiIDAAVTAVPDKECGEIPVAF 498
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  979 VECAGEDGFGQADLNQTDSDQTESERWHRalcerlpaymvptQFVALPRLPRNASGKIDRRAL 1041
Cdd:PLN02574   499 VVRRQGSTLSQEAVINYVAKQVAPYKKVR-------------KVVFVQSIPKSPAGKILRREL 548
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
602-1043 1.22e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 51.18  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  602 LLGAWRAGLSVIPLDTewpqARRAEVVAA----SGCDAVLTDAQGLA-----GFAPSVAIAVDEL----KLDGAGENGSG 668
Cdd:PRK13388    69 LAAAALGGYVLVGLNT----TRRGAALAAdirrADCQLLVTDAEHRPlldglDLPGVRVLDVDTPayaeLVAAAGALTPH 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  669 ENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDrVLHVA-----GLAVdttleqiLAAWS----R 739
Cdd:PRK13388   145 REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-VCYVSmplfhSNAV-------MAGWApavaS 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  740 GACVVARPDelLEPQRFLAFLSE-RAITVTDLAPAYANELVRASVADDwRDLALRcLVVGGDVLPVALAQrwFElgldRR 818
Cdd:PRK13388   217 GAAVALPAK--FSASGFLDDVRRyGATYFNYVGKPLAYILATPERPDD-ADNPLR-VAFGNEASPRDIAE--FS----RR 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  819 --CALINAYGPTEATISshyhrVQAIDASRPVPLGQLLPGRI-----------AAVLDAHGRIV-PRGVCGELA-LGGIG 883
Cdd:PRK13388   287 fgCQVEDGYGSSEGAVI-----VVREPGTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLnADEAIGELVnTAGAG 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  884 LAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAA 963
Cdd:PRK13388   362 FFEGYYNNPEATAERMR-----HG----MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVA 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  964 A-GVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTEserwhralcerLPAYMVPTQFVALPRLPRNASGKIDRRALP 1042
Cdd:PRK13388   433 VyAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPD-----------LGTKAWPRYVRIAADLPSTATNKVLKRELI 501

                   .
gi 1246793773 1043 A 1043
Cdd:PRK13388   502 A 502
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
4029-4084 1.41e-05

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: 45.25  E-value: 1.41e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 4029 RRLAELWRQLLGGELPGRGAH--FFARGGHSLLVVRLAEAIRAEFAIAVPLKSLFEQP 4084
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDtdLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHP 58
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
2051-2218 1.45e-05

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 51.03  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2051 QAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGA--AWL-------PL----- 2116
Cdd:PRK08279    52 DRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntqqrgaVLahsln 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2117 --DPQH--PDARQIAVLDDSGARIVIG---WGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVDADTPAYLIYTSGST 2189
Cdd:PRK08279   132 lvDAKHliVGEELVEAFEEARADLARPprlWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTT 211
                          170       180
                   ....*....|....*....|....*....
gi 1246793773 2190 GTPKGVVVSQGNLANYVAGVLPVLDLGED 2218
Cdd:PRK08279   212 GLPKAAVMSHMRWLKAMGGFGGLLRLTPD 240
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
2297-2498 1.47e-05

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 50.92  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2297 LVTGGEALTGALVQQVRALAPtLRIVNHYGPTETTVGILTctvpeEWPVEQGVPVghplagNEAWVL-----DRFGLPAP 2371
Cdd:COG1541    208 GIFGGEPWSEEMRKEIEERWG-IKAYDIYGLTEVGPGVAY-----ECEAQDGLHI------WEDHFLveiidPETGEPVP 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2372 VGVAGELYLgggnlslgywqraeqTAERFVAHPLapdrLLYRSGDLARLDGEG--------RIVY-LGRGDHQVKIRGYR 2442
Cdd:COG1541    276 EGEEGELVV---------------TTLTKEAMPL----IRYRTGDLTRLLPEPcpcgrthpRIGRiLGRADDMLIIRGVN 336
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2443 VELGEVEQVLAQLPGVEVAAVLALPGANG----VLQLGACIQGSLEGVAEALAQRLPEYL 2498
Cdd:COG1541    337 VFPSQIEEVLLRIPEVGPEYQIVVDREGGldelTVRVELAPGASLEALAEAIAAALKAVL 396
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
2041-2203 1.71e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 50.80  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2041 AQSLLWQMPAQAVAVEEGAASWTYAQLRAAAGRIAGALDAVGVQPGA-HVALCLPRTFAQLAAMAAVW-----------H 2108
Cdd:PRK13388     6 AQLLRDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAAlggyvlvglntT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2109 RGAAWLPLDPQHPDArQIAVLDDSGARIVIGWG--AAPAWVPASVRWLDAesvldVVSAYEEPPRVDVDADTPAYLIYTS 2186
Cdd:PRK13388    86 RRGAALAADIRRADC-QLLVTDAEHRPLLDGLDlpGVRVLDVDTPAYAEL-----VAAAGALTPHREVDAMDPFMLIFTS 159
                          170
                   ....*....|....*..
gi 1246793773 2187 GSTGTPKGVVVSQGNLA 2203
Cdd:PRK13388   160 GTTGAPKAVRCSHGRLA 176
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
672-1041 1.98e-05

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 50.65  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGHA-----ALAAHIDAAAEALALSADDRVL------HVAGLAVDTtleqiLAAWSRG 740
Cdd:PRK08751   206 EPDDIAFLQYTGGTTGVAKGAMLTHRnlvanMQQAHQWLAGTGKLEEGCEVVItalplyHIFALTANG-----LVFMKIG 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  741 AC--VVARPDEL------LEPQRFLAFLSERAITvtdlapayaNELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE 812
Cdd:PRK08751   281 GCnhLISNPRDMpgfvkeLKKTRFTAFTGVNTLF---------NGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQ 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  813 L-GLdrrcALINAYGPTEATISSHYHRVQAIDASRPVplGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGY--R 889
Cdd:PRK08751   352 VtGL----TLVEAYGLTETSPAACINPLTLKEYNGSI--GLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYwkR 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  890 GDAAASerrfaplrlpSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-RAAAAGVVG 968
Cdd:PRK08751   426 PEETAK----------VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVlEVAAVGVPD 495
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  969 EGAAQRLVAWVEcagedgfgQADLNQTDSDQTESERwhralcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK08751   496 EKSGEIVKVVIV--------KKDPALTAEDVKAHAR------ANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2676-2812 2.29e-05

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: 49.99  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2676 HPMLRARF-QRDAAGQWQQTLGDWQadrFAHREADagQREDLLA-QWQAGLSFDGALLRvLALPDPQDGDTRVLFAAHHL 2753
Cdd:cd19545     50 NPILRTRIvQSDSGGLLQVVVKESP---ISWTEST--SLDEYLEeDRAAPMGLGGPLVR-LALVEDPDTERYFVWTIHHA 123
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773 2754 LVDAVSWGIIVDDLQHAYAERRAGRSPAlaaeacgFGAWQAALRQLSaatLDGWRSYWR 2812
Cdd:cd19545    124 LYDGWSLPLILRQVLAAYQGEPVPQPPP-------FSRFVKYLRQLD---DEAAAEFWR 172
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1142-1340 2.42e-05

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: 50.00  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1142 LSPIQRWFFDSAPAQPDR--YHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQD 1219
Cdd:cd19547      4 LAPMQEGMLFRGLFWPDSdaYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWALLD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1220 WRGAaDLDSRVDAaFARMQEATPLAG------PLVALTHAHCDDGERLLICAHH-LIVDAVSWRLLLGELFDGLAALARG 1292
Cdd:cd19547     84 WSGE-DPDRRAEL-LERLLADDRAAGlsladcPLYRLTLVRLGGGRHYLLWSHHhILLDGWCLSLIWGDVFRVYEELAHG 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246793773 1293 -EAWTPSARgaSYADYVEALR----EADDAQRFDAGFWRELAAQPMQALPQDR 1340
Cdd:cd19547    162 rEPQLSPCR--PYRDYVRWIRartaQSEESERFWREYLRDLTPSPFSTAPADR 212
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1139-1341 2.42e-05

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: 49.96  E-value: 2.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1139 EVGLSPIQR--WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPA-PAI 1215
Cdd:cd19538      1 EIPLSFAQRrlWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtPKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1216 QAQDwRGAADLDSRVDAA----FARMQEAtPLAGPLVALthahcDDGER-LLICAHHLIVDAVSWRLLLGELFDGLAALA 1290
Cdd:cd19538     81 EIKE-VDEEELESEINEAvrypFDLSEEP-PFRATLFEL-----GENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773 1291 RGEA--WTPSArgASYADYV----EALREADDAQRFDA---GFWRE-LAAQPMQ-ALPQDRP 1341
Cdd:cd19538    154 KGEApeLAPLP--VQYADYAlwqqELLGDESDPDSLIArqlAYWKKqLAGLPDEiELPTDYP 213
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
2168-2209 2.99e-05

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: 49.91  E-value: 2.99e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1246793773 2168 EPPrvdvDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGV 2209
Cdd:cd05927    109 PPP----KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGV 146
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
679-1038 3.18e-05

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: 49.19  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  679 ILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVDTTLEQilaawSRGACVVArpdELLE 752
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLnmlplfHIAGLNLALATFH-----AGGANVVM---EKFD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  753 PQRFLAFLSERAITV-TDLAPAYANELvrASVADDWRDLA-LRcLVVGGDVlPvALAQRWFELGLDRRCALinaYGPTEA 830
Cdd:cd17637     77 PAEALELIEEEKVTLmGSFPPILSNLL--DAAEKSGVDLSsLR-HVLGLDA-P-ETIQRFEETTGATFWSL---YGQTET 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  831 TISSHYHRVQAIDAS--RPVPLGQLlpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFaplrlpsge 908
Cdd:cd17637    149 SGLVTLSPYRERPGSagRPGPLVRV------RIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--------- 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  909 slR--MYRSGDRVRLLDDGELQFLGRADFQ--VKLRGYRIELEEIEHCLGQLPQVraAAAGVVGEGAAQrlvawvecage 984
Cdd:cd17637    214 --RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAI--AEVCVIGVPDPK----------- 278
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246793773  985 dgFGQADlnqtdsdqteserwhRALCERLPAYMVPTQ----FVA-------LPR-------LPRNASGKIDR 1038
Cdd:cd17637    279 --WGEGI---------------KAVCVLKPGATLTADelieFVGsriarykKPRyvvfveaLPKTADGSIDR 333
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
719-1253 3.23e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 50.26  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  719 LHVAGLAVDTTLeqiLAAWSRGACVV------ARPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLAL 792
Cdd:COG3321    840 LWVAGVPVDWSA---LYPGRGRRRVPlptypfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  793 RCLVVGGDVLPVALAQRWFELGLDRRCALINAYGPTEATISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRG 872
Cdd:COG3321    917 AALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL 996
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  873 VCGELALGGIGLAEGYRGDAAASERRFAPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHC 952
Cdd:COG3321    997 AAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAE 1076
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  953 LGQLPQVRAAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNA 1032
Cdd:COG3321   1077 LALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAA 1156
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1033 SGKIDRRALPAPPVLAQAERTPPRTAEESALCEVWAEVLQCEVGIHDSFFRLGGDSIRSLQVVARLRERGYAVTPKLMYQ 1112
Cdd:COG3321   1157 AALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALL 1236
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1113 YQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLR 1192
Cdd:COG3321   1237 ALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAA 1316
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773 1193 ASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHA 1253
Cdd:COG3321   1317 AAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALA 1377
PRK07529 PRK07529
AMP-binding domain protein; Validated
2061-2522 3.29e-05

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 49.95  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2061 SWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRT----FAQLAAMAAvwhrGAA----WLpLDPQHpdarqIA-VLDD 2131
Cdd:PRK07529    58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLpethFALWGGEAA----GIAnpinPL-LEPEQ-----IAeLLRA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2132 SGARIVI-------------------------------GWGAAPAWVPASVRWLDAESVLDVVSAYEEPPRVDVD----- 2175
Cdd:PRK07529   128 AGAKVLVtlgpfpgtdiwqkvaevlaalpelrtvvevdLARYLPGPKRLAVPLIRRKAHARILDFDAELARQPGDrlfsg 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2176 ----ADTPAYLIYTSGSTGTPKGVVVSQGNLAnYVAGVLP-VLDLGEDASLAT---LSTVAADLgfTALFGALLSGRRVr 2247
Cdd:PRK07529   208 rpigPDDVAAYFHTGGTTGMPKLAQHTHGNEV-ANAWLGAlLLGLGPGDTVFCglpLFHVNALL--VTGLAPLARGAHV- 283
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2248 LLPAELAFDAQALAAH----LQAHPVDCLKIVPShlagllaAAGGTAVLPRE-----CL---VTGGEALTGALVQQVRAl 2315
Cdd:PRK07529   284 VLATPQGYRGPGVIANfwkiVERYRINFLSGVPT-------VYAALLQVPVDghdisSLryaLCGAAPLPVEVFRRFEA- 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2316 APTLRIVNHYGPTETTVgiLTCTVPEEWPVEQGvPVGHPLAGNEAWVL-----DRFGLPAPVGVAGELYLGGGNLSLGYw 2390
Cdd:PRK07529   356 ATGVRIVEGYGLTEATC--VSSVNPPDGERRIG-SVGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGY- 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2391 QRAEQTAERFVAhplapDRLLyRSGDLARLDGEGRIVYLGRGDHQVkIR-GYRVELGEVEQVLAQLPGVEVAAVLALPGA 2469
Cdd:PRK07529   432 LEAAHNKGLWLE-----DGWL-NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDA 504
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2470 N------GVLQLGACIQGSLEGVAEALAQRLPEYLC-PSRWRAVESMPRLGNGKIDRQAL 2522
Cdd:PRK07529   505 HagelpvAYVQLKPGASATEAELLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPAL 564
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1148-1348 3.64e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 50.04  E-value: 3.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1148 WFFDSAPAQPDRYHQYVALRLKQPLDAQHLAQVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADld 1227
Cdd:PRK10252    18 WMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEIIDLRTQPD-- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1228 sRVDAAFARMQeaTPLAGPLvALTHAHCDDGERLLICA----------HHLIVDAVSWRLLLGELFDGLAALARGEAWTP 1297
Cdd:PRK10252    96 -PHAAAQALMQ--ADLQQDL-RVDSGKPLVFHQLIQLGdnrwywyqryHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPA 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1298 SARG------ASYADYvealrEADDAQRFDAGFWRELAAQpmqaLPQdrPVALADAR 1348
Cdd:PRK10252   172 SPFTpfadvvEEYQRY-----RASEAWQRDAAFWAEQRRQ----LPP--PASLSPAP 217
PLN02736 PLN02736
long-chain acyl-CoA synthetase
2058-2216 3.99e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 49.71  E-value: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2058 GAASW-TYAQLRAAAGRIAGALDAVGVQPGAHVALclprTFAQLAAMAAVWHRGAAW----LPL-DPQHPDARQIAV--- 2128
Cdd:PLN02736    74 GEYKWmTYGEAGTARTAIGSGLVQHGIPKGACVGL----YFINRPEWLIVDHACSAYsyvsVPLyDTLGPDAVKFIVnha 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 -------------------LDDSGARIVIGWGAAPAWVP-----ASVRWLDAESVLDVVSAYEEPPRVDVDADTpAYLIY 2184
Cdd:PLN02736   150 evaaifcvpqtlntllsclSEIPSVRLIVVVGGADEPLPslpsgTGVEIVTYSKLLAQGRSSPQPFRPPKPEDV-ATICY 228
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1246793773 2185 TSGSTGTPKGVVVSQGNLANYVAGVLPVLDLG 2216
Cdd:PLN02736   229 TSGTTGTPKGVVLTHGNLIANVAGSSLSTKFY 260
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
675-1053 5.42e-05

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 49.31  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  675 QLAYILYTSGSTGIPKGVEvghaalaahIDAAAEALALSADDRVLHVAGLAVDTTLEQI------------LAAWSRGAC 742
Cdd:PRK12406   153 QPQSMIYTSGTTGHPKGVR---------RAAPTPEQAAAAEQMRALIYGLKPGIRALLTgplyhsapnaygLRAGRLGGV 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  743 VVARPDelLEPQRFLAFLSERAITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPVALAQrwfelgldrrcA 820
Cdd:PRK12406   224 LVLQPR--FDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPCPADVKR-----------A 290
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  821 LINAYGP--------TEATISSHYHRVQAIdaSRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAE-GYRGD 891
Cdd:PRK12406   291 MIEWWGPviyeyygsTESGAVTFATSEDAL--SHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNK 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  892 aaaserrfaPLRLPSGESLRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEG 970
Cdd:PRK12406   369 ---------PEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVfGIPDAE 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  971 AAQRLVAWVECAGEDGFGQADLNQTdsdqteserwhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRALpAPPVLAQA 1050
Cdd:PRK12406   440 FGEALMAVVEPQPGATLDEADIRAQ-------------LKARLAGYKVPKHIEIMAELPREDSGKIFKRRL-RDPYWANA 505

                   ...
gi 1246793773 1051 ERT 1053
Cdd:PRK12406   506 GRK 508
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
673-1037 5.89e-05

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 49.32  E-value: 5.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  673 PNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR------VLHVAGLAVDttleqILAAWSRGACVVAR 746
Cdd:PRK08043   364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRfmsalpLFHSFGLTVG-----LFTPLLTGAEVFLY 438
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  747 PDEL---LEPQrflaFLSERAITVTDLAPAYANELVR-ASVADDWRdlaLRCLVVGGDVLPVALAQRWFE-LGLdrrcAL 821
Cdd:PRK08043   439 PSPLhyrIVPE----LVYDRNCTVLFGTSTFLGNYARfANPYDFAR---LRYVVAGAEKLQESTKQLWQDkFGL----RI 507
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  822 INAYGPTEATisshyhRVQAID---ASRPVPLGQLLPGRIAAVLDAHGriVPRGvcGELALGGIGLAEGYRgdaaaseRR 898
Cdd:PRK08043   508 LEGYGVTECA------PVVSINvpmAAKPGTVGRILPGMDARLLSVPG--IEQG--GRLQLKGPNIMNGYL-------RV 570
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  899 FAP--LRLPSGESLR------MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEH-CLGQLPQVRAAAAGVVGE 969
Cdd:PRK08043   571 EKPgvLEVPTAENARgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDA 650
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  970 GAAQRLVawvecagedgfgqadLNQTDSDQTESERWHRALCERLPAYMVPTQFVALPRLPRNASGKID 1037
Cdd:PRK08043   651 SKGEALV---------------LFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
PRK07868 PRK07868
acyl-CoA synthetase; Validated
3526-4048 6.76e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 49.33  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3526 AEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAILKTGAAYVPVDPHAPA 3605
Cdd:PRK07868   454 AEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPDTDL 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3606 ARRGFILEDSGVCLSVSQRALAVELPGTALCL----------DDPFTRAQLDAVEPG--ELPEVPTEAP------AYLIY 3667
Cdd:PRK07868   534 AAAVRLGGVTEIITDPTNLEAARQLPGRVLVLgggesrdldlPDDADVIDMEKIDPDavELPGWYRPNPglardlAFIAF 613
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3668 -TSGSTGTPKGVVvTHRNVERLFTAATQTGrfsFDEHD-VWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAvcrQPDAF 3745
Cdd:PRK07868   614 sTAGGELVAKQIT-NYRWALSAFGTASAAA---LDRRDtVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGL---DPDRF 686
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3746 LDLLAEYGVTVLNQTpsafyalqsQAMRRELalnVRAVVFGGEALEPSRL-----QP---WR---ERYPQAELVNMYGIT 3814
Cdd:PRK07868   687 VQEVRQYGVTVVSYT---------WAMLREV---VDDPAFVLHGNHPVRLfigsgMPtglWErvvEAFAPAHVVEFFATT 754
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3815 ETTV---HVSFHRLSDEDLQSPTS---RIGSALPDLAVHVLDAAG--QPVPLGVVGELVVEGDGVAQgywqrPELTAERF 3886
Cdd:PRK07868   755 DGQAvlaNVSGAKIGSKGRPLPGAgrvELAAYDPEHDLILEDDRGfvRRAEVNEVGVLLARARGPID-----PTASVKRG 829
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3887 VERGGQRFYRSGDLGRYRADGSLEYRGRGDDQVK-LRG-YRIEPgeIAAKIASLPQVsDAAVTVeGQGEGAWLMAYAVAA 3964
Cdd:PRK07868   830 VFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRtARGpVYTEP--VTDALGRIGGV-DLAVTY-GVEVGGRQLAVAAVT 905
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3965 --DGAEPDPQSLREALRALLPDYMlPRLIQLLPALPLTAN-----GKLDRKALPKPETQD--RDEgvlESASERRLAELW 4035
Cdd:PRK07868   906 lrPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLSATyrptvSALRAAGIPKPGRQAwyFDP---ETNRYRRLTPAV 981
                          570
                   ....*....|...
gi 1246793773 4036 RQLLGGELPGRGA 4048
Cdd:PRK07868   982 RAELTGGHRRGAA 994
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
588-932 7.17e-05

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 48.96  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  588 VALCLPRGLDWYCLLLGAWRAGLSVIPL-DTEWP--QARRAEVVAASGCDAVLTDAQGLAG----FAPSVA------IAV 654
Cdd:PRK07769    82 VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGvrkfFRARPAkerprvIAV 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  655 DELKlDGAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR------VLHVAGLavdt 728
Cdd:PRK07769   162 DAVP-DEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRgvswlpFFHDMGL---- 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  729 tLEQILAAWSRG-------ACVVARPDELLepqRFLAFLSERAITVTDLAPAYANEL--VRASVADDWRDLAL---RCLV 796
Cdd:PRK07769   237 -ITVLLPALLGHyitfmspAAFVRRPGRWI---RELARKPGGTGGTFSAAPNFAFEHaaARGLPKDGEPPLDLsnvKGLL 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  797 VGGDVLPVALAQRWFE----LGLdRRCALINAYGPTEAT--ISS-----------------HYHRVQAIDASRPVPLGQL 853
Cdd:PRK07769   313 NGSEPVSPASMRKFNEafapYGL-PPTAIKPSYGMAEATlfVSTtpmdeeptviyvdrdelNAGRFVEVPADAPNAVAQV 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  854 LPGRI-----AAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDAAASERRFAPL---RLP------SGESLRMYRSGDR 918
Cdd:PRK07769   392 SAGKVgvsewAVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNIlksRLSeshaegAPDDALWVRTGDY 471
                          410
                   ....*....|....
gi 1246793773  919 VRLLdDGELQFLGR 932
Cdd:PRK07769   472 GVYF-DGELYITGR 484
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
824-968 7.23e-05

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: 48.07  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  824 AYGPTEAT---ISSHYHRVQAIDASRPVPLGQLlpgriaAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRFA 900
Cdd:cd17636    142 GYGQTEVMglaTFAALGGGAIGGAGRPSPLVQV------RILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR 215
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  901 plrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAagVVG 968
Cdd:cd17636    216 -----GG----WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAA--VIG 272
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1187-1371 8.50e-05

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: 48.20  E-value: 8.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1187 RHDLLRASFeRADG-----Q--WRQ------QVAAPGPAPAiqaqdwrgAADLDSRVDAAFARM--QEAtplagPLVALT 1251
Cdd:cd19544     51 RHDILRTAI-LWEGlsepvQvvWRQaelpveELTLDPGDDA--------LAQLRARFDPRRYRLdlRQA-----PLLRAH 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1252 HAHCDDGER--LLICAHHLIVDAVSWRLLLGElfdgLAALARGEAWT-PSArgASYADYVEALREADDAQRFDAgFWREL 1328
Cdd:cd19544    117 VAEDPANGRwlLLLLFHHLISDHTSLELLLEE----IQAILAGRAAAlPPP--VPYRNFVAQARLGASQAEHEA-FFREM 189
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1246793773 1329 AAQpmqalpQDRPVA---LADARQ--SNVGRIVQTLDAGLTADLLERA 1371
Cdd:cd19544    190 LGD------VDEPTApfgLLDVQGdgSDITEARLALDAELAQRLRAQA 231
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
2123-2213 9.08e-05

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 48.72  E-value: 9.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2123 ARQIAVLDDSGARIVIGWGAAPAwvPASVRW---LDAESVLDVVSAYEEpprvdVDADTPAYLIYTSGSTGTPKGVVVSQ 2199
Cdd:PRK08180   159 ARALAAVVPADVEVVAVRGAVPG--RAATPFaalLATPPTAAVDAAHAA-----VGPDTIAKFLFTSGSTGLPKAVINTH 231
                           90
                   ....*....|....*..
gi 1246793773 2200 GNL-AN--YVAGVLPVL 2213
Cdd:PRK08180   232 RMLcANqqMLAQTFPFL 248
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
2056-2202 9.63e-05

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 48.63  E-value: 9.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2056 EEGAASWTYAQLRAAAGRIAGAL-DAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-----------HPDA 2123
Cdd:PRK05620    33 GAEQEQTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQlmndqivhiinHAED 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2124 RQIaVLDDSGA-------------RIVIGWGAAPA-----WVPASVRWLDAESVLDVVSA-YEEPprvDVDADTPAYLIY 2184
Cdd:PRK05620   113 EVI-VADPRLAeqlgeilkecpcvRAVVFIGPSDAdsaaaHMPEGIKVYSYEALLDGRSTvYDWP---ELDETTAAAICY 188
                          170
                   ....*....|....*...
gi 1246793773 2185 TSGSTGTPKGVVVSQGNL 2202
Cdd:PRK05620   189 STGTTGAPKGVVYSHRSL 206
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
791-1041 9.67e-05

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 48.51  E-value: 9.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  791 ALRCLVVGGDVLPVALAQRWFELgldRRCALINAYGPTEAT--ISSHYHRVQAIDASRPVPLgqllPGRIAAVLDAHGRI 868
Cdd:PRK08974   326 SLKLSVGGGMAVQQAVAERWVKL---TGQYLLEGYGLTECSplVSVNPYDLDYYSGSIGLPV----PSTEIKLVDDDGNE 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  869 VPRGVCGELALGGIGLAEGY--RGDAAAserrfaplrlpsgESLR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRI 944
Cdd:PRK08974   399 VPPGEPGELWVKGPQVMLGYwqRPEATD-------------EVIKdgWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNV 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  945 ELEEIEHCLGQLPQV-RAAAAGVVGEGAAQRLVAWVEcagedgfgqadlnQTDSDQTESERwhRALCER-LPAYMVPTQF 1022
Cdd:PRK08974   466 YPNEIEDVVMLHPKVlEVAAVGVPSEVSGEAVKIFVV-------------KKDPSLTEEEL--ITHCRRhLTGYKVPKLV 530
                          250
                   ....*....|....*....
gi 1246793773 1023 VALPRLPRNASGKIDRRAL 1041
Cdd:PRK08974   531 EFRDELPKSNVGKILRREL 549
PLN03051 PLN03051
acyl-activating enzyme; Provisional
901-1041 1.03e-04

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 48.27  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  901 PLRLPSGESLRmyRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQ--VRAAAAGVVGEGAAQRLVAW 978
Cdd:PLN03051   349 PMYGSKGMPLR--RHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgiAETAAVGVAPPDGGPELLVI 426
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  979 VECAG--EDGFGQADLNQTdsdqteSERWHRALCERL-PAYMVptQFVAL-PRLPRNASGKIDRRAL 1041
Cdd:PLN03051   427 FLVLGeeKKGFDQARPEAL------QKKFQEAIQTNLnPLFKV--SRVKIvPELPRNASNKLLRRVL 485
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2676-2812 1.18e-04

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: 47.87  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2676 HPMLRARFQRDAAGQWQQTLGDWQADRFAHREADAGQREDLLAQWQAGLS---FD---GALLRVLA--LPdpqDGDTRVL 2747
Cdd:cd19535     53 HPMLRAVFLDDGTQQILPEVPWYGITVHDLRGLSEEEAEAALEELRERLShrvLDverGPLFDIRLslLP---EGRTRLH 129
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246793773 2748 FAAHHLLVDAVSWGIIVDDLQHAYAERRAgrspALAAEACGFGAWQAALRQLSAATLDGWRSYWR 2812
Cdd:cd19535    130 LSIDLLVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQALRETAYERARAYWQ 190
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
3663-3914 1.30e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 48.05  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3663 AYLIYTSGSTGTPKGVVVTHRNVERLFTAATQ-----TGRFSFDEHDVWSLFHSHAFDFAVWELW---GAWL-YGgravl 3733
Cdd:PTZ00216   267 ALIMYTSGTTGDPKGVMHTHGSLTAGILALEDrlndlIGPPEEDETYCSYLPLAHIMEFGVTNIFlarGALIgFG----- 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3734 vpeavcrQPDAFLDL-------LAEYGVTVLNQTPSAF-----------------------YALQSQ------------- 3770
Cdd:PTZ00216   342 -------SPRTLTDTfarphgdLTEFRPVFLIGVPRIFdtikkaveaklppvgslkrrvfdHAYQSRlralkegkdtpyw 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3771 ------AMRRELALNVRAVVFGGEALEPsrlqpwreryPQAELVNM--------YGITETTVHVSFHRLSDEDlqspTSR 3836
Cdd:PTZ00216   415 nekvfsAPRAVLGGRVRAMLSGGGPLSA----------ATQEFVNVvfgmviqgWGLTETVCCGGIQRTGDLE----PNA 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3837 IGSALPDLAVHVLDAAG-----QPVPLGvvgELVVEGDGVAQGYWQRPELTAERFVERGgqrFYRSGDLGRYRADGSLEY 3911
Cdd:PTZ00216   481 VGQLLKGVEMKLLDTEEykhtdTPEPRG---EILLRGPFLFKGYYKQEELTREVLDEDG---WFHTGDVGSIAANGTLRI 554

                   ...
gi 1246793773 3912 RGR 3914
Cdd:PTZ00216   555 IGR 557
PRK09192 PRK09192
fatty acyl-AMP ligase;
2064-2207 1.35e-04

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 48.08  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2064 YAQLRAAAGRIAGALDAVGVQPGAHVALcLPRTFAQLAAM------AAVWhrgAAWLPLdpqhPDA--------RQIAV- 2128
Cdd:PRK09192    52 YQTLRARAEAGARRLLALGLKPGDRVAL-IAETDGDFVEAffacqyAGLV---PVPLPL----PMGfggresyiAQLRGm 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2129 LDDSGARIVIGWGAAPAWVPASVRWLDAESVLDVVSAYEEP-PRVD---VDADTPAYLIYTSGSTGTPKGVVVSQGNL-A 2203
Cdd:PRK09192   124 LASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPeADVAlprPTPDDIAYLQYSSGSTRFPRGVIITHRALmA 203

                   ....
gi 1246793773 2204 NYVA 2207
Cdd:PRK09192   204 NLRA 207
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
3108-3329 1.51e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 47.40  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3108 TVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPSPRQLPHRQVSLPLAEQDWSGLEPaqarsrLSELQAQQCEAgf 3187
Cdd:PRK09294    27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLHPGIVVVDGDAARP------LPELQLDQGVS-- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3188 dlaappLMRLALLRRSADEHWLVWTrHHLIVDGWSSALLLDEVWRLYAALRESRTPQLPAAPPFRDYLHWLrgqdeAAAR 3267
Cdd:PRK09294    99 ------LLALDVVPDDGGARVTLYI-HHSIADAHHSASLLDELWSRYTDVVTTGDPGPIRPQPAPQSLEAV-----LAQR 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3268 AFWREQLTGLE---------------PAALPEATEPAEGYASSTRRFDLAAASAWAQS---HGLTASSLLQGALALVLQR 3329
Cdd:PRK09294   167 GIRRQALSGAErfmpamyayelpptpTAAVLAKPGLPQAVPVTRCRLSKAQTSSLAAFgrrHRLTVNALVSAAILLAEWQ 246
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
674-1041 1.52e-04

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 47.72  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  674 NQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAE--ALALSADDRVL------HVAGLAVDTTLEQIlaawsRGACVVA 745
Cdd:PRK06710   206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwlYNCKEGEEVVLgvlpffHVYGMTAVMNLSIM-----QGYKMVL 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 RPDelLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFELGLDRrcaLINAY 825
Cdd:PRK06710   281 IPK--FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGK---LVEGY 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  826 GPTEATISSHYHRVQaiDASRPVPLGQLLPGRIAAVLDAH-GRIVPRGVCGELALGGIGLAEGYRGDaaaSERRFAPLRl 904
Cdd:PRK06710   356 GLTESSPVTHSNFLW--EKRVPGSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNK---PEETAAVLQ- 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  905 pSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEGAAQRLVAWVeCAG 983
Cdd:PRK06710   430 -DG----WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTiGVPDPYRGETVKAFV-VLK 503
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773  984 EDgfgqadlnqTDSDQTESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK06710   504 EG---------TECSEEELNQFAR---KYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2545-2610 1.77e-04

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: 43.01  E-value: 1.77e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  2545 EVLRELWQKLLGR---EHIGAHDNFFALGGDSILSLQLVARARQA-GLALMPRQLYDHPTLAGLSAQVQA 2610
Cdd:smart00823   15 DLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAA 84
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1019-1558 2.21e-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: 47.56  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1019 PTQFVALPRLPRNASGKIDRRALPAPPVLAQAERTPPRTAEESALCEVWAEVLQCEVGIHDSFFRLGGDSIRSLQVVARL 1098
Cdd:COG3321    857 GRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALA 936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1099 RERGYAVTPKLMYQYQSAAELAPQLIALQAAPAEAAPLVGEVGLSPIQRWFFDSAPAQPDRYHQYVALRLKQPLDAQHLA 1178
Cdd:COG3321    937 AAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAA 1016
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1179 QVWDALWRRHDLLRASFERADGQWRQQVAAPGPAPAIQAQDWRGAADLDSRVDAAFARMQEATPLAGPLVALTHAHCDDG 1258
Cdd:COG3321   1017 AAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1259 ERLLICAHHLIVDAVSWRLLLGELFDGLAALARGEAWTPSARGASYADYVEALREADDAQRFDAGFWRELAAQPMQALPQ 1338
Cdd:COG3321   1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1339 DRPVALADARQSNVGRIVQTLDAGLTADLLERAgeayrcrtdevllialarALATRTG----RNRLWLDRERHGRDVLDG 1414
Cdd:COG3321   1177 LALALAAALAAALAGLAALLLAALLAALLAALL------------------ALALAALaaaaAALLAAAAAAAALALLAL 1238
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1415 RDWSSVLGWYTAVHPLPLDLGVADGPAQIGALKEQIRALARRGLDYMPLVASARIPALPAGQLLFNYHGVVDAGAHPAFE 1494
Cdd:COG3321   1239 AAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAA 1318
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 1495 VEPRTLASGNGADNPPGALVEINARVQAGRLGLVWNYAGEAYDAATIEAWSQAFAAELAALVAH 1558
Cdd:COG3321   1319 AALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALA 1382
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
3190-3778 2.31e-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: 47.56  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3190 AAPPLMRLALLRRSADEHWLVWTrhhLIVDGWSSALLLDevWRLYAALRESRTPQLPAAPpfrdylhWLRgQDEAAARAF 3269
Cdd:COG3321    813 AAGDAVVLPSLRRGEDELAQLLT---ALAQLWVAGVPVD--WSALYPGRGRRRVPLPTYP-------FQR-EDAAAALLA 879
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3270 WREQLTGLEPAALPEATEPAEGYASSTRRFDLAAASAWAQSHGLTASSLLQGALALVLQRyygrdDFALGITIAGRPPEL 3349
Cdd:COG3321    880 AALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA-----AALLALAAAAAAAAA 954
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3350 AGVERMLGVFINSVPLRVTPAGEATPAPWLQALQQRNLDLRTHGYLPLAQIQRAGAADAVSPFDVLLVFENLPTESREER 3429
Cdd:COG3321    955 ALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAA 1034
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3430 SGMRIEELDHRAHSNYPLMLTAIPDAGGLRIEAALDRSKLDGWLVEQMLDDLDFVLQQVPALQRFDALPLLPSQTRSAAW 3509
Cdd:COG3321   1035 LAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAA 1114
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3510 TSRERYACTGNLVSRFAEIARRYPARIAVSAEDGELDYATLDRRSSQLATLLIRQGAGPGQRVGLCLPRGCDLLVALLAI 3589
Cdd:COG3321   1115 LALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAA 1194
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3590 LKTGAAYVPVDPHAPAARRGFILEDSGVCLSVSQRALAVELPGTALCLDDPFTRAQLDAVEPGELPEVPTEAPAYLIYTS 3669
Cdd:COG3321   1195 LLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAAL 1274
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3670 GSTGTPKGVVVTHRNVERLFTAATQTGRFSFDEHDVWSLFHSHAFDFAVWELWGAWLYGGRAVLVPEAVCRQPDAFLDLL 3749
Cdd:COG3321   1275 AAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAA 1354
                          570       580
                   ....*....|....*....|....*....
gi 1246793773 3750 AEYGVTVLNQTPSAFYALQSQAMRRELAL 3778
Cdd:COG3321   1355 AAAAAAAALAAAAGAAAAAAALALAALAA 1383
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2630-2810 2.40e-04

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: 47.06  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2630 LTPIQHWFFEQALDQPahwNMSLYL-----KLPGALDTAAFAAALADVAAAHPMLRARFQRDAAG---QWQ--QTLGDWQ 2699
Cdd:cd19536      4 LSSLQEGMLFHSLLNP---GGSVYLhnytyTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqpvQVVhrQAQVPVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2700 ADRFAHREADAGQREDLLAQWQA-GLSFDGA-LLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAG 2777
Cdd:cd19536     81 ELDLTPLEEQLDPLRAYKEETKIrRFDLGRApLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1246793773 2778 RSPALaAEACGFG---AWQAALRQlSAATLDGWRSY 2810
Cdd:cd19536    161 KPLSL-PPAQPYRdfvAHERASIQ-QAASERYWREY 194
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
948-1035 3.41e-04

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: 41.76  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  948 EIEHCLGQLPQVR-AAAAGVVGEGAAQRLVAWVECAGEDGFGQADLNQtdsdqteserwhrALCERLPAYMVPTQFVALP 1026
Cdd:pfam13193    1 EVESALVSHPAVAeAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVA-------------HVREELGPYAVPKEVVFVD 67

                   ....*....
gi 1246793773 1027 RLPRNASGK 1035
Cdd:pfam13193   68 ELPKTRSGK 76
PRK03584 PRK03584
acetoacetate--CoA ligase;
2041-2200 4.08e-04

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 46.33  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2041 AQSLLWQMPAQAVAV----EEGA-ASWTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWlp 2115
Cdd:PRK03584    89 AENLLRHRRDDRPAIifrgEDGPrRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIW-- 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2116 lDPQHPDARQIAVLD------------------------------------DSGARIVI----GWGAAPAWVPASVRWLD 2155
Cdd:PRK03584   167 -SSCSPDFGVQGVLDrfgqiepkvliavdgyryggkafdrrakvaelraalPSLEHVVVvpylGPAAAAAALPGALLWED 245
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1246793773 2156 AesvldVVSAYEEPPR-VDVDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:PRK03584   246 F-----LAPAEAAELEfEPVPFDHPLWILYSSGTTGLPKCIVHGHG 286
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
2078-2426 4.18e-04

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 46.27  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2078 LDAVG------VQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLD----PQHPDaRQIAVLDDSGARIVIGWGAAPAWV 2147
Cdd:PRK12476    78 LRAVGarlqqvAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGHAE-RLDTALRDAEPTVVLTTTAAAEAV 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2148 PASVRWLDAES-----VLDVV--SAYEEPPRVDVDADTPAYLIYTSGSTGTPKGVVVSQGNL-ANYVAGVLPVLDLGEDA 2219
Cdd:PRK12476   157 EGFLRNLPRLRrprviAIDAIpdSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQMILSIDLLDRNT 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2220 SLATLSTVAADLG-----FTALFGA---LLS--------GRRVRLLPAELAFDAQALAAHLQAHPVDCLKIVPSHLAGLL 2283
Cdd:PRK12476   237 HGVSWLPLYHDMGlsmigFPAVYGGhstLMSptafvrrpQRWIKALSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGDDID 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2284 aaaggtavLPRECLVTGGEALTGALVQQVRA------LAPTLrIVNHYGPTETTVGILTC------TV----PEEWPVEQ 2347
Cdd:PRK12476   317 --------LSNVVLIIGSEPVSIDAVTTFNKafapygLPRTA-FKPSYGIAEATLFVATIapdaepSVvyldREQLGAGR 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2348 GVPV--GHPLA------GNEA---W---VLDRFGLPAPVGVAGELYLGGGNLSLGYWQRAEQTAERFV------------ 2401
Cdd:PRK12476   388 AVRVaaDAPNAvahvscGQVArsqWaviVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegsh 467
                          410       420       430
                   ....*....|....*....|....*....|
gi 1246793773 2402 AHPLAPDRLLYRSGDLA-RLDGE----GRI 2426
Cdd:PRK12476   468 ADGAADDGTWLRTGDLGvYLDGElyitGRI 497
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
4028-4082 4.51e-04

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: 41.76  E-value: 4.51e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 4028 ERRLAELWRQLLG--GELPGRGAHFFAR-GGHSLLVVRLAEAIRAEFAIAVPLKSLFE 4082
Cdd:COG0236      7 EERLAEIIAEVLGvdPEEITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFE 64
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
676-1019 5.09e-04

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: 45.81  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  676 LAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdtTLEQILAAwsrGACVVARpde 749
Cdd:cd05940     83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYtclplyHSTALIV--GWSACLAS---GATLVIR--- 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  750 llepQRFLA--FLSE-RAITVTdlAPAYANELVR----ASVADDWRDLALRCLVVGG---DVlpvalaqrWFEL----GL 815
Cdd:cd05940    155 ----KKFSAsnFWDDiRKYQAT--IFQYIGELCRyllnQPPKPTERKHKVRMIFGNGlrpDI--------WEEFkerfGV 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  816 DRRCALinaYGPTEATISS--HYHRVQAIDASRPVplgQLLPGRIAAV----------LDAHGRI--VPRGVCGEL--AL 879
Cdd:cd05940    221 PRIAEF---YAATEGNSGFinFFGKPGAIGRNPSL---LRKVAPLALVkydlesgepiRDAEGRCikVPRGEPGLLisRI 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  880 GGIGLAEGYrGDAAASERRFAPLRLPSGEslRMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV 959
Cdd:cd05940    295 NPLEPFDGY-TDPAATEKKILRDVFKKGD--AWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGV 371
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  960 RAAAagVVGegaaqrlvawVECAGEDG-FGQADLNQTDSDQTESERWHRALCERLPAYMVP 1019
Cdd:cd05940    372 EEAN--VYG----------VQVPGTDGrAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2631-2859 8.12e-04

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: 44.99  E-value: 8.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2631 TPIQHWFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARF-QRDAAGQWQQ-TLGDWQADRFAHREA 2708
Cdd:cd19542      5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQvVLKSLDPPIEEVETD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2709 D---AGQREDLLaQWQAGlsfDGALLRVLALPDPQDGDTRVLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAae 2785
Cdd:cd19542     85 EdslDALTRDLL-DDPTL---FGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFS-- 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246793773 2786 acgfgawqAALRQLSAATLDGWRSYWRAQAADAEAIALPWQDSDNRYADTVHLHDRferdwTERLLTQTARAYG 2859
Cdd:cd19542    159 --------DYISYLQSQSQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTRR-----SLAKLEAFCASLG 219
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
2174-2493 8.16e-04

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 45.53  E-value: 8.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2174 VDADTPAYLIYTSGSTGTPKGVVVSQGNLANYVAGVLPVLDLGEDASLA-TLSTVAADLGFTALFGALLSGRRVRLLPAE 2252
Cdd:PRK05851   149 PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGcSWLPLYHDMGLAFLLTAALAGAPLWLAPTT 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2253 lAFdaqalaahlQAHPVDCLK-IVPSHLAGLLAAAGGTAVLPR-------------ECLVTGGEALTGALVQQ-VRALAP 2317
Cdd:PRK05851   229 -AF---------SASPFRWLSwLSDSRATLTAAPNFAYNLIGKyarrvsdvdlgalRVALNGGEPVDCDGFERfATAMAP 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2318 ----TLRIVNHYGPTETT---------VGILT--CTVPEEWPVEQGVPVGHPLAGNEAWVLDRFGlPAPVGV--AGELYL 2380
Cdd:PRK05851   299 fgfdAGAAAPSYGLAESTcavtvpvpgIGLRVdeVTTDDGSGARRHAVLGNPIPGMEVRISPGDG-AAGVAGreIGEIEI 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2381 GGGNLSLGYWQRAeqtaerfvahPLAPDRLlYRSGDLARLdGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGVEV 2460
Cdd:PRK05851   378 RGASMMSGYLGQA----------PIDPDDW-FPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVRE 445
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1246793773 2461 AAVLALPGANGVLQLGACIQGSLEGVAEALAQR 2493
Cdd:PRK05851   446 GAVVAVGTGEGSARPGLVIAAEFRGPDEAGARS 478
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
844-1062 8.39e-04

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: 45.38  E-value: 8.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  844 ASRPVPLGQL---LPGRIAAVLDAHGRIVPRGVCGELALGGiGLAEGYRGDAAASERRFAPLRLpsGESLRMYRSGDRVR 920
Cdd:cd05967    404 EPLPIKAGSPgkpVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYL--SKFPGYYDTGDAGY 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  921 LLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVraAAAGVVGegaaqrlvawVECA--GEDGFGQADLNQTDS- 997
Cdd:cd05967    481 KDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAV--AECAVVG----------VRDElkGQVPLGLVVLKEGVKi 548
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773  998 DQTESERWHRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRRALPAppvLAQAER-TPPRTAEESA 1062
Cdd:cd05967    549 TAEELEKELVALVrEQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK---IADGEDyTIPSTIEDPS 612
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
665-967 8.92e-04

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 45.19  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  665 NGSGENaaPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVL------HVAGLAVdTTLEQILAaws 738
Cdd:PRK06334   176 GVSDKD--PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMsflppfHAYGFNS-CTLFPLLS--- 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  739 rGACVVARPDElLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRwfELGLDRR 818
Cdd:PRK06334   250 -GVPVVFAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQE--ALKTFPH 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  819 CALINAYGPTEATISSHYHRVQAIDASRPVplGQLLPGRIAAVLDAHGRI-VPRGVCGELALGGIGLAEGYRGdaAASER 897
Cdd:PRK06334   326 IQLRQGYGTTECSPVITINTVNSPKHESCV--GMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLG--EDFGQ 401
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246793773  898 RFAPLrlpSGESlrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQ---LPQVRAAAAGVV 967
Cdd:PRK06334   402 GFVEL---GGET--WYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAGPLVV 469
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1726-1910 9.19e-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: 44.87  E-value: 9.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1726 LVWSIHHLIVDGWSTPLLVGEMLQRYtagaQGATLRLPPAPgfqaYLDWR--ERQDLARQRGWWRERLSGYAGTAALPAP 1803
Cdd:cd19537    110 LLVVMSHIICDLTTLQLLLREVSAAY----NGKLLPPVRRE----YLDSTawSRPASPEDLDFWSEYLSGLPLLNLPRRT 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1804 VAAAHHPVQREeceRRLSAHDSERLRAFCRERGCTLSDL-IAMVwGLANARYGNHDDVVLGATRSGRPPElaGVESMVGV 1882
Cdd:cd19537    182 SSKSYRGTSRV---FQLPGSLYRSLLQFSTSSGITLHQLaLAAV-ALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGL 255
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1246793773 1883 FINTLPLRLR--IDAGQPALDLLSALR--SQS 1910
Cdd:cd19537    256 FLEPLPIRIRfpSSSDASAADFLRAVRrsSQA 287
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
2049-2200 9.41e-04

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: 45.34  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2049 PAQAVAVEEGAAS-WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWL------------- 2114
Cdd:cd05943     85 PAAIYAAEDGERTeVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSscspdfgvpgvld 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2115 ---PLDP--------------QH-------------PDARQIAVLDDSGARIVIGWGAAPAWVpasvrWLDaesvlDVVS 2164
Cdd:cd05943    165 rfgQIEPkvlfavdaytyngkRHdvrekvaelvkglPSLLAVVVVPYTVAAGQPDLSKIAKAL-----TLE-----DFLA 234
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1246793773 2165 AYEEPPR--VDVDADTPAYLIYTSGSTGTPKGVVVSQG 2200
Cdd:cd05943    235 TGAAGELefEPLPFDHPLYILYSSGTTGLPKCIVHGAG 272
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
3811-3927 1.04e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 45.09  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3811 YGITETTVHVSFHRLSDEDLQSptsrIGSAL-PDLAVHVL-----DAAGQPvPLGvvgELVVEGDGVAQGYWQRPELTAE 3884
Cdd:PTZ00342   493 YGLTETTGPIFVQHADDNNTES----IGGPIsPNTKYKVRtwetyKATDTL-PKG---ELLIKSDSIFSGYFLEKEQTKN 564
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1246793773 3885 RFVERGgqrFYRSGDLGRYRADGSLEYRGRGDDQVKL-RGYRIE 3927
Cdd:PTZ00342   565 AFTEDG---YFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
2447-2516 1.23e-03

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: 40.22  E-value: 1.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2447 EVEQVLAQLPGVEVAAVLALPGANG--------VLQLGAciQGSLEGVAEALAQRLPEYLCPSRWRAVESMPRLGNGK 2516
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKgeapvafvVLKPGV--ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
786-984 1.34e-03

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 44.37  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  786 DWRDLALRCLVVGGDVLPVALAQRwfelgLDRR--CALINAYGPTEATIS--------SHYHrvqaidasrpvpLGQLLp 855
Cdd:COG1541    199 DPRDLSLKKGIFGGEPWSEEMRKE-----IEERwgIKAYDIYGLTEVGPGvayeceaqDGLH------------IWEDH- 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  856 gRIAAVLD-AHGRIVPRGVCGELALGGIGlAEGYrgdaaaserrfaPLrlpsgesLRmYRSGDRVRLLDDGE-------- 926
Cdd:COG1541    261 -FLVEIIDpETGEPVPEGEEGELVVTTLT-KEAM------------PL-------IR-YRTGDLTRLLPEPCpcgrthpr 318
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  927 -LQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAAGVV-GEGAAQRLVAWVECAGE 984
Cdd:COG1541    319 iGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVdREGGLDELTVRVELAPG 378
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2746-2812 1.41e-03

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: 44.37  E-value: 1.41e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2746 VLFAAHHLLVDAVSWGIIVDDLQHAYaerragRSPALAAEACGFGAWqaALRQLSAATLDGWRS---YWR 2812
Cdd:cd19532    125 LIFGYHHIAMDGVSFQIFLRDLERAY------NGQPLLPPPLQYLDF--AARQRQDYESGALDEdlaYWK 186
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
2063-2210 1.48e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 44.58  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2063 TYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGA------AWLpldpqHPDARQIAVLDDSGARI 2136
Cdd:PTZ00216   123 TYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMvaatvyANL-----GEDALAYALRETECKAI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2137 V------------IGWGAAPAWV-------PASVrwlDAESV-----LDVVS-----AYEEPPRVDVDADTPAYLIYTSG 2187
Cdd:PTZ00216   198 VcngknvpnllrlMKSGGMPNTTiiyldslPASV---DTEGCrlvawTDVVAkghsaGSHHPLNIPENNDDLALIMYTSG 274
                          170       180
                   ....*....|....*....|...
gi 1246793773 2188 STGTPKGVVVSQGNLAnyvAGVL 2210
Cdd:PTZ00216   275 TTGDPKGVMHTHGSLT---AGIL 294
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
671-696 1.52e-03

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: 44.51  E-value: 1.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 1246793773  671 AAPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd05927    111 PKPEDLATICYTSGTTGNPKGVMLTH 136
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
861-1036 1.69e-03

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: 44.21  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  861 VLDAHGRI-VPR-GVC-GELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQV 937
Cdd:cd12118    323 VLDPETMKpVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAFR-----GG----WFHSGDLAVIHPDGYIEIKDRSKDII 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  938 KLRGYRIELEEIEHCLGQLPQVRAAAagVVG---EGAAQRLVAWVECagEDGfgqadlnqtdSDQTESE--RWHRalcER 1012
Cdd:cd12118    394 ISGGENISSVEVEGVLYKHPAVLEAA--VVArpdEKWGEVPCAFVEL--KEG----------AKVTEEEiiAFCR---EH 456
                          170       180
                   ....*....|....*....|....
gi 1246793773 1013 LPAYMVPTQFVALPrLPRNASGKI 1036
Cdd:cd12118    457 LAGFMVPKTVVFGE-LPKTSTGKI 479
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2629-2785 1.83e-03

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: 43.90  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2629 GLTPIQH--WFFEQALDQPAHWNMSLYLKLPGALDTAAFAAALADVAAAHPMLRARFQRDAAGQWQQTLG---------D 2697
Cdd:cd19533      3 PLTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPytpvpirhiD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2698 WQADRFAHREADAGQREDL---LAQWQAGLsFDGALLRVlalpdpqdGDTRVLFAA--HHLLVDAVSWGIIVDDLQHAYA 2772
Cdd:cd19533     83 LSGDPDPEGAAQQWMQEDLrkpLPLDNDPL-FRHALFTL--------GDNRHFWYQrvHHIVMDGFSFALFGQRVAEIYT 153
                          170
                   ....*....|...
gi 1246793773 2773 ERRAGRSPALAAE 2785
Cdd:cd19533    154 ALLKGRPAPPAPF 166
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
661-1041 2.19e-03

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 43.86  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  661 GAGENGSGENAAPNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDR-------------VLHVAGLAVD 727
Cdd:PRK07059   191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKprpdqlnfvcalpLYHIFALTVC 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  728 TtleqiLAAWSRGACVVARPDellePQRFLAFLSERAITVTDLAPAyANELVRASV-ADDWRDLALRCLVV---GGDVLP 803
Cdd:PRK07059   271 G-----LLGMRTGGRNILIPN----PRDIPGFIKELKKYQVHIFPA-VNTLYNALLnNPDFDKLDFSKLIVangGGMAVQ 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  804 VALAQRWFELgldRRCALINAYGPTEATISSHYHRVQAIDASRPVplGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIG 883
Cdd:PRK07059   341 RPVAERWLEM---TGCPITEGYGLSETSPVATCNPVDATEFSGTI--GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQ 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  884 LAEGY--RGDAAASerrfapLRLPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQV-R 960
Cdd:PRK07059   416 VMAGYwnRPDETAK------VMTADG----FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVlE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  961 AAAAGVVGEGAAQRLVAWVEcagedgfgQADLNQTDSDQteserwhRALC-ERLPAYMVPTQFVALPRLPRNASGKIDRR 1039
Cdd:PRK07059   486 VAAVGVPDEHSGEAVKLFVV--------KKDPALTEEDV-------KAFCkERLTNYKRPKFVEFRTELPKTNVGKILRR 550

                   ..
gi 1246793773 1040 AL 1041
Cdd:PRK07059   551 EL 552
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
2062-2219 2.37e-03

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: 43.95  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQHPDARQIAVLDDSGARIVIG-- 2139
Cdd:cd17641     12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAed 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2140 ----------WGAAPA------WVPASVRWLDAESVLDVVSAYE--------EPPRVD--VDADTP---AYLIYTSGSTG 2190
Cdd:cd17641     92 eeqvdklleiADRIPSvryviyCDPRGMRKYDDPRLISFEDVVAlgraldrrDPGLYEreVAAGKGedvAVLCTTSGTTG 171
                          170       180
                   ....*....|....*....|....*....
gi 1246793773 2191 TPKGVVVSQGNLANYVAGVLPVLDLGEDA 2219
Cdd:cd17641    172 KPKLAMLSHGNFLGHCAAYLAADPLGPGD 200
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
1719-1853 3.26e-03

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 43.16  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 1719 RGGGRYWLVWSIHHLIVDGWSTPLLVGEMLQRYTAGA-QGATLRLPPAPGFQAYldwrerQDLARQRGWWRERLSG---- 1793
Cdd:PRK09294   106 PDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVVtTGDPGPIRPQPAPQSL------EAVLAQRGIRRQALSGaerf 179
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246793773 1794 ----YAGTAALPAPVAAAHHPVQREEC---ERRLSAHDSERLRAFCRERGCTLSDLIAMVWGLANAR 1853
Cdd:PRK09294   180 mpamYAYELPPTPTAAVLAKPGLPQAVpvtRCRLSKAQTSSLAAFGRRHRLTVNALVSAAILLAEWQ 246
PLN02479 PLN02479
acetate-CoA ligase
875-1043 3.68e-03

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 43.29  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  875 GELALGGIGLAEGYRGDAAASERRFAplrlpSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLG 954
Cdd:PLN02479   403 GEIVMRGNMVMKGYLKNPKANEEAFA-----NG----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  955 QLPQVRAAAagVVGEGAAQrlvaWVE--CAG---EDGFGQADLNQTDSDQTESERwhralcERLPAYMVPTQFVALPrLP 1029
Cdd:PLN02479   474 THPAVLEAS--VVARPDER----WGEspCAFvtlKPGVDKSDEAALAEDIMKFCR------ERLPAYWVPKSVVFGP-LP 540
                          170
                   ....*....|....
gi 1246793773 1030 RNASGKIDRRALPA 1043
Cdd:PLN02479   541 KTATGKIQKHVLRA 554
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
672-696 4.14e-03

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 43.18  E-value: 4.14e-03
                           10        20
                   ....*....|....*....|....*
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:PLN02387   248 SPNDIAVIMYTSGSTGLPKGVMMTH 272
prpE PRK10524
propionyl-CoA synthetase; Provisional
2321-2531 4.27e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 43.01  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2321 IVNHYGPTETTVGILT-CTVPEEWPVEQGVPvGHPLAGNEAWVLDRF-GLPAPVGVAGELYLGGgNLSLGYWQRAEQTAE 2398
Cdd:PRK10524   383 VIDNYWQTETGWPILAiARGVEDRPTRLGSP-GVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG-PLPPGCMQTVWGDDD 460
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2399 RFV-AHPLAPDRLLYRSGDLARLDGEGRIVYLGRGDHQVKIRGYRVELGEVEQVLAQLPGV-EVAAV---LALPG----A 2469
Cdd:PRK10524   461 RFVkTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVaEVAVVgvkDALKGqvavA 540
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246793773 2470 NGVLQLGACIQG-----SLEG-VAEALAQRLPEYLCPSRWRAVESMPRLGNGKIDRQALADLLQQDDA 2531
Cdd:PRK10524   541 FVVPKDSDSLADrearlALEKeIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDP 608
PRK07470 PRK07470
acyl-CoA synthetase; Validated
529-1041 4.62e-03

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 43.11  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  529 PAPRTVGNVVDAIARAADEFPERAALETAQGRLSYRELLTAADARAAALRRRLGAQARSVALCLPRGLDWYCLLLGAWRA 608
Cdd:PRK07470     1 PMSRRVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  609 GLSVIPLDTEWPQARRAEVVAASGCDAVLTDAQ---------------------GLAGFAPSVAIAVDElKLDGAGENGS 667
Cdd:PRK07470    81 GAVWVPTNFRQTPDEVAYLAEASGARAMICHADfpehaaavraaspdlthvvaiGGARAGLDYEALVAR-HLGARVANAA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  668 GENAAPnqlAYILYTSGSTGIPKGVEVGHAALA--AHIDAAAEALALSADDRVLHVAGLAVDTTLEQiLAAWSRGACVVA 745
Cdd:PRK07470   160 VDHDDP---CWFFFTSGTTGRPKAAVLTHGQMAfvITNHLADLMPGTTEQDASLVVAPLSHGAGIHQ-LCQVARGAATVL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  746 RPDELLEPQRFLAFLSERAITVTDLAPAYANELVRASVADDWRDLALRCLVVGGDVLPVALAQRWFE-LGLdrrcALINA 824
Cdd:PRK07470   236 LPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAkLGK----VLVQY 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  825 YGPTEAT-----ISSHYHRVQAIDASRPVPLGQLLPGRIAAVLDAHGRIVPRGVCGELALGGIGLAEGYRGDAAASERRF 899
Cdd:PRK07470   312 FGLGEVTgnitvLPPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  900 aplrlpsgeslR--MYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-----GVVGEgaa 972
Cdd:PRK07470   392 -----------RdgWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlgvpdPVWGE--- 457
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246793773  973 qrlVAWVECAGEDGfgqadlnqTDSDQTESERWhraLCERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK07470   458 ---VGVAVCVARDG--------APVDEAELLAW---LDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
604-1041 4.92e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 42.76  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  604 GAWRAGLSVIPLDTEWPQARRAEVVAASGCDAVLTD------AQGLAGFAPSVAIavdELKLDGAGENGSGENAAPNQLA 677
Cdd:PRK13391    68 AAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSaakldvARALLKQCPGVRH---RLVLDGDGELEGFVGYAEAVAG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  678 Y-------------ILYTSGSTGIPKGV-----EVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSR 739
Cdd:PRK13391   145 LpatpiadeslgtdMLYSSGTTGRPKGIkrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRL 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  740 GACVVARpdELLEPQRFLAFLSERAITVTDLAPAYANELVR--ASVADDWRDLALRCLVVGGDVLPVALAQrwfelgldr 817
Cdd:PRK13391   225 GGTVIVM--EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKE--------- 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  818 rcALINAYGPT--EATISSHYHRVQAIDA----SRPVPLGQLLPGRIaAVLDAHGRIVPRGVCGELALGGiGLAEGYRGD 891
Cdd:PRK13391   294 --QMIDWWGPIihEYYAATEGLGFTACDSeewlAHPGTVGRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLND 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  892 AAaserRFAPLRLPSGEslrMYRSGDRVRLLDDGELQFLGRADFQVKLRGYRIELEEIEHCLGQLPQVRAAAA-GVVGEG 970
Cdd:PRK13391   370 PA----KTAEARHPDGT---WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfGVPNED 442
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246793773  971 AAQRLVAWVECAgEDGFGQADLNQtdsdqtESERWHRalcERLPAYMVPTQFVALPRLPRNASGKIDRRAL 1041
Cdd:PRK13391   443 LGEEVKAVVQPV-DGVDPGPALAA------ELIAFCR---QRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
2062-2198 5.29e-03

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 42.77  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2062 WTYAQLRAAAGRIAGALDAVGVQPGAHVALCLPRTFAQLAAMAAVWHRGAAWLPLDPQ-HPDarQIA-VLDDSGARIVI- 2138
Cdd:PRK07008    40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRlFPE--QIAyIVNHAEDRYVLf 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2139 -------------------GWGAA--PAWVPASV-------RWLDAESvldvvSAYEEPPrvdVDADTPAYLIYTSGSTG 2190
Cdd:PRK07008   118 dltflplvdalapqcpnvkGWVAMtdAAHLPAGStpllcyeTLVGAQD-----GDYDWPR---FDENQASSLCYTSGTTG 189

                   ....*...
gi 1246793773 2191 TPKGVVVS 2198
Cdd:PRK07008   190 NPKGALYS 197
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
672-1024 6.50e-03

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: 42.46  E-value: 6.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  672 APNQLAYILYTSGSTGIPKGVEVGHAALAAHIDAAAEALALSADDRVLHVAGLAVDTTLEQILAAWSRGACVVARPDEL- 750
Cdd:cd05932    135 FPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLd 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  751 -----LEPQRFLAFLS-ERAIT-----VTDLAPA----------YANELVRASVADDWRDLALRCLVVGGDVLPVALAQR 809
Cdd:cd05932    215 tfvedVQRARPTLFFSvPRLWTkfqqgVQDKIPQqklnlllkipVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEW 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  810 WFELGLDrrcaLINAYGPTEATISSHYHRVqaiDASRPVPLGQLLPGriaavldAHGRIVPRgvcGELALGGIGLAEGYR 889
Cdd:cd05932    295 YRSLGLN----ILEAYGMTENFAYSHLNYP---GRDKIGTVGNAGPG-------VEVRISED---GEILVRSPALMMGYY 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773  890 GDAAASERRFAplrlPSGeslrMYRSGDRVRLLDDGELQFLGRADFQVKL-RGYRIELEEIEHCLGQLPQVRAAAagVVG 968
Cdd:cd05932    358 KDPEATAEAFT----ADG----FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVC--VIG 427
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246793773  969 EGAAQRLVAWVecAGEDGFGQADlnqtDSDQTESERWHRALCERLPAYMVPTQFVA 1024
Cdd:cd05932    428 SGLPAPLALVV--LSEEARLRAD----AFARAELEASLRAHLARVNSTLDSHEQLA 477
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2666-3180 6.90e-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: 42.55  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2666 AAALADVAAAHPMLRARFQRDAAGQWQQTLGDWQADRFAHREADAGQREDLLAQWQAGLSFDGALLRVLALPDPQDGDTR 2745
Cdd:COG3321    869 QREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2746 VLFAAHHLLVDAVSWGIIVDDLQHAYAERRAGRSPALAAEACGFGAWQAALRQLSAATLDGWRSywRAQAADAEAIALPW 2825
Cdd:COG3321    949 AAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLL--AAAAAAAALLALAA 1026
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2826 QDSDNRYADTVHLHDRFERDWTERLLTQTARAYGNEPQEVLLTALALALRDGGDAATLWVEMEGHGRDDLGAGLDLSRTV 2905
Cdd:COG3321   1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2906 GWFTARYPLALHLPAGEDLGAALRSTKDRMRAVPDRGLGFGVLRYLHGELAELPVPQVCFNYLGQLRAGERDGWALCEEP 2985
Cdd:COG3321   1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 2986 DGGGRAGGNRRRHLLDVNAMLVDGELRLDWAWPQDAASREAMQALSRRYLAVLRELIACVQTAEPRPTLADLPLAGLDNA 3065
Cdd:COG3321   1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLA 1266
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246793773 3066 PLDALLSQHPQTQDVYPLAPLQEGLLFHSLLNAEADPYINQTTVALHGALDREAFAAAWQQALERHPILRSGFAVQGLPS 3145
Cdd:COG3321   1267 AAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAA 1346
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1246793773 3146 PRQLPHRQVSLPLAEQDWSGLEPAQARSRLSELQA 3180
Cdd:COG3321   1347 AAAAAAAAAAAAAAAALAAAAGAAAAAAALALAAL 1381
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
670-696 7.94e-03

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: 42.20  E-value: 7.94e-03
                           10        20
                   ....*....|....*....|....*..
gi 1246793773  670 NAAPNQLAYILYTSGSTGIPKGVEVGH 696
Cdd:cd17639     84 DGKPDDLACIMYTSGSTGNPKGVMLTH 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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