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Conserved domains on  [gi|499404635|ref|WP_011092102|]
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non-ribosomal peptide synthetase [Pectobacterium atrosepticum]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 15736293)

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

EC:  1.14.-.-
Gene Ontology:  GO:0019184|GO:0031177|GO:0016874
PubMed:  29444491|26429504|20153164|28526268|26604034

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12316 super family cl36106
peptide synthase; Provisional
 73-1981 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12316:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1158.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvNEQGKGEQRIDAYQPFVIQHD 152
Cdd:PRK12316   51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFP-RGADDSLAQVPLDRPLEVEFE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:PRK12316  130 DCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PYPVETTQLNYIDYAHWfnSDSFLDYHNEFK--PFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKR 310
Cdd:PRK12316  210 EPGLPALPIQYADYALW--QRSWLEAGEQERqlEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  311 LCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLS 390
Cdd:PRK12316  288 TARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLG 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  391 AFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ---AKVDFNDLIPGCDAAEETSPVLPAKTDISVKVTELMGEVRLD 467
Cdd:PRK12316  368 AQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQplvADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAA 447

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  468 WLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQpQLTVTDVIEAVAQRDPQ 547
Cdd:PRK12316  448 LTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPL-QRGVHRLFEEQVERTPE 526

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  548 QLAIAFdGEprtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRH 627
Cdd:PRK12316  527 APALAF-GE---ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAY 602

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  628 IITDANLSVILG--GDGQQLAQWSAEQRIDLTDPAVveqWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:PRK12316  603 MLEDSGVQLLLSqsHLGRKLPLAAGVQVLDLDRPAA---WLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA 679

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEQAGATHLIlPTALM 778
Cdd:PRK12316  680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrdpaklvELINREGVDTLHFV-PSMLQ 758

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  779 SIL---DPEQVNGIQAIGMGGEACPNAVVENWADKV---ALYNMYGPTECT--VTALSTRLRKGQPVTIGKPLIHIQALI 850
Cdd:PRK12316  759 AFLqdeDVASCTSLRRIVCSGEALPADAQEQVFAKLpqaGLYNLYGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYI 838

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndVNNAGQGAatlRIYRTGDKARLLNNGDYEYCGRID 930
Cdd:PRK12316  839 LDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFV------PSPFVAGE---RMYRTGDLARYRADGVIEYAGRID 909

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  931 EQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAqvgSRPALVAYaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLL 1010
Cdd:PRK12316  910 HQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV---DGKQLVGY-VVLESEGGDWREALKAHLAASLPEYMVPAQWLAL 984

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1011 EDMPLTPNGKLDMKQLPPVLEANESDGEA--DNPLEADVLAIWRSVLNT-PLGVEDDFFRLGGDSILSIQLTTRLRSAGY 1087
Cdd:PRK12316  985 ERLPLTPNGKLDRKALPAPEASVAQQGYVapRNALERTLAAIWQDVLGVeRVGLDDNFFELGGDSIVSIQVVSRARQAGI 1064

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1088 ACTVKDVFEAKSVRRLCRVLaqnNRDTGTVAEQGTLEGEFALLPIQRWFMEQSLARPEHWNQAAMIQLPE-VDTERLVTM 1166
Cdd:PRK12316 1065 QLSPRDLFQHQTIRSLALVA---KAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQpLDPDRLGRA 1141

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1167 LQALMAQHDALRLGCD--AEGQRYLADVPCpALSTLDYRQLGDDG-LQQAFTALQSEFDPAQGRTMACALVrHHPQADTA 1243
Cdd:PRK12316 1142 LERLVAHHDALRLRFReeDGGWQQAYAAPQ-AGEVLWQRQAASEEeLLALCEEAQRSLDLEQGPLLRALLV-DMADGSQR 1219

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1244 LFLAFHHLVIDAVSWRILVDDLERLY--LGEPLLPKTSSYRQWGAALQHYATQHAEQLTYWQAQEDGVDLTalLAAKDPQ 1321
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYadLDADLPARTSSYQAWARRLHEHAGARAEELDYWQAQLEDAPHE--LPCENPD 1297

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1322 G-----HASAAILTLDAKTTGQLVSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIDPTLDVSRTVGW 1396
Cdd:PRK12316 1298 GalenrHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGW 1377

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1397 FTSTYPVCLQDKPDWASLIQSSKEQLRQVPDKGVGFNPLRYHHPQGNSLTLSP-----IVFNYLGL---SVQAAGTWRPV 1468
Cdd:PRK12316 1378 FTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAAlpqprITFNYLGQfdrQFDEAALFVPA 1457

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1469 DVAPGCCVSPGNKPAEVISLHGGITGGQLTL-----RQVgcLNQRDSERLMTRLTENLRALTEACLTQLSHGVvfTPSDF 1543
Cdd:PRK12316 1458 TESAGAAQDPCAPLANWLSIEGQVYGGELSLhwsfsREM--FAEATVQRLADDYARELQALIEHCCDERNRGV--TPSDF 1533

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1544 PAVNLSQTQLDSLSQRYD-IDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHvLDVEGYRQAWQRQIQRFPALRAA 1622
Cdd:PRK12316 1534 PLAGLSQAQLDALPLPAGeIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSG 1612

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1623 ---LESECASIQVIVKQADLPFYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVI 1699
Cdd:PRK12316 1613 flwQDGLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILM 1692

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1700 DGWSGPQLLGAVHRDYQtlmqgqvlmhGDAPAIQVDRaYVDYARHAVAQ-QSAVDAFWQQRQSLLAQTNDVSMLFAAAGK 1778
Cdd:PRK12316 1693 DGWSNAQLLGEVLQRYA----------GQPVAAPGGR-YRDYIAWLQRQdAAASEAFWKEQLAALEEPTRLAQAARTEDG 1761

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1779 RADLSQHLTQIEPQVTsvslnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSV 1858
Cdd:PRK12316 1762 QVGYGDHQQLLDPAQT---------RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQI 1832

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1859 GLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHATQSL--IALTAGR--SRLFNSLFIYENYPDAKA-EQGQraddP 1933
Cdd:PRK12316 1833 GLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLydIQRWAGQggEALFDSLLVFENYPVAEAlKQGA----P 1908

                        1930      1940      1950      1960
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635 1934 HRLYPEFSAAYEKVEMPLNLVVrEQSGCMLLRFEFDADALDSAQARRV 1981
Cdd:PRK12316 1909 AGLVFGRVSNHEQTNYPLTLAV-TLGETLSLQYSYDRGHFDAAAIERL 1955
TubC_N super family cl39883
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ...
 4-54 1.28e-05

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: 44.43  E-value: 1.28e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 499404635     4 IVTLLKQLERQGVRLALNaQGQLISQSNKEAITAEIGRTIKENKDAIVRCL 54
Cdd:pfam18563    1 IVELLAELYALGIKLWLE-GGRLRFRAPKGVLTPELREKLKERKAEIIAFL 50
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2033-2098 2.53e-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: 43.71  E-value: 2.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  2033 QTLLRAWAQTLHLGEPGLGESDlwsrTLCESGVDSLQRIALAQALSRTLAHPVSVALLQHYPSPQA 2098
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
 73-1981 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1158.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvNEQGKGEQRIDAYQPFVIQHD 152
Cdd:PRK12316   51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFP-RGADDSLAQVPLDRPLEVEFE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:PRK12316  130 DCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PYPVETTQLNYIDYAHWfnSDSFLDYHNEFK--PFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKR 310
Cdd:PRK12316  210 EPGLPALPIQYADYALW--QRSWLEAGEQERqlEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  311 LCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLS 390
Cdd:PRK12316  288 TARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLG 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  391 AFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ---AKVDFNDLIPGCDAAEETSPVLPAKTDISVKVTELMGEVRLD 467
Cdd:PRK12316  368 AQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQplvADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAA 447

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  468 WLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQpQLTVTDVIEAVAQRDPQ 547
Cdd:PRK12316  448 LTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPL-QRGVHRLFEEQVERTPE 526

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  548 QLAIAFdGEprtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRH 627
Cdd:PRK12316  527 APALAF-GE---ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAY 602

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  628 IITDANLSVILG--GDGQQLAQWSAEQRIDLTDPAVveqWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:PRK12316  603 MLEDSGVQLLLSqsHLGRKLPLAAGVQVLDLDRPAA---WLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA 679

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEQAGATHLIlPTALM 778
Cdd:PRK12316  680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrdpaklvELINREGVDTLHFV-PSMLQ 758

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  779 SIL---DPEQVNGIQAIGMGGEACPNAVVENWADKV---ALYNMYGPTECT--VTALSTRLRKGQPVTIGKPLIHIQALI 850
Cdd:PRK12316  759 AFLqdeDVASCTSLRRIVCSGEALPADAQEQVFAKLpqaGLYNLYGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYI 838

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndVNNAGQGAatlRIYRTGDKARLLNNGDYEYCGRID 930
Cdd:PRK12316  839 LDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFV------PSPFVAGE---RMYRTGDLARYRADGVIEYAGRID 909

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  931 EQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAqvgSRPALVAYaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLL 1010
Cdd:PRK12316  910 HQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV---DGKQLVGY-VVLESEGGDWREALKAHLAASLPEYMVPAQWLAL 984

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1011 EDMPLTPNGKLDMKQLPPVLEANESDGEA--DNPLEADVLAIWRSVLNT-PLGVEDDFFRLGGDSILSIQLTTRLRSAGY 1087
Cdd:PRK12316  985 ERLPLTPNGKLDRKALPAPEASVAQQGYVapRNALERTLAAIWQDVLGVeRVGLDDNFFELGGDSIVSIQVVSRARQAGI 1064

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1088 ACTVKDVFEAKSVRRLCRVLaqnNRDTGTVAEQGTLEGEFALLPIQRWFMEQSLARPEHWNQAAMIQLPE-VDTERLVTM 1166
Cdd:PRK12316 1065 QLSPRDLFQHQTIRSLALVA---KAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQpLDPDRLGRA 1141

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1167 LQALMAQHDALRLGCD--AEGQRYLADVPCpALSTLDYRQLGDDG-LQQAFTALQSEFDPAQGRTMACALVrHHPQADTA 1243
Cdd:PRK12316 1142 LERLVAHHDALRLRFReeDGGWQQAYAAPQ-AGEVLWQRQAASEEeLLALCEEAQRSLDLEQGPLLRALLV-DMADGSQR 1219

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1244 LFLAFHHLVIDAVSWRILVDDLERLY--LGEPLLPKTSSYRQWGAALQHYATQHAEQLTYWQAQEDGVDLTalLAAKDPQ 1321
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYadLDADLPARTSSYQAWARRLHEHAGARAEELDYWQAQLEDAPHE--LPCENPD 1297

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1322 G-----HASAAILTLDAKTTGQLVSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIDPTLDVSRTVGW 1396
Cdd:PRK12316 1298 GalenrHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGW 1377

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1397 FTSTYPVCLQDKPDWASLIQSSKEQLRQVPDKGVGFNPLRYHHPQGNSLTLSP-----IVFNYLGL---SVQAAGTWRPV 1468
Cdd:PRK12316 1378 FTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAAlpqprITFNYLGQfdrQFDEAALFVPA 1457

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1469 DVAPGCCVSPGNKPAEVISLHGGITGGQLTL-----RQVgcLNQRDSERLMTRLTENLRALTEACLTQLSHGVvfTPSDF 1543
Cdd:PRK12316 1458 TESAGAAQDPCAPLANWLSIEGQVYGGELSLhwsfsREM--FAEATVQRLADDYARELQALIEHCCDERNRGV--TPSDF 1533

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1544 PAVNLSQTQLDSLSQRYD-IDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHvLDVEGYRQAWQRQIQRFPALRAA 1622
Cdd:PRK12316 1534 PLAGLSQAQLDALPLPAGeIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSG 1612

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1623 ---LESECASIQVIVKQADLPFYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVI 1699
Cdd:PRK12316 1613 flwQDGLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILM 1692

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1700 DGWSGPQLLGAVHRDYQtlmqgqvlmhGDAPAIQVDRaYVDYARHAVAQ-QSAVDAFWQQRQSLLAQTNDVSMLFAAAGK 1778
Cdd:PRK12316 1693 DGWSNAQLLGEVLQRYA----------GQPVAAPGGR-YRDYIAWLQRQdAAASEAFWKEQLAALEEPTRLAQAARTEDG 1761

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1779 RADLSQHLTQIEPQVTsvslnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSV 1858
Cdd:PRK12316 1762 QVGYGDHQQLLDPAQT---------RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQI 1832

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1859 GLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHATQSL--IALTAGR--SRLFNSLFIYENYPDAKA-EQGQraddP 1933
Cdd:PRK12316 1833 GLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLydIQRWAGQggEALFDSLLVFENYPVAEAlKQGA----P 1908

                        1930      1940      1950      1960
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635 1934 HRLYPEFSAAYEKVEMPLNLVVrEQSGCMLLRFEFDADALDSAQARRV 1981
Cdd:PRK12316 1909 AGLVFGRVSNHEQTNYPLTLAV-TLGETLSLQYSYDRGHFDAAAIERL 1955
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 55-1333 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: 806.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   55 TAQQAFERPITPQNATSGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVnEQ 134
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT-RA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  135 GKGEQRIDAYQPFVIQHDDFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSV 214
Cdd:COG1020    80 GRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  215 KNLFADFKPAFLACQNCQPYPVETTQLNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGE 294
Cdd:COG1020   160 GLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  295 VIFSAINNDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDS 374
Cdd:COG1020   240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGD 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  375 QNFVDYLQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQaKVDFNDL-IPGCDAAEETSPVLPAKTDI 453
Cdd:COG1020   320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQ-NAPADELeLPGLTLEPLELDSGTAKFDL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  454 SVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQPQlT 533
Cdd:COG1020   399 TLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADA-T 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  534 VTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAY 613
Cdd:COG1020   478 LHELFEAQAARTPDAVAVVFGDQ----SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  614 VPLDPDYPPERLRHIITDANLSVILGGDG--QQLAQWSAeQRIDLTDPAVVEQwqdlpGDQPPAIPRHAQQLAQVIYTSG 691
Cdd:COG1020   554 VPLDPAYPAERLAYMLEDAGARLVLTQSAlaARLPELGV-PVLALDALALAAE-----PATNPPVPVTPDDLAYVIYTSG 627

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  692 STGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA-----EQA 766
Cdd:COG1020   628 STGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAAlaellARH 707

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  767 GATHLILPTALMSIL---DPEQVNGIQAIGMGGEACPNAVVENWADK---VALYNMYGPTECTVTALSTRLRKGQ----P 836
Cdd:COG1020   708 RVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWRARlpgARLVNLYGPTETTVDSTYYEVTPPDadggS 787

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  837 VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehITlNDVNNAGQgaatlRIYRTGDKAR 916
Cdd:COG1020   788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERF--VA-DPFGFPGA-----RLYRTGDLAR 859

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  917 LLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAK 996
Cdd:COG1020   860 WLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQ-HPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALAL 938

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  997 YLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEANESDGEADNPLEADVLA--IWRSVLNTPLGVEDDFFRLGGDSIL 1074
Cdd:COG1020   939 LLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAalALLLLLVVVVGDDDFFFFGGGLGLL 1018

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1075 SIQLTTRLRSAGYACTVKDVF-------EAKSVRRLCRVLAQNNRDTGTVAEQGTLEGEFALLPIQRWFMEQSLARPEHW 1147
Cdd:COG1020  1019 LLLALARAARLLLLLLLLLLLflaaaaaAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLAL 1098

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1148 NQAAMIQLPEVDTERLVTMLQALMAQHDALRLGCDAEGQRYLADVPCPALSTLDYRQLGDDGLQQAFTALQSEFDPAQGR 1227
Cdd:COG1020  1099 LLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLA 1178

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1228 TMACALVRHHPQADTALFLAFHHLVIDAVSWRILVDDLERLYLGEPLLPKTSSYRQWGAALQHYATQHAEQLTYWQAQED 1307
Cdd:COG1020  1179 LLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAA 1258

                        1290      1300
                  ....*....|....*....|....*.
gi 499404635 1308 GVDLTALLAAKDPQGHASAAILTLDA 1333
Cdd:COG1020  1259 LLALALALLALALLLLALALLLPALA 1284
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 546-1026 7.83e-150

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: 471.63  E-value: 7.83e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd05930     1 PDAVAVVDGDQ----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd05930    77 AYILEDSGAKLVL------------------TDP---------------------DDLAYVIYTSGSTGKPKGVMVEHRG 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA-----EQAGATHLILPTALMSI 780
Cdd:cd05930   118 LVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEAladllAEEGITVLHLTPSLLRL 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  781 L----DPEQVNGIQAIGMGGEACPNAVVENWAD---KVALYNMYGPTECTVTALSTRLRKG----QPVTIGKPLIHIQAL 849
Cdd:cd05930   198 LlqelELAALPSLRLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDdeedGRVPIGRPIPNTRVY 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  850 ILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDVNNAGQgaatlRIYRTGDKARLLNNGDYEYCGRI 929
Cdd:cd05930   278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERF----VPNPFGPGE-----RMYRTGDLVRWLPDGNLEFLGRI 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  930 DEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGS-RPALVAYATVKADsSTPEPAAVLIDVAKYLPEYMVPFRLM 1008
Cdd:cd05930   349 DDQVKIRGYRIELGEIEAALLA-HPGVREAAVVAREDGDgEKRLVAYVVPDEG-GELDEEELRAHLAERLPDYMVPSAFV 426

                         490
                  ....*....|....*...
gi 499404635 1009 LLEDMPLTPNGKLDMKQL 1026
Cdd:cd05930   427 VLDALPLTPNGKVDRKAL 444
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 563-961 3.23e-129

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: 412.04  E-value: 3.23e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   563 TYAELNRQANQLAHWLH-RQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD 641
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   642 GQQLAQWSAEQRIDLTDPAVVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   722 QSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQAEQA------GATHLILPTALMSILDPEQVNGIQAIGM- 794
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaliaehPVTVLNLTPSLLALLAAALPPALASLRLv 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   795 --GGEACPNAVVENWADK---VALYNMYGPTECTVTALSTRL-----RKGQPVTIGKPLIHIQALILDTAGQLCPVGVPG 864
Cdd:TIGR01733  241 ilGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVdpddaPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   865 ELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAATLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGE 944
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERF-------VPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*..
gi 499404635   945 IEAQLAAvCPSLKQIKV 961
Cdd:TIGR01733  394 IEAALLR-HPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
538-936 5.15e-92

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 305.78  E-value: 5.15e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   538 IEAVAQRDPQQLAIAFDGeprTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:pfam00501    1 LERQAARTPDKTALEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   618 PDYPPERLRHIITDANLSVILGGDGQQLAQ----WSAEQRIDLT---DPAVVEQWQDLPGD-------QPPAIPRHAQQL 683
Cdd:pfam00501   78 PRLPAEELAYILEDSGAKVLITDDALKLEElleaLGKLEVVKLVlvlDRDPVLKEEPLPEEakpadvpPPPPPPPDPDDL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   684 AQVIYTSGSTGLPKGVMIEHGSLINLLDDH----RDRIDFTPQSTMFNCMSLSFDAG-NMTTLLPLSSGGTLAFGEPNDR 758
Cdd:pfam00501  158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   759 AIMQA-----EQAGATHLIL-PTALMSILD-----PEQVNGIQAIGMGGEACPNAVVENWADKV--ALYNMYGPTECTVT 825
Cdd:pfam00501  238 LDPAAlleliERYKVTVLYGvPTLLNMLLEagapkRALLSSLRLVLSGGAPLPPELARRFRELFggALVNGYGLTETTGV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   826 ALSTRLRKGQPV---TIGKPLIHIQALILDTA-GQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnagq 901
Cdd:pfam00501  318 VTTPLPLDEDLRslgSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD------------ 385

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 499404635   902 gaaTLRIYRTGDKARLLNNGDYEYCGRIDEQIKLR 936
Cdd:pfam00501  386 ---EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
TubC_N pfam18563
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ...
 4-54 1.28e-05

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: 44.43  E-value: 1.28e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 499404635     4 IVTLLKQLERQGVRLALNaQGQLISQSNKEAITAEIGRTIKENKDAIVRCL 54
Cdd:pfam18563    1 IVELLAELYALGIKLWLE-GGRLRFRAPKGVLTPELREKLKERKAEIIAFL 50
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2033-2098 2.53e-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: 43.71  E-value: 2.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  2033 QTLLRAWAQTLHLGEPGLGESDlwsrTLCESGVDSLQRIALAQALSRTLAHPVSVALLQHYPSPQA 2098
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2035-2105 4.25e-05

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.78  E-value: 4.25e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404635   2035 LLRAWAQTLHLGEPGLGESDlwsRTLCESGVDSLQRIALAQALSRTLAHPVSVALLQHYPSPQALSGHLAQ 2105
Cdd:smart00823   17 VREQVAAVLGHAAAEAIDPD---RPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1035-1109 1.56e-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: 42.24  E-value: 1.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   1035 SDGEADNPLEADVLAIWRSVLNTP----LGVEDDFFRLGGDSILSIQLTTRLRSA-GYACTVKDVFEAKSVRRLCRVLAQ 1109
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHAaaeaIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAA 84
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
 73-1981 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1158.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvNEQGKGEQRIDAYQPFVIQHD 152
Cdd:PRK12316   51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFP-RGADDSLAQVPLDRPLEVEFE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:PRK12316  130 DCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PYPVETTQLNYIDYAHWfnSDSFLDYHNEFK--PFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKR 310
Cdd:PRK12316  210 EPGLPALPIQYADYALW--QRSWLEAGEQERqlEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  311 LCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLS 390
Cdd:PRK12316  288 TARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLG 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  391 AFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ---AKVDFNDLIPGCDAAEETSPVLPAKTDISVKVTELMGEVRLD 467
Cdd:PRK12316  368 AQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQplvADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAA 447

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  468 WLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQpQLTVTDVIEAVAQRDPQ 547
Cdd:PRK12316  448 LTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPL-QRGVHRLFEEQVERTPE 526

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  548 QLAIAFdGEprtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRH 627
Cdd:PRK12316  527 APALAF-GE---ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAY 602

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  628 IITDANLSVILG--GDGQQLAQWSAEQRIDLTDPAVveqWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:PRK12316  603 MLEDSGVQLLLSqsHLGRKLPLAAGVQVLDLDRPAA---WLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA 679

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEQAGATHLIlPTALM 778
Cdd:PRK12316  680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrdpaklvELINREGVDTLHFV-PSMLQ 758

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  779 SIL---DPEQVNGIQAIGMGGEACPNAVVENWADKV---ALYNMYGPTECT--VTALSTRLRKGQPVTIGKPLIHIQALI 850
Cdd:PRK12316  759 AFLqdeDVASCTSLRRIVCSGEALPADAQEQVFAKLpqaGLYNLYGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYI 838

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndVNNAGQGAatlRIYRTGDKARLLNNGDYEYCGRID 930
Cdd:PRK12316  839 LDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFV------PSPFVAGE---RMYRTGDLARYRADGVIEYAGRID 909

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  931 EQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAqvgSRPALVAYaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLL 1010
Cdd:PRK12316  910 HQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV---DGKQLVGY-VVLESEGGDWREALKAHLAASLPEYMVPAQWLAL 984

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1011 EDMPLTPNGKLDMKQLPPVLEANESDGEA--DNPLEADVLAIWRSVLNT-PLGVEDDFFRLGGDSILSIQLTTRLRSAGY 1087
Cdd:PRK12316  985 ERLPLTPNGKLDRKALPAPEASVAQQGYVapRNALERTLAAIWQDVLGVeRVGLDDNFFELGGDSIVSIQVVSRARQAGI 1064

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1088 ACTVKDVFEAKSVRRLCRVLaqnNRDTGTVAEQGTLEGEFALLPIQRWFMEQSLARPEHWNQAAMIQLPE-VDTERLVTM 1166
Cdd:PRK12316 1065 QLSPRDLFQHQTIRSLALVA---KAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQpLDPDRLGRA 1141

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1167 LQALMAQHDALRLGCD--AEGQRYLADVPCpALSTLDYRQLGDDG-LQQAFTALQSEFDPAQGRTMACALVrHHPQADTA 1243
Cdd:PRK12316 1142 LERLVAHHDALRLRFReeDGGWQQAYAAPQ-AGEVLWQRQAASEEeLLALCEEAQRSLDLEQGPLLRALLV-DMADGSQR 1219

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1244 LFLAFHHLVIDAVSWRILVDDLERLY--LGEPLLPKTSSYRQWGAALQHYATQHAEQLTYWQAQEDGVDLTalLAAKDPQ 1321
Cdd:PRK12316 1220 LLLVIHHLVVDGVSWRILLEDLQRAYadLDADLPARTSSYQAWARRLHEHAGARAEELDYWQAQLEDAPHE--LPCENPD 1297

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1322 G-----HASAAILTLDAKTTGQLVSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIDPTLDVSRTVGW 1396
Cdd:PRK12316 1298 GalenrHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDLSRTVGW 1377

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1397 FTSTYPVCLQDKPDWASLIQSSKEQLRQVPDKGVGFNPLRYHHPQGNSLTLSP-----IVFNYLGL---SVQAAGTWRPV 1468
Cdd:PRK12316 1378 FTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAAlpqprITFNYLGQfdrQFDEAALFVPA 1457

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1469 DVAPGCCVSPGNKPAEVISLHGGITGGQLTL-----RQVgcLNQRDSERLMTRLTENLRALTEACLTQLSHGVvfTPSDF 1543
Cdd:PRK12316 1458 TESAGAAQDPCAPLANWLSIEGQVYGGELSLhwsfsREM--FAEATVQRLADDYARELQALIEHCCDERNRGV--TPSDF 1533

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1544 PAVNLSQTQLDSLSQRYD-IDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHvLDVEGYRQAWQRQIQRFPALRAA 1622
Cdd:PRK12316 1534 PLAGLSQAQLDALPLPAGeIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSG 1612

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1623 ---LESECASIQVIVKQADLPFYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVI 1699
Cdd:PRK12316 1613 flwQDGLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILM 1692

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1700 DGWSGPQLLGAVHRDYQtlmqgqvlmhGDAPAIQVDRaYVDYARHAVAQ-QSAVDAFWQQRQSLLAQTNDVSMLFAAAGK 1778
Cdd:PRK12316 1693 DGWSNAQLLGEVLQRYA----------GQPVAAPGGR-YRDYIAWLQRQdAAASEAFWKEQLAALEEPTRLAQAARTEDG 1761

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1779 RADLSQHLTQIEPQVTsvslnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSV 1858
Cdd:PRK12316 1762 QVGYGDHQQLLDPAQT---------RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQI 1832

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1859 GLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHATQSL--IALTAGR--SRLFNSLFIYENYPDAKA-EQGQraddP 1933
Cdd:PRK12316 1833 GLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLydIQRWAGQggEALFDSLLVFENYPVAEAlKQGA----P 1908

                        1930      1940      1950      1960
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635 1934 HRLYPEFSAAYEKVEMPLNLVVrEQSGCMLLRFEFDADALDSAQARRV 1981
Cdd:PRK12316 1909 AGLVFGRVSNHEQTNYPLTLAV-TLGETLSLQYSYDRGHFDAAAIERL 1955
PRK12467 PRK12467
peptide synthase; Provisional
 41-1981 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1117.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   41 RTIKENKD--AIVRCLTAQQAFERPITPQNA--TSGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFD 116
Cdd:PRK12467 1082 RTLFEHQTlaGFAQAVAAQQQGAQPALPDVDrdQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFD 1161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  117 ALAQRHASLRTRFVVNEqGKGEQRIDAYQPFVIQHDdfSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSER 196
Cdd:PRK12467 1162 ALVARHESLRTTFVQED-GRTRQVIHPVGSLTLEEP--LLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAAD 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  197 THVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQPYPVETTQLNYIDYAHWfnSDSFLDYHNEFK--PFWVERLTGIP 274
Cdd:PRK12467 1239 EHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVW--QRQWMDAGERARqlAYWKAQLGGEQ 1316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  275 EVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDI 354
Cdd:PRK12467 1317 PVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAET 1396

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  355 EDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQaKVDFNDL- 433
Cdd:PRK12467 1397 EGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQ-RDDHQAQa 1475

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  434 -IPGCDAAEETSPVLPAKTDISVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDR 512
Cdd:PRK12467 1476 qLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAE 1555

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  513 FAAVLAETQQLPRSYPqPQLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVL 592
Cdd:PRK12467 1556 RRQILEGWNATHTGYP-LARLVHQLIEDQAAATPEAVALVFGEQ----ELTYGELNRRANRLAHRLIALGVGPEVLVGIA 1630

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  593 AKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVIlggdgqqLAQWSAEQRIDLTD---PAVVEQWQDLP 669
Cdd:PRK12467 1631 VERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL-------LTQSHLQARLPLPDglrSLVLDQEDDWL 1703

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  670 GDQPPAIPRHA---QQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSS 746
Cdd:PRK12467 1704 EGYSDSNPAVNlapQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLIN 1783

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  747 GGTLAFGEPN-----DRAIMQAEQAGATHL-ILPTALMSILD-PEQVNG---IQAIGMGGEACPNAVVENWADK---VAL 813
Cdd:PRK12467 1784 GARLVIAPPGahrdpEQLIQLIERQQVTTLhFVPSMLQQLLQmDEQVEHplsLRRVVCGGEALEVEALRPWLERlpdTGL 1863

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  814 YNMYGPTECTVTALSTRLRKGQP-----VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF 888
Cdd:PRK12467 1864 FNLYGPTETAVDVTHWTCRRKDLegrdsVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERF 1943

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  889 ehiTLNDVNNAGQgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGS 968
Cdd:PRK12467 1944 ---VADPFGTVGS-----RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQ-GGVREAVVIAQDGAN 2014

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  969 RPALVAYaTVKADSSTPEPA---AVLIDVAK-----YLPEYMVPFRLMLLEDMPLTPNGKLDMKQLpPVLEANESDGEAD 1040
Cdd:PRK12467 2015 GKQLVAY-VVPTDPGLVDDDeaqVALRAILKnhlkaSLPEYMVPAHLVFLARMPLTPNGKLDRKAL-PAPDASELQQAYV 2092

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1041 NP---LEADVLAIWRSVLNTP-LGVEDDFFRLGGDSILSIQLTTRLRSAGYACTVKDVFEAKSVRRLCRVlAQNNrDTGT 1116
Cdd:PRK12467 2093 APqseLEQRLAAIWQDVLGLEqVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAV-AQEG-DGTV 2170

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1117 VAEQGTLEGEFALLPIQRWFMEQSLARPEHWNQAAMIQLPE-VDTERLVTMLQALMAQHDALRLGCDAEGQRYLA---DV 1192
Cdd:PRK12467 2171 SIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREaLDAELLEAALQALLVHHDALRLGFVQEDGGWSAmhrAP 2250

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1193 PCPALSTLDYRQLGDDG-LQQAFTALQSEFDPAQGRTMAcALVRHHPQADTALFLAFHHLVIDAVSWRILVDDLE----R 1267
Cdd:PRK12467 2251 EQERRPLLWQVVVADKEeLEALCEQAQRSLDLEEGPLLR-AVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQtayrQ 2329

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1268 LYLGEPL-LP-KTSSYRQWGAALQHYATQH--AEQLTYWQAQEDGVdlTALLAAKDPQG-----HASAAILTLDAKTTGQ 1338
Cdd:PRK12467 2330 LQGGQPVkLPaKTSAFKAWAERLQTYAASAalADELGYWQAQLQGA--STELPCDHPQGglqrrHAASVTTHLDSEWTRR 2407

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1339 LVSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIDPTLDVSRTVGWFTSTYPVCLQDKPDWASLIQSS 1418
Cdd:PRK12467 2408 LLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLATSIKTI 2487

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1419 KEQLRQVPDKGVGFNPLRYHHPQGNSLTLSP-----IVFNYLG-----LSVQAAGTWRPVDVAPGCCVSPGNKPAEVISL 1488
Cdd:PRK12467 2488 KEQLRAVPNKGLGFGVLRYLGSEAARQTLQAlpvprITFNYLGqfdgsFDAEKQALFVPSGEFSGAEQSEEAPLGNWLSI 2567

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1489 HGGITGGQLTLRQVGClNQRDSERLMTRLT----ENLRALTEACLTQLSHGVvfTPSDFPAVNLSQTQLDSLS-QRYDID 1563
Cdd:PRK12467 2568 NGQVYGGELNLGWTFS-QEMFDEATIQRLAdayaEELRALIEHCCSNDQRGV--TPSDFPLAGLSQEQLDRLPvAVGDIE 2644

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1564 TLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRyAHVLDVEGYRQAWQRQIQRFPALRAALESECA---SIQVIVKQADLP 1640
Cdd:PRK12467 2645 DIYPLSPMQQGMLFHTLYEGGAGDYINQMRVD-VEGLDVERFRTAWQAVIDRHEILRSGFLWDGEleePLQVVYKQARLP 2723

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1641 FYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQtlmq 1720
Cdd:PRK12467 2724 FSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF---- 2799

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1721 gqvlmhGDAPAIQVDRaYVDYARHAVAQQSAV-DAFWQQRQSLLAQTNDVSMLFAAA-----GKRADLSQHltqiepqvt 1794
Cdd:PRK12467 2800 ------GQPPPAREGR-YRDYIAWLQAQDAEAsEAFWKEQLAALEEPTRLARALYPApaeavAGHGAHYLH--------- 2863

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1795 svsLNEKDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSVGLYINSLPLALSWQQP 1874
Cdd:PRK12467 2864 ---LDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAE 2940

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1875 VSLQQHLVQLQNELMAMNQHATQSL--IALTAGR--SRLFNSLFIYENYP-DAKAEQGQraddPHRLYPEFSAAYEKVEM 1949
Cdd:PRK12467 2941 QTVSDWLQQVQAQNLALREFEHTPLadIQRWAGQggEALFDSILVFENYPiSEALKQGA----PSGLRFGAVSSREQTNY 3016

                        2010      2020      2030
                  ....*....|....*....|....*....|...
gi 499404635 1950 PLNLVVReqSGCML-LRFEFDADALDSAQARRV 1981
Cdd:PRK12467 3017 PLTLAVG--LGDTLeLEFSYDRQHFDAAAIERL 3047
PRK12316 PRK12316
peptide synthase; Provisional
 56-2000 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 1045.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   56 AQQAFERPITPQNATSG---PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvn 132
Cdd:PRK12316 2584 ESGQTSRAPVLQKVTRVqplPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFV-- 2661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  133 eqGKGEQRIDAYQPfVIQHDDFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGW 212
Cdd:PRK12316 2662 --EVGEQTRQVILP-NMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGW 2738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  213 SVKNLFADFKPAFLACQNCQPYPVETTQLNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIPEVHSLPLDKPRPAHQNSG 292
Cdd:PRK12316 2739 SMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHR 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  293 GEVIFSAINNDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQ 372
Cdd:PRK12316 2819 GARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVD 2898

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  373 DSQNFVDYLQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVDFNDLIPGCDAAEETSPVLPAKTD 452
Cdd:PRK12316 2899 AQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFD 2978

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  453 ISVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQpQL 532
Cdd:PRK12316 2979 LALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPL-ER 3057

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK12316 3058 GVHRLFEEQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGA 3133

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRHIITDANLSVILGGDGQQLAQWSAEQRIDltdpavVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGS 692
Cdd:PRK12316 3134 YVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLD------LDRGDENYAEANPAIRTMPENLAYVIYTSGS 3207

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  693 TGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA--EQAGATH 770
Cdd:PRK12316 3208 TGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALlvELINSEG 3287

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  771 LILPTALMSIL-------DPEQVNGIQAIGMGGEACPNAVVENWADKVALYNMYGPTECTVTALSTRLRKGQPVT--IGK 841
Cdd:PRK12316 3288 VDVLHAYPSMLqafleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGR 3367

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  842 PLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnAGQGAATLRIYRTGDKARLLNNG 921
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFV---------PDPFVPGERLYRTGDLARYRADG 3438

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  922 DYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIvAQVGSRpaLVAYaTVKADSSTPEPAAVLIDVAKYLPEY 1001
Cdd:PRK12316 3439 VIEYIGRVDHQVKIRGFRIELGEIEARLLEH-PWVREAVVL-AVDGRQ--LVAY-VVPEDEAGDLREALKAHLKASLPEY 3513

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1002 MVPFRLMLLEDMPLTPNGKLDMKQLPPVLEANESDG--EADNPLEADVLAIWRSVLNTP-LGVEDDFFRLGGDSILSIQL 1078
Cdd:PRK12316 3514 MVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDyvAPVNELERRLAAIWADVLKLEqVGLTDNFFELGGDSIISLQV 3593

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1079 TTRLRSAGYACTVKDVFEAKSVRRLCRVLaqnNRDTGTVAEQGTLEGEFALLPIQRWFMEQSLARPEHWNQAAMIQLPEV 1158
Cdd:PRK12316 3594 VSRARQAGIRFTPKDLFQHQTIQGLARVA---RVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1159 -DTERLVTMLQALMAQHDALRLGCDAEGQRYLAD-VPCPALSTLDYRQLGDDG--LQQAFTALQSEFDPAQGRTMACALV 1234
Cdd:PRK12316 3671 lDAAALEAALQALVEHHDALRLRFVEDAGGWTAEhLPVELGGALLWRAELDDAeeLERLGEEAQRSLDLADGPLLRALLA 3750

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1235 RhHPQADTALFLAFHHLVIDAVSWRILVDDLERLY----LGEPL-LP-KTSSYRQWGAALQHYATQHA--EQLTYWQAQE 1306
Cdd:PRK12316 3751 T-LADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllQGEAPrLPaKTSSFKAWAERLQEHARGEAlkAELAYWQEQL 3829

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1307 DGVdlTALLAAKDPQG-----HASAAILTLDAKTTGQLVSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGR 1381
Cdd:PRK12316 3830 QGV--SSELPCDHPQGalqnrHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGR 3907

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1382 EAIDPTLDVSRTVGWFTSTYPVCLQDKPDWASLIQSSKEQLRQVPDKGVGFNPLRYHHPQGNSLTLSP-----IVFNYLG 1456
Cdd:PRK12316 3908 EDLFADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGlpvprITFNYLG 3987

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1457 L----SVQAAGTWRPVDVAPGCCVSPGNKPAEVISLHGGITGGQLTLrQVGCLNQRDSERLMTRLTEN----LRALTEAC 1528
Cdd:PRK12316 3988 QfdgsFDEEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSL-DWTFSREMFEEATIQRLADDyaaeLTALVEHC 4066

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1529 LTQLSHGVvfTPSDFPAVNLSQTQLDSLS-QRYDIDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRyAHVLDVEGYRQ 1607
Cdd:PRK12316 4067 CDAERHGV--TPSDFPLAGLDQARLDALPlPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVD-VQGLDVERFRA 4143

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1608 AWQRQIQRFPALRAALESECAS---IQVIVKQADLPFYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLG 1684
Cdd:PRK12316 4144 AWQAALDRHDVLRSGFVWQGELgrpLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTA 4223

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1685 EQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQtlmqgqvlmhGDAPAIQVDRaYVDYARHAVAQQSAV-DAFWQQRQSLL 1763
Cdd:PRK12316 4224 EGRHHLIYTNHHILMDGWSNSQLLGEVLERYS----------GRPPAQPGGR-YRDYIAWLQRQDAAAsEAFWREQLAAL 4292

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1764 AQTNDVSMLFAAAGKR--ADLSQHLTQIEPQVTsvslnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVG 1841
Cdd:PRK12316 4293 DEPTRLAQAIARADLRsaNGYGEHVRELDATAT---------ARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFG 4363

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1842 NVLSGRESPVEDVASSVGLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHATQSLIALT----AGRSRLFNSLFIYE 1917
Cdd:PRK12316 4364 ATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQrwagQGGEALFDSLLVFE 4443

                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1918 NYPDAKAEQGQRADDphrLYPEFSAAYEKVEMPLNLVVrEQSGCMLLRFEFDADALDSAQARRVLMRWHDEVVALVnSVP 1997
Cdd:PRK12316 4444 NYPVSEALQQGAPGG---LRFGEVTNHEQTNYPLTLAV-GLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMA-EDP 4518


                  ...
gi 499404635 1998 QQP 2000
Cdd:PRK12316 4519 QRR 4521
PRK05691 PRK05691
peptide synthase; Validated
 73-1920 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 966.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvNEQGKGEQRIDAYQPFVIQHD 152
Cdd:PRK05691 1730 PLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFP-SVDGVPVQQVAEDSGLRMDWQ 1808

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVkNLFA----DFKPAFLAC 228
Cdd:PRK05691 1809 DFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAM-DIFArelgALYEAFLDD 1887

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  229 QncqPYPVETTQLNYIDYA----HWFNS---DSFLDYhnefkpfWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAIN 301
Cdd:PRK05691 1888 R---ESPLEPLPVQYLDYSvwqrQWLESgerQRQLDY-------WKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLS 1957

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  302 NDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYL 381
Cdd:PRK05691 1958 PELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELL 2037

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  382 QYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ------------AKVDF--NDlipgcdaAEETspvl 447
Cdd:PRK05691 2038 EQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQrwefqqsrqlagMTVEYlvND-------ARAT---- 2106

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  448 paKTDISVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSY 527
Cdd:PRK05691 2107 --KFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEA 2184

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  528 PQPQlTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIW 607
Cdd:PRK05691 2185 RLDQ-TLHGLFAAQAARTPQAPALTFAGQ----TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAIL 2259

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  608 KAGAAYVPLDPDYPPERLRHIITDANLSVILGGDG---------QQLAQWSAEQridltDPAVVEqwqDLPGDQPPAI-- 676
Cdd:PRK05691 2260 KAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRAlfealgelpAGVARWCLED-----DAAALA---AYSDAPLPFLsl 2331

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  677 PRHaqqLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGtlafgepn 756
Cdd:PRK05691 2332 PQH---QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGA-------- 2400

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  757 dRAIMQAE-QAGATHL--ILPTALMSILDPEQVNGIQ------------AIGM---GGEACPNavvENWADKVA------ 812
Cdd:PRK05691 2401 -RVVLRAQgQWGAEEIcqLIREQQVSILGFTPSYGSQlaqwlagqgeqlPVRMcitGGEALTG---EHLQRIRQafapql 2476

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  813 LYNMYGPTECTVTALST----RLRKGQ-PVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASR 887
Cdd:PRK05691 2477 FFNAYGPTETVVMPLAClapeQLEEGAaSVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAER 2556

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  888 FehitLNDVNNAGQGaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVG 967
Cdd:PRK05691 2557 F----VADPFAADGG----RLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAVREAVVLALDTP 2627

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  968 SRPALVAYATVKADSSTPEPAAVLIDVAK-----YLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP-PVLEANESDGEA-D 1040
Cdd:PRK05691 2628 SGKQLAGYLVSAVAGQDDEAQAALREALKahlkqQLPDYMVPAHLILLDSLPLTANGKLDRRALPaPDPELNRQAYQApR 2707

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1041 NPLEADVLAIWRSVLNTP-LGVEDDFFRLGGDSILSIQLTTRLRSAGYACTVKDVFEAKSVRRLCRVLaqnNRDTGTVAE 1119
Cdd:PRK05691 2708 SELEQQLAQIWREVLNVErVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVA---THSEAAQAE 2784

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1120 QGTLEGEFALLPIQRWFMEQSLARPEHWNQAAMIQ-LPEVDTERLVTMLQALMAQHDALRLGCDAEGQRYLADvpcpals 1198
Cdd:PRK05691 2785 QGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEpRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAE------- 2857

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1199 tldYRQLGDDGL------------QQAFTALQSEFDPAQGRTMACALVRHhPQADTALFLAFHHLVIDAVSWRILVDDLE 1266
Cdd:PRK05691 2858 ---YRAVTAQELlwqvtvadfaecAALFADAQRSLDLQQGPLLRALLVDG-PQGQQRLLLAIHHLVVDGVSWRVLLEDLQ 2933

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1267 RLY------LGEPLLPKTSSYRQWGAALQHYATQHA--EQLTYWQAQEDGVDltALLAAKDPQG-----HASAAILTLDA 1333
Cdd:PRK05691 2934 ALYrqlsagAEPALPAKTSAFRDWAARLQAYAGSESlrEELGWWQAQLGGPR--AELPCDRPQGgnlnrHAQTVSVRLDA 3011

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1334 KTTGQLVSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIDPTLDVSRTVGWFTSTYPVCLQ----DKP 1409
Cdd:PRK05691 3012 ERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLTpapgDDA 3091

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1410 DWASLIQSSKEQLRQVPDKGVGFNPLRY-----HHPQGNSLTLSPIVFNYLG---LSVQAAGTWRPVDVAPGCCVSPGNK 1481
Cdd:PRK05691 3092 ARGESIKAIKEQLRAVPHKGLGYGVLRYladaaVREAMAALPQAPITFNYLGqfdQSFASDALFRPLDEPAGPAHDPDAP 3171

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1482 PAEVISLHGGITGGQLTLRQVGCLNQRDS---ERLMTRLTENLRALTEACLTQLSHGvvFTPSDFPAVNLSQTQLDSLS- 1557
Cdd:PRK05691 3172 LPNELSVDGQVYGGELVLRWTYSAERYDEqtiAELAEAYLAELQALIAHCLADGAGG--LTPSDFPLAQLTQAQLDALPv 3249

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1558 QRYDIDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL--ESECASIQVIVK 1635
Cdd:PRK05691 3250 PAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFswNAGETMLQVIHK 3329

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1636 QADLPFYYQDL--MQDADPLAVIERYRQQDLRTGFD-LSQPPL-LRIacFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAV 1711
Cdd:PRK05691 3330 PGRTPIDYLDWrgLPEDGQEQRLQALHKQEREAGFDlLNQPPFhLRL--IRVDEARYWFMMSNHHILIDAWCRSLLMNDF 3407

                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1712 HRDYQTLMQGQVLMHGDAPaiqvdrAYVDYARhavaqqsavdafWQQRQSLLA-----QTN--DVSMLFAAAGKRADLSQ 1784
Cdd:PRK05691 3408 FEIYTALGEGREAQLPVPP------RYRDYIG------------WLQRQDLAQarqwwQDNlrGFERPTPIPSDRPFLRE 3469

                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1785 HLTQIEPQVTS---VSLNEKDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSVGLY 1861
Cdd:PRK05691 3470 HAGDSGGMVVGdcyTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLF 3549

                        1930      1940      1950      1960      1970      1980
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635 1862 INSLPLALSW---QQPVSLQQHLVQLQNELMAMNQHATQSLIA------LTAGRSrLFNSLFIYENYP 1920
Cdd:PRK05691 3550 INSIALRVQLpaaGQRCSVRQWLQGLLDSNMELREYEYLPLVAiqecseLPKGQP-LFDSLFVFENAP 3616
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 55-1333 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: 806.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   55 TAQQAFERPITPQNATSGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVnEQ 134
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRT-RA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  135 GKGEQRIDAYQPFVIQHDDFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSV 214
Cdd:COG1020    80 GRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  215 KNLFADFKPAFLACQNCQPYPVETTQLNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGE 294
Cdd:COG1020   160 GLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  295 VIFSAINNDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDS 374
Cdd:COG1020   240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGD 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  375 QNFVDYLQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQaKVDFNDL-IPGCDAAEETSPVLPAKTDI 453
Cdd:COG1020   320 PSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQ-NAPADELeLPGLTLEPLELDSGTAKFDL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  454 SVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQPQlT 533
Cdd:COG1020   399 TLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADA-T 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  534 VTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAY 613
Cdd:COG1020   478 LHELFEAQAARTPDAVAVVFGDQ----SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  614 VPLDPDYPPERLRHIITDANLSVILGGDG--QQLAQWSAeQRIDLTDPAVVEQwqdlpGDQPPAIPRHAQQLAQVIYTSG 691
Cdd:COG1020   554 VPLDPAYPAERLAYMLEDAGARLVLTQSAlaARLPELGV-PVLALDALALAAE-----PATNPPVPVTPDDLAYVIYTSG 627

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  692 STGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA-----EQA 766
Cdd:COG1020   628 STGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAAlaellARH 707

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  767 GATHLILPTALMSIL---DPEQVNGIQAIGMGGEACPNAVVENWADK---VALYNMYGPTECTVTALSTRLRKGQ----P 836
Cdd:COG1020   708 RVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWRARlpgARLVNLYGPTETTVDSTYYEVTPPDadggS 787

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  837 VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehITlNDVNNAGQgaatlRIYRTGDKAR 916
Cdd:COG1020   788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERF--VA-DPFGFPGA-----RLYRTGDLAR 859

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  917 LLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAK 996
Cdd:COG1020   860 WLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQ-HPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALAL 938

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  997 YLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEANESDGEADNPLEADVLA--IWRSVLNTPLGVEDDFFRLGGDSIL 1074
Cdd:COG1020   939 LLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAalALLLLLVVVVGDDDFFFFGGGLGLL 1018

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1075 SIQLTTRLRSAGYACTVKDVF-------EAKSVRRLCRVLAQNNRDTGTVAEQGTLEGEFALLPIQRWFMEQSLARPEHW 1147
Cdd:COG1020  1019 LLLALARAARLLLLLLLLLLLflaaaaaAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLAL 1098

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1148 NQAAMIQLPEVDTERLVTMLQALMAQHDALRLGCDAEGQRYLADVPCPALSTLDYRQLGDDGLQQAFTALQSEFDPAQGR 1227
Cdd:COG1020  1099 LLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLA 1178

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1228 TMACALVRHHPQADTALFLAFHHLVIDAVSWRILVDDLERLYLGEPLLPKTSSYRQWGAALQHYATQHAEQLTYWQAQED 1307
Cdd:COG1020  1179 LLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAA 1258

                        1290      1300
                  ....*....|....*....|....*.
gi 499404635 1308 GVDLTALLAAKDPQGHASAAILTLDA 1333
Cdd:COG1020  1259 LLALALALLALALLLLALALLLPALA 1284
PRK12467 PRK12467
peptide synthase; Provisional
 73-1305 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 715.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKgEQRIDAYQPFVIQHD 152
Cdd:PRK12467   51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGF-RQVIDASLSLTIPLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLA-CQNC 231
Cdd:PRK12467  130 DLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAySQGR 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  232 QPyPVETTQLNYIDYAHWfnSDSFLDYHNEFKP--FWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFK 309
Cdd:PRK12467  210 EP-SLPALPIQYADYAIW--QRSWLEAGERERQlaYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLK 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  310 RLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDL 389
Cdd:PRK12467  287 ALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTAL 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  390 SAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ--AKVDFNDL---IPGCDAAEETSPVLPAKTDISVKVTELMGEV 464
Cdd:PRK12467  367 GAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQntATGGRDREgaqLPGLTVEELSWARHTAQFDLALDTYESAQGL 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  465 RLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQPqlTVTDVIEAVAQR 544
Cdd:PRK12467  447 WAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPD--CVHQLIEAQARQ 524

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  545 DPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPER 624
Cdd:PRK12467  525 HPERPALVFGEQ----VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR 600

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  625 LRHIITDANLSVILgGDGQQLAQW---SAEQRIDLTDPAvvEQWQDLPGDQPPaIPRHAQQLAQVIYTSGSTGLPKGVMI 701
Cdd:PRK12467  601 LAYMLDDSGVRLLL-TQSHLLAQLpvpAGLRSLCLDEPA--DLLCGYSGHNPE-VALDPDNLAYVIYTSGSTGQPKGVAI 676

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  702 EHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEQAGATHlILP 774
Cdd:PRK12467  677 SHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCArdaeafaALMADQGVTVLK-IVP 755

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  775 TALMSILD---PEQVNGIQAIGMGGEACPNAVVENW---ADKVALYNMYGPTECTVTALSTRLRK----GQPVTIGKPLI 844
Cdd:PRK12467  756 SHLQALLQasrVALPRPQRALVCGGEALQVDLLARVralGPGARLINHYGPTETTVGVSTYELSDeerdFGNVPIGQPLA 835

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  845 HIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDvnnaGQGAATLRIYRTGDKARLLNNGDYE 924
Cdd:PRK12467  836 NLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERF----VPD----PFGADGGRLYRTGDLARYRADGVIE 907

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  925 YCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQiKVIVAQVGSRPA-LVAYATVKADSSTPEPAAVLIDVAKY----LP 999
Cdd:PRK12467  908 YLGRMDHQVKIRGFRIELGEIEARLLAQ-PGVRE-AVVLAQPGDAGLqLVAYLVPAAVADGAEHQATRDELKAQlrqvLP 985

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1000 EYMVPFRLMLLEDMPLTPNGKLDMKQLP-PVLEANESDGEA-DNPLEADVLAIWRSVLNT-PLGVEDDFFRLGGDSILSI 1076
Cdd:PRK12467  986 DYMVPAHLLLLDSLPLTPNGKLDRKALPkPDASAVQATFVApQTELEKRLAAIWADVLKVeRVGLTDNFFELGGHSLLAT 1065

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1077 QLTTRLRSA-GYACTVKDVFEAKSVRRLCRVLAQNNRDTGTVAEQGTLEGEFALLPIQ--RWFMEQSLARPEHWNQAAMI 1153
Cdd:PRK12467 1066 QVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQerQWFLWQLEPGSAAYHIPQAL 1145

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1154 QLP-EVDTERLVTMLQALMAQHDALRLGCDAEGQRYLaDVPCPALS-TLDYR--QLGDDGLQQAFTALQSE----FDPAQ 1225
Cdd:PRK12467 1146 RLKgPLDIEALERSFDALVARHESLRTTFVQEDGRTR-QVIHPVGSlTLEEPllLAADKDEAQLKVYVEAEarqpFDLEQ 1224

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1226 GRTMACALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERLYLGE--------PLLP-KTSSY----RQWGAalqhyA 1292
Cdd:PRK12467 1225 GPLLRVGLLRLAAD-EHVLVLTLHHIVSDGWSMQVLVDELVALYAAYsqgqslqlPALPiQYADYavwqRQWMD-----A 1298

                        1290
                  ....*....|...
gi 499404635 1293 TQHAEQLTYWQAQ 1305
Cdd:PRK12467 1299 GERARQLAYWKAQ 1311
PRK05691 PRK05691
peptide synthase; Validated
 12-1305 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 668.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   12 ERQGVRLALNaqgQLISQSNKEAITAEIGRTIKEN---KDAIVRcLTAQQAFerpitpqnatsgPLSSSQSGLWFIEQYE 88
Cdd:PRK05691  629 DELGIDLNLR---QLFEAPTLAAFSAAVARQLAGGgaaQAAIAR-LPRGQAL------------PQSLAQNRLWLLWQLD 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   89 EQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvNEQGKGEQRIDAYQPFVIQHDDFSLLPEAEREGRLQQ 168
Cdd:PRK05691  693 PQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFY-ERDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQ 771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  169 QVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQPYPVETTQLNYIDYAH 248
Cdd:PRK05691  772 IREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGA 851

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  249 W-------FNSDSFLDYhnefkpfWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKRLCQRYNTSNFI 321
Cdd:PRK05691  852 WqrqwlaqGEAARQLAY-------WKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFM 924

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  322 GLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLSAFDHQLYRFEA 401
Cdd:PRK05691  925 VLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQ 1004

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  402 LSEAIGSDRTTAinpIFQVMLVYQAKvDFNDL--IPGCdAAEEtspvLP-----AKTDISVKVTE-LMGEVRLDWLFATA 473
Cdd:PRK05691 1005 LVEALPQAREQG---LFQVMFNHQQR-DLSALrrLPGL-LAEE----LPwhsreAKFDLQLHSEEdRNGRLTLSFDYAAE 1075

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  474 LFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRfAAVLAETQQLPrsYPQPQLTVTDVIEAVAQRDPQQLAIAF 553
Cdd:PRK05691 1076 LFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAE-RAQLAQWGQAP--CAPAQAWLPELLNEQARQTPERIALVW 1152

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  554 DGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDAN 633
Cdd:PRK05691 1153 DGG----SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  634 LSVILGGDG--QQLAQWSAEQRIDLtDPAVVEQWQdlpgDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLD 711
Cdd:PRK05691 1229 VELLLTQSHllERLPQAEGVSAIAL-DSLHLDSWP----SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQ 1303

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  712 DHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEQAGATHLILPTALMSILDP- 783
Cdd:PRK05691 1304 WMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHrdpqriaELVQQYGVTTLHFVPPLLQLFIDEPl 1383

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  784 -EQVNGIQAIGMGGEACPNAV---VENWADKVALYNMYGPTEC--TVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQL 857
Cdd:PRK05691 1384 aAACTSLRRLFSGGEALPAELrnrVLQRLPQVQLHNRYGPTETaiNVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNL 1463

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  858 CPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNDvnnagQGAatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRG 937
Cdd:PRK05691 1464 LPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGE-----DGA---RLYRTGDRARWNADGALEYLGRLDQQVKLRG 1535

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  938 YRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVKAdSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTP 1017
Cdd:PRK05691 1536 FRVEPEEIQARLLAQ-PGVAQAAVLVREGAAGAQLVGYYTGEA-GQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGP 1613

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1018 NGKLDMKQLP-PVLEANESDgEADNPLEADVLAIWRSVLNTP-LGVEDDFFRLGGDSILSIQLTTRLRSagyACTV---- 1091
Cdd:PRK05691 1614 SGKLDRRALPePVWQQREHV-EPRTELQQQIAAIWREVLGLPrVGLRDDFFALGGHSLLATQIVSRTRQ---ACDVelpl 1689

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1092 KDVFEAKSVRRLCRVLAQnNRDTGTVAEQGTLEGEFALLPI------QR-WFMEQSLARPEHWNQAAMIQLPEV-DTERL 1163
Cdd:PRK05691 1690 RALFEASELGAFAEQVAR-IQAAGERNSQGAIARVDRSQPVplsysqQRmWFLWQMEPDSPAYNVGGMARLSGVlDVDRF 1768

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1164 VTMLQALMAQHDALRL---GCDAEGQRYLADVPCPALSTLDYRQLGDDGLQQAFTALQSE-----FDPAQGRTMACALVR 1235
Cdd:PRK05691 1769 EAALQALILRHETLRTtfpSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSeahqpFDLERGPLLRACLVK 1848

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1236 HHPQaDTALFLAFHHLVIDAVSWRILVDDLERLY------LGEPLLPKTSSY-------RQWgaaLQhyATQHAEQLTYW 1302
Cdd:PRK05691 1849 AAER-EHYFVLTLHHIVTEGWAMDIFARELGALYeaflddRESPLEPLPVQYldysvwqRQW---LE--SGERQRQLDYW 1922


                  ...
gi 499404635 1303 QAQ 1305
Cdd:PRK05691 1923 KAQ 1925
PRK12316 PRK12316
peptide synthase; Provisional
 54-1421 2.33e-162

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 559.19  E-value: 2.33e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   54 LTAQQAFERPI-TPQNATSGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGpLDVAALEFAFDALAQRHASLRTRFVvn 132
Cdd:PRK12316 1538 LSQAQLDALPLpAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFL-- 1614

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  133 EQGkgeqriDAYQPFVIQHDDFSLlPEAEREGR--------LQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQ 204
Cdd:PRK12316 1615 WQD------GLEQPLQVIHKQVEL-PFAELDWRgredlgqaLDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTN 1687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  205 HHIISDGWSVKNLFADFKPAFLAcqncqpYPVETTQLNYIDYAHWFNSDSFLDYHNefkpFWVERLTGIPEVHSLPLDKP 284
Cdd:PRK12316 1688 HHILMDGWSNAQLLGEVLQRYAG------QPVAAPGGRYRDYIAWLQRQDAAASEA----FWKEQLAALEEPTRLAQAAR 1757

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  285 RPAHQNSGGE--VIFSAINNDLWDKFKRlcQRYNTSNFIgLHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGF 360
Cdd:PRK12316 1758 TEDGQVGYGDhqQLLDPAQTRALAEFAR--AQKVTLNTL-VQAAWLLLLQRYTGQETVAFGATVAGRpaELPGIEQQIGL 1834

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  361 FVNTIVLRTQLQDSQNFVDYLQYCREQDLSAFDHQ---LYRFEALSEAIGSdrttainPIFQVMLVYQAKVDFNDLIPGC 437
Cdd:PRK12316 1835 FINTLPVIAAPRPDQSVADWLQEVQALNLALREHEhtpLYDIQRWAGQGGE-------ALFDSLLVFENYPVAEALKQGA 1907

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  438 DAAEETSPVLP-AKTDISVKVTELMGE-VRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAA 515
Cdd:PRK12316 1908 PAGLVFGRVSNhEQTNYPLTLAVTLGEtLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQR 1987

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  516 VLAETQQLPRSYPQpQLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKR 595
Cdd:PRK12316 1988 ILADWDRTPEAYPR-GPGVHQRIAEQAARAPEAIAVVFGDQ----HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAER 2062

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  596 DRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGDG--QQLAQWSAEQRIDLTDPAvveQWQDLPgDQP 673
Cdd:PRK12316 2063 SFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHllERLPLPAGVARLPLDRDA---EWADYP-DTA 2138

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  674 PAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFG 753
Cdd:PRK12316 2139 PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIR 2218

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  754 EPN----DRAIMQAEQAGATHLILPTA-LMSILDPEQVNG----IQAIGMGGEACPNAVVENWA---DKVALYNMYGPTE 821
Cdd:PRK12316 2219 DDElwdpEQLYDEMERHGVTILDFPPVyLQQLAEHAERDGrppaVRVYCFGGEAVPAASLRLAWealRPVYLFNGYGPTE 2298

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  822 CTVTALSTRLRKGQP-----VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDV 896
Cdd:PRK12316 2299 AVVTPLLWKCRPQDPcgaayVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERF----VPDP 2374

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  897 NNAGQGaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQiKVIVAQVG-SRPALVAY 975
Cdd:PRK12316 2375 FSASGE----RLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH-PAVRE-AVVVAQDGaSGKQLVAY 2448

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  976 aTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP-PVLEANESDGEA-DNPLEADVLAIWRS 1053
Cdd:PRK12316 2449 -VVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPkPDVSQLRQAYVApQEGLEQRLAAIWQA 2527

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1054 VLNTP-LGVEDDFFRLGGDSILSIQLTTRLR-SAGYACTVKDVFEAKSVRRLCRVLAQNNRDTGTVAEQGTLEGEFALLP 1131
Cdd:PRK12316 2528 VLKVEqVGLDDHFFELGGHSLLATQVVSRVRqDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSH 2607

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1132 IQR--WFMEQSLARPEHWNQAAMIQLPE-VDTERLVTMLQALMAQHDALRLGCDAEGQRYLADVPcPALSTLDYRQLGDD 1208
Cdd:PRK12316 2608 AQQrqWFLWQLEPESAAYHLPSALHLRGvLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVIL-PNMSLRIVLEDCAG 2686

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1209 GLQQAFTA-----LQSEFDPAQGRTMACALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERLYLGE------PLLPK 1277
Cdd:PRK12316 2687 VADAAIRQrvaeeIQRPFDLARGPLLRVRLLALDGQ-EHVLVITQHHIVSDGWSMQVMVDELVQAYAGArrgeqpTLPPL 2765

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1278 TSSYRQWGAALQHY--ATQHAEQLTYWQAQEDGVDLTALLAAKDP----QGHASAAILT-LDAKTTGQLVSEANRAFNTd 1350
Cdd:PRK12316 2766 PLQYADYAAWQRAWmdSGEGARQLDYWRERLGGEQPVLELPLDRPrpalQSHRGARLDVaLDVALSRELLALARREGVT- 2844

                        1370      1380      1390      1400      1410      1420      1430
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404635 1351 VSDLLLSALTRTLNDLGWGDKARIMLEGHGREaidpTLDVSRTVGWFTSTYPVCLQDKPDWA--SLIQSSKEQ 1421
Cdd:PRK12316 2845 LFMLLLASFQVLLHRYSGQSDIRVGVPIANRN----RAETERLIGFFVNTQVLRAQVDAQLAfrDLLGQVKEQ 2913
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 546-1026 7.83e-150

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: 471.63  E-value: 7.83e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd05930     1 PDAVAVVDGDQ----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd05930    77 AYILEDSGAKLVL------------------TDP---------------------DDLAYVIYTSGSTGKPKGVMVEHRG 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA-----EQAGATHLILPTALMSI 780
Cdd:cd05930   118 LVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEAladllAEEGITVLHLTPSLLRL 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  781 L----DPEQVNGIQAIGMGGEACPNAVVENWAD---KVALYNMYGPTECTVTALSTRLRKG----QPVTIGKPLIHIQAL 849
Cdd:cd05930   198 LlqelELAALPSLRLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDdeedGRVPIGRPIPNTRVY 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  850 ILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDVNNAGQgaatlRIYRTGDKARLLNNGDYEYCGRI 929
Cdd:cd05930   278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERF----VPNPFGPGE-----RMYRTGDLVRWLPDGNLEFLGRI 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  930 DEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGS-RPALVAYATVKADsSTPEPAAVLIDVAKYLPEYMVPFRLM 1008
Cdd:cd05930   349 DDQVKIRGYRIELGEIEAALLA-HPGVREAAVVAREDGDgEKRLVAYVVPDEG-GELDEEELRAHLAERLPDYMVPSAFV 426

                         490
                  ....*....|....*...
gi 499404635 1009 LLEDMPLTPNGKLDMKQL 1026
Cdd:cd05930   427 VLDALPLTPNGKVDRKAL 444
PRK12316 PRK12316
peptide synthase; Provisional
 73-1108 3.85e-149

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 518.36  E-value: 3.85e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGpLDVAALEFAFDALAQRHASLRTRFVvnEQGKGEQridayqPFVIQHD 152
Cdd:PRK12316 4104 PLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFV--WQGELGR------PLQVVHK 4174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLlPEAEREGRLQQQVKA--------EISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPA 224
Cdd:PRK12316 4175 QVSL-PFAELDWRGRADLQAaldalaaaERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLER 4253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  225 FLACQNCQPypvettQLNYIDYAHWFNSDSfldyHNEFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFS-AINND 303
Cdd:PRK12316 4254 YSGRPPAQP------GGRYRDYIAWLQRQD----AAASEAFWREQLAALDEPTRLAQAIARADLRSANGYGEHVrELDAT 4323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  304 LWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYL 381
Cdd:PRK12316 4324 ATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWL 4403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  382 QYCREQDLSAFDHQLYRFEALSEAIGSdrttAINPIFQVMLVYQAKVDFNDLIPGCDAAEETSPVLP-AKTDISVKVTEL 460
Cdd:PRK12316 4404 QQVQRQNLALREHEHTPLYEIQRWAGQ----GGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNhEQTNYPLTLAVG 4479

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  461 MGE-VRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQpQLTVTDVIE 539
Cdd:PRK12316 4480 LGEtLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA-TRCVHQLVA 4558

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  540 AVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPD 619
Cdd:PRK12316 4559 ERARMTPDAVAVVFDEE----KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  620 YPPERLRHIITDANLSVILgGDGQQLAQWSAEQRIDLTDPAVVEQWQDLPgDQPPAIPRHAQQLAQVIYTSGSTGLPKGV 699
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLL-TQSHLLQRLPIPDGLASLALDRDEDWEGFP-AHDPAVRLHPDNLAYVIYTSGSTGRPKGV 4712

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  700 MIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPN----DRAIMQAEQAGATHLILPT 775
Cdd:PRK12316 4713 AVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSlwdpERLYAEIHEHRVTVLVFPP 4792

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  776 ALMSIL---DPEQVN--GIQAIGMGGEACPNAVVENW---ADKVALYNMYGPTECTVTALSTRLRKGQP-----VTIGKP 842
Cdd:PRK12316 4793 VYLQQLaehAERDGEppSLRVYCFGGEAVAQASYDLAwraLKPVYLFNGYGPTETTVTVLLWKARDGDAcgaayMPIGTP 4872

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  843 LIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehiTLNDVNNAGQgaatlRIYRTGDKARLLNNGD 922
Cdd:PRK12316 4873 LGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERF---VPDPFGAPGG-----RLYRTGDLARYRADGV 4944

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  923 YEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQiKVIVAQVGSRPA-LVAYaTVKADS---STPEPAAVLIDVAK-- 996
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARLREH-PAVRE-AVVIAQEGAVGKqLVGY-VVPQDPalaDADEAQAELRDELKaa 5021

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  997 ---YLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPP--------VLEANESDgeadnpLEADVLAIWRSVLNTP-LGVEDD 1064
Cdd:PRK12316 5022 lreRLPEYMVPAHLVFLARMPLTPNGKLDRKALPQpdasllqqAYVAPRSE------LEQQVAAIWAEVLQLErVGLDDN 5095

                        1050      1060      1070      1080
                  ....*....|....*....|....*....|....*....|....*
gi 499404635 1065 FFRLGGDSILSIQLTTRLRSA-GYACTVKDVFEAKSVRRLCRVLA 1108
Cdd:PRK12316 5096 FFELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFVELAA 5140
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
69-1108 4.54e-136

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 461.05  E-value: 4.54e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   69 ATSGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKgEQRIDAYQPF- 147
Cdd:PRK10252    5 SQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEV-WQWVDPALTFp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  148 VIQHDDFSLLPEAEREGRLQQQvkAEISRPFDLTAGD-LTRVRLVKMSERTHVLMITQHHIISDGWSVkNLFADFKPA-F 225
Cdd:PRK10252   84 LPEIIDLRTQPDPHAAAQALMQ--ADLQQDLRVDSGKpLVFHQLIQLGDNRWYWYQRYHHLLVDGFSF-PAITRRIAAiY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  226 LACQNCQPYPVET-TQLNYI--DYAHWFNSDSF-LDyhnefKPFWVERLTGIPEVHSLpldKPRPAHQNSGGEVIFSAIN 301
Cdd:PRK10252  161 CAWLRGEPTPASPfTPFADVveEYQRYRASEAWqRD-----AAFWAEQRRQLPPPASL---SPAPLPGRSASADILRLKL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  302 NDLWDKFKRL------CQRYNTsnfigLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQ 375
Cdd:PRK10252  233 EFTDGAFRQLaaqasgVQRPDL-----ALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQE 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  376 NFVDYLQYCREQDLSAFDHQLYRFEAL---SEAIGSDRTTaINPIFQVMlVYQAKVDFndliPGCDAAEE---TSPVlpa 449
Cdd:PRK10252  308 TLPELATRLAAQLKKMRRHQRYDAEQIvrdSGRAAGDEPL-FGPVLNIK-VFDYQLDF----PGVQAQTHtlaTGPV--- 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  450 kTDISVKV-TELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDrfaavlaETQQLPR--- 525
Cdd:PRK10252  379 -NDLELALfPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPG-------EYAQLAQvna 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  526 -SYPQPQLTVTDVIEAVAQRDPQQLAIAFDGeprtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALL 604
Cdd:PRK10252  451 tAVEIPETTLSALVAQQAAKTPDAPALADAR----YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALH 526

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  605 AIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGDGQQlAQWSAeqrIDLTDPAVVEQWQdLPGDQPPAIPRHAQQLA 684
Cdd:PRK10252  527 AIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQL-PRFAD---VPDLTSLCYNAPL-APQGAAPLQLSQPHHTA 601

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  685 QVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPN---DRAIM 761
Cdd:PRK10252  602 YIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEahrDPLAM 681

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  762 QA----EQAGATHLIlPT---ALMSILDPEQVNGIQA----IGMGGEACPNAVVENW--ADKVALYNMYGPTECTV---- 824
Cdd:PRK10252  682 QQffaeYGVTTTHFV-PSmlaAFVASLTPEGARQSCAslrqVFCSGEALPADLCREWqqLTGAPLHNLYGPTEAAVdvsw 760

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  825 ---TALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndVNNAGQ 901
Cdd:PRK10252  761 ypaFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFI------ADPFAP 834

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  902 GAatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIkVIVAQV--------GSRPALV 973
Cdd:PRK10252  835 GE---RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQAL-PDVEQA-VTHACVinqaaatgGDARQLV 909

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  974 AYaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP-PVLEANESDGEADNPLEADVLAIWR 1052
Cdd:PRK10252  910 GY-LVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPlPELKAQVPGRAPKTGTETIIAAAFS 988

                        1050      1060      1070      1080      1090
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635 1053 SVLN-TPLGVEDDFFRLGGDSILSIQLTTRLRSA-GYACTVKDVFEAKSVRRLCRVLA 1108
Cdd:PRK10252  989 SLLGcDVVDADADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLATLLD 1046
PRK12467 PRK12467
peptide synthase; Provisional
 73-1103 9.29e-132

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 463.48  E-value: 9.29e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGpLDVAALEFAFDALAQRHASLRTRFV-VNEQGKGEQRIDAYQPFVIQH 151
Cdd:PRK12467 2648 PLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLwDGELEEPLQVVYKQARLPFSR 2726

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  152 DDFSLLPEAEREgrLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADfkpaflACQNC 231
Cdd:PRK12467 2727 LDWRDRADLEQA--LDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGE------VLQRY 2798

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  232 QPYPVETTQLNYIDYAHWFNSDSfldyHNEFKPFWVERLTGIPEVHSL-PLDKPRPAHQNSGGEVIFSAINNDLWDKFKR 310
Cdd:PRK12467 2799 FGQPPPAREGRYRDYIAWLQAQD----AEASEAFWKEQLAALEEPTRLaRALYPAPAEAVAGHGAHYLHLDATQTRQLIE 2874

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  311 LCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQD 388
Cdd:PRK12467 2875 FARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQN 2954

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  389 LSAFDHQ---LYRFEALSEAIGSdrttainPIFQVMLVYQAkvdfndlIPGCDAAEETSP------------VLPAKTDI 453
Cdd:PRK12467 2955 LALREFEhtpLADIQRWAGQGGE-------ALFDSILVFEN-------YPISEALKQGAPsglrfgavssreQTNYPLTL 3020

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  454 SVKVTELMGevrLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQpQLT 533
Cdd:PRK12467 3021 AVGLGDTLE---LEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPS-ERL 3096

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  534 VTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAY 613
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGDQ----QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAY 3172

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  614 VPLDPDYPPERLRHIITDANLSVILGGDG--QQLAQWSAEQRIDLTDPAvveqWQDLPgDQPPAIPRHAQQLAQVIYTSG 691
Cdd:PRK12467 3173 VPLDPEYPRERLAYMIEDSGVKLLLTQAHllEQLPAPAGDTALTLDRLD----LNGYS-ENNPSTRVMGENLAYVIYTSG 3247

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  692 STGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTL--AFGEPND----RAIMQAEQ 765
Cdd:PRK12467 3248 STGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLvvRDNDLWDpeelWQAIHAHR 3327

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  766 AGATHLIlPTALMSIL---DPEQVNGIQAIGMGGEACPNA---VVENWADKVALYNMYGPTECTVTAL-----STRLRKG 834
Cdd:PRK12467 3328 ISIACFP-PAYLQQFAedaGGADCASLDIYVFGGEAVPPAafeQVKRKLKPRGLTNGYGPTEAVVTVTlwkcgGDAVCEA 3406

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  835 QPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAATlRIYRTGDK 914
Cdd:PRK12467 3407 PYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERF-------VADPFSGSGG-RLYRTGDL 3478

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  915 ARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYaTVKADSSTPEPAAVLIDV 994
Cdd:PRK12467 3479 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQH-PSVREAVVLARDGAGGKQLVAY-VVPADPQGDWRETLRDHL 3556

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  995 AKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP-PVLEANESDGEADNPLEADVLAIWRSVLNTP-LGVEDDFFRLGGDS 1072
Cdd:PRK12467 3557 AASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPdPDAKGSREYVAPRSEVEQQLAAIWADVLGVEqVGVTDNFFELGGDS 3636

                        1050      1060      1070
                  ....*....|....*....|....*....|..
gi 499404635 1073 ILSIQLTTRLR-SAGYACTVKDVFEAKSVRRL 1103
Cdd:PRK12467 3637 LLALQVLSRIRqSLGLKLSLRDLMSAPTIAEL 3668
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 546-1027 3.32e-130

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


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 416.27  E-value: 3.32e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd17652     1 PDAPAVVFGDE----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILggdgqqlaqwsaeqridltdpavveqwqdlpgdqppaipRHAQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd17652    77 AYMLADARPALLL---------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRG 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQ--AEQAGA---THLILPTALMSI 780
Cdd:cd17652   118 LANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEplADLLREhriTHVTLPPAALAA 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  781 LDPEQVNGIQAIGMGGEACPNAVVENWADKVALYNMYGPTECTVTALSTR-LRKGQPVTIGKPLIHIQALILDTAGQLCP 859
Cdd:cd17652   198 LPPDDLPDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGpLPGGGVPPIGRPVPGTRVYVLDARLRPVP 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  860 VGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNN--AGQGAatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRG 937
Cdd:cd17652   278 PGVPGELYIAGAGLARGYLNRPGLTAERF-------VADpfGAPGS---RMYRTGDLARWRADGQLEFLGRADDQVKIRG 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  938 YRIEPGEIEAQLAAvCPSLKQIKVIVAQVG-SRPALVAYAtVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLT 1016
Cdd:cd17652   348 FRIELGEVEAALTE-HPGVAEAVVVVRDDRpGDKRLVAYV-VPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLT 425

                         490
                  ....*....|.
gi 499404635 1017 PNGKLDMKQLP 1027
Cdd:cd17652   426 PNGKLDRRALP 436
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 563-961 3.23e-129

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: 412.04  E-value: 3.23e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   563 TYAELNRQANQLAHWLH-RQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD 641
Cdd:TIGR01733    1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   642 GQQLAQWSAEQRIDLTDPAVVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   722 QSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQAEQA------GATHLILPTALMSILDPEQVNGIQAIGM- 794
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaliaehPVTVLNLTPSLLALLAAALPPALASLRLv 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   795 --GGEACPNAVVENWADK---VALYNMYGPTECTVTALSTRL-----RKGQPVTIGKPLIHIQALILDTAGQLCPVGVPG 864
Cdd:TIGR01733  241 ilGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVdpddaPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   865 ELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAATLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGE 944
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERF-------VPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*..
gi 499404635   945 IEAQLAAvCPSLKQIKV 961
Cdd:TIGR01733  394 IEAALLR-HPGVREAVV 409
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 73-498 9.65e-129

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: 411.75  E-value: 9.65e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVnEQGKGEQRIDAYQPFVIQHD 152
Cdd:cd19531     3 PLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE-VDGEPVQVILPPLPLPLPVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:cd19531    82 DLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PYPVETTQLNYIDYAHW----FNSDSF---LDYhnefkpfWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLW 305
Cdd:cd19531   162 PSPLPPLPIQYADYAVWqrewLQGEVLerqLAY-------WREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELT 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  306 DKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCR 385
Cdd:cd19531   235 AALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVR 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  386 EQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVDFNDLIPGCDAAEETSPVLPAKTDISVKVTELMGEVR 465
Cdd:cd19531   315 ETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLR 394

                         410       420       430
                  ....*....|....*....|....*....|...
gi 499404635  466 LDWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19531   395 GSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 536-1026 4.02e-124

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: 400.81  E-value: 4.02e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVP 615
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDR----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  616 LDPDYPPERLRHIITDANLSVIlggdgqqLAQWSAEQRIDLTDPAVVEQWQDLPGDQ-PPAIPRHAQQLAQVIYTSGSTG 694
Cdd:cd12117    77 LDPELPAERLAFMLADAGAKVL-------LTDRSLAGRAGGLEVAVVIDEALDAGPAgNPAVPVSPDDLAYVMYTSGSTG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  695 LPKGVMIEHGSLINLLDDhRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAF---GEPNDRAIMQA--EQAGAT 769
Cdd:cd12117   150 RPKGVAVTHRGVVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLapkGTLLDPDALGAliAEEGVT 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  770 HLILPTALMSIL---DPEQVNGIQAIGMGGEACP----NAVVENWADkVALYNMYGPTECTVTALSTRLRKGQPVT---- 838
Cdd:cd12117   229 VLWLTAALFNQLadeDPECFAGLRELLTGGEVVSpphvRRVLAACPG-LRLVNGYGPTENTTFTTSHVVTELDEVAgsip 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  839 IGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAAtlRIYRTGDKARLL 918
Cdd:cd12117   308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERF-------VADPFGPGE--RLYRTGDLARWL 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  919 NNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIV-AQVGSRPALVAYATVKAdssTPEPAAVLIDVAKY 997
Cdd:cd12117   379 PDGRLEFLGRIDDQVKIRGFRIELGEIEAALRA-HPGVREAVVVVrEDAGGDKRLVAYVVAEG---ALDAAELRAFLRER 454

                         490       500
                  ....*....|....*....|....*....
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd12117   455 LPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 538-1027 3.89e-122

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: 395.56  E-value: 3.89e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:cd17651     1 FERQAARTPDAPALVAEGR----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  618 PDYPPERLRHIITDANLSVILGgdgQQLAQWSAEQRIDLTDPAVVEQWQDLPGDqPPAIPRHAQQLAQVIYTSGSTGLPK 697
Cdd:cd17651    77 PAYPAERLAFMLADAGPVLVLT---HPALAGELAVELVAVTLLDQPGAAAGADA-EPDPALDADDLAYVIYTSGSTGRPK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  698 GVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFgePNDRAIMQAE-------QAGATH 770
Cdd:cd17651   153 GVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL--PPEEVRTDPPalaawldEQRISR 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  771 LILPTALMSILDPEQVNG------IQAIGMGGEA--CPNAVVENWADK--VALYNMYGPTECTV-TALSTR---LRKGQP 836
Cdd:cd17651   231 VFLPTVALRALAEHGRPLgvrlaaLRYLLTGGEQlvLTEDLREFCAGLpgLRLHNHYGPTETHVvTALSLPgdpAAWPAP 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  837 VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDVNNAGQgaatlRIYRTGDKAR 916
Cdd:cd17651   311 PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERF----VPDPFVPGA-----RMYRTGDLAR 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  917 LLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIV-AQVGSRPALVAYATVKADSStPEPAAVLIDVA 995
Cdd:cd17651   382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALAR-HPGVREAVVLArEDRPGEKRLVAYVVGDPEAP-VDAAELRAALA 459

                         490       500       510
                  ....*....|....*....|....*....|..
gi 499404635  996 KYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17651   460 THLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 535-1026 1.25e-121

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: 393.95  E-value: 1.25e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  535 TDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYV 614
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGR----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  615 PLDPDYPPERLRHIITDANLSVILGGDGQqlaqwsAEQRIDLTDPAVVEQWQDL-PGDQPPAIPRHAQQLAQVIYTSGST 693
Cdd:cd17646    77 PLDPGYPADRLAYMLADAGPAVVLTTADL------AARLPAGGDVALLGDEALAaPPATPPLVPPRPDNLAYVIYTSGST 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  694 GLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEQA 766
Cdd:cd17646   151 GRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHrdpaylaALIREHGV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  767 GATHLIlPTALMSIL---DPEQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECTVTALSTRLRKGQ---PVT 838
Cdd:cd17646   231 TTCHFV-PSMLRVFLaepAAGSCASLRRVFCSGEALPPELAARFLALpgAELHNLYGPTEAAIDVTHWPVRGPAetpSVP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  839 IGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNA-GQGAatlRIYRTGDKARL 917
Cdd:cd17646   310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERF-------VPDPfGPGS---RMYRTGDLARW 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  918 LNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIV-AQVGSRPALVAYATVKADSSTPEPAAVLIDVAK 996
Cdd:cd17646   380 RPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAA-HPAVTHAVVVArAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAE 458

                         490       500       510
                  ....*....|....*....|....*....|
gi 499404635  997 YLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd17646   459 RLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 534-1026 1.65e-120

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: 390.36  E-value: 1.65e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  534 VTDVIEAVAQRDPQQLAI-AFDGEprtdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:cd05918     1 VHDLIEERARSQPDAPAVcAWDGS-----LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRHIITDANLSVILggdgqqlaqwsaeqridlTDpavveqwqdlpgdqppaiprHAQQLAQVIYTSGS 692
Cdd:cd05918    76 FVPLDPSHPLQRLQEILQDTGAKVVL------------------TS--------------------SPSDAAYVIFTSGS 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  693 TGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFgePNDRAIMQ-----AEQAG 767
Cdd:cd05918   118 TGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNdlagfINRLR 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  768 ATHLILPTALMSILDPEQVNGIQAIGMGGEACPNAVVENWADKVALYNMYGPTECTV-TALSTRLRKGQPVTIGKPL--- 843
Cdd:cd05918   196 VTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIaATVSPVVPSTDPRNIGRPLgat 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  844 IHIqaLILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF-EHITLNDVNNAGQGAatlRIYRTGDKARLLNNGD 922
Cdd:cd05918   276 CWV--VDPDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiEDPAWLKQEGSGRGR---RLYRTGDLVRYNPDGS 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  923 YEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIV---AQVGSRPALVAYATVKADSSTP--------EPAAVL 991
Cdd:cd05918   351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSgdgdslflEPSDEF 430

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 499404635  992 IDVAKY--------LPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05918   431 RALVAElrsklrqrLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 546-1026 1.67e-119

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: 387.03  E-value: 1.67e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd12116     1 PDATAVRDDDR----SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILGGDGqqlaqwsAEQRIDLTDPAV--VEQWQDLPGDQPPAiPRHAQQLAQVIYTSGSTGLPKGVMIEH 703
Cdd:cd12116    77 RYILEDAEPALVLTDDA-------LPDRLPAGLPVLllALAAAAAAPAAPRT-PVSPDDLAYVIYTSGSTGRPKGVVVSH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  704 GSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFgepndraimqaeqAGATHLILPTALMSILDP 783
Cdd:cd12116   149 RNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVI-------------APRETQRDPEALARLIEA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  784 EQVNGIQAI----------------GM----GGEACPNAVVENWADKVA-LYNMYGPTECTVTALSTRLRKGQ-PVTIGK 841
Cdd:cd12116   216 HSITVMQATpatwrmlldagwqgraGLtalcGGEALPPDLAARLLSRVGsLWNLYGPTETTIWSTAARVTAAAgPIPIGR 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  842 PLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAATlRIYRTGDKARLLNNG 921
Cdd:cd12116   296 PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERF-------VPDPFAGPGS-RLYRTGDLVRRRADG 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  922 DYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVKaDSSTPEPAAVLIDVAKYLPEY 1001
Cdd:cd12116   368 RLEYLGRADGQVKIRGHRIELGEIEAALAAH-PGVAQAAVVVREDGGDRRLVAYVVLK-AGAAPDAAALRAHLRATLPAY 445

                         490       500
                  ....*....|....*....|....*
gi 499404635 1002 MVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd12116   446 MVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 538-1027 1.75e-117

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: 382.06  E-value: 1.75e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:cd17655     3 FEEQAEKTPDHTAVVFEDQ----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  618 PDYPPERLRHIITDANLSVILgGDGQQLAQWSAEQRIDLTDPavvEQWQDLPGDQPPaIPRHAQQLAQVIYTSGSTGLPK 697
Cdd:cd17655    79 PDYPEERIQYILEDSGADILL-TQSHLQPPIAFIGLIDLLDE---DTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  698 GVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA-----EQAGATHLI 772
Cdd:cd17655   154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQAltqyiRQNRITIID 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  773 LPTALMSILDPEQVNG---IQAIGMGGEACPNAVVENW----ADKVALYNMYGPTECTVTA----LSTRLRKGQPVTIGK 841
Cdd:cd17655   234 LTPAHLKLLDAADDSEglsLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDAsiyqYEPETDQQVSVPIGK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  842 PLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDVNNAGQgaatlRIYRTGDKARLLNNG 921
Cdd:cd17655   314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKF----VDDPFVPGE-----RMYRTGDLARWLPDG 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  922 DYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVA--QVGSrPALVAYATVKADSSTpepAAVLIDVAKYLP 999
Cdd:cd17655   385 NIEFLGRIDHQVKIRGYRIELGEIEARLLQH-PDIKEAVVIARkdEQGQ-NYLCAYIVSEKELPV---AQLREFLARELP 459

                         490       500
                  ....*....|....*....|....*...
gi 499404635 1000 EYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17655   460 DYMIPSYFIKLDEIPLTPNGKVDRKALP 487
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 546-1027 6.89e-116

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: 375.94  E-value: 6.89e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd17649     1 PDAVALVFGDQ----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILGgdgqqlaqwsaeqridltdpavveqwqdlpgdqppaipRHAQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd17649    77 RYMLEDSGAGLLLT--------------------------------------HHPRQLAYVIYTSGSTGTPKGVAVSHGP 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPN-----DRAIMQAEQAGATHLILPTA---- 776
Cdd:cd17649   119 LAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwasaDELAEMVRELGVTVLDLPPAylqq 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  777 ---LMSILDPEQVNGIQAIGMGGEACPNAVVENW-ADKVALYNMYGPTECTVTAL----STRLRKGQP-VTIGKPLIHIQ 847
Cdd:cd17649   199 laeEADRTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLvwkcEAGAARAGAsMPIGRPLGGRS 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  848 ALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAgQGAATLRIYRTGDKARLLNNGDYEYCG 927
Cdd:cd17649   279 AYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERF-------VPDP-FGAPGSRLYRTGDLARWRDDGVIEYLG 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  928 RIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVKADSSTPE-PAAVLIDVAKYLPEYMVPFR 1006
Cdd:cd17649   351 RVDHQVKIRGFRIELGEIEAALLEH-PGVREAAVVALDGAGGKQLVAYVVLRAAAAQPElRAQLRTALRASLPDYMVPAH 429

                         490       500
                  ....*....|....*....|.
gi 499404635 1007 LMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17649   430 LVFLARLPLTPNGKLDRKALP 450
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 536-1026 2.34e-114

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


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 370.87  E-value: 2.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAVAQRDPQQLAIafdgEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVP 615
Cdd:cd17653     1 DAFERIAAAHPDAVAV----ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  616 LDPDYPPERLRHIITDANLSVILGGDGQQlaqwsaeqridltdpavveqwqdlpgdqppaiprhaqQLAQVIYTSGSTGL 695
Cdd:cd17653    77 LDAKLPSARIQAILRTSGATLLLTTDSPD-------------------------------------DLAYIIFTSGSTGI 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  696 PKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQAEQAGATHlILPT 775
Cdd:cd17653   120 PKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTVDALM-STPS 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  776 ALmSILDPEQVNGIQAIGMGGEACPNAVVENWADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAG 855
Cdd:cd17653   199 IL-STLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADL 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  856 QLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNDvnnaGQgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKL 935
Cdd:cd17653   278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWP----GS-----RMYRTGDYGRWTEDGGLEFLGREDNQVKV 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  936 RGYRIEPGEIEAQLAAVCPSLKQIKVIVaqvgSRPALVAYATvkadsstpePAAVLID-----VAKYLPEYMVPFRLMLL 1010
Cdd:cd17653   349 RGFRINLEEIEEVVLQSQPEVTQAAAIV----VNGRLVAFVT---------PETVDVDglrseLAKHLPSYAVPDRIIAL 415

                         490
                  ....*....|....*.
gi 499404635 1011 EDMPLTPNGKLDMKQL 1026
Cdd:cd17653   416 DSFPLTANGKVDRKAL 431
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 536-1026 5.17e-110

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: 358.94  E-value: 5.17e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAVAQRDPQQLAIAfDGEPRtdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVP 615
Cdd:cd12115     3 DLVEAQAARTPDAIALV-CGDES---LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  616 LDPDYPPERLRHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGL 695
Cdd:cd12115    79 LDPAYPPERLRFILEDAQARLVL------------------TDP---------------------DDLAYVIYTSGSTGR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  696 PKGVMIEHGSLINLLDDHRDriDFTPQ--STMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEpNDRAIMQAEQAGATHLI- 772
Cdd:cd12115   120 PKGVAIEHRNAAAFLQWAAA--AFSAEelAGVLASTSICFDLSVFELFGPLATGGKVVLAD-NVLALPDLPAAAEVTLIn 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  773 -LPTALMSILDPEQV-NGIQAIGMGGEACPNAVVENWADK---VALYNMYGPTECTVTALSTRLRKG--QPVTIGKPLIH 845
Cdd:cd12115   197 tVPSAAAELLRHDALpASVRVVNLAGEPLPRDLVQRLYARlqvERVVNLYGPSEDTTYSTVAPVPPGasGEVSIGRPLAN 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  846 IQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndVNNAGQGAatlRIYRTGDKARLLNNGDYEY 925
Cdd:cd12115   277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFL------PDPFGPGA---RLYRTGDLVRWRPDGLLEF 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  926 CGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQiKVIVAQVGS--RPALVAYATVKADSStPEPAAVLIDVAKYLPEYMV 1003
Cdd:cd12115   348 LGRADNQVKVRGFRIELGEIEAALRSI-PGVRE-AVVVAIGDAagERRLVAYIVAEPGAA-GLVEDLRRHLGTRLPAYMV 424

                         490       500
                  ....*....|....*....|...
gi 499404635 1004 PFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd12115   425 PSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 546-1026 2.47e-108

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: 354.31  E-value: 2.47e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd17643     1 PEAVAVVDEDR----RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd17643    77 AFILADSGPSLLL------------------TDP---------------------DDLAYVIYTSGSTGRPKGVVVSHAN 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQS--TMFNcmSLSFDAGNMTTLLPLSSGGTLAFgEPNDRAIMQAE------QAGATHL-ILPTA 776
Cdd:cd17643   118 VLALFAATQRWFGFNEDDvwTLFH--SYAFDFSVWEIWGALLHGGRLVV-VPYEVARSPEDfarllrDEGVTVLnQTPSA 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  777 ---LMSILD--PEQVNGIQAIGMGGEACPNAVVENWADKV-----ALYNMYGPTECTV-------TALSTRLRKGQPvtI 839
Cdd:cd17643   195 fyqLVEAADrdGRDPLALRYVIFGGEALEAAMLRPWAGRFgldrpQLVNMYGITETTVhvtfrplDAADLPAAAASP--I 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  840 GKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAgQGAATLRIYRTGDKARLLN 919
Cdd:cd17643   273 GRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERF-------VANP-FGGPGSRMYRTGDLARRLP 344

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  920 NGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGS-RPALVAYaTVKADSSTPEPAAVLIDVAKYL 998
Cdd:cd17643   345 DGELEYLGRADEQVKIRGFRIELGEIEAALAT-HPSVRDAAVIVREDEPgDTRLVAY-VVADDGAAADIAELRALLKELL 422

                         490       500
                  ....*....|....*....|....*...
gi 499404635  999 PEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd17643   423 PDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 539-1027 4.76e-105

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: 345.19  E-value: 4.76e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  539 EAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDP 618
Cdd:cd17644     7 EEQVERTPDAVAVVFEDQ----QLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  619 DYPPERLRHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGLPKG 698
Cdd:cd17644    83 NYPQERLTYILEDAQISVLL------------------TQP---------------------ENLAYVIYTSGSTGKPKG 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  699 VMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAF--GE--PNDRAIMQ-AEQAGATHLIL 773
Cdd:cd17644   124 VMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLrpEEmrSSLEDFVQyIQQWQLTVLSL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  774 PTA----LMSILDPEQ---VNGIQAIGMGGEACPNAVVENWA----DKVALYNMYGPTECTVTALSTRLRKGQP-----V 837
Cdd:cd17644   204 PPAywhlLVLELLLSTidlPSSLRLVIVGGEAVQPELVRQWQknvgNFIQLINVYGPTEATIAATVCRLTQLTErnitsV 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  838 TIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAATLRIYRTGDKARL 917
Cdd:cd17644   284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKF-------ISHPFNSSESERLYKTGDLARY 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  918 LNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVA--QVGSRpALVAYaTVKADSSTPEPAAVLIDVA 995
Cdd:cd17644   357 LPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQH-NDVKTAVVIVRedQPGNK-RLVAY-IVPHYEESPSTVELRQFLK 433

                         490       500       510
                  ....*....|....*....|....*....|..
gi 499404635  996 KYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17644   434 AKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
PRK05691 PRK05691
peptide synthase; Validated
 73-1085 6.98e-105

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 377.20  E-value: 6.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQRIDAYQPFVIQHD 152
Cdd:PRK05691 3259 PLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYL 3338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:PRK05691 3339 DWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGR 3418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PyPVETTQLNYIDYAHWFNSDSFldyhNEFKPFWVERLTGIPEVHSLPLDKP--RPAHQNSGGEVI---FSAINNDLWDK 307
Cdd:PRK05691 3419 E-AQLPVPPRYRDYIGWLQRQDL----AQARQWWQDNLRGFERPTPIPSDRPflREHAGDSGGMVVgdcYTRLDAADGAR 3493

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  308 FKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGFFVNTIVLRTQL-QDSQ--NFVDYLQ 382
Cdd:PRK05691 3494 LRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLpAAGQrcSVRQWLQ 3573

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  383 YCREQDLSAFDHQLYRFEALSEaigSDRTTAINPIFQVMLVYQ-AKVDFNDLipgcDAAEE---TSPVLPAKTDISVKVT 458
Cdd:PRK05691 3574 GLLDSNMELREYEYLPLVAIQE---CSELPKGQPLFDSLFVFEnAPVEVSVL----DRAQSlnaSSDSGRTHTNFPLTAV 3646

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  459 ELMGE-VRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVWHLPLMETDRFAAVLAETQQLPRSYPQPQLTVtDV 537
Cdd:PRK05691 3647 CYPGDdLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPLEQSYV-RL 3725

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:PRK05691 3726 FEAQVAAHPQRIAASCLDQ----QWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLD 3801

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  618 PDYPPERLRHIITDANLSVILggdgqqLAQWSAEQRIDLTDpAVVEQ-------WQDLPGDQP----PAIPRHAQQLAQV 686
Cdd:PRK05691 3802 PGLPAQRLQRIIELSRTPVLV------CSAACREQARALLD-ELGCAnrprllvWEEVQAGEVashnPGIYSGPDNLAYV 3874

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  687 IYTSGSTGLPKGVMIE-HGSLINLLD-------DHRDRIDFTPqstmfncmSLSFDAGNMTTLLPLSSGGTLAFgEPNDR 758
Cdd:PRK05691 3875 IYTSGSTGLPKGVMVEqRGMLNNQLSkvpylalSEADVIAQTA--------SQSFDISVWQFLAAPLFGARVEI-VPNAI 3945

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  759 A------IMQAEQAGATHL-ILPTALMSIL--DPEQVNGIQAIGMGGEACPNAVVENWADK---VALYNMYGPTECT--- 823
Cdd:PRK05691 3946 AhdpqglLAHVQAQGITVLeSVPSLIQGMLaeDRQALDGLRWMLPTGEAMPPELARQWLQRypqIGLVNAYGPAECSddv 4025

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  824 ----VTALSTRlrkGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF-EHITlndvnn 898
Cdd:PRK05691 4026 affrVDLASTR---GSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvPHPF------ 4096

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  899 agqGAATLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATv 978
Cdd:PRK05691 4097 ---GAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQ-AEVREAAVAVQEGVNGKHLVGYLV- 4171

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  979 kADSSTPEPAAVLIDVAKY----LPEYMVPFRLMLLEDMPLTPNGKLDMKQLpPVLEANESDGEA----DNPLEADVLAI 1050
Cdd:PRK05691 4172 -PHQTVLAQGALLERIKQRlraeLPDYMVPLHWLWLDRLPLNANGKLDRKAL-PALDIGQLQSQAylapRNELEQTLATI 4249

                        1050      1060      1070
                  ....*....|....*....|....*....|....*.
gi 499404635 1051 WRSVLNTP-LGVEDDFFRLGGDSILSIQLTTRLRSA 1085
Cdd:PRK05691 4250 WADVLKVErVGVHDNFFELGGHSLLATQIASRVQKA 4285
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 539-1027 1.39e-100

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: 331.44  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  539 EAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDP 618
Cdd:cd17645     5 EEQVERTPDHVAVVDRGQ----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  619 DYPPERLRHIITDANLSVILggdgqqlaqwsaeqridltdpavveqwqdlpgdqppaipRHAQQLAQVIYTSGSTGLPKG 698
Cdd:cd17645    81 DYPGERIAYMLADSSAKILL---------------------------------------TNPDDLAYVIYTSGSTGLPKG 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  699 VMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIMQA-----EQAGATHLIL 773
Cdd:cd17645   122 VMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDAlndyfNQEGITISFL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  774 PTALMSILDPEQVNGIQAIGMGGEACPNAVVENWAdkvaLYNMYGPTECTVTALSTRLRKG-QPVTIGKPLIHIQALILD 852
Cdd:cd17645   202 PTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYK----LVNNYGPTENTVVATSFEIDKPyANIPIGKPIDNTRVYILD 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  853 TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDVNNAGQgaatlRIYRTGDKARLLNNGDYEYCGRIDEQ 932
Cdd:cd17645   278 EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKF----IVHPFVPGE-----RMYRTGDLAKFLPDGNIEFLGRLDQQ 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  933 IKLRGYRIEPGEIEAQLAAVcPSLKQIKVI-VAQVGSRPALVAYATVKADSstpEPAAVLIDVAKYLPEYMVPFRLMLLE 1011
Cdd:cd17645   349 VKIRGYRIEPGEIEPFLMNH-PLIELAAVLaKEDADGRKYLVAYVTAPEEI---PHEELREWLKNDLPDYMIPTYFVHLK 424

                         490
                  ....*....|....*.
gi 499404635 1012 DMPLTPNGKLDMKQLP 1027
Cdd:cd17645   425 ALPLTANGKVDRKALP 440
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 534-1026 1.57e-98

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: 326.00  E-value: 1.57e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  534 VTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAY 613
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGR----RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  614 VPLDPDYPPERLRHIITDANLSVILGgdgqqlaqwsaeqridltdpavveqwqdlpgdqppaiprhaqqlAQVIYTSGST 693
Cdd:COG0318    77 VPLNPRLTAEELAYILEDSGARALVT--------------------------------------------ALILYTSGTT 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  694 GLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAG-NMTTLLPLSSGGTLAFGEPND-RAIMQA-EQAGATH 770
Cdd:COG0318   113 GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPRFDpERVLELiERERVTV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  771 LIL-PTALMSILD-----PEQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECTVTALSTRLRKGQ--PVTIG 840
Cdd:COG0318   193 LFGvPTMLARLLRhpefaRYDLSSLRLVVSGGAPLPPELLERFEERfgVRIVEGYGLTETSPVVTVNPEDPGErrPGSVG 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  841 KPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndvnnagqgaatlRIYRTGDKARLLNN 920
Cdd:COG0318   273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD----------------GWLRTGDLGRLDED 336

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  921 GDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI---VAQVGSRPALVAyatVKADSSTPEPAAVLIDVAKY 997
Cdd:COG0318   337 GYLYIVGRKKDMIISGGENVYPAEVEEVLAA-HPGVAEAAVVgvpDEKWGERVVAFV---VLRPGAELDAEELRAFLRER 412

                         490       500
                  ....*....|....*....|....*....
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:COG0318   413 LARYKVPRRVEFVDELPRTASGKIDRRAL 441
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 546-1026 7.41e-98

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: 324.99  E-value: 7.41e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd12114     1 PDATAVICGDG----TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILggdgqqLAQWSAEQRIDLTDPAVVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd12114    77 EAILADAGARLVL------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDR----AIMQA-EQAGATHLILPTALMSI 780
Cdd:cd12114   151 ALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRrdpaHWAELiERHGVTLWNSVPALLEM 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  781 L-----DPEQVN-GIQAIGMGGE----ACPNAVVENWADkVALYNMYGPTECTVTALSTRLRKGQP--VTI--GKPLIHI 846
Cdd:cd12114   231 LldvleAAQALLpSLRLVLLSGDwiplDLPARLRALAPD-ARLISLGGATEASIWSIYHPIDEVPPdwRSIpyGRPLANQ 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  847 QALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF-EHITLndvnnagqgaatLRIYRTGDKARLLNNGDYEY 925
Cdd:cd12114   310 RYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvTHPDG------------ERLYRTGDLGRYRPDGTLEF 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  926 CGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPF 1005
Cdd:cd12114   378 LGRRDGQVKVRGYRIELGEIEAALQAH-PGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPS 456

                         490       500
                  ....*....|....*....|.
gi 499404635 1006 RLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd12114   457 RVIALEALPLTANGKVDRAAL 477
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 73-498 1.49e-96

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: 319.37  E-value: 1.49e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGkGEQRI-DAYQpfviqh 151
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGG-PYQVVlPAAE------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  152 DDFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLA-CQN 230
Cdd:cd19540    76 ARPDLTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAArRAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  231 C----QPYPVEttqlnYIDYAHW--------FNSDSF----LDYhnefkpfWVERLTGIPEVHSLPLDKPRPAHQ-NSGG 293
Cdd:cd19540   156 RapdwAPLPVQ-----YADYALWqrellgdeDDPDSLaarqLAY-------WRETLAGLPEELELPTDRPRPAVAsYRGG 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  294 EVIFSaINNDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQD 373
Cdd:cd19540   224 TVEFT-IDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSG 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  374 SQNFVDYLQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ----AKVDFndliPGCDAAEETSPVLPA 449
Cdd:cd19540   303 DPTFAELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQntaaATLEL----PGLTVEPVPVDTGVA 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  450 KTDISVKVTELMGE------VRLDWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19540   379 KFDLSFTLTERRDAdgapagLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 542-1026 2.71e-96

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


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 319.19  E-value: 2.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQqlAIAFDGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYP 621
Cdd:cd05945     1 AAANPD--RPAVVEGGRT--LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  622 PERLRHIItdanlsvilggdgqqlaqwsaeqriDLTDPAVVEQWQDlpgdqppaiprhaqQLAQVIYTSGSTGLPKGVMI 701
Cdd:cd05945    77 AERIREIL-------------------------DAAKPALLIADGD--------------DNAYIIFTSGSTGRPKGVQI 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  702 EHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAfgePNDRAIMQAEQAGATHL---------- 771
Cdd:cd05945   118 SHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLV---PVPRDATADPKQLFRFLaehgitvwvs 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  772 ---ILPTALMS-ILDPEQVNGIQAIGMGGEACPNAVVENW---ADKVALYNMYGPTECTVTALSTRLRKGQ-----PVTI 839
Cdd:cd05945   195 tpsFAAMCLLSpTFTPESLPSLRHFLFCGEVLPHKTARALqqrFPDARIYNTYGPTEATVAVTYIEVTPEVldgydRLPI 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  840 GKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITlndvnnaGQGAatlriYRTGDKARLLN 919
Cdd:cd05945   275 GYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-------GQRA-----YRTGDLVRLEA 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  920 NGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVG-SRPALVAYATVKADSSTPEPAAVLIDVAKYL 998
Cdd:cd05945   343 DGLLFYRGRLDFQVKLNGYRIELEEIEAALRQ-VPGVKEAVVVPKYKGeKVTELIAFVVPKPGAEAGLTKAIKAELAERL 421

                         490       500
                  ....*....|....*....|....*...
gi 499404635  999 PEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05945   422 PPYMIPRRFVYLDELPLNANGKIDRKAL 449
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1126-1528 8.10e-96

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: 317.27  E-value: 8.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1126 EFALLPIQRWFMEQSLARPEHWNQAAMIQLPE-VDTERLVTMLQALMAQHDALRLGCDAEG----QRYLADVPCP-ALST 1199
Cdd:cd19534     1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQgLDPDALRQALRALVEHHDALRMRFRREDggwqQRIRGDVEELfRLEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1200 LDYRQL-GDDGLQQAFTALQSEFDPAQGRTMACALVRHHPQADTaLFLAFHHLVIDAVSWRILVDDLERLYL----GEPL 1274
Cdd:cd19534    81 VDLSSLaQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDR-LLLVIHHLVVDGVSWRILLEDLEAAYEqalaGEPI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1275 -LPKTSSYRQWGAALQHYATQHA--EQLTYWQAQEDGvDLTALlaAKDP---QGHASAAILTLDAKTTGQLVSEANRAFN 1348
Cdd:cd19534   160 pLPSKTSFQTWAELLAEYAQSPAllEELAYWRELPAA-DYWGL--PKDPeqtYGDARTVSFTLDEEETEALLQEANAAYR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1349 TDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIDPTLDVSRTVGWFTSTYPVCLQDKP--DWASLIQSSKEQLRQVP 1426
Cdd:cd19534   237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLRRIP 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1427 DKGVGFNPLRYHHPQGNS----LTLSPIVFNYLG-LSVQAAGTWRPVDVAPGCC--VSPGNKPAEVISLHGGITGGQLTL 1499
Cdd:cd19534   317 NKGIGYGILRYLTPEGTKrlafHPQPEISFNYLGqFDQGERDDALFVSAVGGGGsdIGPDTPRFALLDINAVVEGGQLVI 396

                         410       420       430
                  ....*....|....*....|....*....|....
gi 499404635 1500 -----RQVgcLNQRDSERLMTRLTENLRALTEAC 1528
Cdd:cd19534   397 tvsysRNM--YHEETIQQLADSYKEALEALIEHC 428
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 546-1027 3.51e-94

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: 313.57  E-value: 3.51e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFdGEPRtdtLTYAELNRQANQLAHWLHRQGLGE-QSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPER 624
Cdd:cd17648     1 PDRVAVVY-GDKR---LTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDER 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  625 LRHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGLPKGVMIEHG 704
Cdd:cd17648    77 IQFILEDTGARVVI------------------TNS---------------------TDLAYAIYTSGTTGKPKGVLVEHG 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  705 SLINLLDDHRDRIDFTPQSTMfNCMSLS---FDAGNMTTLLPLSSGGTLAFGEPNDR-------AIMQAEqaGATHLILP 774
Cdd:cd17648   118 SVVNLRTSLSERYFGRDNGDE-AVLFFSnyvFDFFVEQMTLALLNGQKLVVPPDEMRfdpdrfyAYINRE--KVTYLSGT 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  775 TALMSILDPEQVNGIQAIGMGGEACPNAVVENWADKVA--LYNMYGPTECTVTALSTRLRKGQPV--TIGKPLIHIQALI 850
Cdd:cd17648   195 PSVLQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAglIINAYGPTETTVTNHKRFFPGDQRFdkSLGRPVRNTKCYV 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQGAATL------RIYRTGDKARLLNNGDYE 924
Cdd:cd17648   275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERF-------LPNPFQTEQERargrnaRLYKTGDLVRWLPSGELE 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  925 YCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI------VAQVGSRPALVAYATvkADSSTPEPAAVLIDVAKYL 998
Cdd:cd17648   348 YLGRNDFQVKIRGQRIEPGEVEAALAS-YPGVRECAVVakedasQAQSRIQKYLVGYYL--PEPGHVPESDLLSFLRAKL 424

                         490       500
                  ....*....|....*....|....*....
gi 499404635  999 PEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17648   425 PRYMVPARLVRLEGIPVTINGKLDVRALP 453
AMP-binding pfam00501
AMP-binding enzyme;
538-936 5.15e-92

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 305.78  E-value: 5.15e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   538 IEAVAQRDPQQLAIAFDGeprTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:pfam00501    1 LERQAARTPDKTALEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   618 PDYPPERLRHIITDANLSVILGGDGQQLAQ----WSAEQRIDLT---DPAVVEQWQDLPGD-------QPPAIPRHAQQL 683
Cdd:pfam00501   78 PRLPAEELAYILEDSGAKVLITDDALKLEElleaLGKLEVVKLVlvlDRDPVLKEEPLPEEakpadvpPPPPPPPDPDDL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   684 AQVIYTSGSTGLPKGVMIEHGSLINLLDDH----RDRIDFTPQSTMFNCMSLSFDAG-NMTTLLPLSSGGTLAFGEPNDR 758
Cdd:pfam00501  158 AYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPA 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   759 AIMQA-----EQAGATHLIL-PTALMSILD-----PEQVNGIQAIGMGGEACPNAVVENWADKV--ALYNMYGPTECTVT 825
Cdd:pfam00501  238 LDPAAlleliERYKVTVLYGvPTLLNMLLEagapkRALLSSLRLVLSGGAPLPPELARRFRELFggALVNGYGLTETTGV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   826 ALSTRLRKGQPV---TIGKPLIHIQALILDTA-GQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnagq 901
Cdd:pfam00501  318 VTTPLPLDEDLRslgSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD------------ 385

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 499404635   902 gaaTLRIYRTGDKARLLNNGDYEYCGRIDEQIKLR 936
Cdd:pfam00501  386 ---EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 546-1027 8.12e-90

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: 301.70  E-value: 8.12e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd17656     2 PDAVAVVFENQ----KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVIlggdgqqLAQWSAEQRIDLTDPAVVEQWQDLP--GDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEH 703
Cdd:cd17656    78 IYIMLDSGVRVV-------LTQRHLKSKLSFNKSTILLEDPSISqeDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  704 GSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAF-GEPNDRAIMQAEQAGATH----LILPTALM 778
Cdd:cd17656   151 KNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIiREETKRDVEQLFDLVKRHnievVFLPVAFL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  779 SILDPEQ------VNGIQAIGMGGE--ACPNAVVENWADK-VALYNMYGPTECTVTALSTrLRKGQPVT----IGKPLIH 845
Cdd:cd17656   231 KFIFSERefinrfPTCVKHIITAGEqlVITNEFKEMLHEHnVHLHNHYGPSETHVVTTYT-INPEAEIPelppIGKPISN 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  846 IQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndvnNAGQGAATLRIYRTGDKARLLNNGDYEY 925
Cdd:cd17656   310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKF---------FPDPFDPNERMYRTGDLARYLPDGNIEF 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  926 CGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGSRPA-LVAYATVKADSSTPEPAAVLidvAKYLPEYMVP 1004
Cdd:cd17656   381 LGRADHQVKIRGYRIELGEIEAQLLN-HPGVSEAVVLDKADDKGEKyLCAYFVMEQELNISQLREYL---AKQLPEYMIP 456

                         490       500
                  ....*....|....*....|...
gi 499404635 1005 FRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17656   457 SFFVPLDQLPLTPNGKVDRKALP 479
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 73-499 2.29e-89

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: 299.63  E-value: 2.29e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635    73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQRIDAYQPFVIQHD 152
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPFELEII 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:pfam00668   86 DISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   233 PYPVETTQlNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIPEVHSLPLDKPRPAHQN-SGGEVIFSaINNDLWDKFKRL 311
Cdd:pfam00668  166 PLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSfKGDRLSFT-LDEDTEELLRKL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   312 CQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLSA 391
Cdd:pfam00668  244 AKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSA 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   392 FDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ------AKVDFNDLiPGCDAAEETSPVLPAKTDISVKVTELMGEVR 465
Cdd:pfam00668  324 EPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQnylgqdSQEEEFQL-SELDLSVSSVIEEEAKYDLSLTASERGGGLT 402

                          410       420       430
                   ....*....|....*....|....*....|....
gi 499404635   466 LDWLFATALFERQTIQYYADRFIRLIEAVVENPE 499
Cdd:pfam00668  403 IKIDYNTSLFDEETIERFAEHFKELLEQAIAHPS 436
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 546-1026 2.46e-88

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: 296.30  E-value: 2.46e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDgeprTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL 625
Cdd:cd17650     1 PDAIAVSDA----TRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 RHIITDANLSVILggdgqqlaqwsaeqridlTDPavveqwqdlpgdqppaiprhaQQLAQVIYTSGSTGLPKGVMIEHGS 705
Cdd:cd17650    77 QYMLEDSGAKLLL------------------TQP---------------------EDLAYVIYTSGTTGKPKGVMVEHRN 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  706 LINLLDDHRDRIDFTPQST-MFNCMSLSFDAGNMTTLLPLSSGGTLAFGePNDraiMQAEQAGATHLIL----------P 774
Cdd:cd17650   118 VAHAAHAWRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVIC-PDE---VKLDPAALYDLILksritlmestP 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  775 T---ALMSILDPEQVN--GIQAIGMGGEACPNA----VVENWADKVALYNMYGPTECTVTalST-------RLRKGQPVT 838
Cdd:cd17650   194 AlirPVMAYVYRNGLDlsAMRLLIVGSDGCKAQdfktLAARFGQGMRIINSYGVTEATID--STyyeegrdPLGDSANVP 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  839 IGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLndvnnagqgAATLRIYRTGDKARLL 918
Cdd:cd17650   272 IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF---------APGERMYRTGDLARWR 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  919 NNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPA-LVAYATVKADSSTPEPAAVLidvAKY 997
Cdd:cd17650   343 ADGNVELLGRVDHQVKIRGFRIELGEIESQLARH-PAIDEAVVAVREDKGGEArLCAYVVAAATLNTAELRAFL---AKE 418

                         490       500
                  ....*....|....*....|....*....
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd17650   419 LPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1566-1982 1.37e-83

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: 281.78  E-value: 1.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALESECAS--IQVIVKQADLPFYY 1643
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGepLQVVLKDRKLPWRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1644 QDL--MQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQG 1721
Cdd:cd19543    82 LDLshLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 QvlmhgdAPAIQVDRAYVDYARHAVAQ-QSAVDAFWQQRqslLAQTNDVSMLFAAAGKRADLSQhltqiEPQVTSVSLNE 1800
Cdd:cd19543   162 Q------PPSLPPVRPYRDYIAWLQRQdKEAAEAYWREY---LAGFEEPTPLPKELPADADGSY-----EPGEVSFELSA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1801 KDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSVGLYINSLPLALSWQQPVSLQQH 1880
Cdd:cd19543   228 ELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLEL 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1881 LVQLQNELMAMNQHATQSLI---ALTAGRSRLFNSLFIYENYPDAKAEQGQRADDPHRLYPEfsAAYEKVEMPLNLVVRE 1957
Cdd:cd19543   308 LKDLQAQQLELREHEYVPLYeiqAWSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRITDV--SAEEQTNYPLTVVAIP 385

                         410       420
                  ....*....|....*....|....*
gi 499404635 1958 QSGcMLLRFEFDADALDSAQARRVL 1982
Cdd:cd19543   386 GEE-LTIKLSYDAEVFDEATIERLL 409
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 73-498 5.18e-83

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: 280.30  E-value: 5.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEqgkGEqridAYQpfVIQHD 152
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEED---GV----PYQ--LILEE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLP----EAEREgRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLAC 228
Cdd:cd19538    74 DEATPKleikEVDEE-ELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRAR 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  229 QNCQPYPVETTQLNYIDYAHW----FNSDSFLDYHNEFK-PFWVERLTGIPEVHSLPLDKPRPA-HQNSGGEVIFSaINN 302
Cdd:cd19538   153 CKGEAPELAPLPVQYADYALWqqelLGDESDPDSLIARQlAYWKKQLAGLPDEIELPTDYPRPAeSSYEGGTLTFE-IDS 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  303 DLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQ 382
Cdd:cd19538   232 ELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLE 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  383 YCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVDFNDLIPGCDAAEETSPVLPAKTDISVKVTELMG 462
Cdd:cd19538   312 RVKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQYN 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 499404635  463 -------EVRLDwlFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19538   392 dgtpngiEGFIE--YRTDLFDHETIEALAQRYLLLLESAVENP 432
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 73-498 1.13e-75

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: 258.85  E-value: 1.13e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQRIDAYQPFVIQHD 152
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLlPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:cd19539    83 DLSD-PDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PYPVETTQLNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIpEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKRLC 312
Cdd:cd19539   162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  313 QRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLSAF 392
Cdd:cd19539   241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  393 DHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVDFNDLIPGCDAAEETSPVLP-AKTDISVKVTELMGEVRLDWLFA 471
Cdd:cd19539   321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDgAKFDLNLTVTEEGTGLRGSLGYA 400

                         410       420
                  ....*....|....*....|....*..
gi 499404635  472 TALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19539   401 TSLFDEETIQGFLADYLQVLRQLLANP 427
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
538-1026 7.03e-67

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 235.95  E-value: 7.03e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGE----KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  618 PDYPPERLRHIITDANLSVILGgdgqqlaqwSAEQRIDLTDPAVV--EQWQDLPGDQPPAIPRHAQQLAQV---IYTSGS 692
Cdd:PRK04813   84 VSSPAERIEMIIEVAKPSLIIA---------TEELPLEILGIPVItlDELKDIFATGNPYDFDHAVKGDDNyyiIFTSGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  693 TGLPKGVMIEHGSLIN----LLDDHRdridfTPQ-STMFNCMSLSFDAGNMTTLLPLSSGGTLaFGEPNDrAIMQAEQAG 767
Cdd:PRK04813  155 TGKPKGVQISHDNLVSftnwMLEDFA-----LPEgPQFLNQAPYSFDLSVMDLYPTLASGGTL-VALPKD-MTANFKQLF 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  768 AThliLPT------------ALMSILDP----EQVNGIQAIGMGGEACPNAVVENWAD---KVALYNMYGPTECTVtALS 828
Cdd:PRK04813  228 ET---LPQlpinvwvstpsfADMCLLDPsfneEHLPNLTHFLFCGEELPHKTAKKLLErfpSATIYNTYGPTEATV-AVT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  829 ----TR--LRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHItlndvnnAGQg 902
Cdd:PRK04813  304 sieiTDemLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF-------DGQ- 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  903 aatlRIYRTGDKARLlNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL--------AAVCPSLKQIKVIvaqvgsrpALVA 974
Cdd:PRK04813  376 ----PAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLrqssyvesAVVVPYNKDHKVQ--------YLIA 442

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  975 YATVKADSSTPEPA---AVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK04813  443 YVVPKEEDFEREFEltkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 73-498 1.62e-63

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: 223.83  E-value: 1.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVvNEQGKGEQRI-DAYQPFVIQH 151
Cdd:cd19066     3 PLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVVlDKTVRFRIEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  152 DDFSLLpeAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNC 231
Cdd:cd19066    82 IDLRNL--ADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  232 QPYPVETTqLNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIPEVHSLPLDKPRPA-HQNSGGEVIFSaINNDLWDKFKR 310
Cdd:cd19066   160 KPTLPPPV-GSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQvASYEVLTLEFF-LRSEETKRLRE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  311 LCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLS 390
Cdd:cd19066   238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSRE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  391 AFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVDFNDLIPGCDAAEET-SPVLPAKTDISVKVTELM-GEVRLDW 468
Cdd:cd19066   318 AIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVyTSSEGTVFDLDLEASEDPdGDLLLRL 397

                         410       420       430
                  ....*....|....*....|....*....|
gi 499404635  469 LFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19066   398 EYSRGVYDERTIDRFAERYMTALRQLIENP 427
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 682-1022 3.21e-63

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: 219.46  E-value: 3.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  682 QLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPND--RA 759
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDpeAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  760 IMQAEQAGATHLIL-PTALMSILDPEQVNG-----IQAIGMGGEACPNAVVENWAD--KVALYNMYGPTECTVTALSTRL 831
Cdd:cd04433    81 LELIEREKVTILLGvPTLLARLLKAPESAGydlssLRALVSGGAPLPPELLERFEEapGIKLVNGYGLTETGGTVATGPP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  832 RKG--QPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnagQGAatlriY 909
Cdd:cd04433   161 DDDarKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDE-----------DGW-----Y 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  910 RTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIV---AQVGSRPALVayaTVKADSSTPE 986
Cdd:cd04433   225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVGvpdPEWGERVVAV---VVLRPGADLD 300

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 499404635  987 PAAvLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:cd04433   301 AEE-LRAhVRERLAPYKVPRRVVFVDALPRTASGKID 336
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 73-498 1.32e-62

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: 220.92  E-value: 1.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQRIDAYQPFVIQHD 152
Cdd:cd19543     3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWREL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:cd19543    83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PYPVETTQlNYIDYAHWfnsdsfLDYHN--EFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKR 310
Cdd:cd19543   163 PPSLPPVR-PYRDYIAW------LQRQDkeAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  311 LCQRYN-TSNFIgLHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQ 387
Cdd:cd19543   236 LARQHGvTLNTV-VQGAWALLLSRYSGRDDVVFGTTVSGRpaELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  388 DLSAFDHQ---LYRFEALSEAIGsdrttainPIFQVMLVYQ--------------AKVDFNDLipgcDAAEETSpvlpak 450
Cdd:cd19543   315 QLELREHEyvpLYEIQAWSEGKQ--------ALFDHLLVFEnypvdesleeeqdeDGLRITDV----SAEEQTN------ 376

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635  451 TDISVKVTELmGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19543   377 YPLTVVAIPG-EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 538-1026 1.72e-62

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: 223.10  E-value: 1.72e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   538 IEAVAQRDPQQLAIAFdgepRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLD 617
Cdd:TIGR01734    6 IQAFAETYPQTIAYRY----QGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   618 PDYPPERLRHIITDANLSVILGgdgqqlaqwSAEQRIDLTDPAV--VEQWQDLPGDQPPAIPRHA---QQLAQVIYTSGS 692
Cdd:TIGR01734   82 TSIPSERIEMIIEAAGPELVIH---------TAELSIDAVGTQIitLSALEQAETSGGPVSFDHAvkgDDNYYIIYTSGS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   693 TGLPKGVMIEHGSLINLLDDHRDriDF-TPQSTMF-NCMSLSFDAGNMTTLLPLSSGGTLafgEPNDRAIMQA-----EQ 765
Cdd:TIGR01734  153 TGNPKGVQISHDNLVSFTNWMLA--DFpLSEGKQFlNQAPFSFDLSVMDLYPCLASGGTL---HCLDKDITNNfkllfEE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   766 AGATHLILPT-----ALMSILDP----EQVNGIQAIGMGGEACPNAVVENWAD---KVALYNMYGPTECTVTALSTRLRK 833
Cdd:TIGR01734  228 LPKTGLNVWVstpsfVDMCLLDPnfnqENYPHLTHFLFCGEELPVKTAKALLErfpKATIYNTYGPTEATVAVTSVKITQ 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   834 GQ-------PVTIGKPLIHIQalILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlNDVNNagqgaatL 906
Cdd:TIGR01734  308 EIldqyprlPIGFAKPDMNLF--IMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF-----FSHEG-------Q 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   907 RIYRTGDKARLlNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL--------AAVCPSL-KQIKVIvaqvgsrpALVAYAT 977
Cdd:TIGR01734  374 PAYRTGDAGTI-TDGQLFYQGRLDFQIKLHGYRIELEDIEFNLrqssyiesAVVVPKYnKDHKVE--------YLIAAIV 444

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 499404635   978 VKADSSTPE---PAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:TIGR01734  445 PETEDFEKEfqlTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 73-496 1.57e-60

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: 215.20  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQgKGEQRIDAYQPFVIQHD 152
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDD-FGEQQVLDDPSFHLIVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSllPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQ 232
Cdd:cd20483    82 DLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  233 PY-PVETTQLNYIDYAHWFN---SDSFLDYHNEFkpfWVERLTGIPEVHS-LPLDK-PRPAHQNSGGEVIFSAINNDLWD 306
Cdd:cd20483   160 DLaTVPPPPVQYIDFTLWHNallQSPLVQPLLDF---WKEKLEGIPDASKlLPFAKaERPPVKDYERSTVEATLDKELLA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  307 KFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCRE 386
Cdd:cd20483   237 RMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  387 QDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQ-----AKVDFNDLipgcDAAEETSPVLPAKTDISVKVTELM 461
Cdd:cd20483   317 TCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgkfPEYDTGDF----KFTDYDHYDIPTACDIALEAEEDP 392

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 499404635  462 -GEVRLDWLFATALFERQTIQYYADRFIRLIEAVVE 496
Cdd:cd20483   393 dGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVIR 428
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 71-498 1.87e-60

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: 214.63  E-value: 1.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   71 SGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVN-EQGKGEQRIDAYQPFVI 149
Cdd:cd19532     1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDpEDGEPMQGVLASSPLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  150 QHDDFSLLPEAERE-GRLQQQVkaeisrpFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFlac 228
Cdd:cd19532    81 EHVQISDEAEVEEEfERLKNHV-------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  229 qNCQPYPVETTQlnYIDYAhwfnSDSFLDYHN-EFKP---FWVERLTGIPEVhsLPL-----DKPRPAHQNSGGEVIFSA 299
Cdd:cd19532   151 -NGQPLLPPPLQ--YLDFA----ARQRQDYESgALDEdlaYWKSEFSTLPEP--LPLlpfakVKSRPPLTRYDTHTAERR 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  300 INNDLWDKFKRLCQRYNTSNFiglH---AVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQN 376
Cdd:cd19532   222 LDAALAARIKEASRKLRVTPF---HfylAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQT 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  377 FVDYLQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVdfNDLIPGCDAAEETSPVLPAKT--DIS 454
Cdd:cd19532   299 FADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGV--AESRPFGDCELEGEEFEDARTpyDLS 376

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 499404635  455 VKVTEL-MGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19532   377 LDIIDNpDGDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 74-318 1.72e-58

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 202.58  E-value: 1.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   74 LSSSQSGLWFIEQyeeQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVnEQGKGEQRIDAYQPFVIQHDD 153
Cdd:COG4908     1 LSPAQKRFLFLEP---GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVE-EDGEPVQRIDPDADLPLEVVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  154 FSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQNCQP 233
Cdd:COG4908    77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  234 YPVETTQLNYIDYAHWFNSDSFLDYHNEFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKRLCQ 313
Cdd:COG4908   157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236


                  ....*
gi 499404635  314 RYNTS 318
Cdd:COG4908   237 AHGAT 241
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 265-1085 8.02e-58

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: 221.48  E-value: 8.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   265 FWVERLTGiPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLwdkfkrLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGS 344
Cdd:TIGR03443    1 RWSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAE------VTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   345 PLAYRERPdiedvvgffvntIVLRTQLQDSQNFVD-YLQYCREQDLSAFDHQLyRFEALSEAIGSDRTTAINPIFqVMLV 423
Cdd:TIGR03443   74 SSNKSGRP------------FVLRLNITPELSFLQlYAKVSEEEKEGASDIGV-PFDELSEHIQAAKKLERTPPL-FRLA 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   424 YQAKVDFNDlipgcDAAEETSPvlpakTDISVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENPETDVW 503
Cdd:TIGR03443  140 FQDAPDNQQ-----TTYSTGST-----TDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   504 HLPLMETDrfaavlaETQQLPRsyPQPQL-------TVTDVIEAVAQRDPQQLAI-----AFDGEPRTDTLTYAELNRQA 571
Cdd:TIGR03443  210 KVSLITPS-------QKSLLPD--PTKDLdwsgfrgAIHDIFADNAEKHPDRTCVvetpsFLDPSSKTRSFTYKQINEAS 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   572 NQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPErlRHIITdanLSV------ILGGDGQQL 645
Cdd:TIGR03443  281 NILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPA--RQTIY---LSVakpralIVIEKAGTL 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   646 AQwSAEQRID------LTDPAVveQWQD---LPGDQPPA----IPRHAQQLAQ----VI----------YTSGSTGLPKG 698
Cdd:TIGR03443  356 DQ-LVRDYIDkelelrTEIPAL--ALQDdgsLVGGSLEGgetdVLAPYQALKDtptgVVvgpdsnptlsFTSGSEGIPKG 432

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   699 VMIEHGSLINLLDDHRDRIDFTPQS--TMfncmsLSFDAG-----NMTTllPLSSGGTLA------FGEPNDRA-IMQAE 764
Cdd:TIGR03443  433 VLGRHFSLAYYFPWMAKRFGLSENDkfTM-----LSGIAHdpiqrDMFT--PLFLGAQLLvptaddIGTPGRLAeWMAKY 505

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   765 QAGATHLilpTALMSildpeQVNGIQAIgmggEACP---NAV-------------VENWADKVALYNMYGPTEC------ 822
Cdd:TIGR03443  506 GATVTHL---TPAMG-----QLLSAQAT----TPIPslhHAFfvgdiltkrdclrLQTLAENVCIVNMYGTTETqravsy 573

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   823 ----TVTALSTRLRKGQPVT-IGKPLIHIQALIL---DTAgQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF------ 888
Cdd:TIGR03443  574 feipSRSSDSTFLKNLKDVMpAGKGMKNVQLLVVnrnDRT-QTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFvnnwfv 652

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   889 ---EHITLNDVNNAGQGAATL----RIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKV 961
Cdd:TIGR03443  653 dpsHWIDLDKENNKPEREFWLgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL 732

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   962 IVAQVGSRPALVAYATVKADSSTPEPAAVLIDVA-------------------------KYLPEYMVPFRLMLLEDMPLT 1016
Cdd:TIGR03443  733 VRRDKDEEPTLVSYIVPQDKSDELEEFKSEVDDEessdpvvkglikyrklikdireylkKKLPSYAIPTVIVPLKKLPLN 812

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1017 PNGKLDMKQLP-P-----VLEANESDGEAD----NPLEADVLAIWRSVL---NTPLGVEDDFFRLGGDSILSIQLTTRLR 1083
Cdd:TIGR03443  813 PNGKVDKPALPfPdtaqlAAVAKNRSASAAdeefTETEREIRDLWLELLpnrPATISPDDSFFDLGGHSILATRMIFELR 892


                   ..
gi 499404635  1084 SA 1085
Cdd:TIGR03443  893 KK 894
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 542-1022 3.92e-57

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


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 205.54  E-value: 3.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYP 621
Cdd:cd17631     5 ARRHPDRTALVFGGR----SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  622 PERLRHIITDANLSVILGgdgqqlaqwsaeqridltdpavveqwqdlpgdqppaiprhaqQLAQVIYTSGSTGLPKGVMI 701
Cdd:cd17631    81 PPEVAYILADSGAKVLFD------------------------------------------DLALLMYTSGTTGRPKGAML 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  702 EHGSLINLLDDHRDRIDFTPQSTMFNCMSLS-FDAGNMTTLLPLSSGGTL----AFgEPnDRAIMQAEQAGATHLIL-PT 775
Cdd:cd17631   119 THRNLLWNAVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVvilrKF-DP-ETVLDLIERHRVTSFFLvPT 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  776 ALMSILDPEQVN-----GIQAIGMGGEACPNAVVENWADK-VALYNMYGPTECT--VTALSTRLRKGQPVTIGKPLIHIQ 847
Cdd:cd17631   197 MIQALLQHPRFAttdlsSLRAVIYGGAPMPERLLRALQARgVKFVQGYGMTETSpgVTFLSPEDHRRKLGSAGRPVFFVE 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  848 ALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndvnnaGQgaatlriYRTGDKARLLNNGDYEYCG 927
Cdd:cd17631   277 VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD---------GW-------FHTGDLGRLDEDGYLYIVD 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  928 RIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIV---AQVGSRPALVAyatVKADSSTPEPAAVLIDVAKYLPEYMVP 1004
Cdd:cd17631   341 RKKDMIISGGENVYPAEVEDVLYEH-PAVAEVAVIGvpdEKWGEAVVAVV---VPRPGAELDEDELIAHCRERLARYKIP 416

                         490
                  ....*....|....*...
gi 499404635 1005 FRLMLLEDMPLTPNGKLD 1022
Cdd:cd17631   417 KSVEFVDALPRNATGKIL 434
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 536-1026 8.08e-56

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: 202.79  E-value: 8.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAVAQRDPQQLAIAFDGEPrtdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVP 615
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRK----LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  616 LDPDYPPERLRHIITDANLSVILggdgqqlaqwsaeqrIDLTDPAVVEQWQDLPGDQPpaipRHAQQLAQVIYTSGSTGL 695
Cdd:cd05936    79 LNPLYTPRELEHILNDSGAKALI---------------VAVSFTDLLAAGAPLGERVA----LTPEDVAVLQYTSGTTGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  696 PKGVMIEHGSLI-NLLD-DHRDRIDFTPQSTMFNCMSLsFDAGNMTT--LLPLSSGGTLAFgEPN--DRAIMQA-EQAGA 768
Cdd:cd05936   140 PKGAMLTHRNLVaNALQiKAWLEDLLEGDDVVLAALPL-FHVFGLTValLLPLALGATIVL-IPRfrPIGVLKEiRKHRV 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  769 THLI-LPTALMSIL-----DPEQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECT-VTALSTRLRKGQPVTI 839
Cdd:cd05936   218 TIFPgVPTMYIALLnapefKKRDFSSLRLCISGGAPLPVEVAERFEELtgVPIVEGYGLTETSpVVAVNPLDGPRKPGSI 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  840 GKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAgqgaatlriYRTGDKARLLN 919
Cdd:cd05936   298 GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-------VDGW---------LRTGDIGYMDE 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  920 NGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQikviVAQVG-----SRPALVAYAtVKADSSTPEPAAVLIDV 994
Cdd:cd05936   362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEH-PAVAE----AAVVGvpdpySGEAVKAFV-VLKEGASLTEEEIIAFC 435

                         490       500       510
                  ....*....|....*....|....*....|..
gi 499404635  995 AKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05936   436 REQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
542-1021 1.24e-55

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 204.96  E-value: 1.24e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAFDGEPRTD-TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDY 620
Cdd:COG0365    19 AEGRGDKVALIWEGEDGEErTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  621 PPERLRHIITDANLSVILGGDGQqlaqWSAEQRIDLT---DPAV-----VEQ------------------WQDLPGDQP- 673
Cdd:COG0365    99 GAEALADRIEDAEAKVLITADGG----LRGGKVIDLKekvDEALeelpsLEHvivvgrtgadvpmegdldWDELLAAASa 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  674 --PAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGS-LINLLDDHRDRIDFTPQSTMFnCMSlsfDAGNMTTLL-----PLS 745
Cdd:COG0365   175 efEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFW-CTA---DIGWATGHSyivygPLL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  746 SG-------GTLAFGEPnDRAIMQAEQAGATHLIL-PTALMSIL--DPEQVNG-----IQAIGMGGEACPNAVVENWAD- 809
Cdd:COG0365   251 NGatvvlyeGRPDFPDP-GRLWELIEKYGVTVFFTaPTAIRALMkaGDEPLKKydlssLRLLGSAGEPLNPEVWEWWYEa 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  810 -KVALYNMYGPTECTVTALSTRLrkGQPV---TIGKPLIHIQALILDTAGQLCPVGVPGELCLAG--LGLARGYLNQPQm 883
Cdd:COG0365   330 vGVPIVDGWGQTETGGIFISNLP--GLPVkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPE- 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  884 tasRFEHITLNDVNNagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL--------AAVCPS 955
Cdd:COG0365   407 ---RYRETYFGRFPG---------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALvshpavaeAAVVGV 474

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404635  956 LKQIKvivaqvGSRPalVAYATVKADSstpEPAAVLID-----VAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:COG0365   475 PDEIR------GQVV--KAFVVLKPGV---EPSDELAKelqahVREELGPYAYPREIEFVDELPKTRSGKI 534
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1124-1543 7.05e-53

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: 193.70  E-value: 7.05e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1124 EGEFALLPIQ--RWFMEQSLARPEHWNQAAMIQL-PEVDTERLVTMLQALMAQHDALRLGCDAEG-----QRYLADVPCP 1195
Cdd:pfam00668    2 QDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLtGELDPERLEKALQELINRHDALRTVFIRQEngepvQVILEERPFE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1196 aLSTLDYRQLGDDGLQQAFTA-----LQSEFDPAQGRTMACALVRHHPQADTaLFLAFHHLVIDAVSWRILVDDLERLYL 1270
Cdd:pfam00668   82 -LEIIDISDLSESEEEEAIEAfiqrdLQSPFDLEKGPLFRAGLFRIAENRHH-LLLSMHHIIVDGVSLGILLRDLADLYQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1271 ----GEPL-LPKTSSYRQWGAALQHYATQHA--EQLTYWQAQEDGVDLTALLA---AKDPQGHASAAILTLD-AKTTGQL 1339
Cdd:pfam00668  160 qllkGEPLpLPPKTPYKDYAEWLQQYLQSEDyqKDAAYWLEQLEGELPVLQLPkdyARPADRSFKGDRLSFTlDEDTEEL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1340 VSEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREaiDPtlDVSRTVGWFTSTYPVCLQDKP--DWASLIQS 1417
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP--SP--DIERMVGMFVNTLPLRIDPKGgkTFSELIKR 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1418 SKEQLRQV-PDKGVGFNPLRYHHPQGNSLTLSP-----IVF-NYLGLSVQaAGTWRPVDVAPGCCVSPGNKPAEVISLHG 1490
Cdd:pfam00668  316 VQEDLLSAePHQGYPFGDLVNDLRLPRDLSRHPlfdpmFSFqNYLGQDSQ-EEEFQLSELDLSVSSVIEEEAKYDLSLTA 394

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  1491 GITGGQLTLR---QVGCLNQRDSERLMTRLTENLRALTEACLTQLSHgvVFTPSDF 1543
Cdd:pfam00668  395 SERGGGLTIKidyNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSE--LDLLSDA 448
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 533-1026 5.17e-52

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: 192.69  E-value: 5.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   533 TVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDR----TLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   613 YVPLDPDYPPERLRHIITDANLSVILggdgqqlaqwSAEQRIDLTDPAVVE--------------------------QWQ 666
Cdd:TIGR03098   77 FVPINPLLKAEQVAHILADCNVRLLV----------TSSERLDLLHPALPGchdlrtliivgdpahaseghpgeepaSWP 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   667 DLP--GDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPL 744
Cdd:TIGR03098  147 KLLalGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAF 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   745 SSGGTLAFGE---PND--RAIMQAEQAGATHLILPTALMSILD--PEQVNGIQAIGMGGEACPNAVV---ENWADKVALY 814
Cdd:TIGR03098  227 YVGATVVLHDyllPRDvlKALEKHGITGLAAVPPLWAQLAQLDwpESAAPSLRYLTNSGGAMPRATLsrlRSFLPNARLF 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   815 NMYGPTEC-TVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITL 893
Cdd:TIGR03098  307 LMYGLTEAfRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPP 386

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   894 NDVNNAGQGAATLriyrTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVAQV--GSRPA 971
Cdd:TIGR03098  387 FPGELHLPELAVW----SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPtlGQAIV 462

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635   972 LVAYATVKAdssTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:TIGR03098  463 LVVTPPGGE---ELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 71-498 3.86e-51

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: 187.91  E-value: 3.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   71 SGPLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTrfVVNEQ-GKGEQRIDAYQPFVI 149
Cdd:cd20484     1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKS--VIEEEdGVPFQKIEPSKPLSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  150 QHDDFSLLPEAEREGRLQQQVKaeisRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQ 229
Cdd:cd20484    79 QEEDISSLKESEIIAYLREKAK----EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  230 NCQPYPVETTQLNYIDYAHWfnSDSFLDYHN--EFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDK 307
Cdd:cd20484   155 QGKQPTLASSPASYYDFVAW--EQDMLAGAEgeEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  308 FKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQ 387
Cdd:cd20484   233 IKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLT 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  388 DLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVMLVYQAKVDFNDLIpgcDAAEETSPVLP----------AKTDISVKV 457
Cdd:cd20484   313 VLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTSLQ---QFLAEYQDVLSiefvegihqeGEYELVLEV 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 499404635  458 TELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd20484   390 YEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1567-2005 9.03e-50

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: 184.46  E-value: 9.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1567 PLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALESECAS--IQVIVKQADLPFYYQ 1644
Cdd:pfam00668    6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGepVQVILEERPFELEII 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1645 DL--MQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQ 1722
Cdd:pfam00668   86 DIsdLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1723 VLmhgDAPAIQvdrAYVDYA-RHAVAQQSAV----DAFWQQRqslLAQTNDVSMLFAAAGKRADLSqhltqIEPQVTSVS 1797
Cdd:pfam00668  166 PL---PLPPKT---PYKDYAeWLQQYLQSEDyqkdAAYWLEQ---LEGELPVLQLPKDYARPADRS-----FKGDRLSFT 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1798 LNEKDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPveDVASSVGLYINSLPLALSWQQPVSL 1877
Cdd:pfam00668  232 LDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKGGKTF 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1878 QQHLVQLQNELMAMNQHA--------TQSLIALTAGRSRLFNSLFIYENYP--DAKAEQGQRADDPhrlYPEFSAAYEKV 1947
Cdd:pfam00668  310 SELIKRVQEDLLSAEPHQgypfgdlvNDLRLPRDLSRHPLFDPMFSFQNYLgqDSQEEEFQLSELD---LSVSSVIEEEA 386

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635  1948 EMPLNLVVREQSGCMLLRFEFDADALDSAqarrVLMRWHDEVVALVNSVPQQPAEIIG 2005
Cdd:pfam00668  387 KYDLSLTASERGGGLTIKIDYNTSLFDEE----TIERFAEHFKELLEQAIAHPSQPLS 440
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 73-498 2.19e-48

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: 179.49  E-value: 2.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEqGKGEQRIDAYQPFVIQHD 152
Cdd:cd19533     3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-GEPYQWIDPYTPVPIRHI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DFSllPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVkNLF----ADFKPAFLAC 228
Cdd:cd19533    82 DLS--GDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSF-ALFgqrvAEIYTALLKG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  229 QNCQPYPVETTQLNYIDYAHWFNSDSFLdyhnEFKPFWVERLTGIPEVHSLpldKPRPAHQNSGGEVIFSAINNDLWDKF 308
Cdd:cd19533   159 RPAPPAPFGSFLDLVEEEQAYRQSERFE----RDRAFWTEQFEDLPEPVSL---ARRAPGRSLAFLRRTAELPPELTRTL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  309 KRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQD 388
Cdd:cd19533   232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  389 LSAFDHQLYRFEALSEAIG--SDRTTAINPIFQVMlVYQAKVDFndliPGCDAAEETSPVLPAkTDISVKVTELM--GEV 464
Cdd:cd19533   312 RSLLRHQRYRYEDLRRDLGltGELHPLFGPTVNYM-PFDYGLDF----GGVVGLTHNLSSGPT-NDLSIFVYDRDdeSGL 385

                         410       420       430
                  ....*....|....*....|....*....|....
gi 499404635  465 RLDWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19533   386 RIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 563-1027 2.65e-48

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: 179.41  E-value: 2.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  563 TYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDAnlsvilggdG 642
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHS---------G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  643 QQLAqwsaeqridLTDPAvveqwqdlpgdqppaiprhaqqlaQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQ 722
Cdd:cd05934    76 AQLV---------VVDPA------------------------SILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  723 STMFNCMSLSF-DAGNMTTLLPLSSGGTLAFGE--PNDRAIMQAEQAGAT--HLI--LPTALMSilDPEQVNGIQA---I 792
Cdd:cd05934   123 DVYLTVLPLFHiNAQAVSVLAALSVGATLVLLPrfSASRFWSDVRRYGATvtNYLgaMLSYLLA--QPPSPDDRAHrlrA 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  793 GMGGEAcPNAVVENWADK--VALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCL-- 868
Cdd:cd05934   201 AYGAPN-PPELHEEFEERfgVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrg 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  869 -AGLGLARGYLNQPQMTASRFEHItlndvnnagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:cd05934   280 lRGWGFFKGYYNMPEATAEAMRNG----------------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLAAVcPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd05934   344 AILRH-PAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 571-1026 3.28e-48

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: 179.94  E-value: 3.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  571 ANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA----YVPLDPDYPPERLRHIITDANLSVILGGDGqqLA 646
Cdd:cd05922     3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAG--AA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  647 QWSAEQRIDLTDPAVV---EQWQDlPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQS 723
Cdd:cd05922    81 DRLRDALPASPDPGTVldaDGIRA-ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  724 TMFNCMSLSFDAGNMTTLLPLSSGGTLAF---GEPNDRAIMQAEQAGATHL-ILPTaLMSIL-----DPEQVNGIQAIGM 794
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLtndGVLDDAFWEDLREHGATGLaGVPS-TYAMLtrlgfDPAKLPSLRYLTQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 GGEACPNAVVENWADKVA---LYNMYGPTECT--VTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLA 869
Cdd:cd05922   239 AGGRLPQETIARLRELLPgaqVYVMYGQTEATrrMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  870 GLGLARGYLNQPQmtasrfehitlndvnNAGQGAATLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL 949
Cdd:cd05922   319 GPNVMKGYWNDPP---------------YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404635  950 AAVcpslKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05922   384 RSI----GLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1565-1981 6.59e-44

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: 166.47  E-value: 6.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1565 LLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRA--ALESECASIQVIVKQADLPFY 1642
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTsfIEDGLGQPVQVVHRQAQVPVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1643 YQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVL-LSCHHSVIDGWSGPQLLGavhrDYQTLMQG 1721
Cdd:cd19536    81 ELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVK----EILAVYNQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 QVLMHGDAPAIQVDraYVDYARH--AVAQQSAVDAFWQQRqslLAqtnDVSMLFAAAGKRAdLSQHLTQIEPQVTSVSLn 1799
Cdd:cd19536   157 LLEYKPLSLPPAQP--YRDFVAHerASIQQAASERYWREY---LA---GATLATLPALSEA-VGGGPEQDSELLVSVPL- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1800 ekdQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSVGLYINSLPLALSWQQpVSLQQ 1879
Cdd:cd19536   227 ---PVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSE-ETVED 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1880 HLVQLQNELMAM--NQHATQSLIALTAGRSRLFNSLFIYENYPDAKAEQGQRADDPHRLYPEFSAayEKVEMPLNLVVRE 1957
Cdd:cd19536   303 LLKRAQEQELESlsHEQVPLADIQRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSE--FKSNYDVNLSVLP 380

                         410       420
                  ....*....|....*....|....
gi 499404635 1958 QSGCMLLRFEFDADALDSAQARRV 1981
Cdd:cd19536   381 KQDRLELKLAYNSQVLDEEQAQRL 404
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 550-1026 1.60e-43

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: 166.11  E-value: 1.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  550 AIAFDGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHII 629
Cdd:cd17654     5 ALIIDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  630 TDANLSVILGGDGQ---QLAQWSAEQRIDLtdpavveqwqdlpgdqppaipRHAQQLAQVIYTSGSTGLPKGVMIEHGSL 706
Cdd:cd17654    85 KKCHVSYLLQNKELdnaPLSFTPEHRHFNI---------------------RTDECLAYVIHTSGTTGTPKIVAVPHKCI 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  707 INLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGE-----------PNDRAIMQAEQAGATHLILPT 775
Cdd:cd17654   144 LPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPtsvkvlpsklaDILFKRHRITVLQATPTLFRR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  776 ALMSILDPEQVNGIQAI---GMGGEACP-NAVVENWA---DKVALYNMYGPTECTVTALSTRLRKGQ-PVTIGKPLIHIQ 847
Cdd:cd17654   224 FGSQSIKSTVLSATSSLrvlALGGEPFPsLVILSSWRgkgNRTRIFNIYGITEVSCWALAYKVPEEDsPVQLGSPLLGTV 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  848 ALILDtagqLCPVGVPGELCLAGL---GLARGYLNQPQMTasrfehitlndvnnagqgaatlrIYRTGDKARlLNNGDYE 924
Cdd:cd17654   304 IEVRD----QNGSEGTGQVFLGGLnrvCILDDEVTVPKGT-----------------------MRATGDFVT-VKDGELF 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  925 YCGRIDEQIKLRGYRIEPGEIEaqlaAVCPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDvakyLPEYMVP 1004
Cdd:cd17654   356 FLGRKDSQIKRRGKRINLDLIQ----QVIESCLGVESCAVTLSDQQRLIAFIVGESSSSRIHKELQLTL----LSSHAIP 427

                         490       500
                  ....*....|....*....|..
gi 499404635 1005 FRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd17654   428 DTFVQIDKLPLTSHGKVDKSEL 449
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 549-1026 2.11e-42

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: 162.46  E-value: 2.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  549 LAIAFDGeprtDTLTYAELNRQANQLAHWLHRQG-LGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRH 627
Cdd:cd05941     3 IAIVDDG----DSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  628 IITDANLSVILggdgqqlaqwsaeqridltDPAVVeqwqdlpgdqppaiprhaqqlaqvIYTSGSTGLPKGVMIEHGSLI 707
Cdd:cd05941    79 VITDSEPSLVL-------------------DPALI------------------------LYTSGTTGRPKGVVLTHANLA 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  708 NLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGT---LAFGEPNDRAIMQAEQAGATHLILPTALMSILD- 782
Cdd:cd05941   116 ANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLcPLFAGASvefLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQy 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  783 ----PEQVNGIQAIGM--------GGEACPNAVVENWADKV--ALYNMYGPTEcTVTALSTRLrKGQPV--TIGKPLIHI 846
Cdd:cd05941   196 yeahFTDPQFARAAAAerlrlmvsGSAALPVPTLEEWEAITghTLLERYGMTE-IGMALSNPL-DGERRpgTVGMPLPGV 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  847 QALILDT-AGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndvnnagqgaATLRIYRTGDKARLLNNGDYEY 925
Cdd:cd05941   274 QARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF---------------TDDGWFKTGDLGVVDEDGYYWI 338

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  926 CGRI-DEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI-VAQVGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMV 1003
Cdd:cd05941   339 LGRSsVDIIKSGGYKVSALEIERVLLAH-PGVSECAVIgVPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLAPYKR 417

                         490       500
                  ....*....|....*....|...
gi 499404635 1004 PFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05941   418 PRRLILVDELPRNAMGKVNKKEL 440
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 559-1021 3.01e-42

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: 163.15  E-value: 3.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  559 TDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVIL 638
Cdd:cd05911     8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  639 gGDGQQL-------AQWSAEQRIDLTDPAV-----VEQ-WQDLPG----DQPPAIPRHAQQLAQVIYTSGSTGLPKGVMI 701
Cdd:cd05911    88 -TDPDGLekvkeaaKELGPKDKIIVLDDKPdgvlsIEDlLSPTLGeedeDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  702 EHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFD--AGNMTTLLPLSSGGTL-AFGEPNDRAIMQA-EQAGATHLILPTAL 777
Cdd:cd05911   167 SHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYhiYGLFTTLASLLNGATViIMPKFDSELFLDLiEKYKITFLYLVPPI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  778 MSIL------DPEQVNGIQAIGMGGEACPNAVVE---NWADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQA 848
Cdd:cd05911   247 AAALakspllDKYDLSSLRVILSGGAPLSKELQEllaKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEA 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  849 LILDTAG-QLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndvnnagQGaatlrIYRTGDKARLLNNGDYEYCG 927
Cdd:cd05911   327 KIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE----------DG-----WLHTGDIGYFDEDGYLYIVD 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  928 RIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI---VAQVGSRPAlvAYaTVKADSSTPEPAAVLIDVAKYLPEYmvp 1004
Cdd:cd05911   392 RKKELIKYKGFQVAPAELEAVLLEH-PGVADAAVIgipDEVSGELPR--AY-VVRKPGEKLTEKEVKDYVAKKVASY--- 464

                         490       500
                  ....*....|....*....|.
gi 499404635 1005 FRL----MLLEDMPLTPNGKL 1021
Cdd:cd05911   465 KQLrggvVFVDEIPKSASGKI 485
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 73-498 3.98e-40

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: 155.72  E-value: 3.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFvVNEQGKGEQRI---DAYQPfvi 149
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF-PGDGGDVHQRIldaDAARP--- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  150 qhdDFSLLPEAEREgrLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFLACQ 229
Cdd:cd19546    82 ---ELPVVPATEEE--LPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  230 NCQPYPVETTQLNYIDYAHWF--------NSDSFLdyhNEFKPFWVERLTGIPEVHSLPLDKPRPAHQNSGGEVIFSAIN 301
Cdd:cd19546   157 EGRAPERAPLPLQFADYALWErellagedDRDSLI---GDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  302 NDLWDKFKRLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYR-ERPDIEDVVGFFVNTIVLRTQLQDSQNFVDY 380
Cdd:cd19546   234 AEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDdEEGDLEGMVGPFARPLALRTDLSGDPTFREL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  381 LQYCREQDLSAFDHQLYRFEALSEAIGSDRTTAINPIFQVML-VYQAKVDFNDL--IPGCDAAEETSPVLPAKTDISVKV 457
Cdd:cd19546   314 LGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALdVRDDDNDPWDApeLPGLRTSPVPLGTEAMELDLSLAL 393

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 499404635  458 TE----------LMGEVRldwlFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19546   394 TErrnddgdpdgLDGSLR----YAADLFDRATAAALARRLVRVLEQVAADP 440
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 558-1027 6.11e-40

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: 157.29  E-value: 6.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  558 RTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERlrhiiTDANLSVi 637
Cdd:cd17647    17 KTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR-----QNIYLGV- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  638 lggdgqqlaqwsAEQR--IDLTDPAVVEQwqdlpgdqPPAIPrhaqqlaQVIYTSGSTGLPKGVMIEHGSLINLLDDHRD 715
Cdd:cd17647    91 ------------AKPRglIVIRAAGVVVG--------PDSNP-------TLSFTSGSEGIPKGVLGRHFSLAYYFPWMAK 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  716 RIDFTPqSTMFNCMS-LSFDAGNMTTLLPLSSGGTLAFGEPND-----RAIMQAEQAGATHLILPTALMSILDPEQVNGI 789
Cdd:cd17647   144 RFNLSE-NDKFTMLSgIAHDPIQRDMFTPLFLGAQLLVPTQDDigtpgRLAEWMAKYGATVTHLTPAMGQLLTAQATTPF 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  790 ----QAIGMGG----EACpnAVVENWADKVALYNMYGPTEC--TVTALSTRLRKGQP---------VTIGKPLIHIQALI 850
Cdd:cd17647   223 pklhHAFFVGDiltkRDC--LRLQTLAENVRIVNMYGTTETqrAVSYFEVPSRSSDPtflknlkdvMPAGRGMLNVQLLV 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LD--TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF--------EH-ITLNDVNNAGQGAATL----RIYRTGDKA 915
Cdd:cd17647   301 VNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvepDHwNYLDKDNNEPWRQFWLgprdRLYRTGDLG 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  916 RLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVAQVGSRPALVAY--------------ATVKAD 981
Cdd:cd17647   381 RYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYivprfdkpddesfaQEDVPK 460

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635  982 SSTPEPAA-------VLID-----VAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:cd17647   461 EVSTDPIVkgligyrKLIKdirefLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
PRK05691 PRK05691
peptide synthase; Validated
 532-1400 6.84e-40

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 163.80  E-value: 6.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAVAQRDPQQLAIAF--DGEPRTDTLTYAELNRQANQLAHWLHRQ-GLGEQSLVGVLAKRDryFVIALLAIWK 608
Cdd:PRK05691    9 LTLVQALQRRAAQTPDRLALRFlaDDPGEGVVLSYRDLDLRARTIAAALQARaSFGDRAVLLFPSGPD--YVAAFFGCLY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  609 AGAAYVPLdpdYPPE--------RLRHIITDANLSVILGGDG-----QQLAQWSAEQR-----IDLTDPAVVEQWQDlpg 670
Cdd:PRK05691   87 AGVIAVPA---YPPEsarrhhqeRLLSIIADAEPRLLLTVADlrdslLQMEELAAANApellcVDTLDPALAEAWQE--- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  671 dqpPAIPrhAQQLAQVIYTSGSTGLPKGVMIEHGSLI--NLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSG 747
Cdd:PRK05691  161 ---PALQ--PDDIAFLQYTSGSTALPKGVQVSHGNLVanEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLqPIFSG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  748 GTLAFGEPND------RAIMQAEQAGAT---------HLILPTALMSILDPEQVNGIQAIGMGGEACPNAVVENWADKVA 812
Cdd:PRK05691  236 VPCVLMSPAYflerplRWLEAISEYGGTisggpdfayRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  813 --------LYNMYGPTECTVTALSTRLRKGQP----------------------VTIGKPLIHIQALILDTA-GQLCPVG 861
Cdd:PRK05691  316 acgfdpdsFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgtgsvlMSCGRSQPGHAVLIVDPQsLEVLGDN 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  862 VPGELCLAGLGLARGYLNQPQMTASRFehitlndVNNAGQgaatlRIYRTGDKArLLNNGDYEYCGRIDEQIKLRGYRIE 941
Cdd:PRK05691  396 RVGEIWASGPSIAHGYWRNPEASAKTF-------VEHDGR-----TWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLY 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  942 PGEIEAQLAAVCPSLKQIKVI---VAQVGSRPALVAyATVKADSSTPEPAAVLID-----VAKYLPEymVPFRLMLLED- 1012
Cdd:PRK05691  463 PQDIEKTVEREVEVVRKGRVAafaVNHQGEEGIGIA-AEISRSVQKILPPQALIKsirqaVAEACQE--APSVVLLLNPg 539

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1013 -MPLTPNGK--------------LDMKQLPPVLEANESDGEADNP--LEADVLAIWRSVLNTP-LGVEDDFFRLGGDSIL 1074
Cdd:PRK05691  540 aLPKTSSGKlqrsacrlrladgsLDSYALFPALQAVEAAQTAASGdeLQARIAAIWCEQLKVEqVAADDHFFLLGGNSIA 619

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1075 SIQLTTRLR-SAGYACTVKDVFEAKSVRRLCRVLAQnnrdtgTVAEQGTLEGEFALLPIQRWFmEQSLARPEHW------ 1147
Cdd:PRK05691  620 ATQVVARLRdELGIDLNLRQLFEAPTLAAFSAAVAR------QLAGGGAAQAAIARLPRGQAL-PQSLAQNRLWllwqld 692

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1148 NQAAMIQLP-------EVDTERLVTMLQALMAQHDALRLGCDAEG----QRYLADVPCPaLSTLDYRQLGDDGLQQAFTA 1216
Cdd:PRK05691  693 PQSAAYNIPgglhlrgELDEAALRASFQRLVERHESLRTRFYERDgvalQRIDAQGEFA-LQRIDLSDLPEAEREARAAQ 771

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1217 LQSE-----FDPAQGRTMACALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERLYL----GEP--LLPKTSSYRQWG 1285
Cdd:PRK05691  772 IREEearqpFDLEKGPLLRVTLVRLDDE-EHQLLVTLHHIVADGWSLNILLDEFSRLYAaacqGQTaeLAPLPLGYADYG 850

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1286 AALQHYATQH--AEQLTYWQAQEDGVDLTALLAAKDPQGH---ASAAILTLD-AKTTGQLVSEANRAFNTDVSDLLLSAL 1359
Cdd:PRK05691  851 AWQRQWLAQGeaARQLAYWKAQLGDEQPVLELATDHPRSArqaHSAARYSLRvDASLSEALRGLAQAHQATLFMVLLAAF 930

                         970       980       990      1000
                  ....*....|....*....|....*....|....*....|.
gi 499404635 1360 TRTLNDLGWGDKARIMLEGHGReaidPTLDVSRTVGWFTST 1400
Cdd:PRK05691  931 QALLHRYSGQGDIRIGVPNANR----PRLETQGLVGFFINT 967
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 562-1021 4.04e-39

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: 152.49  E-value: 4.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILggd 641
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 gqqlaqwsaeqrIDLTDPAVVeqwqdlpgdqppaiprhaqqlaqvIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:cd05972    78 ------------TDAEDPALI------------------------YFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRP 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  722 QSTMFNCMSLSFDAGNMTTLL-PLSSGGT--LAFGEPND--RAIMQAEQAGATHLIL-PTA--LMSILDPEQVN--GIQA 791
Cdd:cd05972   122 DDIHWNIADPGWAKGAWSSFFgPWLLGATvfVYEGPRFDaeRILELLERYGVTSFCGpPTAyrMLIKQDLSSYKfsHLRL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  792 IGMGGEACPNAVVENWADKVAL--YNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELC-- 867
Cdd:cd05972   202 VVSAGEPLNPEVIEWWRAATGLpiRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAik 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  868 LAGLGLARGYLNQPQMTASRFEhitlNDVnnagqgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:cd05972   282 LPPPGLFLGYVGDPEKTEASIR----GDY------------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVES 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLaavcpsLKQIKVIVAQVGSRPALVAYATVKAD---SSTPEPAAVLID-----VAKYLPEYMVPFRLMLLEDMPLTPNG 1019
Cdd:cd05972   346 AL------LEHPAVAEAAVVGSPDPVRGEVVKAFvvlTSGYEPSEELAEelqghVKKVLAPYKYPREIEFVEELPKTISG 419


                  ..
gi 499404635 1020 KL 1021
Cdd:cd05972   420 KI 421
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1566-2000 1.24e-38

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: 150.15  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSMLYHRLRCPqdDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAA-LESECAS--IQVIVKQADLPFY 1642
Cdd:cd19542     2 YPCTPMQEGMLLSQLRSP--GLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVfVESSAEGtfLQVVLKSLDPPIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1643 -YQDLMQdadplaVIERYRQQDLRTGFDLSQPPLlRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQtlmqG 1721
Cdd:cd19542    80 eVETDED------SLDALTRDLLDDPTLFGQPPH-RLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN----G 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 QVLmhGDAPAiqvdraYVDYARHAVAQ-QSAVDAFWQQrqsLLAqtndvsmlfaaaGKRADLSQHLTQIEPQVTSVSLNE 1800
Cdd:cd19542   149 QLL--PPAPP------FSDYISYLQSQsQEESLQYWRK---YLQ------------GASPCAFPSLSPKRPAERSLSSTR 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1801 KDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSVGLYINSLPLALSWQQPVSLQQH 1880
Cdd:cd19542   206 RSLAKLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1881 LVQLQNELMAMNQHATQSLIAL-----TAGRSRLFNSLFIYENYPDAKAEQGQRAddphrLYPEFSAAYEKVEMPLNLVV 1955
Cdd:cd19542   286 LRQLQQQYLRSLPHQHLSLREIqralgLWPSGTLFNTLVSYQNFEASPESELSGS-----SVFELSAAEDPTEYPVAVEV 360

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 499404635 1956 REQSGCMLLRFEFDADALDSAQARRVLmrwhDEVVALVNSVPQQP 2000
Cdd:cd19542   361 EPSGDSLKVSLAYSTSVLSEEQAEELL----EQFDDILEALLANP 401
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 542-981 1.71e-38

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: 153.16  E-value: 1.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAF--DGEPRTDTLTYAELNRQANQLAHWLHRQGL-GEqsLVGVLAKRDRYFVIALLAIWKAGAAYVPLDP 618
Cdd:cd05931     3 AAARPDRPAYTFldDEGGREETLTYAELDRRARAIAARLQAVGKpGD--RVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  619 DYPP---ERLRHIITDANLSVIL--GGDGQQLAQWSAEQRIDLTDP-AVVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGS 692
Cdd:cd05931    81 PTPGrhaERLAAILADAGPRVVLttAAALAAVRAFAASRPAAGTPRlLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  693 TGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTLAFGEPND---------RAImq 762
Cdd:cd05931   161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLtPLYSGGPSVLMSPAAflrrplrwlRLI-- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  763 aEQAGATHLILPT-AL------MSILDPEQVN--GIQAIGMGGEACPNAVVENWADKVALYNM--------YGPTECTVt 825
Cdd:cd05931   239 -SRYRATISAAPNfAYdlcvrrVRDEDLEGLDlsSWRVALNGAEPVRPATLRRFAEAFAPFGFrpeafrpsYGLAEATL- 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  826 ALSTRLRKGQPVTI---------------------------GKPLIHIQALILDTAG-QLCPVGVPGELCLAGLGLARGY 877
Cdd:cd05931   317 FVSGGPPGTGPVVLrvdrdalagravavaaddpaarelvscGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGPSVASGY 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  878 LNQPQMTASRFEHItlndvnnAGQGAATLriYRTGDKARLLnNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLK 957
Cdd:cd05931   397 WGRPEATAETFGAL-------AATDEGGW--LRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALR 466

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 499404635  958 --------------QIKVIVAQVGSRPALVAYATVKAD 981
Cdd:cd05931   467 pgcvaafsvpddgeERLVVVAEVERGADPADLAAIAAA 504
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 529-1026 1.81e-38

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 152.65  E-value: 1.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  529 QPQLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWK 608
Cdd:PRK06187    3 DYPLTIGRILRHGARKHPDKEAVYFDGR----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  609 AGAAYVPLDPDYPPERLRHIITDANLSVILGGDG------QQLAQ-------WSAEQRIDLTDPAVVEQWQDLPGDQPPA 675
Cdd:PRK06187   79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvpllaAILPQlptvrtvIVEGDGPAAPLAPEVGEYEELLAAASDT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  676 IPRHA---QQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQST------MFNCMSLsfdagnMTTLLPLSS 746
Cdd:PRK06187  159 FDFPDideNDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVylvivpMFHVHAW------GLPYLALMA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  747 GGTL----AFgEPnDRAIMQAEQAGATHLIL-PTALMSILD-----PEQVNGIQAIGMGGEACPNAVVENWADK--VALY 814
Cdd:PRK06187  233 GAKQviprRF-DP-ENLLDLIETERVTFFFAvPTIWQMLLKaprayFVDFSSLRLVIYGGAALPPALLREFKEKfgIDLV 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  815 NMYGPTECTVTALSTRLRKGQP------VTIGKPLIHIQALILDTAGQLCPV--GVPGELCLAGLGLARGYLNQPQMTAS 886
Cdd:PRK06187  311 QGYGMTETSPVVSVLPPEDQLPgqwtkrRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAE 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  887 RFEHitlndvnnaGQgaatlriYRTGDKARLLNNGdYEY-CGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI-VA 964
Cdd:PRK06187  391 TIDG---------GW-------LHTGDVGYIDEDG-YLYiTDRIKDVIISGGENIYPRELEDALYG-HPAVAEVAVIgVP 452

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404635  965 --QVGSRPalVAYATVKADsSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK06187  453 deKWGERP--VAVVVLKPG-ATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 561-982 9.98e-38

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: 148.90  E-value: 9.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAkRDRY-FVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG 639
Cdd:cd05907     5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILS-RNRPeWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 GDgqqlaqwsaeqridltdpavveqwqdlPGDqppaiprhaqqLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDF 719
Cdd:cd05907    84 ED---------------------------PDD-----------LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  720 TPQSTMFNCMSLSFDAGNMTTL-LPLSSGGTLAFGEPnDRAIMQAEQAgathlILPTALMS---ILDPEQvNGIQAIGM- 794
Cdd:cd05907   126 TEGDRHLSFLPLAHVFERRAGLyVPLLAGARIYFASS-AETLLDDLSE-----VRPTVFLAvprVWEKVY-AAIKVKAVp 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 --------------------GGEACPNAVVENW-ADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPL--IHIQalil 851
Cdd:cd05907   199 glkrklfdlavggrlrfaasGGAPLPAELLHFFrALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLpgVEVR---- 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  852 dtagqlcpVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndvnnagQGAatlriYRTGDKARLLNNGDYEYCGRIDE 931
Cdd:cd05907   275 --------IADDGEILVRGPNVMLGYYKNPEATAEALDA----------DGW-----LHTGDLGEIDEDGFLHITGRKKD 331

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499404635  932 QIKLR-GYRIEPGEIEAQLAAvCPSLKQIkVIVAQvgSRPALVAYATVKADS 982
Cdd:cd05907   332 LIITSgGKNISPEPIENALKA-SPLISQA-VVIGD--GRPFLVALIVPDPEA 379
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 532-1026 1.26e-37

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 150.05  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGA 611
Cdd:PRK07656    5 MTLPELLARAARRFGDKEAYVFGDQ----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  612 AYVPLDPDYPPERLRHIITDANLSVILGGDGQQLAQWSA-------EQRIDLTDPAVVEQ------WQDL--PGDQP-PA 675
Cdd:PRK07656   81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAttrlpalEHVVICETEEDDPHtekmktFTDFlaAGDPAeRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  676 IPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQST------MFN--CMSLSFDAgnmttllPLSSG 747
Cdd:PRK07656  161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRylaanpFFHvfGYKAGVNA-------PLMRG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  748 GTLaFGEPN---DRAIMQAEQAGAThlIL---PTALMSILD-----PEQVNGIQAIGMGGEACPNAVVENWADKVALYNM 816
Cdd:PRK07656  234 ATI-LPLPVfdpDEVFRLIETERIT--VLpgpPTMYNSLLQhpdrsAEDLSSLRLAVTGAASMPVALLERFESELGVDIV 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  817 ---YGPTECTVTALSTRL---RKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTasrfeh 890
Cdd:PRK07656  311 ltgYGLSEASGVTTFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEAT------ 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  891 itlndvnnagqgAATLRI---YRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI----- 962
Cdd:PRK07656  385 ------------AAAIDAdgwLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEH-PAVAEAAVIgvpde 451

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  963 -VAQVGsrpalVAYATVKADSSTPEpaAVLIDVAK-YLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK07656  452 rLGEVG-----KAYVVLKPGAELTE--EELIAYCReHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 533-1021 2.51e-36

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 146.23  E-value: 2.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK08316   12 TIGDILRRSARRYPDKTALVFGDR----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRHIITDANLSVILGGDG-----QQLAQWSAEQRIDLTDPAV----------VEQWQDLPGDQPPAIP 677
Cdd:PRK08316   88 HVPVNFMLTGEELAYILDHSGARAFLVDPAlaptaEAALALLPVDTLILSLVLGgreapggwldFADWAEAGSVAEPDVE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  678 RHAQQLAQVIYTSGSTGLPKGVMIEHGSLIN-----LLDdhrdrIDFTPQSTMFNCMSLSFDAGNMTTLLP-LSSGGT-L 750
Cdd:PRK08316  168 LADDDLAQILYTSGTESLPKGAMLTHRALIAeyvscIVA-----GDMSADDIPLHALPLYHCAQLDVFLGPyLYVGATnV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  751 AFGEPNDRAIMQA-EQAGATHLIL-PTALMSIL-----DPEQVNGIQAIGMGGEACPNAVVENWADK---VALYNMYGPT 820
Cdd:PRK08316  243 ILDAPDPELILRTiEAERITSFFApPTVWISLLrhpdfDTRDLSSLRKGYYGASIMPVEVLKELRERlpgLRFYNCYGQT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  821 EctVTALSTRLR----KGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndv 896
Cdd:PRK08316  323 E--IAPLATVLGpeehLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG------ 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  897 nnaGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL--------AAV--CPSLKQIKVIVAQV 966
Cdd:PRK08316  395 ---GW-------FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALythpavaeVAVigLPDPKWIEAVTAVV 464

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  967 gsrpalvayatVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK08316  465 -----------VPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 508-1032 2.03e-34

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 141.33  E-value: 2.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  508 METDRFAAVLAETQQ------LPRS--YPQPQLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLH 579
Cdd:PRK06178    1 MAEEAYLAELRALQQaawpagIPREpeYPHGERPLTEYLRAWARERPQRPAIIFYGH----VITYAELDELSDRFAALLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  580 RQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD------GQQLAQWSAEQR 653
Cdd:PRK06178   77 QRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDqlapvvEQVRAETSLRHV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  654 I--DLTD-----------------PAVVEQWQDL------PGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLI- 707
Cdd:PRK06178  157 IvtSLADvlpaeptlplpdslrapRLAAAGAIDLlpalraCTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVy 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  708 ----NLLDDHRDRIDftpqSTMFNCMSLSFDAG-NMTTLLPLSSGGTLAFGEPND-RAIMQA-EQAGATHLILPT-ALMS 779
Cdd:PRK06178  237 taaaAYAVAVVGGED----SVFLSFLPEFWIAGeNFGLLFPLFSGATLVLLARWDaVAFMAAvERYRVTRTVMLVdNAVE 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  780 ILD-PE----------QVNGIQAIgmggEACPNAVVENWAD---KVALYNMYGPTEcTVTALSTRL--------RKGQPV 837
Cdd:PRK06178  313 LMDhPRfaeydlsslrQVRVVSFV----KKLNPDYRQRWRAltgSVLAEAAWGMTE-THTCDTFTAgfqdddfdLLSQPV 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  838 TIGKPLIHIQALILD-TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTasrfehitlndvnnagqgAATLR--IYRTGDK 914
Cdd:PRK06178  388 FVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEAT------------------AEALRdgWLHTGDI 449

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  915 ARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAavcpslKQIKVIVAQVGSRP------ALVAYATVKADSSTpEPA 988
Cdd:PRK06178  450 GKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLG------QHPAVLGSAVVGRPdpdkgqVPVAFVQLKPGADL-TAA 522

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 499404635  989 AVLIDVAKYLPEYMVPfRLMLLEDMPLTPNGKLDMKQLPPVLEA 1032
Cdd:PRK06178  523 ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEE 565
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 562-1026 3.04e-34

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: 138.00  E-value: 3.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVilggd 641
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKV----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 gqqlaqwsaeqridltdpAVVEQWQDlpgdqppaiprhaqQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:cd05935    77 ------------------AVVGSELD--------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  722 QSTMFNCMSLSFDAGNMTTL-LPLSSGGTLAFGEPNDR--AIMQAEQAGATHLI-LPTALMSIL-DPE----QVNGIQAI 792
Cdd:cd05935   125 SDVILACLPLFHVTGFVGSLnTAVYVGGTYVLMARWDRetALELIEKYKVTFWTnIPTMLVDLLaTPEfktrDLSSLKVL 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  793 GMGGEACPNAVVENWADKVALYNM--YGPTE-CTVTALSTRLR-KGQpvTIGKPLIHIQALILD-TAGQLCPVGVPGELC 867
Cdd:cd05935   205 TGGGAPMPPAVAEKLLKLTGLRFVegYGLTEtMSQTHTNPPLRpKLQ--CLGIP*FGVDARVIDiETGRELPPNEVGEIV 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  868 LAGLGLARGYLNQPQMTASRFehITLNdvnnaGQgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:cd05935   283 VRGPQIFKGYWNRPEETEESF--IEIK-----GR-----RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLAAvCPSLKQIKVIVA---QVGSRP-ALVAYATVKADSSTPEpaavliDVAKYLPEYM----VPFRLMLLEDMPLTPNG 1019
Cdd:cd05935   351 KLYK-HPAI*EVCVISVpdeRVGEEVkAFIVLRPEYRGKVTEE------DIIEWAREQMaaykYPREVEFVDELPRSASG 423


                  ....*..
gi 499404635 1020 KLDMKQL 1026
Cdd:cd05935   424 KILWRLL 430
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1565-1984 4.23e-34

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: 137.54  E-value: 4.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1565 LLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAA-LESECASIQVIVKQADLP-FY 1642
Cdd:cd19066     1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRfCEEAGRYEQVVLDKTVRFrIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1643 YQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQ 1722
Cdd:cd19066    81 IIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1723 vlmhgDAPAIQVDrAYVDYA------RHAVAQQSAVdAFWqqrQSLLAQTNDVSMLFaAAGKRADLSqhltQIEPQVTSV 1796
Cdd:cd19066   161 -----PTLPPPVG-SYADYAawlekqLESEAAQADL-AYW---TSYLHGLPPPLPLP-KAKRPSQVA----SYEVLTLEF 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1797 SLNEKDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPveDVASSVGLYINSLPLALSWQQPVS 1876
Cdd:cd19066   226 FLRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDAT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1877 LQQHLVQLQNELMAMNQHATQSLI--------ALTAGRSRLFNSLFIYENYPDAKAEQGQRADDPHRLYPEFSAAYEkve 1948
Cdd:cd19066   304 FPELLKRTKEQSREAIEHQRVPFIelvrhlgvVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFD--- 380

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 499404635 1949 mpLNLVVREQS-GCMLLRFEFDADALDSAQARRVLMR 1984
Cdd:cd19066   381 --LDLEASEDPdGDLLLRLEYSRGVYDERTIDRFAER 415
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1563-2000 6.22e-34

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: 143.46  E-value: 6.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1563 DTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALESECASIQVIVKQ---ADL 1639
Cdd:COG1020    15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPvvaAPL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1640 PFYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLM 1719
Cdd:COG1020    95 PVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAY 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1720 QGQVLMHGDAPAIQVDRAYVDYARHAVAQQSAVDAFWQQRQSLLAqtnDVSMLFAAAGKRADLSQHLTQIepqvtSVSLN 1799
Cdd:COG1020   175 AGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLP---PLLELPTDRPRPAVQSYRGARV-----SFRLP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1800 EKDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPveDVASSVGLYINSLPLALSWQQPVSLQQ 1879
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGLVGFFVNTLPLRVDLSGDPSFAE 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1880 HLVQLQNELMAMNQHATQSLIAL--------TAGRSRLFNSLFIYENYPDAKAEQGQRADDPHRLypefsaAYEKVEMPL 1951
Cdd:COG1020   325 LLARVRETLLAAYAHQDLPFERLveelqperDLSRNPLFQVMFVLQNAPADELELPGLTLEPLEL------DSGTAKFDL 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 499404635 1952 NLVVREQSGCMLLRFEFDADALDSAQARRVLMRWHDEVVALVNSvPQQP 2000
Cdd:COG1020   399 TLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD-PDQP 446
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
533-974 6.57e-34

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 140.24  E-value: 6.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAF--DGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAkRDRY-FVIALLAIWKA 609
Cdd:COG1022    12 TLPDLLRRRAARFPDRVALREkeDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILS-DNRPeWVIADLAILAA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  610 GAAYVPLDPDYPPERLRHIITDANLSVILGGDGQQLAQ--------------WSAEQRIDLTDPAVV--EQWQDLpGDQP 673
Cdd:COG1022    89 GAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKllevrdelpslrhiVVLDPRGLRDDPRLLslDELLAL-GREV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  674 PAIPRHAQQLAQV--------IYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLS 745
Cdd:COG1022   168 ADPAELEARRAAVkpddlatiIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALA 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  746 SGGTLAFGE-------------PN-------------DRAIMQAEQAGAT-----HLILPTALMSILDPEQVNGI----- 789
Cdd:COG1022   248 AGATVAFAEspdtlaedlrevkPTfmlavprvwekvyAGIQAKAEEAGGLkrklfRWALAVGRRYARARLAGKSPslllr 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  790 ---------------QAIG-------MGGEACPNAVVE-NWADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHI 846
Cdd:COG1022   328 lkhaladklvfsklrEALGgrlrfavSGGAALGPELARfFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGV 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  847 QALILDTagqlcpvgvpGELCLAGLGLARGYLNQPQMTasrfehitlndvnnagqgAATLRI---YRTGDKARLLNNGDY 923
Cdd:COG1022   408 EVKIAED----------GEILVRGPNVMKGYYKNPEAT------------------AEAFDAdgwLHTGDIGELDEDGFL 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499404635  924 EYCGRIDEQIKLR-GYRIEPGEIEAQLAAvCPSLKQIkVIVAQvgSRPALVA 974
Cdd:COG1022   460 RITGRKKDLIVTSgGKNVAPQPIENALKA-SPLIEQA-VVVGD--GRPFLAA 507
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 561-1021 6.82e-34

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: 137.13  E-value: 6.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILgg 640
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 dgqqlaqwsAEQRIDLTDPAvveqwqDLPGDqppaiprhaqqLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFT 720
Cdd:cd05903    79 ---------VPERFRQFDPA------AMPDA-----------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  721 PQSTMFNCMSLSFDAGNM-TTLLPLSSGGT---LAFGEPnDRAIMQAEQAGATHLILPTA-LMSILD-----PEQVNGIQ 790
Cdd:cd05903   133 PGDVFLVASPMAHQTGFVyGFTLPLLLGAPvvlQDIWDP-DKALALMREHGVTFMMGATPfLTDLLNaveeaGEPLSRLR 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  791 AIGMGGEACPNAVVENWADKVALY--NMYGPTEC--TVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGEL 866
Cdd:cd05903   212 TFVCGGATVPRSLARRAAELLGAKvcSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGEL 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  867 CLAGLGLARGYLNQPQMTASRFEhitlndvnnagQGaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIE 946
Cdd:cd05903   292 LSRGPSVFLGYLDRPDLTADAAP-----------EG-----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVE 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  947 AQLAAVcPSLKQIKVIV---AQVGSRPALVAYATVKADSSTPEPAAVL--IDVAK-YLPEymvpfRLMLLEDMPLTPNGK 1020
Cdd:cd05903   356 DLLLGH-PGVIEAAVVAlpdERLGERACAVVVTKSGALLTFDELVAYLdrQGVAKqYWPE-----RLVHVDDLPRTPSGK 429


                  .
gi 499404635 1021 L 1021
Cdd:cd05903   430 V 430
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1567-1982 8.50e-34

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: 136.67  E-value: 8.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1567 PLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL--ESECASIQVIVKQADLPFYYQ 1644
Cdd:cd19547     3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFtwRDRAEPLQYVRDDLAPPWALL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1645 DLMQDaDP---LAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQG 1721
Cdd:cd19547    83 DWSGE-DPdrrAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 QvlmhgdAPAIQVDRAYVDYA---RHAVAQQSAVDAFWQQrqsLLAQTNDVSMLFAAAGKRADLSQHLTQIEPQVTSVsL 1798
Cdd:cd19547   162 R------EPQLSPCRPYRDYVrwiRARTAQSEESERFWRE---YLRDLTPSPFSTAPADREGEFDTVVHEFPEQLTRL-V 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1799 NEKdqatltafAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPVEDVASSVGLYINSLPLALSWQQPVSLQ 1878
Cdd:cd19547   232 NEA--------ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1879 QHLVQLQNEL--MAMNQHATQSLIALTAGRSRL-----FNSLFIYENYPDAKA---EQGQRADDPHrlypefsaAYEKVE 1948
Cdd:cd19547   304 GLLETIHRDLatTAAHGHVPLAQIKSWASGERLsggrvFDNLVAFENYPEDNLpgdDLSIQIIDLH--------AQEKTE 375

                         410       420       430
                  ....*....|....*....|....*....|....
gi 499404635 1949 MPLNLVVREQSGcMLLRFEFDADALDSAQARRVL 1982
Cdd:cd19547   376 YPIGLIVLPLQK-LAFHFNYDTTHFTRAQVDRFI 408
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 559-1022 1.70e-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: 137.50  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  559 TDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITD--ANLSV 636
Cdd:cd05959    27 AGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDsrARVVV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  637 ILGGDGQQLAQ-----WSAEQRIDLTDPA--------VVEQWQDLPGDQPPAiPRHAQQLAQVIYTSGSTGLPKGVMIEH 703
Cdd:cd05959   107 VSGELAPVLAAaltksEHTLVVLIVSGGAgpeagallLAELVAAEAEQLKPA-ATHADDPAFWLYSSGSTGRPKGVVHLH 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  704 GSLINLLDDH-RDRIDFTPQSTMFNCMSLSF--DAGNMTTLlPLSSGGT--LAFGEPNDRAIMQAEQAGATHLI--LPTA 776
Cdd:cd05959   186 ADIYWTAELYaRNVLGIREDDVCFSAAKLFFayGLGNSLTF-PLSVGATtvLMPERPTPAAVFKRIRRYRPTVFfgVPTL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  777 LMSIL-DPE-QVNGIQAIGM---GGEACPNAVVENWADK--VALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQAL 849
Cdd:cd05959   265 YAAMLaAPNlPSRDLSSLRLcvsAGEALPAEVGERWKARfgLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVE 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  850 ILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndvnnagQGAATlriyRTGDKARLLNNGDYEYCGRI 929
Cdd:cd05959   345 LRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------------QGEWT----RTGDKYVRDDDGFYTYAGRA 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  930 DEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGSR-PALVAYATVKADSSTPEPAAV-LIDVAK-YLPEYMVPFR 1006
Cdd:cd05959   409 DDMLKVSGIWVSPFEVESALVQ-HPAVLEAAVVGVEDEDGlTKPKAFVVLRPGYEDSEALEEeLKEFVKdRLAPYKYPRW 487

                         490
                  ....*....|....*.
gi 499404635 1007 LMLLEDMPLTPNGKLD 1022
Cdd:cd05959   488 IVFVDELPKTATGKIQ 503
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 563-1026 3.26e-33

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


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 135.27  E-value: 3.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   563 TYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD- 641
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   642 -GQQLAQWSAEQRIDLTDPAVVEQWQDLPGDQPpaiprhaqqlAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFT 720
Cdd:TIGR01923   81 lEEKDFQADSLDRIEAAGRYETSLSASFNMDQI----------ATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFT 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   721 PQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEP-NDRAIMQAEQAgATHLIL-PTALMSILDPEQVN-GIQAIGMGGE 797
Cdd:TIGR01923  151 EDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKfNQLLEMIANER-VTHISLvPTQLNRLLDEGGHNeNLRKILLGGS 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   798 ACPNAVVENWADK-VALYNMYGPTE--CTVTALSTRLRKGQPvTIGKPLIHIQALIldtaGQLCPVGVpGELCLAGLGLA 874
Cdd:TIGR01923  230 AIPAPLIEEAQQYgLPIYLSYGMTEtcSQVTTATPEMLHARP-DVGRPLAGREIKI----KVDNKEGH-GEIMVKGANLM 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   875 RGYLNQPQMTASRFEHITLNdvnnagqgaatlriyrTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEaQLAAVCP 954
Cdd:TIGR01923  304 KGYLYQGELTPAFEQQGWFN----------------TGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIE-TVLYQHP 366

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635   955 SLKQIKVIVAQ---VGSRPalVAYATVKADSStpepAAVLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:TIGR01923  367 GIQEAVVVPKPdaeWGQVP--VAYIVSESDIS----QAKLIAyLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 557-1022 4.13e-33

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: 135.90  E-value: 4.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  557 PRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSV 636
Cdd:cd05926    10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  637 ILGGDGQQLAQWSAEQR---------IDLTDPAVVEQWQDLPG---DQPPAIPR---HAQQLAQVIYTSGSTGLPKGVMI 701
Cdd:cd05926    90 VLTPKGELGPASRAASKlglailelaLDVGVLIRAPSAESLSNllaDKKNAKSEgvpLPDDLALILHTSGTTGRPKGVPL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  702 EHGSLI----NLLDDHRdridFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGtlafgepndRAIMQA-----------EQ 765
Cdd:cd05926   170 THRNLAasatNITNTYK----LTPDDRTLVVMPLFHVHGLVASLLsTLAAGG---------SVVLPPrfsastfwpdvRD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  766 AGATHL-ILPTALMSILDPEQVNGIQA------IGMGGEACPNAVVENWADKVA--LYNMYGPTECTVTALSTRLRKGQ- 835
Cdd:cd05926   237 YNATWYtAVPTIHQILLNRPEPNPESPppklrfIRSCSASLPPAVLEALEATFGapVLEAYGMTEAAHQMTSNPLPPGPr 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  836 -PVTIGKPlIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHItlndvnnagqgaatlRIYRTGDK 914
Cdd:cd05926   317 kPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD---------------GWFRTGDL 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  915 ARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQikviVAQVGSRPAL----VAYATVKADSSTPEPAAV 990
Cdd:cd05926   381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLS-HPAVLE----AVAFGVPDEKygeeVAAAVVLREGASVTEEEL 455

                         490       500       510
                  ....*....|....*....|....*....|..
gi 499404635  991 LIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:cd05926   456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1568-1817 8.66e-33

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 128.62  E-value: 8.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1568 LSSLQQSMLYHRlrcPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIVKQADLPFYYQDL 1646
Cdd:COG4908     1 LSPAQKRFLFLE---PGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFvEEDGEPVQRIDPDADLPLEVVDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1647 MQ--DADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQVL 1724
Cdd:COG4908    78 SAlpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1725 MHGDAPaiqvdRAYVDYAR--HAVAQQSAVDA---FWQQRQSLLAQTNDVSMLFAAAGKRADLSQHLTqiepqvtsVSLN 1799
Cdd:COG4908   158 PLPELP-----IQYADYAAwqRAWLQSEALEKqleYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLS--------FTLP 224

                         250
                  ....*....|....*...
gi 499404635 1800 EKDQATLTAFAREVGITP 1817
Cdd:COG4908   225 AELTEALKALAKAHGATV 242
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 559-1021 1.23e-32

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: 133.36  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  559 TDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDAnlsvil 638
Cdd:cd05919     8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  639 ggdgqqlaqwsaeqridltdpavveqwqdlpgdQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDH-RDRI 717
Cdd:cd05919    82 ---------------------------------EARLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREAL 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  718 DFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGT--LAFGEPN-DRAIMQAEQAGATHLI-LPTALMSILD-----PEQVN 787
Cdd:cd05919   129 GLTPGDRVFSSAKMFFGYGLGNSLWfPLAVGASavLNPGWPTaERVLATLARFRPTVLYgVPTFYANLLDscagsPDALR 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  788 GIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGE 865
Cdd:cd05919   209 SLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGD 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  866 LCLAGLGLARGYLNQPQMTASRFehitlndvnNAGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEI 945
Cdd:cd05919   289 LLVRGPSAAVGYWNNPEKSRATF---------NGGW-------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635  946 EAQLAAVCPSLKQIKVIVAQV--GSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:cd05919   353 ESLIIQHPAVAEAAVVAVPEStgLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 73-498 5.18e-32

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: 130.89  E-value: 5.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGlwFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFV-VNEQGKGEQRI-DAYQPFVIQ 150
Cdd:cd19542     3 PCTPMQEG--MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVeSSAEGTFLQVVlKSLDPPIEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  151 HDDfsllpeaeREGRLQQQVKAEISRPFdLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKpaflACQN 230
Cdd:cd19542    81 VET--------DEDSLDALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLA----AAYN 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  231 CQPyPVETTQL-NYIDYAHWFNSDSFLDYhnefkpfWVERLTGIPEVHsLPLDKPRPAHQNSGGEVIFSainndlWDKFK 309
Cdd:cd19542   148 GQL-LPPAPPFsDYISYLQSQSQEESLQY-------WRKYLQGASPCA-FPSLSPKRPAERSLSSTRRS------LAKLE 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  310 RLCQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRE--RPDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQ 387
Cdd:cd19542   213 AFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQ 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  388 DLSAFDHQLYRFEALSEAIGSDRTTainPIFQVMLVYQAKVDFNDLIP-GCDAAEETSPVLPAKTDISVKVTELMGEVRL 466
Cdd:cd19542   293 YLRSLPHQHLSLREIQRALGLWPSG---TLFNTLVSYQNFEASPESELsGSSVFELSAAEDPTEYPVAVEVEPSGDSLKV 369

                         410       420       430
                  ....*....|....*....|....*....|..
gi 499404635  467 DWLFATALFERQTIQYYADRFIRLIEAVVENP 498
Cdd:cd19542   370 SLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 531-1022 1.81e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 131.93  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  531 QLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAG 610
Cdd:PRK07798    2 AWNIADLFEAVADAVPDRVALVCGDR----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  611 AAYVPLDPDYPPERLRHIITDANLSVILGGDgqQLAQWSAEQRIDLTDPAVVEQWQD------LPG------------DQ 672
Cdd:PRK07798   78 AVPVNVNYRYVEDELRYLLDDSDAVALVYER--EFAPRVAEVLPRLPKLRTLVVVEDgsgndlLPGavdyedalaagsPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  673 PPAIPRHAQQLaQVIYTSGSTGLPKGVMIEH---------------GSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGN 737
Cdd:PRK07798  156 RDFGERSPDDL-YLLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQ 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  738 MTTLLPLSSGGTLAFGEPN----DRAIMQAEQAGATHLILPTALM------SILDPEQVN--GIQAIGMGGEACPNAVVE 805
Cdd:PRK07798  235 WAAFAALFSGQTVVLLPDVrfdaDEVWRTIEREKVNVITIVGDAMarplldALEARGPYDlsSLFAIASGGALFSPSVKE 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  806 NWAD---KVALYNMYGPTECTVTALSTrLRKGQPVTiGKPLIHIQA--LILDTAGQLCPVGVPGELCLAGLG-LARGYLN 879
Cdd:PRK07798  315 ALLEllpNVVLTDSIGSSETGFGGSGT-VAKGAVHT-GGPRFTIGPrtVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYK 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  880 QPQMTASRFehITLNDVnnagqgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQi 959
Cdd:PRK07798  393 DPEKTAETF--PTIDGV----------RYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAH-PDVAD- 458

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635  960 kVIVAQV-----GSR-PALVAyatvKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:PRK07798  459 -ALVVGVpderwGQEvVAVVQ----LREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 558-1028 2.01e-31

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: 129.86  E-value: 2.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  558 RTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVI 637
Cdd:cd05971     3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  638 LggdgqqlaqwsaeqridlTDPAvveqwqdlpgDQPpaiprhaqqlAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRI 717
Cdd:cd05971    83 V------------------TDGS----------DDP----------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPF 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  718 DFTPQSTmfNCMSLSFD----AGNMTTLLPlssggTLAFGEP----------NDRAIMQAEQAGATHLILP-TALMSI-- 780
Cdd:cd05971   125 NLFPRDG--DLYWTPADwawiGGLLDVLLP-----SLYFGVPvlahrmtkfdPKAALDLMSRYGVTTAFLPpTALKMMrq 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  781 ----LDPEQVNgIQAIGMGGEAcPNAVVENWAD---KVALYNMYGPTECT-VTALSTRLRKGQPVTIGKPLI-HIQAlIL 851
Cdd:cd05971   198 qgeqLKHAQVK-LRAIATGGES-LGEELLGWAReqfGVEVNEFYGQTECNlVIGNCSALFPIKPGSMGKPIPgHRVA-IV 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  852 DTAGQLCPVGVPGELCL------AGLGlargYLNQPQMTASRFehitlndvnnAGQgaatlrIYRTGDKARLLNNGDYEY 925
Cdd:cd05971   275 DDNGTPLPPGEVGEIAVelpdpvAFLG----YWNNPSATEKKM----------AGD------WLLTGDLGRKDSDGYFWY 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  926 CGRIDEQIKLRGYRIEPGEIEAQLaavcpsLKQIKVIVAQVGSRPALV------AYATVKADSSTPEPAAVLID--VAKY 997
Cdd:cd05971   335 VGRDDDVITSSGYRIGPAEIEECL------LKHPAVLMAAVVGIPDPIrgeivkAFVVLNPGETPSDALAREIQelVKTR 408

                         490       500       510
                  ....*....|....*....|....*....|.
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGKLDMKQLPP 1028
Cdd:cd05971   409 LAAHEYPREIEFVNELPRTATGKIRRRELRA 439
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 542-1021 3.57e-31

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 130.31  E-value: 3.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAFDGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYP 621
Cdd:PRK09088    5 ARLQPQRLAAVDLALGRR--WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  622 PERLRHIITDANLSVILGGDGQQLAqwsaeqRIDLTDPAVVEQWQD-LPGDQPPAIPRHAQQLaqVIYTSGSTGLPKGVM 700
Cdd:PRK09088   83 ASELDALLQDAEPRLLLGDDAVAAG------RTDVEDLAAFIASADaLEPADTPSIPPERVSL--ILFTSGTSGQPKGVM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  701 IEHGSL----INL----LDDHRDRidFTPQSTMFNCMSLsfdagnMTTLLP-LSSGGTLAFG---EPNDRAIMQAEQA-G 767
Cdd:PRK09088  155 LSERNLqqtaHNFgvlgRVDAHSS--FLCDAPMFHIIGL------ITSVRPvLAVGGSILVSngfEPKRTLGRLGDPAlG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  768 ATHLILPTALMSIL------DPEQVNGIQAIGMGGEACPNAVVENW-ADKVALYNMYGPTEC-TVTALSTR--LRKGQPV 837
Cdd:PRK09088  227 ITHYFCVPQMAQAFraqpgfDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEAgTVFGMSVDcdVIRAKAG 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  838 TIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnaGQGAatlriYRTGDKARL 917
Cdd:PRK09088  307 AAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT----------GDGW-----FRTGDIARR 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  918 LNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKViVAQVGSRPALVAY-ATVKADSSTPEPAAVLIDVAK 996
Cdd:PRK09088  372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADH-PGIRECAV-VGMADAQWGEVGYlAIVPADGAPLDLERIRSHLST 449

                         490       500
                  ....*....|....*....|....*
gi 499404635  997 YLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK09088  450 RLAKYKVPKHLRLVDALPRTASGKL 474
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 533-1026 3.94e-31

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: 129.94  E-value: 3.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAfdgEPRTDT-LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGA 611
Cdd:cd05923     2 TVFEMLRRAASRAPDACAIA---DPARGLrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  612 AYVPLDPDYPPERLRHIITDANLSVILGGDGQQLAQWSAE---------QRIDLTDPAVVeqwqdlpGDQPPAIPRHAQQ 682
Cdd:cd05923    79 VPALINPRLKAAELAELIERGEMTAAVIAVDAQVMDAIFQsgvrvlalsDLVGLGEPESA-------GPLIEDPPREPEQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  683 LAQVIYTSGSTGLPKGVMIEHGSLIN--LLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTLAFGEPNDRA 759
Cdd:cd05923   152 PAFVFYTSGTTGLPKGAVIPQRAAESrvLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVVEEFDPA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  760 ----IMQAEQ-----AGATHL--ILPTALMSildPEQVNGIQAIGMGGEACPNAVVE--NWADKVALYNMYGPTEctvTA 826
Cdd:cd05923   232 dalkLIEQERvtslfATPTHLdaLAAAAEFA---GLKLSSLRHVTFAGATMPDAVLErvNQHLPGEKVNIYGTTE---AM 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 LSTRLRKGQPVTIGKPLIHIQ---ALILDTAGQLCPVGVPGELCLAGLGLA--RGYLNQPQMTASRfehitLNDvnnagq 901
Cdd:cd05923   306 NSLYMRDARTGTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKK-----LQD------ 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  902 gaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIkVIVAQVGSRPALVAYATVKAD 981
Cdd:cd05923   375 -----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRH-PGVTEV-VVIGVADERWGQSVTACVVPR 447

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635  982 SSTpePAAVLID---VAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05923   448 EGT--LSADELDqfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 537-1028 5.02e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 130.82  E-value: 5.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  537 VIEAVAQRDPQQLAIAFDgeprTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPL 616
Cdd:PRK07788   54 LVAHAARRAPDRAALIDE----RGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  617 DPDYPPERL-----RH----IITDANLSVILGGDGQQLAQWSAEQRIDLTDPAVVEQWQDLpgDQ---------PPAIPR 678
Cdd:PRK07788  130 NTGFSGPQLaevaaREgvkaLVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETL--DDliagsstapLPKPPK 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  679 HAqqlAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFgepndR 758
Cdd:PRK07788  208 PG---GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVL-----R 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  759 AIMQAEQA-------GATHLIL-PTALMSILD-PEQVNG------IQAIGMGGEACPNAVVENWADKVA--LYNMYGPTE 821
Cdd:PRK07788  280 RRFDPEATlediakhKATALVVvPVMLSRILDlGPEVLAkydtssLKIIFVSGSALSPELATRALEAFGpvLYNLYGSTE 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  822 CTVTALSTR--LRKGqPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYlnqpqmTASRFEHItlndVNNa 899
Cdd:PRK07788  360 VAFATIATPedLAEA-PGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGRDKQI----IDG- 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  900 gqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI-V--AQVGSRpaLVAYA 976
Cdd:PRK07788  428 --------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGH-PDVVEAAVIgVddEEFGQR--LRAFV 496

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499404635  977 tVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPP 1028
Cdd:PRK07788  497 -VKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 562-1021 5.91e-31

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: 128.40  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHiitdanlsvILGGD 641
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEH---------RLRTS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 GQQLAQWSAEQRIDLTDPAVVEqwqdlpgdqppaiprhaqqlaqvIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:cd05973    72 GARLVVTDAANRHKLDSDPFVM-----------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRP 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  722 QSTMFNCMSLSFDAGNMTTLL-PLSSG--GTL---AFGEPNDRAIMqaEQAGATHLI-LPTALMSILD-----PEQVNG- 788
Cdd:cd05973   129 EDSFWNAADPGWAYGLYYAITgPLALGhpTILlegGFSVESTWRVI--ERLGVTNLAgSPTAYRLLMAagaevPARPKGr 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  789 IQAIGMGGEACpNAVVENWADK---VALYNMYGPTE-----CTVTALSTRLRKGqpvTIGKPLIHIQALILDTAGQLCPV 860
Cdd:cd05973   207 LRRVSSAGEPL-TPEVIRWFDAalgVPIHDHYGQTElgmvlANHHALEHPVHAG---SAGRAMPGWRVAVLDDDGDELGP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  861 GVPGElclaglgLARGYLNQPQMtasrfehiTLNDVNNAGQGAATLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRI 940
Cdd:cd05973   283 GEPGR-------LAIDIANSPLM--------WFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  941 EPGEIEAQLAAvCPSLKQIKVIVAQVGSRPALV-AYATVKAD-SSTPEPAAVL-IDVAKYLPEYMVPFRLMLLEDMPLTP 1017
Cdd:cd05973   348 GPFDVESALIE-HPAVAEAAVIGVPDPERTEVVkAFVVLRGGhEGTPALADELqLHVKKRLSAHAYPRTIHFVDELPKTP 426


                  ....
gi 499404635 1018 NGKL 1021
Cdd:cd05973   427 SGKI 430
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1126-1456 9.89e-31

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: 127.53  E-value: 9.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1126 EFALLPIQR--WFMEQSLARPEHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLGCDAEGQRY----LADVPCPALS 1198
Cdd:cd19066     1 KIPLSPMQRgmWFLKKLATDPSAFNVAIEMFLTgSLDLARLKQALDAVMERHDVLRTRFCEEAGRYeqvvLDKTVRFRIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1199 TLDYRQLGD------DGLQQAftaLQSEFDPAQGRTMACALVRHHPQADTaLFLAFHHLVIDAVSWRILVDDLERLYLG- 1271
Cdd:cd19066    81 IIDLRNLADpearllELIDQI---QQTIYDLERGPLVRVALFRLADERDV-LVVAIHHIIVDGGSFQILFEDISSVYDAa 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1272 ----EPLLPKTSSYRQWGAALQHYAT--QHAEQLTYWQAQEDGVDLTA-LLAAKDPQGHASAAILTLDAKTTGQLVS--- 1341
Cdd:cd19066   157 erqkPTLPPPVGSYADYAAWLEKQLEseAAQADLAYWTSYLHGLPPPLpLPKAKRPSQVASYEVLTLEFFLRSEETKrlr 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1342 EANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREAIdptlDVSRTVGWFTSTYPVCLQD--KPDWASLIQSSK 1419
Cdd:cd19066   237 EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE----AVEDTIGLFLNLLPLRIDTspDATFPELLKRTK 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 499404635 1420 EQLRQVPDKGVGFNPLRYHH----PQGNSLTLSPIVFNYLG 1456
Cdd:cd19066   313 EQSREAIEHQRVPFIELVRHlgvvPEAPKHPLFEPVFTFKN 353
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 562-984 5.60e-30

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: 126.81  E-value: 5.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGd 641
Cdd:cd05932     7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 gqQLAQWSAEQ--------RIDLTDPAVV---EQWQDLPGDQPP---AIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLI 707
Cdd:cd05932    86 --KLDDWKAMApgvpegliSISLPPPSAAncqYQWDDLIAQHPPleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  708 NLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTLAFGEPNDRAIMQAEQAGATHLI-------------- 772
Cdd:cd05932   164 WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGgSLYGGVLVAFAESLDTFVEDVQRARPTLFFsvprlwtkfqqgvq 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  773 --LPTA----LMSI-----------LDPEQVNGIQAIGMGGEACPNAVVEnWADKVAL--YNMYGPTECTVTALSTRLRK 833
Cdd:cd05932   244 dkIPQQklnlLLKIpvvnslvkrkvLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLniLEAYGMTENFAYSHLNYPGR 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  834 GQPVTIGKPLIHIQALILDTagqlcpvgvpGELCLAGLGLARGYLNQPQMTASRFehitlndvNNAGqgaatlrIYRTGD 913
Cdd:cd05932   323 DKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAF--------TADG-------FLRTGD 377

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  914 KARLLNNGDYEYCGRIDEQIKL-RGYRIEPGEIEAQLaAVCPSLKQIKVIVAQVGSRPALV---AYATVKADSST 984
Cdd:cd05932   378 KGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKL-AEHDRVEMVCVIGSGLPAPLALVvlsEEARLRADAFA 451
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1567-1982 1.40e-29

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: 123.56  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1567 PLSSLQQSMLYHRLRcpQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECA-SIQVIVKQADLPFYYQ 1644
Cdd:cd19545     3 PCTPLQEGLMALTAR--QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGgLLQVVVKESPISWTES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1645 DLMQDadplavierYRQQDLRTGFDLSQPpLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQtlmqgqvl 1724
Cdd:cd19545    81 TSLDE---------YLEEDRAAPMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ-------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1725 mhGDAPAIQVD-RAYVDYARHAvaQQSAVDAFWQQRqslLAqtNDVSMLFAAagkradLSQHLTQIEPQVT-SVSLNEKD 1802
Cdd:cd19545   143 --GEPVPQPPPfSRFVKYLRQL--DDEAAAEFWRSY---LA--GLDPAVFPP------LPSSRYQPRPDATlEHSISLPS 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1803 QATLtafarevGITPSIIAQYAWHRLLARSTG-DAVSIvGNVLSGRESPVEDVASSVGLYINSLPLA--LSWQQPVslQQ 1879
Cdd:cd19545   208 SASS-------GVTLATVLRAAWALVLSRYTGsDDVVF-GVTLSGRNAPVPGIEQIVGPTIATVPLRvrIDPEQSV--ED 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1880 HLVQLQNELMAMNQHATQSL-----IALTAGRSRLFNSLFIYENYPDAKAEQGQRADDPHRL--YPEFSAAyekvemPLN 1952
Cdd:cd19545   278 FLQTVQKDLLDMIPFEHTGLqnirrLGPDARAACNFQTLLVVQPALPSSTSESLELGIEEESedLEDFSSY------GLT 351

                         410       420       430
                  ....*....|....*....|....*....|
gi 499404635 1953 LVVREQSGCMLLRFEFDADALDSAQARRVL 1982
Cdd:cd19545   352 LECQLSGSGLRVRARYDSSVISEEQVERLL 381
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 523-949 2.08e-29

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 125.84  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  523 LPRSYPQPQLTVTDVIEAVAQRDPQQLAIAFDGEPrtdtLTYAELNRQANQLAHWLHRQ-GLGEQSLVGVLAKRDRYFVI 601
Cdd:PRK08314    1 LPKSLTLPETSLFHNLEVSARRYPDKTAIVFYGRA----ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  602 ALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSV-ILGGD-GQQLAQWSAEQRI------------------------- 654
Cdd:PRK08314   77 AYYAILRANAVVVPVNPMNREEELAHYVTDSGARVaIVGSElAPKVAPAVGNLRLrhvivaqysdylpaepeiavpawlr 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  655 ------DLTDPAVVeQWQDL--PGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMF 726
Cdd:PRK08314  157 aepplqALAPGGVV-AWKEAlaAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  727 NCMSLsFDAGNMTTLL--PLSSGGTLAFGEPNDRAImqAEQAGATHLI-----LPTALMSILDPEQVNG-----IQAIGM 794
Cdd:PRK08314  236 AVLPL-FHVTGMVHSMnaPIYAGATVVLMPRWDREA--AARLIERYRVthwtnIPTMVVDFLASPGLAErdlssLRYIGG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 GGEACPNAVVENWADKVALYNM--YGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTA-GQLCPVGVPGELCLAGL 871
Cdd:PRK08314  313 GGAAMPEAVAERLKELTGLDYVegYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGP 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635  872 GLARGYLNQPQMTASRFehITLNdvnnaGQgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL 949
Cdd:PRK08314  393 QVFKGYWNRPEATAEAF--IEID-----GK-----RFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLL 458
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 682-1026 3.39e-29

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: 120.51  E-value: 3.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  682 QLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAIM 761
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  762 QAEQAGATHLIL-PTALMSILD----PEQVNGIQAIGMGGEACPNAVVENWADK-VALYNMYGPTE--CTVTALSTRLRK 833
Cdd:cd17630    81 DLAPPGVTHVSLvPTQLQRLLDsgqgPAALKSLRAVLLGGAPIPPELLERAADRgIPLYTTYGMTEtaSQVATKRPDGFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  834 GQPVtiGKPLIHIQALILDtagqlcpvgvPGELCLAGLGLARGYLNQPqmtasrfehiTLNDVNNAGqgaatlrIYRTGD 913
Cdd:cd17630   161 RGGV--GVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQ----------LVPEFNEDG-------WFTTKD 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  914 KARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQ---VGSRPALVayatVKADSStPEPAAV 990
Cdd:cd17630   212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAH-PAVRDAFVVGVPdeeLGQRPVAV----IVGRGP-ADPAEL 285

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 499404635  991 LIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd17630   286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 560-954 5.85e-29

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: 123.50  E-value: 5.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  560 DTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG 639
Cdd:cd05904    31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 gDGQQLAQW-SAEQRIDLTDPAVVEQW------QDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDD 712
Cdd:cd05904   111 -TAELAEKLaSLALPVVLLDSAEFDSLsfsdllFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQ 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  713 HRDRIDFTPQST--------MFNCMSLSFdagnmTTLLPLSSGGTL-AFGEPNDRAIMQAEQA-GATHL-ILPTALM--- 778
Cdd:cd05904   190 FVAGEGSNSDSEdvflcvlpMFHIYGLSS-----FALGLLRLGATVvVMPRFDLEELLAAIERyKVTHLpVVPPIVLalv 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  779 --SILDPEQVNGIQAIGMGGEACPNAVVENWADK---VALYNMYGPTECTVTALSTRLRKGQPV---TIGKPLIHIQALI 850
Cdd:cd05904   265 ksPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpnVDLGQGYGMTESTGVVAMCFAPEKDRAkygSVGRLVPNVEAKI 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LDTA-GQLCPVGVPGELCLAGLGLARGYLNQPQMTASrfehiTLNDvnnagQGaatlrIYRTGDKARLLNNGDYEYCGRI 929
Cdd:cd05904   345 VDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAA-----TIDK-----EG-----WLHTGDLCYIDEDGYLFIVDRL 409

                         410       420       430
                  ....*....|....*....|....*....|...
gi 499404635  930 DEQIKLRGYRIEPGEIEAQL--------AAVCP 954
Cdd:cd05904   410 KELIKYKGFQVAPAELEALLlshpeildAAVIP 442
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 536-1021 1.17e-28

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: 123.37  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAVAQRDPQQLAIAF---DGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:cd05970    21 DVVDAMAKEYPDKLALVWcddAGEERI--FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRHIITDANLSVILGGDGQQLAQ---------WSAEQRIDLTDPaVVEQWQD---LPGDQPPAIPR-H 679
Cdd:cd05970    99 AIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEeiekaapecPSKPKLVWVGDP-VPEGWIDfrkLIKNASPDFERpT 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  680 A------QQLAQVIYTSGSTGLPKgvMIEH------GSLI------NLLDD--HRDRIDFTPQSTMFNCMSLSFDAGnmt 739
Cdd:cd05970   178 AnsypcgEDILLVYFSSGTTGMPK--MVEHdftyplGHIVtakywqNVREGglHLTVADTGWGKAVWGKIYGQWIAG--- 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  740 tllplSSGGTLAFGEPNDRAIMQ-AEQAGATHLILPTALMSILDPEQV-----NGIQAIGMGGEACPNAVVENWADK--V 811
Cdd:cd05970   253 -----AAVFVYDYDKFDPKALLEkLSKYGVTTFCAPPTIYRFLIREDLsrydlSSLRYCTTAGEALNPEVFNTFKEKtgI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  812 ALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCL-----AGLGLARGYLNQPQMTAS 886
Cdd:cd05970   328 KLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgKPVGLFGGYYKDAEKTAE 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  887 RFEHitlndvnnagqgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLaavcpsLKQIKVIVAQV 966
Cdd:cd05970   408 VWHD----------------GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL------IQHPAVLECAV 465

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404635  967 GSRPALVAYATVKAD---SSTPEPAAVLID-----VAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:cd05970   466 TGVPDPIRGQVVKATivlAKGYEPSEELKKelqdhVKKVTAPYKYPRIVEFVDELPKTISGKI 528
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 688-1020 1.69e-28

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 119.30  E-value: 1.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  688 YTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTM------FNCMSLSfdagnMTTLLPLSSGGTLAFGEP--NDRA 759
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplFHCFGSV-----LGVLACLTHGATMVFPSPsfDPLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  760 IMQA---EQAGATHLIlPTALMSILD-PEQVN--------GIqaigMGGEACPNAVVEnwaDKVALYNM------YGPTE 821
Cdd:cd05917    84 VLEAiekEKCTALHGV-PTMFIAELEhPDFDKfdlsslrtGI----MAGAPCPPELMK---RVIEVMNMkdvtiaYGMTE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  822 CTVTALSTRLRKGQP---VTIGKPLIHIQALILD-TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfEHITlNDvn 897
Cdd:cd05917   156 TSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTA---EAID-GD-- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  898 nagqgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLaavcpsLKQIKVIVAQVGSRP------A 971
Cdd:cd05917   230 ---------GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFL------HTHPKVSDVQVVGVPderygeE 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499404635  972 LVAYATVKADSSTPEPaavliDVAKYLPE----YMVPFRLMLLEDMPLTPNGK 1020
Cdd:cd05917   295 VCAWIRLKEGAELTEE-----DIKAYCKGkiahYKVPRYVFFVDEFPLTVSGK 342
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 543-1021 2.00e-28

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: 123.07  E-value: 2.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  543 QRDPQQLAIAFDGE--PRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDY 620
Cdd:cd17634    64 RENGDRTAIIYEGDdtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  621 PPERLRHIITDANLSVILGGDG-----------------QQLAQWSAEQRIDLTDPAVVEQWQ--------DLPGDQPPA 675
Cdd:cd17634   144 APEAVAGRIIDSSSRLLITADGgvragrsvplkknvddaLNPNVTSVEHVIVLKRTGSDIDWQegrdlwwrDLIAKASPE 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  676 ---IPRHAQQLAQVIYTSGSTGLPKGVMIEHGS-LINLLDDHRDRIDFTPqSTMFNCMSlsfDAGNMTT---LL--PLSS 746
Cdd:cd17634   224 hqpEAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGP-GDIYWCTA---DVGWVTGhsyLLygPLAC 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  747 GGT--LAFGEPN----DRAIMQAEQAGATHLIL-PTALMSIL--DPEQVNG-----IQAIGMGGEACpNAVVENWADKV- 811
Cdd:cd17634   300 GATtlLYEGVPNwptpARMWQVVDKHGVNILYTaPTAIRALMaaGDDAIEGtdrssLRILGSVGEPI-NPEAYEWYWKKi 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  812 -----ALYNMYGPTEcTVTALSTRLRKGQPVTIG---KPLIHIQALILDTAGQLCPVGVPGELCLAGL--GLARGYLNQP 881
Cdd:cd17634   379 gkekcPVVDTWWQTE-TGGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH 457

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  882 QmtasRFEHITLNDVNNagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQikv 961
Cdd:cd17634   458 E----RFEQTYFSTFKG---------MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAH-PKVAE--- 520

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404635  962 iVAQVGSRPAL-----VAYATVKA-DSSTPEPAAVLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:cd17634   521 -AAVVGIPHAIkgqapYAYVVLNHgVEPSPELYAELRNwVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK07529 PRK07529
AMP-binding domain protein; Validated
 527-1020 3.60e-28

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 122.76  E-value: 3.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  527 YPQPQLTVT--DVIEAVAQRDPQQLAIAF--DGEP--RTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFV 600
Cdd:PRK07529   18 LAARDLPAStyELLSRAAARHPDAPALSFllDADPldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  601 IALLAIWKAGAAyVPLDPDYPPERLRHIITDANLSVI--LGGD-GQQLAQWSAEQR-----------IDLTDPAVVEQWQ 666
Cdd:PRK07529   98 FALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLvtLGPFpGTDIWQKVAEVLaalpelrtvveVDLARYLPGPKRL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  667 DLPGDQPPAI----------------------PRHAQQLAQVIYTSGSTGLPKGVMIEHGS------LINLLddhrdrID 718
Cdd:PRK07529  177 AVPLIRRKAHarildfdaelarqpgdrlfsgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanawLGALL------LG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  719 FTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTLAFGEP---NDRAIMQ-----AEQAGATHLI-LPTALMSILD-PeqVN 787
Cdd:PRK07529  251 LGPGDTVFCGLPLFHVNALLVTGLaPLARGAHVVLATPqgyRGPGVIAnfwkiVERYRINFLSgVPTVYAALLQvP--VD 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  788 GIQ------AIGmGGEACPNAVVENWADK--VALYNMYGPTECT-VTALSTRLRKGQPVTIGKPLIH--IQALILDTAGQ 856
Cdd:PRK07529  329 GHDisslryALC-GAAPLPVEVFRRFEAAtgVRIVEGYGLTEATcVSSVNPPDGERRIGSVGLRLPYqrVRVVILDDAGR 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  857 L---CPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNdvnnagqgaatlriyrTGDKARLLNNGDYEYCGRIDEQI 933
Cdd:PRK07529  408 YlrdCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLN----------------TGDLGRIDADGYFWLTGRAKDLI 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  934 KLRGYRIEPGEIEAQLA---AVcpslkqikVIVAQVGsRPAL------VAYATVKADSSTPEPAavLIDVAK-YLPE-YM 1002
Cdd:PRK07529  472 IRGGHNIDPAAIEEALLrhpAV--------ALAAAVG-RPDAhagelpVAYVQLKPGASATEAE--LLAFARdHIAErAA 540

                         570
                  ....*....|....*...
gi 499404635 1003 VPFRLMLLEDMPLTPNGK 1020
Cdd:PRK07529  541 VPKHVRILDALPKTAVGK 558
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 533-1016 1.17e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 120.23  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQqlAIAFDGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK06164   11 TLASLLDAHARARPD--AVALIDEDRP--LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRHIITDA--------------NLSVILGGDGQQLAQwsAEQRIDLTD----------PAVVEQWQDL 668
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGrarwlvvwpgfkgiDFAAILAAVPPDALP--PLRAIAVVDdaadatpapaPGARVQLFAL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  669 PGDQPP--AIPRHAQQLAQVIY--TSGSTGLPKGVMIEHGSLInlldDHRDRI----DFTPQSTMFnCMSLSFDAGNMTT 740
Cdd:PRK06164  165 PDPAPPaaAGERAADPDAGALLftTSGTTSGPKLVLHRQATLL----RHARAIarayGYDPGAVLL-AALPFCGVFGFST 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  741 LL-PLSSGGTL----AFGEPndRAIMQAEQAGATHLILPTALMS-ILDPEQVNG----IQAIGMGGEACPNAVVENWADK 810
Cdd:PRK06164  240 LLgALAGGAPLvcepVFDAA--RTARALRRHRVTHTFGNDEMLRrILDTAGERAdfpsARLFGFASFAPALGELAALARA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  811 --VALYNMYGPTEctVTALSTRLRKGQPVTI----GKPLIHIQAL--ILDTA-GQLCPVGVPGELCLAGLGLARGYLNQP 881
Cdd:PRK06164  318 rgVPLTGLYGSSE--VQALVALQPATDPVSVriegGGRPASPEARvrARDPQdGALLPDGESGEIEIRAPSLMRGYLDNP 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  882 QMTAsrfEHITLNDvnnagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKV 961
Cdd:PRK06164  396 DATA---RALTDDG------------YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA-LPGVAAAQV 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  962 IVAQVGSRPalVAYATVKADSST-PEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLT 1016
Cdd:PRK06164  460 VGATRDGKT--VPVAFVIPTDGAsPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 677-1026 2.72e-27

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: 118.20  E-value: 2.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  677 PRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAG-NMTTLLPLSSGGTLAFgEP 755
Cdd:cd05909   143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGlTGCLWLPLLSGIKVVF-HP 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  756 ND---RAIMQ-AEQAGATHLI-LPTALMSIL---DPEQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECT-V 824
Cdd:cd05909   222 NPldyKKIPElIYDKKATILLgTPTFLRGYAraaHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSpV 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  825 TALSTRLRKGQPVTIGKPLIHIQALILDTAGQL-CPVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndvnnagqga 903
Cdd:cd05909   302 ISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD------------- 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  904 atlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVAQVGSR-PALVAYATvkadS 982
Cdd:cd05909   369 ---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKgEKIVLLTT----T 441

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 499404635  983 STPEPAAvLIDVAKY--LPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05909   442 TDTDPSS-LNDILKNagISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1129-1351 7.83e-27

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 111.28  E-value: 7.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1129 LLPIQR--WFMEQSLArpeHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLGCDAEG----QRYLADVPCPaLSTLD 1201
Cdd:COG4908     1 LSPAQKrfLFLEPGSN---AYNIPAVLRLEgPLDVEALERALRELVRRHPALRTRFVEEDgepvQRIDPDADLP-LEVVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1202 YRQLGDDGLQQAFTALQSE-----FDPAQGRTMACALVRHHPQADtALFLAFHHLVIDAVSWRILVDDLERLY----LGE 1272
Cdd:COG4908    77 LSALPEPEREAELEELVAEeasrpFDLARGPLLRAALIRLGEDEH-VLLLTIHHIISDGWSLGILLRELAALYaallEGE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1273 PLL--PKTSSYRQWGAALQHYATQHA--EQLTYWQAQEDGVDLTALLAAKDPQG-----HASAAILTLDAKTTGQLVSEA 1343
Cdd:COG4908   156 PPPlpELPIQYADYAAWQRAWLQSEAleKQLEYWRQQLAGAPPVLELPTDRPRPavqtfRGATLSFTLPAELTEALKALA 235


                  ....*...
gi 499404635 1344 nRAFNTDV 1351
Cdd:COG4908   236 -KAHGATV 242
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 530-1028 1.72e-26

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 115.47  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  530 PQLTVTDVIEAVAQRDpqqlAIAFDGeprtDTLTYAELNRQANQLAHWLHRQGLgeqslVGVLAKRDRYFVIALLAIWKA 609
Cdd:PRK07787    2 ASLNPAAVAAAADIAD----AVRIGG----RVLSRSDLAGAATAVAERVAGARR-----VAVLATPTLATVLAVVGALIA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  610 GAAYVPLDPDYPPERLRHIITDANLSVILGGDGQQLAqwsAEQRIDLTDPAVVEQWQDLPGDQPPAIprhaqqlaqVIYT 689
Cdd:PRK07787   69 GVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPA---GLPHVPVRLHARSWHRYPEPDPDAPAL---------IVYT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  690 SGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTLA-FGEPNDRAIMQAEQAG 767
Cdd:PRK07787  137 SGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLgPLRIGNRFVhTGRPTPEAYAQALSEG 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  768 ATHLI-LPTALMSIL-DPEQ---VNGIQAIGMGGEACPNAVVENWADKV--ALYNMYGPTEcTVTALSTRL---RKgqPV 837
Cdd:PRK07787  217 GTLYFgVPTVWSRIAaDPEAaraLRGARLLVSGSAALPVPVFDRLAALTghRPVERYGMTE-TLITLSTRAdgeRR--PG 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  838 TIGKPLIHIQALILDTAGQLCPVGVP--GELCLAGLGLARGYLNQPQMTASRFehitlndvnnAGQGaatlrIYRTGDKA 915
Cdd:PRK07787  294 WVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAF----------TADG-----WFRTGDVA 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  916 RLLNNGDYEYCGR--IDeQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVA---QVGSRpaLVAYATvkadSSTPEPAAV 990
Cdd:PRK07787  359 VVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLG-HPGVREAAVVGVpddDLGQR--IVAYVV----GADDVAADE 430

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 499404635  991 LID-VAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPP 1028
Cdd:PRK07787  431 LIDfVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
 551-954 1.73e-26

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


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 116.09  E-value: 1.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   551 IAFDGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIIT 630
Cdd:TIGR02262   22 TAFIDDISS--LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLE 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   631 DANLSVILG------------GDGQQLaqwsaEQRIDLTDPAVVE-QWQDLPGDQPP---AIPRHAQQLAQVIYTSGSTG 694
Cdd:TIGR02262  100 DSRARVVFVsgallpvikaalGKSPHL-----EHRVVVGRPEAGEvQLAELLATESEqfkPAATQADDPAFWLYSSGSTG 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   695 LPKGVMIEHGSLINLLDDH-RDRIDFTPQSTMFNCMSLSF--DAGNMTTLlPLSSGGT-LAFGE-PNDRAIMQAEQAGAT 769
Cdd:TIGR02262  175 MPKGVVHTHSNPYWTAELYaRNTLGIREDDVCFSAAKLFFayGLGNALTF-PMSVGATtVLMGErPTPDAVFDRLRRHQP 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   770 HLI--LPTALMSIL-DP----EQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECTVTALSTRLRKGQPVTIG 840
Cdd:TIGR02262  254 TIFygVPTLYAAMLaDPnlpsEDQVRLRLCTSAGEALPAEVGQRWQARfgVDIVDGIGSTEMLHIFLSNLPGDVRYGTSG 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   841 KPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndvnnagQGAATlriyRTGDKARLLNN 920
Cdd:TIGR02262  334 KPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF------------QGEWT----RSGDKYVRNDD 397

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 499404635   921 GDYEYCGRIDEQIKLRGYRIEPGEIEAQL--------AAVCP 954
Cdd:TIGR02262  398 GSYTYAGRTDDMLKVSGIYVSPFEIESALiqhpavleAAVVG 439
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 533-1026 1.82e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 116.24  E-value: 1.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAFDGeprtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK06188   13 TYGHLLVSALKRYPDRPALVLGD----TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRHIITDANLSVILGGDGQ-------------QLAQW----SAEQRIDLTDPAVVEQWQDL-PGDQPP 674
Cdd:PRK06188   89 RTALHPLGSLDDHAYVLEDAGISTLIVDPAPfveralallarvpSLKHVltlgPVPDGVDLLAAAAKFGPAPLvAAALPP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  675 AIprhaqqlAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGnmTTLLP-LSSGGTL--- 750
Cdd:PRK06188  169 DI-------AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG--AFFLPtLLRGGTVivl 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  751 -AFgEPND--RAImQAEQAGAThLILPTALMSILDPEQV-----NGIQAIGMGGEA-CPNAVVEnwADKV---ALYNMYG 818
Cdd:PRK06188  240 aKF-DPAEvlRAI-EEQRITAT-FLVPTMIYALLDHPDLrtrdlSSLETVYYGASPmSPVRLAE--AIERfgpIFAQYYG 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  819 PTECTVTAlsTRLRKG-----QPVTI---GKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEH 890
Cdd:PRK06188  315 QTEAPMVI--TYLRKRdhdpdDPKRLtscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  891 ITLndvnnagqgaatlriyRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI-VAQVGSR 969
Cdd:PRK06188  393 GWL----------------HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEH-PAVAQVAVIgVPDEKWG 455

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499404635  970 PALVAYATVKADSStPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK06188  456 EAVTAVVVLRPGAA-VDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 95-497 2.68e-26

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: 113.82  E-value: 2.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   95 NMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEqGKGEQRIDAYQPFVIQHDDFSllpeaeregrlqqqVKAEI 174
Cdd:cd19537    25 NVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRD-GGLRRSYSSSPPRVQRVDTLD--------------VWKEI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  175 SRPFDLTAGDLTRVRlvkMSERThvLMITQHHIISDGWSVKNLFADFKpafLACQNCQPYPVettQLNYIDYAHWFN--S 252
Cdd:cd19537    90 NRPFDLEREDPIRVF---ISPDT--LLVVMSHIICDLTTLQLLLREVS---AAYNGKLLPPV---RREYLDSTAWSRpaS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  253 DSFLDyhnefkpFWVERLTGIPevhslPLDKPRPAHQNS-GGEVIFSAINNDLWDKFKRLCqrynTSNFIGLH----AVF 327
Cdd:cd19537   159 PEDLD-------FWSEYLSGLP-----LLNLPRRTSSKSyRGTSRVFQLPGSLYRSLLQFS----TSSGITLHqlalAAV 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  328 SLMLARISGEKDIVIGSPLAYRERPDIEDVVGFFVNTIVLRTQLQDSQN--FVDYLQYCREQDLSAFDHQLyRFEALSEA 405
Cdd:cd19537   223 ALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSSSDasAADFLRAVRRSSQAALAHAI-PWHQLLEH 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  406 IGSDRTTAINPIFQVMlvyqakVDFNDL--------IPGCDaaeetspVLP-----AKTDISVKVTELMGE---VRLDWl 469
Cdd:cd19537   302 LGLPPDSPNHPLFDVM------VTFHDDrgvslalpIPGVE-------PLYtwaegAKFPLMFEFTALSDDsllLRLEY- 367

                         410       420
                  ....*....|....*....|....*...
gi 499404635  470 fATALFERQTIQYYADRFIRLIEAVVEN 497
Cdd:cd19537   368 -DTDCFSEEEIDRIESLILAALELLVEG 394
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1567-1982 5.41e-26

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: 112.92  E-value: 5.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1567 PLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALESECAS--IQVIVKQADLPFYYQ 1644
Cdd:cd19544     3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSepVQVVWRQAELPVEEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1645 DLMQDADPLA-VIERYRQQDLRtgFDLSQPPLLRIACFRLGEQD-YRVLLSCHHSVIDGWSgpqlLGAVHRDYQTLMQGQ 1722
Cdd:cd19544    83 TLDPGDDALAqLRARFDPRRYR--LDLRQAPLLRAHVAEDPANGrWLLLLLFHHLISDHTS----LELLLEEIQAILAGR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1723 VlmHGDAPAIQVdRAYVDYARHAVAQQSAVDAFwqqrQSLLAqtnDVSM------LFAAAGKRADLSQHLTQIEPQVTsv 1796
Cdd:cd19544   157 A--AALPPPVPY-RNFVAQARLGASQAEHEAFF----REMLG---DVDEptapfgLLDVQGDGSDITEARLALDAELA-- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1797 slnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTG--DAVsiVGNVLSGRESPVEDVASSVGLYINSLPLALSWQQp 1874
Cdd:cd19544   225 -------QRLRAQARRLGVSPASLFHLAWALVLARCSGrdDVV--FGTVLSGRMQGGAGADRALGMFINTLPLRVRLGG- 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1875 VSLQQHLVQLQNELMAMNQHATQSLiALT------AGRSRLFNSLFiyeNYP-DAKAEQGQRADDPHRLypEFSAAYEKV 1947
Cdd:cd19544   295 RSVREAVRQTHARLAELLRHEHASL-ALAqrcsgvPAPTPLFSALL---NYRhSAAAAAAAALAAWEGI--ELLGGEERT 368

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 499404635 1948 EMPLNLVVREQSGcmllRFEFDADALDSAQARRVL 1982
Cdd:cd19544   369 NYPLTLSVDDLGD----GFSLTAQVVAPIDAERVC 399
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 514-1027 7.00e-26

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 114.32  E-value: 7.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  514 AAVLAETQQLPR--SYPQPQLTVTdvieavAQRDPQQLAIAFDgeprTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGV 591
Cdd:PRK13383   21 RAVLRLLREASRggTNPYTLLAVT------AARWPGRTAIIDD----DGALSYRELQRATESLARRLTRDGVAPGRAVGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  592 LAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD--GQQLAqwSAEQRIDLTDPAVVEqwqdlp 669
Cdd:PRK13383   91 MCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNefAERIA--GADDAVAVIDPATAG------ 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  670 GDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEH------GSLINLLDDHRDRID--FTPQSTMFNCMSLSFdagnmtTL 741
Cdd:PRK13383  163 AEESGGRPAVAAPGRIVLLTSGTTGKPKGVPRAPqlrsavGVWVTILDRTRLRTGsrISVAMPMFHGLGLGM------LM 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  742 LPLSSGGTLAFGEPND--RAIMQAEQAGATHL-ILPTALMSILD-PEQVNG------IQAIGMGGEACPNAVVENWADKV 811
Cdd:PRK13383  237 LTIALGGTVLTHRHFDaeAALAQASLHRADAFtAVPVVLARILElPPRVRArnplpqLRVVMSSGDRLDPTLGQRFMDTY 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  812 A--LYNMYGPTECTVTALST--RLRKGqPVTIGKPLIHIQALILDTAGQlcPVGvpgelclaglglargylnqPQMTASR 887
Cdd:PRK13383  317 GdiLYNGYGSTEVGIGALATpaDLRDA-PETVGKPVAGCPVRILDRNNR--PVG-------------------PRVTGRI 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  888 FEHITLN-DVNNAGQGAATLR-IYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI-VA 964
Cdd:PRK13383  375 FVGGELAgTRYTDGGGKAVVDgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAA-HPAVADNAVIgVP 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  965 --QVGSRpaLVAYATVKADSSTpePAAVLIDVAK-YLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:PRK13383  454 deRFGHR--LAAFVVLHPGSGV--DAAQLRDYLKdRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
PRK12316 PRK12316
peptide synthase; Provisional
 1539-2003 1.73e-25

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 116.60  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1539 TPSDFPAVNLSQTQLDSLS-QRYDIDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFP 1617
Cdd:PRK12316 2575 TLAAFAASLESGQTSRAPVlQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHE 2654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1618 ALRAALESECA-SIQVIVKQADLPFYYQDLMQDADplAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHH 1696
Cdd:PRK12316 2655 TLRTRFVEVGEqTRQVILPNMSLRIVLEDCAGVAD--AAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHH 2732

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1697 SVIDGWSGPQLLGAVHRDYQTLMQGQVLMHGDAPAIQVDRAYVDYARHAVAQQSAVDAFWQQRqsllAQTNDVSMLFAAA 1776
Cdd:PRK12316 2733 IVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRER----LGGEQPVLELPLD 2808

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1777 GKRADLSQHLTQIEPQVTSVSLNEKdqatLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPveDVAS 1856
Cdd:PRK12316 2809 RPRPALQSHRGARLDVALDVALSRE----LLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETER 2882

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1857 SVGLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHA----TQSLIALTAGRSR----LFNSLFIYENYPDAKAEQGq 1928
Cdd:PRK12316 2883 LIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQdlpfEQLVEALQPERSLshspLFQVMYNHQSGERAAAQLP- 2961

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404635 1929 rADDPHRLYPEFSAAyekvEMPLNLVVREQSGCMLLRFEFDADALDSAQARRVLMRWHDEVVALVNSVPQQPAEI 2003
Cdd:PRK12316 2962 -GLHIESFAWDGAAT----QFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDEL 3031
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 532-1021 1.77e-25

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 113.06  E-value: 1.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGA 611
Cdd:PRK06145    2 FNLSASIAFHARRTPDRAALVYRDQ----EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  612 AYVPLDPDYPPERLRHIITDANLSVILgGDGQQLAQWSAEQRIDLTDPAVVEQWQDL--PGDQ-PPAIPRHAQQLAQVIY 688
Cdd:PRK06145   78 VFLPINYRLAADEVAYILGDAGAKLLL-VDEEFDAIVALETPKIVIDAAAQADSRRLaqGGLEiPPQAAVAPTDLVRLMY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  689 TSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSL-SFDAGNMTTLLPLSSGGTLAFGEPND-RAIMQAEQ- 765
Cdd:PRK06145  157 TSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLyHVGAFDLPGIAVLWVGGTLRIHREFDpEAVLAAIEr 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  766 ----AGATHLILPTALMSILDPEQ--VNGIQAIGMGGEACPNAVVENWAD---KVALYNMYGPTE-CTVTALSTRLRKGQ 835
Cdd:PRK06145  237 hrltCAWMAPVMLSRVLTVPDRDRfdLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTEtCSGDTLMEAGREIE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  836 PV-TIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDvnnagqgaatlrIYRTGDK 914
Cdd:PRK06145  317 KIgSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF----YGD------------WFRSGDV 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  915 ARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVA---QVGSRPALVayaTVKADSSTPEPAAVL 991
Cdd:PRK06145  381 GYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYEL-PEVAEAAVIGVhddRWGERITAV---VVLNPGATLTLEALD 456

                         490       500       510
                  ....*....|....*....|....*....|
gi 499404635  992 IDVAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK06145  457 RHCRQRLASFKVPRQLKVRDELPRNPSGKV 486
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 532-1026 4.18e-25

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: 112.16  E-value: 4.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAVAQRDPQQLAIAfDGEPRtdtLTYAELNRQANQLAHWLHRQGLGeqslvgvlaKRDR---------YFVIA 602
Cdd:COG1021    25 ETLGDLLRRRAERHPDRIAVV-DGERR---LSYAELDRRADRLAAGLLALGLR---------PGDRvvvqlpnvaEFVIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  603 LLAIWKAGAAYVPLdpdYPPER---LRHII--TDANLSVILGGDG---------QQLAQWSA-EQRIDLTDPAVVEQWQD 667
Cdd:COG1021    92 FFALFRAGAIPVFA---LPAHRraeISHFAeqSEAVAYIIPDRHRgfdyralarELQAEVPSlRHVLVVGDAGEFTSLDA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  668 L---PGDQPPAIPrHAQQLAQVIYTSGSTGLPKgvMIEHgslinlldDHRDRI----------DFTPQSTMFNCMSLsfd 734
Cdd:COG1021   169 LlaaPADLSEPRP-DPDDVAFFQLSGGTTGLPK--LIPR--------THDDYLysvrasaeicGLDADTVYLAALPA--- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  735 AGNMTTLLP-----LSSGGTLAF---GEPnDRAIMQAEQAGATHLIL-PTALMSILD-----PEQVNGIQAIGMGGEACP 800
Cdd:COG1021   235 AHNFPLSSPgvlgvLYAGGTVVLapdPSP-DTAFPLIERERVTVTALvPPLALLWLDaaersRYDLSSLRVLQVGGAKLS 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  801 NAVvenwADKV------ALYNMYGPTECTVTalSTRLrkGQPV-----TIGKPL-IHIQALILDTAGQLCPVGVPGELCL 868
Cdd:COG1021   314 PEL----ARRVrpalgcTLQQVFGMAEGLVN--YTRL--DDPEeviltTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLT 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  869 AGLGLARGYLNQPQMTASRFEHitlndvnnagQGaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQ 948
Cdd:COG1021   386 RGPYTIRGYYRAPEHNARAFTP----------DG-----FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENL 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  949 LAAvCPSlkqikviVAQVgsrpALVAY----------ATVKADSSTPEPAAVLidvaKYL-----PEYMVPFRLMLLEDM 1013
Cdd:COG1021   451 LLA-HPA-------VHDA----AVVAMpdeylgerscAFVVPRGEPLTLAELR----RFLrerglAAFKLPDRLEFVDAL 514

                         570
                  ....*....|...
gi 499404635 1014 PLTPNGKLDMKQL 1026
Cdd:COG1021   515 PLTAVGKIDKKAL 527
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
 1414-1556 5.29e-25

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: 103.12  E-value: 5.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  1414 LIQSSKEQLRQVPDKGVGFNPLRYHHPQGNSLTLSP---IVFNYLG---LSVQaAGTWRPVDVAPGCCVSPGNKPAEVIS 1487
Cdd:TIGR01720    5 LIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAASPqpeISFNYLGqfdADSN-DELFQPSSYSPGEAISPESPRPYALE 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635  1488 LHGGITGGQLTLRQV--GCLNQRDS-ERLMTRLTENLRALTEACLTQLSHGvvFTPSDFPAVNLSQTQLDSL 1556
Cdd:TIGR01720   84 INAMIEDGELTLTWSypTQLFSEDTiEQLADRFKEALEALIAHCAGKEGGG--LTPSDFSLKDLTQDELDEL 153
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 554-1026 9.00e-25

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


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 111.18  E-value: 9.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  554 DGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLA-KRDRYFViALLAIWKAGAAYVPLDPDYPPERL------- 625
Cdd:cd12119    18 THEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAwNTHRHLE-LYYAVPGMGAVLHTINPRLFPEQIayiinha 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  626 --RHIITDANLS---------------VILGGDGQQLA------QWSAEQRIDLTDPavVEQWQDLPGDQPPAIprhaqq 682
Cdd:cd12119    97 edRVVFVDRDFLplleaiaprlptvehVVVMTDDAAMPepagvgVLAYEELLAAESP--EYDWPDFDENTAAAI------ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  683 laqvIYTSGSTGLPKGVMIEHGSLInLlddHrdridftpqsTMFNCMSLSFDAGNMTTLLPLS----------------S 746
Cdd:cd12119   169 ----CYTSGTTGNPKGVVYSHRSLV-L---H----------AMAALLTDGLGLSESDVVLPVVpmfhvnawglpyaaamV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  747 GGTLAFGEPNDRA-----IMQAEQAGATHLIlPTALMSILDPEQVNG-----IQAIGMGGEACPNAVVENWADK-VALYN 815
Cdd:cd12119   231 GAKLVLPGPYLDPaslaeLIEREGVTFAAGV-PTVWQGLLDHLEANGrdlssLRRVVIGGSAVPRSLIEAFEERgVRVIH 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  816 MYGPTE----CTVTALSTRLRKGQP-------VTIGKPLIHIQALILDTAGQLCPV-GVP-GELCLAGLGLARGYLNQPQ 882
Cdd:cd12119   310 AWGMTEtsplGTVARPPSEHSNLSEdeqlalrAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  883 MTASRFEHITLndvnnagqgaatlriyRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI 962
Cdd:cd12119   390 ESEALTEDGWL----------------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMA-HPAVAEAAVI 452

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499404635  963 VA---QVGSRPALVayaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd12119   453 GVphpKWGERPLAV---VVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 506-1021 9.01e-25

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 111.30  E-value: 9.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  506 PLMETDRFAAVLAETQQLPRsypqpqlTVTDVIEAVAQRDPQQLAI--AFDGEPRTDTLTYAELNRQANQLAHWLHRQGL 583
Cdd:PRK13295    5 AVLLPPRRAASIAAGHWHDR-------TINDDLDACVASCPDKTAVtaVRLGTGAPRRFTYRELAALVDRVAVGLARLGV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  584 GEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVIL------GGDGQQLAQ-----WSAEQ 652
Cdd:PRK13295   78 GRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVvpktfrGFDHAAMARrlrpeLPALR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  653 RI-------------DLTDPAvveqWQDLPGDQPP-AIPR-HAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRI 717
Cdd:PRK13295  158 HVvvvggdgadsfeaLLITPA----WEQEPDAPAIlARLRpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  718 DFTPQSTMFNCMSLSFDAGNMTTL-LPLSSGGTLAFGE--PNDRAIMQAEQAGATHLILPTALMSIL------DPEQVNG 788
Cdd:PRK13295  234 GLGADDVILMASPMAHQTGFMYGLmMPVMLGATAVLQDiwDPARAAELIRTEGVTFTMASTPFLTDLtravkeSGRPVSS 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  789 IQAIGMGGEACPNAVVENwADKV---ALYNMYGPTEC---TVTALSTRLRKGQpVTIGKPLIHIQALILDTAGQLCPVGV 862
Cdd:PRK13295  314 LRTFLCAGAPIPGALVER-ARAAlgaKIVSAWGMTENgavTLTKLDDPDERAS-TTDGCPLPGVEVRVVDADGAPLPAGQ 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  863 PGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnaGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEP 942
Cdd:PRK13295  392 IGRLQVRGCSNFGGYLKRPQLNGTDAD----------GW-------FDTGDLARIDADGYIRISGRSKDVIIRGGENIPV 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  943 GEIEAQLAAvCPSLKQIKVIV---AQVGSRpaLVAYATVKADSSTPEPAAV-LID---VAK-YLPEymvpfRLMLLEDMP 1014
Cdd:PRK13295  455 VEIEALLYR-HPAIAQVAIVAypdERLGER--ACAFVVPRPGQSLDFEEMVeFLKaqkVAKqYIPE-----RLVVRDALP 526


                  ....*..
gi 499404635 1015 LTPNGKL 1021
Cdd:PRK13295  527 RTPSGKI 533
PRK13382 PRK13382
bile acid CoA ligase;
508-1027 1.34e-24

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 110.62  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  508 METDRFAAVLAETQQLprsypqpQLTVTDVIEAVAQRDPQQLAIAFDgeprTDTLTYAELNRQANQLAHWLHRQGLGEQS 587
Cdd:PRK13382   26 MRPDRYLRIVAAMRRE-------GMGPTSGFAIAAQRCPDRPGLIDE----LGTLTWRELDERSDALAAALQALPIGEPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  588 LVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD------GQQLAQWSAEQRI----DLT 657
Cdd:PRK13382   95 VVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEefsatvDRALADCPQATRIvawtDED 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  658 DPAVVEQWQDLP-GDQPPAIPRHAQqlaQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQST------MFNC-- 728
Cdd:PRK13382  175 HDLTVEVLIAAHaGQRPEPTGRKGR---VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPtvivapMFHAwg 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  729 -----MSLSFdAGNMTTLLPLSSGGTLAFGEPNDraimqaeqagATHL-ILPTALMSILD-PEQV------NGIQAIGMG 795
Cdd:PRK13382  252 fsqlvLAASL-ACTIVTRRRFDPEATLDLIDRHR----------ATGLaVVPVMFDRIMDlPAEVrnrysgRSLRFAAAS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  796 GEACPNAVVENWADKV--ALYNMYGPTECTVTALST--RLRKgQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAgl 871
Cdd:PRK13382  321 GSRMRPDVVIAFMDQFgdVIYNNYNATEAGMIATATpaDLRA-APDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVR-- 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  872 glargylnqpqmTASRFEHITLNDVNNAGQGAATlriyrTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAA 951
Cdd:PRK13382  398 ------------NDTQFDGYTSGSTKDFHDGFMA-----SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLAT 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  952 VcPSLKQIKVIVA---QVGSRpaLVAYATVKADSS-TPEPAAVliDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:PRK13382  461 H-PDVAEAAVIGVddeQYGQR--LAAFVVLKPGASaTPETLKQ--HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 525-1021 2.04e-23

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 107.15  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  525 RSYPQPQLTVTDVIEAVAQRDPQQLAIAFDGEPRTdtltYAELNRQANQLAHWLHRQGLGEQSLVGVL-AKRDRYFVIAL 603
Cdd:PRK06155   14 DPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWT----YAEAARAAAAAAHALAAAGVKRGDRVALMcGNRIEFLDVFL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  604 LAIWkAGAAYVPLDPDYPPERLRHIITD-------------ANLSVILGGDGQQLAQWSAEQRIDLTDPAVVEQWQDLPG 670
Cdd:PRK06155   90 GCAW-LGAIAVPINTALRGPQLEHILRNsgarllvveaallAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  671 DQ--PPAIPRHAQQLAqVIYTSGSTGLPKGVMIEHGSL----INLLDDhrdrIDFTPQSTMFNCMSLsFDAGNMTTLLP- 743
Cdd:PRK06155  169 DApaPAAAVQPGDTAA-ILYTSGTTGPSKGVCCPHAQFywwgRNSAED----LEIGADDVLYTTLPL-FHTNALNAFFQa 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  744 LSSGGTLAFGEpndR-------AIMQAEQAGATHLIlpTALMSILD-----PEQVNGIQAIGMGGeACPNAVVENWADK- 810
Cdd:PRK06155  243 LLAGATYVLEP---RfsasgfwPAVRRHGATVTYLL--GAMVSILLsqparESDRAHRVRVALGP-GVPAALHAAFRERf 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  811 -VALYNMYGPTEcTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAG---LGLARGYLNQPqmtas 886
Cdd:PRK06155  317 gVDLLDGYGSTE-TNFVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMP----- 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  887 rfehitlndvnnagqgAATLRIYR-----TGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKV 961
Cdd:PRK06155  391 ----------------EKTVEAWRnlwfhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLS-HPAVAAAAV 453

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  962 IVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK06155  454 FPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV 513
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 542-1026 4.33e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 105.93  E-value: 4.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAI--AFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPD 619
Cdd:PRK13391    7 AQTTPDKPAVimASTGE----VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  620 YPPERLRHIITDANlSVILGGDGQQL--AQWSAEQ------RIDLTDPAVVEQWQDLPG--DQPPAIPRHAQQLAQ-VIY 688
Cdd:PRK13391   83 LTPAEAAYIVDDSG-ARALITSAAKLdvARALLKQcpgvrhRLVLDGDGELEGFVGYAEavAGLPATPIADESLGTdMLY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  689 TSGSTGLPKGVMIEHGSLinllddhrdRIDFTPQSTMFNCMSLSFDAGnMTTLLP---------------LSSGGTLAFG 753
Cdd:PRK13391  162 SSGTTGRPKGIKRPLPEQ---------PPDTPLPLTAFLQRLWGFRSD-MVYLSPaplyhsapqravmlvIRLGGTVIVM 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  754 EPND--RAIMQAEQAGATH-LILPTALMSILD-PEQVNG------IQAIGMGGEACPNAVVE---NWADKVaLYNMYGPT 820
Cdd:PRK13391  232 EHFDaeQYLALIEEYGVTHtQLVPTMFSRMLKlPEEVRDkydlssLEVAIHAAAPCPPQVKEqmiDWWGPI-IHEYYAAT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  821 ECT-VTALSTRLRKGQPVTIGKPLIHIqALILDTAGQLCPVGVPGELCLAGlGLARGYLNQPQMTA-SRFEHITLNDVNN 898
Cdd:PRK13391  311 EGLgFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAeARHPDGTWSTVGD 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  899 AGQGAATLRIYRTGDKARLLNNGdyeycgrideqiklrGYRIEPGEIEaQLAAVCPslkqiKVIVAQVGSRP-------- 970
Cdd:PRK13391  389 IGYVDEDGYLYLTDRAAFMIISG---------------GVNIYPQEAE-NLLITHP-----KVADAAVFGVPnedlgeev 447

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635  971 -ALVayATVKADSSTPEPAAVLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKLdMKQL 1026
Cdd:PRK13391  448 kAVV--QPVDGVDPGPALAAELIAfCRQRLSRQKCPRSIDFEDELPRLPTGKL-YKRL 502
PRK12467 PRK12467
peptide synthase; Provisional
 1548-2031 4.60e-23

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 108.32  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1548 LSQTQLDSLSQrYDIDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESE 1626
Cdd:PRK12467 1100 QQQGAQPALPD-VDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFvQED 1178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1627 CASIQVIVKQADLPFYYQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQ 1706
Cdd:PRK12467 1179 GRTRQVIHPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQV 1258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1707 LLGAVHRDYQTLMQGQVLmhgDAPAIQVDraYVDYarhAVAQQSAVDAFWQQRQ-----SLLAQTNDVSMLFAAAGKRAD 1781
Cdd:PRK12467 1259 LVDELVALYAAYSQGQSL---QLPALPIQ--YADY---AVWQRQWMDAGERARQlaywkAQLGGEQPVLELPTDRPRPAV 1330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1782 LS----QHLTQIEPQVTSvslnekdqaTLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESpvEDVASS 1857
Cdd:PRK12467 1331 QShrgaRLAFELPPALAE---------GLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR--AETEGL 1399

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1858 VGLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHA----TQSLIALTAGRSRLFNSLF--IYENYPDAKAEQGQrad 1931
Cdd:PRK12467 1400 IGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQdlpfEQLVEALQPERSLSHSPLFqvMFNHQRDDHQAQAQ--- 1476

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1932 dPHRLYPE-FSAAYEKVEMPLNLVVREQSGCMLLRFEFDADALDSAQARRVLMRWHDevvaLVNSVPQQPAEIIGhdKAT 2010
Cdd:PRK12467 1477 -LPGLSVEsLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLN----LLQGLVADPERRLG--ELD 1549

                         490       500
                  ....*....|....*....|.
gi 499404635 2011 GLVAAQKTVADSGINQPDTSF 2031
Cdd:PRK12467 1550 LLDEAERRQILEGWNATHTGY 1570
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 73-425 4.60e-23

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: 104.45  E-value: 4.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQRIDAYQPFVIQHD 152
Cdd:cd19536     3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTEL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  153 DfsLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLM-ITQHHIISDGWSVKNLFADFKPAFLACQNC 231
Cdd:cd19536    83 D--LTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  232 QPYPVETTQlNYIDYAHWfNSDSFLDyhNEFKPFWVERLTGipeVHSLPLDKPRPAHQNSGGEVIFSAINNDLWDKFKRL 311
Cdd:cd19536   161 KPLSLPPAQ-PYRDFVAH-ERASIQQ--AASERYWREYLAG---ATLATLPALSEAVGGGPEQDSELLVSVPLPVRSRSL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  312 CQRYNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGFFVNTIVLRTQLQDsQNFVDYLQYCREQDL 389
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLSE-ETVEDLLKRAQEQEL 312

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 499404635  390 SAFDHQLYRFEALSeaigsdRTTAINPIFQVMLVYQ 425
Cdd:cd19536   313 ESLSHEQVPLADIQ------RCSEGEPLFDSIVNFR 342
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 524-1020 4.73e-23

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 106.24  E-value: 4.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  524 PRSYPQPQLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIAL 603
Cdd:PRK05605   24 PHDLDYGDTTLVDLYDNAVARFGDRPALDFFGA----TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  604 LAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGDG-----QQLA---------------------QWS-------- 649
Cdd:PRK05605  100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKvaptvERLRrttpletivsvnmiaampllqRLAlrlpipal 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  650 AEQRIDLTDPAV-VEQWQDLPGDQPPA---IPRH----AQQLAQVIYTSGSTGLPKGVMIEHGSLI-NLL------DDHR 714
Cdd:PRK05605  180 RKARAALTGPAPgTVPWETLVDAAIGGdgsDVSHprptPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAqgkawvPGLG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  715 DRidftpQSTMFNCMSLsFDAGNMTTLLPLSS--GGTLA-FGEPNDRAIMQA-EQAGATHL-ILPTALMSILDPEQVNGI 789
Cdd:PRK05605  260 DG-----PERVLAALPM-FHAYGLTLCLTLAVsiGGELVlLPAPDIDLILDAmKKHPPTWLpGVPPLYEKIAEAAEERGV 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  790 QAIGM-----GGEACPNAVVENWADKVA--LYNMYGPTECTVTALSTRLRKG-QPVTIGKPLIHIQALILD--TAGQLCP 859
Cdd:PRK05605  334 DLSGVrnafsGAMALPVSTVELWEKLTGglLVEGYGLTETSPIIVGNPMSDDrRPGYVGVPFPDTEVRIVDpeDPDETMP 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  860 VGVPGELCLAGLGLARGYLNQPQMTASRFehitLNDvnnagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYR 939
Cdd:PRK05605  414 DGEEGELLVRGPQVFKGYWNRPEETAKSF----LDG------------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFN 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  940 IEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNG 1019
Cdd:PRK05605  478 VYPAEVEEVLREH-PGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556


                  .
gi 499404635 1020 K 1020
Cdd:PRK05605  557 K 557
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1566-1980 4.83e-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: 104.36  E-value: 4.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSM-LYHRLRcPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIVKQADLPFYY 1643
Cdd:cd19531     2 LPLSFAQQRLwFLDQLE-PGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFvEVDGEPVQVILPPLPLPLPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1644 QDL--MQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQG 1721
Cdd:cd19531    81 VDLsgLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 Q--VLmhgDAPAIQvdraYVDYAR--HAVAQQSAVD---AFWQQRqslLAQTNDVSML-----------FAAAGKRADLS 1783
Cdd:cd19531   161 RpsPL---PPLPIQ----YADYAVwqREWLQGEVLErqlAYWREQ---LAGAPPVLELptdrprpavqsFRGARVRFTLP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1784 QHLTQiepqvtsvslnekdqaTLTAFAREVGITPSIIAQYAWHRLLARSTG--DAVsiVGNVLSGRESP-VEDVassVGL 1860
Cdd:cd19531   231 AELTA----------------ALRALARREGATLFMTLLAAFQVLLHRYSGqdDIV--VGTPVAGRNRAeLEGL---IGF 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1861 YINSLPL--ALSWQQPVS--LQQ-----------------HLVQ-LQNElmamnqhatQSLialtaGRSRLFNSLFIYEN 1918
Cdd:cd19531   290 FVNTLVLrtDLSGDPTFRelLARvretaleayahqdlpfeKLVEaLQPE---------RDL-----SRSPLFQVMFVLQN 355

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635 1919 YPDAKAEQGQRADDPHRLYPEfSAAYEkvempLNLVVREQSGCMLLRFEFDADALDSAQARR 1980
Cdd:cd19531   356 APAAALELPGLTVEPLEVDSG-TAKFD-----LTLSLTETDGGLRGSLEYNTDLFDAATIER 411
PRK08315 PRK08315
AMP-binding domain protein; Validated
 524-946 6.92e-23

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 105.66  E-value: 6.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  524 PRSYPQPQLTVTDVIEAVAQRDPQQLAIAF-DGEPRtdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIA 602
Cdd:PRK08315    8 PTDVPLLEQTIGQLLDRTAARYPDREALVYrDQGLR---WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  603 LLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGDG----------QQLAQWSAEQ-----------------RID 655
Cdd:PRK08315   85 QFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlYELAPELATCepgqlqsarlpelrrviFLG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  656 LTDPAVVEQWQDLPGD----QPPAIPRHAQQLA--QVI---YTSGSTGLPKGVMIEHGsliNLLDDHR---DRIDFTPQS 723
Cdd:PRK08315  165 DEKHPGMLNFDELLALgravDDAELAARQATLDpdDPIniqYTSGTTGFPKGATLTHR---NILNNGYfigEAMKLTEED 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  724 TM------FNC--MSLsfdaGNMTTLlplSSGGTLAFgePNDR----AIMQA-EQAGATHLI-LPTALMSILD-PEQVN- 787
Cdd:PRK08315  242 RLcipvplYHCfgMVL----GNLACV---THGATMVY--PGEGfdplATLAAvEEERCTALYgVPTMFIAELDhPDFARf 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  788 -------GIqaigMGGEACPNAVVENWADKValyNM------YGPTEC----TVTALSTRLRKgQPVTIGKPLIHIQALI 850
Cdd:PRK08315  313 dlsslrtGI----MAGSPCPIEVMKRVIDKM---HMsevtiaYGMTETspvsTQTRTDDPLEK-RVTTVGRALPHLEVKI 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  851 LDTA-GQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfEHItlnDVNnagqgaatlRIYRTGDKARLLNNGdyeYC--- 926
Cdd:PRK08315  385 VDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTA---EAI---DAD---------GWMHTGDLAVMDEEG---YVniv 446

                         490       500
                  ....*....|....*....|.
gi 499404635  927 GRIDEQIkLR-GYRIEPGEIE 946
Cdd:PRK08315  447 GRIKDMI-IRgGENIYPREIE 466
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
538-1026 8.84e-23

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 104.56  E-value: 8.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWL-HRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPL 616
Cdd:PRK06839    8 IEKRAYLHPDRIAIITEEE----EMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  617 DPDYPPERLRHIITDANLSVILGGDGQQLAQWSAEQR------IDLTDPAVVEQWQ----DLPGDQPPAIprhaqqlaqV 686
Cdd:PRK06839   84 NIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVsyvqrvISITSLKEIEDRKidnfVEKNESASFI---------I 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  687 IYTSGSTGLPKGVMIEH-----GSLINLLddhrdRIDFTPQSTMFNCMSLSFDAG-NMTTLLPLSSGGTLAFG---EPnD 757
Cdd:PRK06839  155 CYTSGTTGKPKGAVLTQenmfwNALNNTF-----AIDLTMHDRSIVLLPLFHIGGiGLFAFPTLFAGGVIIVPrkfEP-T 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  758 RAIMQAEQAGATHLI-LPT---ALMSILDPEQVNgIQAIGM---GGEACPNAVVENWADKVALYNM-YGPTEC--TVTAL 827
Cdd:PRK06839  229 KALSMIEKHKVTVVMgVPTihqALINCSKFETTN-LQSVRWfynGGAPCPEELMREFIDRGFLFGQgFGMTETspTVFML 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  828 STRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfehitlNDVNNAGqgaatlr 907
Cdd:PRK06839  308 SEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE--------ETIQDGW------- 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  908 iYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEaQLAAVCPSLKQIKVIvaqvgSRPAlVAYATVKADSSTPEP 987
Cdd:PRK06839  373 -LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVE-QVINKLSDVYEVAVV-----GRQH-VKWGEIPIAFIVKKS 444

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 499404635  988 AAVLID------VAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK06839  445 SSVLIEkdviehCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
520-1022 9.19e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 104.97  E-value: 9.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  520 TQQLPRSYPQPQLTvtDVIEAVAQRDPQQLAIAFDGEpRTdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYF 599
Cdd:PRK05852    6 GAAPMASDFGPRIA--DLVEVAATRLPEAPALVVTAD-RI-AISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  600 VIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG---GDGQQLAQ----WSAEQRI---DLTDPAVVEQWQDLP 669
Cdd:PRK05852   82 VVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIdadGPHDRAEPttrwWPLTVNVggdSGPSGGTLSVHLDAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  670 GdQPPAIPRHAQQL----AQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLP-L 744
Cdd:PRK05852  162 T-EPTPATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAtL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  745 SSGGTL---AFGEPNDRAIM-QAEQAGAT--------HLIL------------PTALMSI------LDPEQVNGIQAIGM 794
Cdd:PRK05852  241 ASGGAVllpARGRFSAHTFWdDIKAVGATwytavptiHQILleraatepsgrkPAALRFIrscsapLTAETAQALQTEFA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 GGEACPnavvenwadkvalynmYGPTECTVTALSTRL----RKGQPVTIGKPLIH---IQALILDTAGQLCPVGVPGELC 867
Cdd:PRK05852  321 APVVCA----------------FGMTEATHQVTTTQIegigQTENPVVSTGLVGRstgAQIRIVGSDGLPLPAGAVGEVW 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  868 LAGLGLARGYLNQPQMTASRFEHITLndvnnagqgaatlriyRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:PRK05852  385 LRGTTVVRGYLGDPTITAANFTDGWL----------------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEG 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLAAvCPSlkqikVIVAQVGSRP-----ALVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:PRK05852  449 VLAS-HPN-----VMEAAVFGVPdqlygEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLD 522
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 561-1021 9.41e-23

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: 104.06  E-value: 9.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGG 640
Cdd:cd05914     7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 DgqqlaqwsaeqridltdpavveqwqdlpgdqppaiprhAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHR------ 714
Cdd:cd05914    87 D--------------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKevvllg 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  715 --DRI-DFTPQSTMFNCMslsfdagnMTTLLPLSSGGTLAFGE--PNDRAIMQAEQAGATHLILPTAL-------MSILD 782
Cdd:cd05914   129 kgDKIlSILPLHHIYPLT--------FTLLLPLLNGAHVVFLDkiPSAKIIALAFAQVTPTLGVPVPLviekifkMDIIP 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  783 P----------------------------EQVNG-IQAIGMGGEACPNAVVENwadkvaLYNM-------YGPTECTVTA 826
Cdd:cd05914   201 KltlkkfkfklakkinnrkirklafkkvhEAFGGnIKEFVIGGAKINPDVEEF------LRTIgfpytigYGMTETAPII 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 LSTRLRKGQPVTIGKPLIHIQALILDTAgqlcPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlnDVNNAgqgaatl 906
Cdd:cd05914   275 SYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAF------DKDGW------- 337

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  907 riYRTGDKARLLNNGDYEYCGRIDEQIKL-RGYRIEPGEIEAQLAAVCPSLkqIKVIVAQVGSRPALV----AYATVKAD 981
Cdd:cd05914   338 --FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVL--ESLVVVQEKKLVALAyidpDFLDVKAL 413

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 499404635  982 SSTPEPAAVLIDVA-KY---LPEY--MVPFRLMlLEDMPLTPNGKL 1021
Cdd:cd05914   414 KQRNIIDAIKWEVRdKVnqkVPNYkkISKVKIV-KEEFEKTPKGKI 458
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 561-1026 2.35e-22

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


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 102.56  E-value: 2.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWL-HRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG 639
Cdd:cd05958    10 EWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 GDGqqlaqwsaeqridLTdpavveqwqdlpgdqppaiprHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDH-RDRID 718
Cdd:cd05958    90 AHA-------------LT---------------------ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYaVNVLR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  719 FTPQSTMFNCMSLSFDAGNMTTLL-PLSSGG-TLAFGE--PNDRAIMQAEQAGATHLILPTALMSILD--PEQVNGIQAI 792
Cdd:cd05958   136 LREDDRFVGSPPLAFTFGLGGVLLfPFGVGAsGVLLEEatPDLLLSAIARYKPTVLFTAPTAYRAMLAhpDAAGPDLSSL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  793 GM---GGEACPNAVVENW--ADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELC 867
Cdd:cd05958   216 RKcvsAGEALPAALHRAWkeATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  868 LAGLGLARGYLNQPQMTASRFEHITlndvnnagqgaatlriyrTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:cd05958   296 VRGPTGCRYLADKRQRTYVQGGWNI------------------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVED 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLAAvCPSLKQIKVIVAQVGSRPALV-AYATVKAD-SSTPEPAAVLIDVAK-YLPEYMVPFRLMLLEDMPLTPNGKLDMK 1024
Cdd:cd05958   358 VLLQ-HPAVAECAVVGHPDESRGVVVkAFVVLRPGvIPGPVLARELQDHAKaHIAPYKYPRAIEFVTELPRTATGKLQRF 436


                  ..
gi 499404635 1025 QL 1026
Cdd:cd05958   437 AL 438
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 683-1026 2.44e-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: 101.02  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  683 LAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTLAFGEP---NDR 758
Cdd:cd05944     4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLtPLASGAHVVLAGPagyRNP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  759 AIMQ-----AEQAGATHLI-LPT---ALMSILDPEQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECT-VTA 826
Cdd:cd05944    84 GLFDnfwklVERYRITSLStVPTvyaALLQVPVNADISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTEATcLVA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 LSTRLRKGQPVTIGKPLIHIQA--LILDTAGQL---CPVGVPGELCLAGLGLARGYLNqpqmtasrfehiTLNDVNNAGQ 901
Cdd:cd05944   164 VNPPDGPKRPGSVGLRLPYARVriKVLDGVGRLlrdCAPDEVGEICVAGPGVFGGYLY------------TEGNKNAFVA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  902 GaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI---VAQVGSRPalVAYATV 978
Cdd:cd05944   232 D----GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR-HPAVAFAGAVgqpDAHAGELP--VAYVQL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 499404635  979 KADSSTpEPAAVLIDVAKYLPEY-MVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05944   305 KPGAVV-EEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 562-1035 3.14e-22

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: 102.20  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGgd 641
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 GQQLAqwsaeQRIDLTDPAVveqwqdlpgdqppaiprhaqqlaqVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:cd05969    79 TEELY-----ERTDPEDPTL------------------------LHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHP 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  722 QStMFNCMSlsfDAGNMTTLL-----PLSSGGTLAFGEPNDRA-----IMQAEQAGATHlILPTA--LMSILDPEQV--- 786
Cdd:cd05969   130 DD-IYWCTA---DPGWVTGTVygiwaPWLNGVTNVVYEGRFDAeswygIIERVKVTVWY-TAPTAirMLMKEGDELArky 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  787 --NGIQAIGMGGEAC-PNAVVenWADKV---ALYNMYGPTECTVTALSTRL-RKGQPVTIGKPLIHIQALILDTAGQLCP 859
Cdd:cd05969   205 dlSSLRFIHSVGEPLnPEAIR--WGMEVfgvPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVDENGNELP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  860 VGVPGELCL-AGL-GLARGYLNQPQmtasRFEHITLNDvnnagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRG 937
Cdd:cd05969   283 PGTKGILALkPGWpSMFRGIWNDEE----RYKNSFIDG------------WYLTGDLAYRDEDGYFWFVGRADDIIKTSG 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  938 YRIEPGEIEAQLAAvCPSLKQIKVIVAQ---VGSRPalVAYATVKADSSTPEPAAVLID--VAKYLPEYMVPFRLMLLED 1012
Cdd:cd05969   347 HRVGPFEVESALME-HPAVAEAGVIGKPdplRGEII--KAFISLKEGFEPSDELKEEIInfVRQKLGAHVAPREIEFVDN 423

                         490       500
                  ....*....|....*....|...
gi 499404635 1013 MPLTPNGKLdMKQlppVLEANES 1035
Cdd:cd05969   424 LPKTRSGKI-MRR---VLKAKEL 442
PRK09274 PRK09274
peptide synthase; Provisional
 538-928 3.58e-22

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 103.44  E-value: 3.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIAF------DGEPRTDTLTYAELNRQANQLAHWLHRQGL--GEQSLVGVLAKRDryFVIALLAIWKA 609
Cdd:PRK09274   12 LPRAAQERPDQLAVAVpggrgaDGKLAYDELSFAELDARSDAIAHGLNAAGIgrGMRAVLMVTPSLE--FFALTFALFKA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  610 GAAYVPLDPDYPPERLRHIITDANLSVILGgdgQQLAQW----------SAEQRIdltdpaVVEQ---W---------QD 667
Cdd:PRK09274   90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIG---IPKAHLarrlfgwgkpSVRRLV------TVGGrllWggttlatllRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  668 LPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSL---INLLDDH----RDRIDftpqSTMFNCMSLsFD-AGNMT 739
Cdd:PRK09274  161 GAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFeaqIEALREDygiePGEID----LPTFPLFAL-FGpALGMT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  740 TLLPlssggTLAFGEP---NDRAIMQA-EQAGATHLILPTALMSIL------DPEQVNGIQAIGMGGEACPNAVVENW-- 807
Cdd:PRK09274  236 SVIP-----DMDPTRPatvDPAKLFAAiERYGVTNLFGSPALLERLgrygeaNGIKLPSLRRVISAGAPVPIAVIERFra 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  808 --ADKVALYNMYGPTEC---TVTALSTRLRKGQPVT-------IGKPL----IHIQAL----ILDTAGQL-CPVGVPGEL 866
Cdd:PRK09274  311 mlPPDAEILTPYGATEAlpiSSIESREILFATRAATdngagicVGRPVdgveVRIIAIsdapIPEWDDALrLATGEIGEI 390

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635  867 CLAGLGLARGYLNQPQMTAsrfehitLNDVNNagqGAATLRiYRTGDKARLLNNGDYEYCGR 928
Cdd:PRK09274  391 VVAGPMVTRSYYNRPEATR-------LAKIPD---GQGDVW-HRMGDLGYLDAQGRLWFCGR 441
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 528-753 5.02e-22

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 103.03  E-value: 5.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  528 PQPQLTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIW 607
Cdd:PRK08279   33 PDSKRSLGDVFEEAAARHPDRPALLFEDQ----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  608 KAGAAYVPLDPDYPPERLRHII--TDANLsVILGGD--------GQQLA----QWSAEQrIDLTDPAVVEQWQDLPGDQP 673
Cdd:PRK08279  109 KLGAVVALLNTQQRGAVLAHSLnlVDAKH-LIVGEElveafeeaRADLArpprLWVAGG-DTLDDPEGYEDLAAAAAGAP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  674 PAIPRHAQQL-----AQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCmslsfdagnmttlLPL--SS 746
Cdd:PRK08279  187 TTNPASRSGVtakdtAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCC-------------LPLyhNT 253


                  ....*..
gi 499404635  747 GGTLAFG 753
Cdd:PRK08279  254 GGTVAWS 260
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 100-498 6.54e-22

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: 100.45  E-value: 6.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  100 FRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQRIDAYQPFVIQHddFSLLPEAeregrLQQQVkaeiSRPFD 179
Cdd:cd19545    28 FELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWTE--STSLDEY-----LEEDR----AAPMG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  180 LtAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADFKPAFlacQNCQPYPVettqlnyidyaHWFNS-DSFLDY 258
Cdd:cd19545    97 L-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAY---QGEPVPQP-----------PPFSRfVKYLRQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  259 HN--EFKPFWVERLTGIPEVHSLPLdkPRPAHQNSGGEVIFSAINNDlwdkfKRLCQRYNTSNFIglHAVFSLMLARISG 336
Cdd:cd19545   162 LDdeAAAEFWRSYLAGLDPAVFPPL--PSSRYQPRPDATLEHSISLP-----SSASSGVTLATVL--RAAWALVLSRYTG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  337 EKDIVIGSPLAYRERP--DIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLSAFDHQLYRFEALSeAIGSDRTTAI 414
Cdd:cd19545   233 SDDVVFGVTLSGRNAPvpGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIR-RLGPDARAAC 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  415 NpiFQVMLVYQAKVDFNDLIPGCDAAEETSPVLPAKTD--ISVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIE 492
Cdd:cd19545   312 N--FQTLLVVQPALPSSTSESLELGIEEESEDLEDFSSygLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQ 389


                  ....*.
gi 499404635  493 AVVENP 498
Cdd:cd19545   390 QLASAP 395
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
563-1021 8.75e-22

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 102.13  E-value: 8.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  563 TYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG--- 639
Cdd:PRK06087   51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptl 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 ---GDGQQLAQWSAEQ-----RIDLTD---PAVVE-QWQDLPGDQPP---AIPRHAQQLAQVIYTSGSTGLPKGVMIEHG 704
Cdd:PRK06087  131 fkqTRPVDLILPLQNQlpqlqQIVGVDklaPATSSlSLSQIIADYEPlttAITTHGDELAAVLFTSGTEGLPKGVMLTHN 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  705 sliNLLDDHR---DRIDFTPQSTMFNCMSLSFDAGNMTTL-LPLSSGGTLAFGE--PNDRAIMQAEQA------GATHLI 772
Cdd:PRK06087  211 ---NILASERaycARLNLTWQDVFMMPAPLGHATGFLHGVtAPFLIGARSVLLDifTPDACLALLEQQrctcmlGATPFI 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  773 lptalMSIL-----DPEQVNGIQAIGMGGEACPNAVVEN-WADKVALYNMYGPTECTVTALstrLRKGQPV-----TIGK 841
Cdd:PRK06087  288 -----YDLLnllekQPADLSALRFFLCGGTTIPKKVAREcQQRGIKLLSVYGSTESSPHAV---VNLDDPLsrfmhTDGY 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  842 PLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASrfehiTLNDvnnagQGAatlriYRTGDKARLLNNG 921
Cdd:PRK06087  360 AAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTAR-----ALDE-----EGW-----YYSGDLCRMDEAG 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  922 DYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVA---QVGSRpaLVAYATVKADSSTPEPAAVLIDVA-KY 997
Cdd:PRK06087  425 YIKITGRKKDIIVRGGENISSREVEDILLQ-HPKIHDACVVAMpdeRLGER--SCAYVVLKAPHHSLTLEEVVAFFSrKR 501

                         490       500
                  ....*....|....*....|....
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK06087  502 VAKYKYPEHIVVIDKLPRTASGKI 525
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 541-1024 9.76e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 102.43  E-value: 9.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  541 VAQRDPqqlaiafdGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDY 620
Cdd:PRK12582   68 LAQREP--------GHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAY 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  621 PP-----ERLRHIITDANLSVILGGDGQQLAQWSAEqrIDLTDPAVVEqwQDLPGDQPPAIP---------------RHA 680
Cdd:PRK12582  140 SLmshdhAKLKHLFDLVKPRVVFAQSGAPFARALAA--LDLLDVTVVH--VTGPGEGIASIAfadlaatpptaavaaAIA 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  681 Q----QLAQVIYTSGSTGLPKGVMIEHGSL---INLLDDHRDRIDFTPQSTMFNCMSLSFD-AGNMTTLLPLSSGGTLAF 752
Cdd:PRK12582  216 AitpdTVAKYLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPVSLDWMPWNHTmGGNANFNGLLWGGGTLYI 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  753 GEPNDRAIMQAEQAGATHLILPT----------ALMSILDPEQV------NGIQAIGMGGEACPNAVVENWAD------- 809
Cdd:PRK12582  296 DDGKPLPGMFEETIRNLREISPTvygnvpagyaMLAEAMEKDDAlrrsffKNLRLMAYGGATLSDDLYERMQAlavrttg 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  810 -KVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQAlildtagQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF 888
Cdd:PRK12582  376 hRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVEL-------KLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF 448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  889 EHitlndvnnagQGaatlrIYRTGDKARLLNNGDYE----YCGRIDEQIKL-RGYRIEPGEIEAQLAAVCPSLKQIKVIV 963
Cdd:PRK12582  449 DE----------EG-----FYRLGDAARFVDPDDPEkgliFDGRVAEDFKLsTGTWVSVGTLRPDAVAACSPVIHDAVVA 513

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  964 AQvgSRP---ALV------AYATVKADSSTPEPAAVLIDVAKYLPEYMVPF------------RLMLLEDMPLTPNGKLD 1022
Cdd:PRK12582  514 GQ--DRAfigLLAwpnpaaCRQLAGDPDAAPEDVVKHPAVLAILREGLSAHnaeaggsssriaRALLMTEPPSIDAGEIT 591


                  ..
gi 499404635 1023 MK 1024
Cdd:PRK12582  592 DK 593
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 525-1026 1.09e-21

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: 101.25  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  525 RSYPQPQlTVTDVIEAVAQRDPQQLAIAfDGEPRtdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALL 604
Cdd:cd05920     9 AGYWQDE-PLGDLLARSAARHPDRIAVV-DGDRR---LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  605 AIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGDgqqlaqwsaeqRIDLTDPavVEQWQDLPGDQPpaiprhaqQLA 684
Cdd:cd05920    84 ALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPD-----------RHAGFDH--RALARELAESIP--------EVA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  685 QVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAgnmttllPLSSGG---TLAFG-------- 753
Cdd:cd05920   143 LFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNF-------PLACPGvlgTLLAGgrvvlapd 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  754 -EPNDR-AIMQAEQAGATHLILPTALM-------SILDPEQVNGIQAIGMGGEACPNAVVENwADKVALYNMYGPTECTV 824
Cdd:cd05920   216 pSPDAAfPLIEREGVTVTALVPALVSLwldaaasRRADLSSLRLLQVGGARLSPALARRVPP-VLGCTLQQVFGMAEGLL 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  825 TAlsTRLRKGQPV---TIGKPLI-HIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvnnaG 900
Cdd:cd05920   295 NY--TRLDDPDEViihTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFT----------P 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  901 QGaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQ---VGSRpaLVAYAT 977
Cdd:cd05920   363 DG-----FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRH-PAVHDAAVVAMPdelLGER--SCAFVV 434

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499404635  978 VKadsstpEPAAVLIDVAKYLPE-----YMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05920   435 LR------DPPPSAAQLRRFLRErglaaYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 677-1026 1.82e-21

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 102.69  E-value: 1.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  677 PRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCM----SLSFDAgnmTTLLPLSSG-GTLA 751
Cdd:PRK08633  778 TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLpffhSFGLTV---TLWLPLLEGiKVVY 854

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  752 FGEPND-RAIMQ-AEQAGATHLI-LPTALMSIL-----DPEQVNGIQAIGMGGEACPNAVVENWADK--VALYNMYGPTE 821
Cdd:PRK08633  855 HPDPTDaLGIAKlVAKHRATILLgTPTFLRLYLrnkklHPLMFASLRLVVAGAEKLKPEVADAFEEKfgIRILEGYGATE 934

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  822 CT-VTALST---------RLRKGQPVTIGKPLIHIQALILD-TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfEH 890
Cdd:PRK08633  935 TSpVASVNLpdvlaadfkRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTA---EV 1011

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  891 ITLNDvnnagqgaaTLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVA----QV 966
Cdd:PRK08633 1012 IKDID---------GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVFAVTAvpdeKK 1082

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635  967 GSRPALVAyatvkadSSTPEPAAVLIDVAK--YLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK08633 1083 GEKLVVLH-------TCGAEDVEELKRAIKesGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 533-1021 1.89e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 101.00  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAFdgEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK12583   19 TIGDAFDATVARFPDREALVV--RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPPERLRH----------IITDA----NLSVILGGDGQQLAQWSAEQ-------------RIDLTDPAVVEQW 665
Cdd:PRK12583   97 LVNINPAYRASELEYalgqsgvrwvICADAfktsDYHAMLQELLPGLAEGQPGAlacerlpelrgvvSLAPAPPPGFLAW 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  666 QDLPGdQPPAIPRHAQQLAQ----------VIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTM------FNCM 729
Cdd:PRK12583  177 HELQA-RGETVSREALAERQasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLcvpvplYHCF 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  730 SLSfdagnMTTLLPLSSGGTLAFgePNDR----AIMQA-EQAGATHLI-LPTALMSILD-PEQVN--------GIqaigM 794
Cdd:PRK12583  256 GMV-----LANLGCMTVGACLVY--PNEAfdplATLQAvEEERCTALYgVPTMFIAELDhPQRGNfdlsslrtGI----M 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 GGEACPNAVVENWADKVALYNM---YGPTECT-VTALSTR---LRKgQPVTIGKPLIHIQALILDTAGQLCPVGVPGELC 867
Cdd:PRK12583  325 AGAPCPIEVMRRVMDEMHMAEVqiaYGMTETSpVSLQTTAaddLER-RVETVGRTQPHLEVKVVDPDGATVPRGEIGELC 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  868 LAGLGLARGYLNQPQMTAsrfEHITLNDvnnagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:PRK12583  404 TRGYSVMKGYWNNPEATA---ESIDEDG------------WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEE 468

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLaavcpsLKQIKVIVAQVGSRP------ALVAYATVKadsstPEPAAVLIDVAKY----LPEYMVPFRLMLLEDMPLTP 1017
Cdd:PRK12583  469 FL------FTHPAVADVQVFGVPdekygeEIVAWVRLH-----PGHAASEEELREFckarIAHFKVPRYFRFVDEFPMTV 537


                  ....
gi 499404635 1018 NGKL 1021
Cdd:PRK12583  538 TGKV 541
PRK12467 PRK12467
peptide synthase; Provisional
 1566-2075 2.82e-21

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 102.55  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIVKQADLPFYYQ 1644
Cdd:PRK12467   50 IPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFvQDEEGFRQVIDASLSLTIPLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1645 DL--MQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQ 1722
Cdd:PRK12467  130 DLanEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGR 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1723 VLMHGDAPaiqvdrayVDYARHAVAQQSAVDA--------FWQQR----QSLLAQTND----VSMLFAAAGKRADLSQHL 1786
Cdd:PRK12467  210 EPSLPALP--------IQYADYAIWQRSWLEAgererqlaYWQEQlggeHTVLELPTDrprpAVPSYRGARLRVDLPQAL 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1787 TqiepqvtsvslnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESpvEDVASSVGLYINSLP 1866
Cdd:PRK12467  282 S----------------AGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQV 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1867 LALSWQQPVSLQQHLVQLQNELMAMNQHA----TQSLIALTAGRSRLFNSLF--IYENYPDAKA-EQGQRADDPHRLYPE 1939
Cdd:PRK12467  344 LKAEVDPQASFLELLQQVKRTALGAQAHQdlpfEQLVEALQPERSLSHSPLFqvMFNHQNTATGgRDREGAQLPGLTVEE 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1940 FSAAYEKVEMPLNLVVREQSGCMLLRFEFDADALDSAQARRVLMRWHDEVVALVNSVPQQPAEIIGHDKATglvaAQKTV 2019
Cdd:PRK12467  424 LSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEE----RAREL 499

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635 2020 ADSgiNQPDTSFA-QTLLRAW---------AQTLHLGEPGLGESDLWSRT------LCESGVDSLQRIALAQ 2075
Cdd:PRK12467  500 VRW--NAPATEYApDCVHQLIeaqarqhpeRPALVFGEQVLSYAELNRQAnrlahvLIAAGVGPDVLVGIAV 569
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 551-1021 3.12e-21

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 99.98  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  551 IAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRD-RYFVIALLAIwKAGAAYVPLDPDYPPERLRHII 629
Cdd:PRK08276    5 MAPSGE----VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNpEFFEVYWAAR-RSGLYYTPINWHLTAAEIAYIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  630 TDANLSVILGGDG--QQLAQWSAEQRIDLT----DPAVVEQWQDLP---GDQPP-AIPRHAQQlAQVIYTSGSTGLPKGV 699
Cdd:PRK08276   80 DDSGAKVLIVSAAlaDTAAELAAELPAGVPlllvVAGPVPGFRSYEealAAQPDtPIADETAG-ADMLYSSGTTGRPKGI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  700 MIEHgslinlldDHRDRIDFTPQSTMFNCMSLSFDAGNmTTLLP---------------LSSGGTLAFGEPND-----RA 759
Cdd:PRK08276  159 KRPL--------PGLDPDEAPGMMLALLGFGMYGGPDS-VYLSPaplyhtaplrfgmsaLALGGTVVVMEKFDaeealAL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  760 ImqaEQAGATHLIL-PTALMSILD-PEQVNG------IQAIGMGGEACPNAV----VENWADkvALYNMYGPTE-CTVTA 826
Cdd:PRK08276  230 I---ERYRVTHSQLvPTMFVRMLKlPEEVRArydvssLRVAIHAAAPCPVEVkramIDWWGP--IIHEYYASSEgGGVTV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 LSTR--LRKgqPVTIGKPLIHiQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASrfehitlndvNNAGQGAA 904
Cdd:PRK08276  305 ITSEdwLAH--PGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA----------ARNPHGWV 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  905 TLriyrtGDKARLLNNGdYEY-CGRIDEQIKLRGYRIEPGEIEAQL--------AAVcpslkqIKVIVAQVGSRpalvay 975
Cdd:PRK08276  372 TV-----GDVGYLDEDG-YLYlTDRKSDMIISGGVNIYPQEIENLLvthpkvadVAV------FGVPDEEMGER------ 433

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499404635  976 atVKA-----DSSTPEP--AAVLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK08276  434 --VKAvvqpaDGADAGDalAAELIAwLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 73-496 6.23e-21

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: 98.09  E-value: 6.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSglWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFvVNEQGKGEQRI--DAYQPFVIQ 150
Cdd:cd19534     3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRF-RREDGGWQQRIrgDVEELFRLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  151 -HDDFSLLPEAEREGRLqqqvkAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDG--WSVknLFADFKPAFLA 227
Cdd:cd19534    80 vVDLSSLAQAAAIEALA-----AEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGvsWRI--LLEDLEAAYEQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  228 CQNCQPYPVETTQlnyiDYAHWfnSDSFLDYHNEFK-----PFWVERLTgiPEVHSLPLDkpRPAHQNSGGEVIFSainn 302
Cdd:cd19534   153 ALAGEPIPLPSKT----SFQTW--AELLAEYAQSPAlleelAYWRELPA--ADYWGLPKD--PEQTYGDARTVSFT---- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  303 dlWDK------FKRLCQRYNTS-NFIgLHAVFSLMLARISGEKDIVI-----GsplayRE----RPDIEDVVGFFVNTIV 366
Cdd:cd19534   219 --LDEeetealLQEANAAYRTEiNDL-LLAALALAFQDWTGRAPPAIfleghG-----REeidpGLDLSRTVGWFTSMYP 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  367 LRTQLQDSQNFVDYLQYCREQdLSA-----FDHQLYRF--EALSEAIGSDRTTAINpiFQVMLVYQAKVDFNDLipGCDA 439
Cdd:cd19534   291 VVLDLEASEDLGDTLKRVKEQ-LRRipnkgIGYGILRYltPEGTKRLAFHPQPEIS--FNYLGQFDQGERDDAL--FVSA 365

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404635  440 AEETSPVLPAKT------DISVKVTElmGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVE 496
Cdd:cd19534   366 VGGGGSDIGPDTprfallDINAVVEG--GQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 519-1026 1.11e-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: 99.10  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  519 ETQQLPRSYPQPQLTV---TDVIEAVAQRDPQ----QLAIAFDGEP-RTDTLTYAELNRQANQLAHWLHRQGLGEQSLVG 590
Cdd:cd05968    41 QTLDLSGGKPWAAWFVggrMNIVEQLLDKWLAdtrtRPALRWEGEDgTSRTLTYGELLYEVKRLANGLRALGVGKGDRVG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  591 VLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGDGQqlaqWSAEQRIDLTDPA---------- 660
Cdd:cd05968   121 IYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGF----TRRGREVNLKEEAdkacaqcptv 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  661 ---VVEQ---------------WQDLPGDQPPAIPR-HAQQLAQVIYTSGSTGLPKGVMIEHGSL-INLLDDHRDRIDFT 720
Cdd:cd05968   197 ekvVVVRhlgndftpakgrdlsYDEEKETAGDGAERtESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLK 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  721 PQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAF--GEPN----DRAIMQAEQAGATHLILPTALMSILDP--------EQV 786
Cdd:cd05968   277 PGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydGAPDhpkaDRLWRMVEDHEITHLGLSPTLIRALKPrgdapvnaHDL 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  787 NGIQAIGMGGEacP-NAVVENW------ADKVALYNMYGPTECTVTALSTRL-RKGQPVTIGKPLIHIQALILDTAGQLC 858
Cdd:cd05968   357 SSLRVLGSTGE--PwNPEPWNWlfetvgKGRNPIINYSGGTEISGGILGNVLiKPIKPSSFNGPVPGMKADVLDESGKPA 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  859 PVGVpGELCLAG--LGLARGYLNQP----QMTASRFEHITLNdvnnagqgaatlriyrtGDKARLLNNGDYEYCGRIDEQ 932
Cdd:cd05968   435 RPEV-GELVLLApwPGMTRGFWRDEdrylETYWSRFDNVWVH-----------------GDFAYYDEEGYFYILGRSDDT 496

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  933 IKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVAQVGSRPALVAYATVKAD-SSTPEPAAVLID-VAKYLPEYMVPFRLMLL 1010
Cdd:cd05968   497 INVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGvTPTEALAEELMErVADELGKPLSPERILFV 576

                         570
                  ....*....|....*.
gi 499404635 1011 EDMPLTPNGKLdMKQL 1026
Cdd:cd05968   577 KDLPKTRNAKV-MRRV 591
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1135-1305 1.19e-20

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: 97.14  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1135 WFMEQSLARPEHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLgC---DAEG----QRYLADVPCpalsTLDYRQLG 1206
Cdd:cd19532    12 WFLQQYLEDPTTFNVTFSYRLTgPLDVARLERAVRAVGQRHEALRT-CfftDPEDgepmQGVLASSPL----RLEHVQIS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1207 DDG-LQQAFTALQS-EFDPAQGRTMACALVRHHPQADTaLFLAFHHLVIDAVSWRILVDDLERLYLGEPLLPKTSSYRQW 1284
Cdd:cd19532    87 DEAeVEEEFERLKNhVYDLESGETMRIVLLSLSPTEHY-LIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQYLDF 165

                         170       180
                  ....*....|....*....|....
gi 499404635 1285 gAALQH--YAT-QHAEQLTYWQAQ 1305
Cdd:cd19532   166 -AARQRqdYESgALDEDLAYWKSE 188
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 550-1026 1.31e-20

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: 98.37  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  550 AIAFDGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHII 629
Cdd:cd17642    33 TIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  630 TDANLSVILGGDG--QQLAQWSAEQRI-----------DL----TDPAVVEQwQDLPGDQ-----PPAIPRHaQQLAQVI 687
Cdd:cd17642   113 NISKPTIVFCSKKglQKVLNVQKKLKIiktiiildskeDYkgyqCLYTFITQ-NLPPGFNeydfkPPSFDRD-EQVALIM 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  688 YTSGSTGLPKGVMIEHGSLINLLDDHRDRI---DFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLA----FGEP----- 755
Cdd:cd17642   191 NSSGSTGLPKGVQLTHKNIVARFSHARDPIfgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVlmykFEEElflrs 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  756 -NDRAIMQAeqagathLILPTaLMS------ILDPEQVNGIQAIGMGGEACPNAVVENWADKVALYNM---YGPTECTVT 825
Cdd:cd17642   271 lQDYKVQSA-------LLVPT-LFAffakstLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrqgYGLTETTSA 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  826 ALSTRLRKGQPVTIGK--PLIHIQALILDTaGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRfehitlndVNNAGQga 903
Cdd:cd17642   343 ILITPEGDDKPGAVGKvvPFFYAKVVDLDT-GKTLGPNERGELCVKGPMIMKGYVNNPEATKAL--------IDKDGW-- 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  904 atlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLaavcpsLKQIKVIVAQVGSRPalvayatvkaDSS 983
Cdd:cd17642   412 -----LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESIL------LQHPKIFDAGVAGIP----------DED 470

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635  984 TPE-PAA-VLIDVAKYLPEYMV----------PFRL----MLLEDMPLTPNGKLDMKQL 1026
Cdd:cd17642   471 AGElPAAvVVLEAGKTMTEKEVmdyvasqvstAKRLrggvKFVDEVPKGLTGKIDRRKI 529
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1567-1982 1.35e-20

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: 97.06  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1567 PLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALESECASI--QVIVKQADLPFYYQ 1644
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVprQEILPPGPAPLEVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1645 DLM-QDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSgpqlLGAVHRD----YQTLM 1719
Cdd:cd19539    83 DLSdPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWS----LDVFARDlaalYAARR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1720 QGQVlmhGDAPAIQVdrAYVDYA----RHAVAQQSAVD-AFWQQRQSLLAQTNDVSMLFAAAGKRADLSQHLTQIEPQVT 1794
Cdd:cd19539   159 KGPA---APLPELRQ--QYKEYAawqrEALAAPRAAELlDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1795 svslnekdqATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPveDVASSVGLYINSLPLALSWQQP 1874
Cdd:cd19539   234 ---------AALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDC 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1875 VSLQQHLVQLQNELMAMNQHAT---QSLIAL-----TAGRSRLFNSLFIYENYPDA-KAEQGQRAddphrlYPEFSAAYE 1945
Cdd:cd19539   303 ATFRDLIARVRKALVDAQRHQElpfQQLVAElpvdrDAGRHPLVQIVFQVTNAPAGeLELAGGLS------YTEGSDIPD 376

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 499404635 1946 KVEMPLNLVVREQSGCMLLRFEFDADALDSAQARRVL 1982
Cdd:cd19539   377 GAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFL 413
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1566-1970 1.63e-20

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: 96.67  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIVKQADLPFYYQ 1644
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFtEEEGEPYQWIDPYTPVPIRHI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1645 DLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQVL 1724
Cdd:cd19533    82 DLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1725 mhGDAPAIQVDRAYVDYARHAVAQQSAVD-AFWQQRqslLAQTND-VSMLFAAAGKRADLSQHltqiepqvtSVSLNEKD 1802
Cdd:cd19533   162 --PPAPFGSFLDLVEEEQAYRQSERFERDrAFWTEQ---FEDLPEpVSLARRAPGRSLAFLRR---------TAELPPEL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1803 QATLTAFAREVGITPSIIAQYAWHRLLARSTG--DAV--SIVGNVLSGRESPVedvassVGLYINSLPLALSWQQPVSLQ 1878
Cdd:cd19533   228 TRTLLEAAEAHGASWPSFFIALVAAYLHRLTGanDVVlgVPVMGRLGAAARQT------PGMVANTLPLRLTVDPQQTFA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1879 QHLVQLQNELMAMNQHatQSL--------IALTAGRSRLFNSLFIYENYPdakaeQGQRADDPHRLYPEFSAAYEKvemP 1950
Cdd:cd19533   302 ELVAQVSRELRSLLRH--QRYryedlrrdLGLTGELHPLFGPTVNYMPFD-----YGLDFGGVVGLTHNLSSGPTN---D 371

                         410       420
                  ....*....|....*....|
gi 499404635 1951 LNLVVREQSGCMLLRFEFDA 1970
Cdd:cd19533   372 LSIFVYDRDDESGLRIDFDA 391
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 542-986 5.63e-20

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 95.32  E-value: 5.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYP 621
Cdd:PRK09029   13 AQVRPQAIALRLNDE----VLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  622 PERLRHIITDANLSVILGGDGQQLAQWSAEQRIDLTDPAVVEQWQdlpgdqppaiprhAQQLAQVIYTSGSTGLPKGVMi 701
Cdd:PRK09029   89 QPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQ-------------PQRLATMTLTSGSTGLPKAAV- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  702 eHgSLINLLDDHR---DRIDFTPQSTMFncmsLSfdagnmttlLP-------------LSSGGTLAFGEPNDraiMQAEQ 765
Cdd:PRK09029  155 -H-TAQAHLASAEgvlSLMPFTAQDSWL----LS---------LPlfhvsgqgivwrwLYAGATLVVRDKQP---LEQAL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  766 AGATHLIL-PTALMSILD-PEQVNGIQAIGMGGEACPNAVVENWADK-VALYNMYGPTE--CTVTALSTRLRKGqpvtIG 840
Cdd:PRK09029  217 AGCTHASLvPTQLWRLLDnRSEPLSLKAVLLGGAAIPVELTEQAEQQgIRCWCGYGLTEmaSTVCAKRADGLAG----VG 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  841 KPLIHIQALILDtagqlcpvgvpGELCLAGLGLARGYLNQPQMtasrfehITLndVNNAGQgaatlriYRTGDKARlLNN 920
Cdd:PRK09029  293 SPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQL-------VPL--VNDEGW-------FATRDRGE-WQN 344

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635  921 GDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQikVIV-----AQVGSRP-ALVAYATVKADSSTPE 986
Cdd:PRK09029  345 GELTILGRLDNLFFSGGEGIQPEEIERVINQH-PLVQQ--VFVvpvadAEFGQRPvAVVESDSEAAVVNLAE 413
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 98-397 6.09e-20

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


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 94.86  E-value: 6.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   98 VYFRLTGP-LDVAALEFAFDALAQRHASLRTRFvvNEQgkGEQRIDAYQP-FVIQHDDFSLLPEAEREGRLqQQVKAEIS 175
Cdd:cd19535    28 AYLEFDGEdLDPDRLERAWNKLIARHPMLRAVF--LDD--GTQQILPEVPwYGITVHDLRGLSEEEAEAAL-EELRERLS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  176 -RPFDLTAGDLTRVRLVKMSERTHVLmitqhHI-----ISDGWSVKNLFADfkpaFLACQNCQPYPVETTQLNYIDYAHW 249
Cdd:cd19535   103 hRVLDVERGPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRE----LAALYEDPGEPLPPLELSFRDYLLA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  250 FNSDSFLDYHNEfKPFWVERLTGIPEVHSLPLDKpRPAhqnSGGEVIFS----AINNDLWDKFKRLCQRYNTSNFIGLHA 325
Cdd:cd19535   174 EQALRETAYERA-RAYWQERLPTLPPAPQLPLAK-DPE---EIKEPRFTrrehRLSAEQWQRLKERARQHGVTPSMVLLT 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404635  326 VFSLMLARISGEKDIVIGSPLAYRER--PDIEDVVGFFVNTIVLRTQLQDSQNFVDYLQYCREQDLSAFDHQLY 397
Cdd:cd19535   249 AYAEVLARWSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSY 322
PRK05691 PRK05691
peptide synthase; Validated
 1520-1914 8.34e-20

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 97.55  E-value: 8.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1520 NLRALTEACltqlshgvvfTPSDFPAvNLSQTQLDSLSQRYDIDTLLPLSSLQQSMLYHRLRC-----PQDDAYHLQTPI 1594
Cdd:PRK05691  636 NLRQLFEAP----------TLAAFSA-AVARQLAGGGAAQAAIARLPRGQALPQSLAQNRLWLlwqldPQSAAYNIPGGL 704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1595 RYAHVLDVEGYRQAWQRQIQRFPALRAA-LESECASIQVIVKQADLPFYYQDL--MQDADPLAVIERYRQQDLRTGFDLS 1671
Cdd:PRK05691  705 HLRGELDEAALRASFQRLVERHESLRTRfYERDGVALQRIDAQGEFALQRIDLsdLPEAEREARAAQIREEEARQPFDLE 784

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1672 QPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQVLMHGDAPAiqvdrAYVDYA---RHAVAQ 1748
Cdd:PRK05691  785 KGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPL-----GYADYGawqRQWLAQ 859

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1749 QSAVdafwQQRQSLLAQTNDVSMLFAAAGKRADLSQHltQIEPQVTSVSLNEKDQATLTAFAREVGITPSIIAQYAWHRL 1828
Cdd:PRK05691  860 GEAA----RQLAYWKAQLGDEQPVLELATDHPRSARQ--AHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQAL 933

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1829 LARSTGDAVSIVGnvLSGRESPVEDVASSVGLYINSLPLALSWQQPVSLQQHLVQLQNELMAMNQHA----TQSLIALTA 1904
Cdd:PRK05691  934 LHRYSGQGDIRIG--VPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQdlpfEQLVEALPQ 1011

                         410
                  ....*....|.
gi 499404635 1905 GRSR-LFNSLF 1914
Cdd:PRK05691 1012 AREQgLFQVMF 1022
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1567-2000 5.29e-19

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: 91.99  E-value: 5.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1567 PLSSLQQS--MLyHRLrCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALESECAS-IQVIVKQADLPFYY 1643
Cdd:cd20484     3 PLSEGQKGlwML-QKM-SPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVpFQKIEPSKPLSFQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1644 QDLMqDADPLAVIErYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQV 1723
Cdd:cd20484    81 EDIS-SLKESEIIA-YLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1724 LMHGDAPAIQVDraYVDYARHAVAQQSAVD--AFWQQRqslLAQTNDVSMLFaaagkrADLSQHLTQ-IEPQVTSVSLNE 1800
Cdd:cd20484   159 PTLASSPASYYD--FVAWEQDMLAGAEGEEhrAYWKQQ---LSGTLPILELP------ADRPRSSAPsFEGQTYTRRLPS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1801 KDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGResPVEDVASSVGLYINSLPLALSWQQPVSLQQH 1880
Cdd:cd20484   228 ELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGR--PEERFDSLIGYFINMLPIRSRILGEETFSDF 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1881 LVQLQNELMAMNQHA-------TQSL-IALTAGRSRLFNSLFIYENYPDAKAEQGQRADDPHRLYPEF-SAAYEKVEMPL 1951
Cdd:cd20484   306 IRKLQLTVLDGLDHAaypfpamVRDLnIPRSQANSPVFQVAFFYQNFLQSTSLQQFLAEYQDVLSIEFvEGIHQEGEYEL 385

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 499404635 1952 NLVVREQSGCMLLRFEFDADALDSAQARRVLmrwhDEVVALVNSVPQQP 2000
Cdd:cd20484   386 VLEVYEQEDRFTLNIKYNPDLFDASTIERMM----EHYVKLAEELIANP 430
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 561-1026 7.73e-19

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: 91.25  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDpdyppERLRHiitdanlsvilgg 640
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN-----TRLTP------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 dgQQLAQWSAEQRIDLTDpavveqwqdlpgdqppaiprhaqqLAQVIYTSGSTGLPKGVMI---EH-----GSLINL-LD 711
Cdd:cd05912    63 --NELAFQLKDSDVKLDD------------------------IATIMYTSGTTGKPKGVQQtfgNHwwsaiGSALNLgLT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  712 DHRDRIDFTPqstMFNCMSLS-----------------FDAGNMTTLLplssggtlafgepNDRAImqaeqagaTHLILP 774
Cdd:cd05912   117 EDDNWLCALP---LFHISGLSilmrsviygmtvylvdkFDAEQVLHLI-------------NSGKV--------TIISVV 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  775 TA----LMSILDPEQVNGIQAIGMGGEACPNAVVENWADK-VALYNMYGPTE-----CTVTALSTRLRKGqpvTIGKPLI 844
Cdd:cd05912   173 PTmlqrLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIPVYQSYGMTEtcsqiVTLSPEDALNKIG---SAGKPLF 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  845 HIQALILDTAGqlcPVGVPGELCLAGLGLARGYLNQPQMTASRFEhitlndvNNAgqgaatlriYRTGDKARLLNNGdYE 924
Cdd:cd05912   250 PVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFE-------NGW---------FKTGDIGYLDEEG-FL 309

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  925 YC-GRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIV---AQVGSRPalVAYatVKADSSTPEpaAVLID-VAKYLP 999
Cdd:cd05912   310 YVlDRRSDLIISGGENIYPAEIEEVLLSH-PAIKEAGVVGipdDKWGQVP--VAF--VVSERPISE--EELIAyCSEKLA 382

                         490       500
                  ....*....|....*....|....*..
gi 499404635 1000 EYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05912   383 KYKVPKKIYFVDELPRTASGKLLRHEL 409
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 523-1032 1.94e-18

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: 91.57  E-value: 1.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  523 LPRSYPQPQlTVTDVIEAVAQRDPQQ--LAIAFDGEPrtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFV 600
Cdd:cd05906     2 LHRPEGAPR-TLLELLLRAAERGPTKgiTYIDADGSE--EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  601 IALLAIWKAGAAYVPLD--PDYPP-----ERLRHIITDANLSVILGGDG--QQLAQWSAEQRIDLTDPAVVEQWQDLPGD 671
Cdd:cd05906    79 PAFWACVLAGFVPAPLTvpPTYDEpnarlRKLRHIWQLLGSPVVLTDAElvAEFAGLETLSGLPGIRVLSIEELLDTAAD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  672 qPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAG-NMTTLLPLSSGgtl 750
Cdd:cd05906   159 -HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGlVELHLRAVYLG--- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  751 afgepndraiMQAEQAgATHLIL--PTALMSILDPEQVN---------------------------GIQAIGMGGEACPN 801
Cdd:cd05906   235 ----------CQQVHV-PTEEILadPLRWLDLIDRYRVTitwapnfafallndlleeiedgtwdlsSLRYLVNAGEAVVA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  802 AVVENWADKVALYNM--------YGPTE----CTVTALSTRLRKGQP---VTIGKPLIHIQALILDTAGQLCPVGVPGEL 866
Cdd:cd05906   304 KTIRRLLRLLEPYGLppdairpaFGMTEtcsgVIYSRSFPTYDHSQAlefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRL 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  867 CLAGLGLARGYLNQPQMTASRFehitLNDvnnaGQgaatlriYRTGDKArLLNNGDYEYCGRIDEQIKLRGYRIEPGEIE 946
Cdd:cd05906   384 QVRGPVVTKGYYNNPEANAEAF----TED----GW-------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIE 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  947 A---QLAAVCPSLkqikviVAQVGSRPA-------LVAYATVKADSstPEPAAVLIDVAKYL-------PEYMVPFRlml 1009
Cdd:cd05906   448 AaveEVPGVEPSF------TAAFAVRDPgaeteelAIFFVPEYDLQ--DALSETLRAIRSVVsrevgvsPAYLIPLP--- 516

                         570       580
                  ....*....|....*....|...
gi 499404635 1010 LEDMPLTPNGKLDMKQLPPVLEA 1032
Cdd:cd05906   517 KEEIPKTSLGKIQRSKLKAAFEA 539
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
542-1026 3.14e-18

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 90.41  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYP 621
Cdd:PRK03640   12 AFLTPDRTAIEFEEK----KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  622 PERLRHIITDANLSVILGGD-------GQQLAQWSAEQRIDLTDPAVVEQWQDlpgdqppaiprhaQQLAQVIYTSGSTG 694
Cdd:PRK03640   88 REELLWQLDDAEVKCLITDDdfeakliPGISVKFAELMNGPKEEAEIQEEFDL-------------DEVATIMYTSGTTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  695 LPKGVMI---EH-----GSLINL-LDDHRDRIDFTPqstMFNCMSLS-----------------FDAGNMTTLLpLSSGG 748
Cdd:PRK03640  155 KPKGVIQtygNHwwsavGSALNLgLTEDDCWLAAVP---IFHISGLSilmrsviygmrvvlvekFDAEKINKLL-QTGGV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  749 TlafgepndraIMQAEQAgathliLPTALMSILDPEQVNG-IQAIGMGGEACPNAVVENWADK-VALYNMYGPTE----- 821
Cdd:PRK03640  231 T----------IISVVST------MLQRLLERLGEGTYPSsFRCMLLGGGPAPKPLLEQCKEKgIPVYQSYGMTEtasqi 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  822 CTVTALSTRLRKGqpvTIGKPLIHIQALILDTaGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNdvnnagq 901
Cdd:PRK03640  295 VTLSPEDALTKLG---SAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFK------- 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  902 gaatlriyrTGDKARLLNNGdYEYC-GRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI---VAQVGSRPalVAYat 977
Cdd:PRK03640  364 ---------TGDIGYLDEEG-FLYVlDRRSDLIISGGENIYPAEIEEVLLSH-PGVAEAGVVgvpDDKWGQVP--VAF-- 428

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 499404635  978 VKADSSTPEpaAVLIDVAK-YLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK03640  429 VVKSGEVTE--EELRHFCEeKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 561-1026 3.71e-18

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 90.65  E-value: 3.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQ-GLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLS--VI 637
Cdd:PRK12492   49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARalVY 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  638 LGGDGQQLAQWSAEQRI---------DLTDPA-------VVEQWQD------LP-------------GDQPPAIPRHAQQ 682
Cdd:PRK12492  129 LNMFGKLVQEVLPDTGIeylieakmgDLLPAAkgwlvntVVDKVKKmvpayhLPqavpfkqalrqgrGLSLKPVPVGLDD 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  683 LAQVIYTSGSTGLPKGVMIEHGSLI-NLLDDH----RDRIDFTP-----QSTMF-------------NCMSLSFdAGNMT 739
Cdd:PRK12492  209 IAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRaclsQLGPDGQPlmkegQEVMIaplplyhiyaftaNCMCMMV-SGNHN 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  740 TLL--PLSSGGTlafgepndraIMQAEQAGATHLI----LPTALMSILDPEQVN--GIQAIGMGGEACPNAVVENWADKV 811
Cdd:PRK12492  288 VLItnPRDIPGF----------IKELGKWRFSALLglntLFVALMDHPGFKDLDfsALKLTNSGGTALVKATAERWEQLT 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  812 --ALYNMYGPTECTVTALS----TRLRKGqpvTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTA 885
Cdd:PRK12492  358 gcTIVEGYGLTETSPVASTnpygELARLG---TVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATA 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  886 SRFEhitlndvnnaGQGAatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvcpslkQIKVIVAQ 965
Cdd:PRK12492  435 EALD----------AEGW-----FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA------HPKVANCA 493

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  966 VGSRPALVAYATVKADSSTPEPAAVLIDVAKYLPE----YMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK12492  494 AIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKEnftgYKVPKHIVLRDSLPMTPVGKILRREL 558
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 73-382 4.70e-18

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: 89.29  E-value: 4.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   73 PLSSSQSGLWFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFVVNEQGKGEQ--RIDAYQPFVIQ 150
Cdd:cd19547     3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQyvRDDLAPPWALL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  151 hdDFSLLPEAEREGRLQQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFAD-FKPAFLACQ 229
Cdd:cd19547    83 --DWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDvFRVYEELAH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  230 NCQPY--PVETtqlnYIDYAHWFNSDSflDYHNEFKPFWVERLTGIpevhslpldKPRP-AHQNSGGEVIFSAINNDLWD 306
Cdd:cd19547   161 GREPQlsPCRP----YRDYVRWIRART--AQSEESERFWREYLRDL---------TPSPfSTAPADREGEFDTVVHEFPE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  307 KFKRL----CQRYN-TSNFIGlHAVFSLMLARISGEKDIVIGSPLAYR--ERPDIEDVVGFFVNTIVLRTQLQDSQNFVD 379
Cdd:cd19547   226 QLTRLvneaARGYGvTTNAIS-QAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTG 304


                  ...
gi 499404635  380 YLQ 382
Cdd:cd19547   305 LLE 307
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 542-1020 1.54e-17

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: 88.77  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAIAFDGEPRTD--TLTYAELNRQANQLAHWLHRQGLGeqslvgvlaKRDR---YF------VIALLAIWKAG 610
Cdd:cd05966    63 LKERGDKVAIIWEGDEPDQsrTITYRELLREVCRFANVLKSLGVK---------KGDRvaiYMpmipelVIAMLACARIG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  611 AAYVPLDPDYPPERLRHIITDANLSVILGGDGQqlaqWSAEQRIDL---TDPAV-----VEQ------------------ 664
Cdd:cd05966   134 AVHSVVFAGFSAESLADRINDAQCKLVITADGG----YRGGKVIPLkeiVDEALekcpsVEKvlvvkrtggevpmtegrd 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  665 --WQDLPGDQPPAIP---RHAQQLAQVIYTSGSTGLPKGVMieH---GSLINLLDDHRDRIDFTPQSTMFnCMSlsfDAG 736
Cdd:cd05966   210 lwWHDLMAKQSPECEpewMDSEDPLFILYTSGSTGKPKGVV--HttgGYLLYAATTFKYVFDYHPDDIYW-CTA---DIG 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  737 NMT-----TLLPLSSGGT-LAF-GEPN----DRAIMQAEQAGATHL-ILPTA---LMSiLDPEQVNG-----IQAIGMGG 796
Cdd:cd05966   284 WITghsyiVYGPLANGATtVMFeGTPTypdpGRYWDIVEKHKVTIFyTAPTAiraLMK-FGDEWVKKhdlssLRVLGSVG 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  797 EacP-NAVVENWadkvaLYNMYGPTECTV--------------TAL--STRLRkgqPVTIGKPLIHIQALILDTAGQLCP 859
Cdd:cd05966   363 E--PiNPEAWMW-----YYEVIGKERCPIvdtwwqtetggimiTPLpgATPLK---PGSATRPFFGIEPAILDEEGNEVE 432

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  860 VGVPGELCLAGL--GLARGYLNQPQmtasRFEHITLNDVNNagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRG 937
Cdd:cd05966   433 GEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPG---------YYFTGDGARRDEDGYYWITGRVDDVINVSG 499

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  938 YRIEPGEIEAQLAAvCPslkqiKVIVAQVGSRP------ALVAYATVKADSS-TPEPAAVLID-VAKYLPEYMVPFRLML 1009
Cdd:cd05966   500 HRLGTAEVESALVA-HP-----AVAEAAVVGRPhdikgeAIYAFVTLKDGEEpSDELRKELRKhVRKEIGPIATPDKIQF 573

                         570
                  ....*....|.
gi 499404635 1010 LEDMPLTPNGK 1020
Cdd:cd05966   574 VPGLPKTRSGK 584
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 561-1020 3.53e-17

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: 86.64  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVIlgg 640
Cdd:cd05940     3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 dgqqlaqwsaeqridLTDPAVveqwqdlpgdqppaiprhaqqlaqVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFT 720
Cdd:cd05940    80 ---------------VVDAAL------------------------YIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  721 PQSTMFNCMSLSFDAGNMTTLLP-LSSGGTLAFGepndraimqaEQAGATHlilptaLMSILDPEQVNGIQAIG------ 793
Cdd:cd05940   121 PSDVLYTCLPLYHSTALIVGWSAcLASGATLVIR----------KKFSASN------FWDDIRKYQATIFQYIGelcryl 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  794 MGGEACPN-------AVVEN------WADKVALYNM------YGPTECTVTAL------------STRLRKGQPVTIGKP 842
Cdd:cd05940   185 LNQPPKPTerkhkvrMIFGNglrpdiWEEFKERFGVpriaefYAATEGNSGFInffgkpgaigrnPSLLRKVAPLALVKY 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  843 LIHIQALILDTAGQL--CPVGVPGELCLAGLGLAR--GYLNQPQMTASRfehitLNDVNNAGQgaatlRIYRTGDKARLL 918
Cdd:cd05940   265 DLESGEPIRDAEGRCikVPRGEPGLLISRINPLEPfdGYTDPAATEKKI-----LRDVFKKGD-----AWFNTGDLMRLD 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  919 NNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLI-DVAKY 997
Cdd:cd05940   335 GEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAF-PGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAaHLEKN 413

                         490       500
                  ....*....|....*....|...
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGK 1020
Cdd:cd05940   414 LPGYARPLFLRLQPEMEITGTFK 436
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 548-949 6.55e-17

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 86.87  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  548 QLAIAFDGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPE---- 623
Cdd:PRK04319   60 KVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEavrd 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  624 RL-----RHIITDANL-------------SVILGGDGQQLAqwsaEQRIDLtdPAVVEQwqdlPGDQPPAIPRHAQQLAQ 685
Cdd:PRK04319  140 RLedseaKVLITTPALlerkpaddlpslkHVLLVGEDVEEG----PGTLDF--NALMEQ----ASDEFDIEWTDREDGAI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 VIYTSGSTGLPKGVMIEHGSLIN-------LLDDHRDRIdftpqstmFNCMSlsfDAGNMT-----TLLPLSSGGTLAFg 753
Cdd:PRK04319  210 LHYTSGSTGKPKGVLHVHNAMLQhyqtgkyVLDLHEDDV--------YWCTA---DPGWVTgtsygIFAPWLNGATNVI- 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  754 epnDRAIMQAEqagATHLIL-----------PTA---LMSiLDPEQVNG-----IQAIGMGGEAC-PNAVVenWADKVal 813
Cdd:PRK04319  278 ---DGGRFSPE---RWYRILedykvtvwytaPTAirmLMG-AGDDLVKKydlssLRHILSVGEPLnPEVVR--WGMKV-- 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  814 YNM-----YGPTE------CTVTALSTRlrkgqPVTIGKPLIHIQALILDTAGQLCPVGVPGELCL-AGL-GLARGYLNQ 880
Cdd:PRK04319  347 FGLpihdnWWMTEtggimiANYPAMDIK-----PGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGWpSMMRGIWNN 421

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635  881 PQmtasRFEHITLNDvnnagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQL 949
Cdd:PRK04319  422 PE----KYESYFAGD------------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL 474
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 562-1026 8.06e-17

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 85.91  E-value: 8.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD 641
Cdd:PRK12406   12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 G--QQLA----------------QWSAEQRID---LTDPAVVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVm 700
Cdd:PRK12406   92 DllHGLAsalpagvtvlsvptppEIAAAYRISpalLTPPAGAIDWEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGV- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  701 iehgslinllddhrDRIDFTPQSTMFNCMSLSFDAG---NMTTLLPlssgGTLAFGEPNDRAIMQAEQAGA--------- 768
Cdd:PRK12406  171 --------------RRAAPTPEQAAAAEQMRALIYGlkpGIRALLT----GPLYHSAPNAYGLRAGRLGGVlvlqprfdp 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  769 ------------THL-ILPTALMSILD-PEQV------NGIQAIGMGGEACP----NAVVENWADkvALYNMYGPTECTV 824
Cdd:PRK12406  233 eellqlierhriTHMhMVPTMFIRLLKlPEEVrakydvSSLRHVIHAAAPCPadvkRAMIEWWGP--VIYEYYGSTESGA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  825 TALSTR---LRKgqPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLAR-GYLNQPQMTAS--RFEHITLNDVNn 898
Cdd:PRK12406  311 VTFATSedaLSH--PGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidRGGFITSGDVG- 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  899 agqgaatlriyrtgdkarLLNNGDYEY-CGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI---VAQVGSrpALVA 974
Cdd:PRK12406  388 ------------------YLDADGYLFlCDRKRDMVISGGVNIYPAEIEAVLHA-VPGVHDCAVFgipDAEFGE--ALMA 446

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499404635  975 YATVKAdSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK12406  447 VVEPQP-GATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 561-1035 1.05e-16

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 86.05  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQ-GLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVI-- 637
Cdd:PLN02574   66 SISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAft 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  638 -------LGGDGQQLAQWSAEQRIDLTDPAVVEQWQDLPGDQP--PAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLIN 708
Cdd:PLN02574  146 spenvekLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIA 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  709 LLDDHrdrIDF------TPQST--------MFNCMSLSFDAGNMttllpLSSGGTLAFGEPND--RAIMQAEQAGATHL- 771
Cdd:PLN02574  226 MVELF---VRFeasqyeYPGSDnvylaalpMFHIYGLSLFVVGL-----LSLGSTIVVMRRFDasDMVKVIDRFKVTHFp 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  772 ILPTALMSILDPEQVNGIQAIGMGGEACPNAV------VENWAD---KVALYNMYGPTECTvtALSTR------LRKGQP 836
Cdd:PLN02574  298 VVPPILMALTKKAKGVCGEVLKSLKQVSCGAAplsgkfIQDFVQtlpHVDFIQGYGMTEST--AVGTRgfntekLSKYSS 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  837 VTIGKPliHIQALILD-TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRfehitlndVNNAGQgaatlriYRTGDKA 915
Cdd:PLN02574  376 VGLLAP--NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQST--------IDKDGW-------LRTGDIA 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  916 RLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCpslKQIKVIVAQVGSRPA---LVAYaTVKADSSTPEPAAVLI 992
Cdd:PLN02574  439 YFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHP---EIIDAAVTAVPDKECgeiPVAF-VVRRQGSTLSQEAVIN 514

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 499404635  993 DVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEANES 1035
Cdd:PLN02574  515 YVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVS 557
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 520-1021 2.37e-16

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 84.83  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  520 TQQLPRSYPQPQLTV----TDVIEAVAQRDPQQLAIAFDGeprtDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKR 595
Cdd:PRK07786    1 TRALTLAQEQPYLARrqnwVNQLARHALMQPDAPALRFLG----NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  596 DRYFVIALLAIWKAGAAYVPLDPDY-PPE--------RLRHIITDANLS---------------VILGGDGQQLAQWSAE 651
Cdd:PRK07786   77 RTEFVESVLAANMLGAIAVPVNFRLtPPEiaflvsdcGAHVVVTEAALApvatavrdivpllstVVVAGGSSDDSVLGYE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  652 QRIDLTDPAVveQWQDLPGDQPPAIprhaqqlaqvIYTSGSTGLPKGVMIEHGSL----INLLD----DHRDRIDFTpQS 723
Cdd:PRK07786  157 DLLAEAGPAH--APVDIPNDSPALI----------MYTSGTTGRPKGAVLTHANLtgqaMTCLRtngaDINSDVGFV-GV 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  724 TMFNCMSLsfdaGNMTTLLPLssGGTL------AFgEPNDRA-IMQAEQAGATHLIlPTALMSILDPEQVNG----IQAI 792
Cdd:PRK07786  224 PLFHIAGI----GSMLPGLLL--GAPTviyplgAF-DPGQLLdVLEAEKVTGIFLV-PAQWQAVCAEQQARPrdlaLRVL 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  793 GMGGEACPNAVVENWAD---KVALYNMYGPTECT-VTAL---STRLRKGQPVtiGKPLIHIQALILDTAGQLCPVGVPGE 865
Cdd:PRK07786  296 SWGAAPASDTLLRQMAAtfpEAQILAAFGQTEMSpVTCMllgEDAIRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGE 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  866 LCLAGLGLARGYLNQPQMTASRFEhitlndvnnAGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEI 945
Cdd:PRK07786  374 IVYRAPTLMSGYWNNPEATAEAFA---------GGW-------FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEV 437

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  946 EAQLAAvCPSLKQIKVI---VAQVGSRPalVAYATVKADSSTPEpaavLIDVAKYLPE----YMVPFRLMLLEDMPLTPN 1018
Cdd:PRK07786  438 ENVLAS-HPDIVEVAVIgraDEKWGEVP--VAVAAVRNDDAALT----LEDLAEFLTDrlarYKHPKALEIVDALPRNPA 510


                  ...
gi 499404635 1019 GKL 1021
Cdd:PRK07786  511 GKV 513
PLN02246 PLN02246
4-coumarate--CoA ligase
 560-1033 4.19e-16

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 83.88  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  560 DTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDY-PPE--------RLRHIIT 630
Cdd:PLN02246   49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYtPAEiakqakasGAKLIIT 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  631 DANLSVILggdgQQLAQWSAEQRIDLTDPA--VVEQWQDLPGDQ--PPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSL 706
Cdd:PLN02246  129 QSCYVDKL----KGLAEDDGVTVVTIDDPPegCLHFSELTQADEneLPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  707 IN----LLDDHRDRIDFTPQST------MFNCMSLsfdagNMTTLLPLSSGGTLAfgepndraIMQAEQAGA------TH 770
Cdd:PLN02246  205 VTsvaqQVDGENPNLYFHSDDVilcvlpMFHIYSL-----NSVLLCGLRVGAAIL--------IMPKFEIGAlleliqRH 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  771 ----------LILPTALMSILDPEQVNGIQAIgMGGEA-------------CPNAVvenwadkvaLYNMYGPTEC-TVTA 826
Cdd:PLN02246  272 kvtiapfvppIVLAIAKSPVVEKYDLSSIRMV-LSGAAplgkeledafrakLPNAV---------LGQGYGMTEAgPVLA 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 LSTRLRKgQPVTI-----GKPLIHIQALILDT-AGQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfehitlndvnnag 900
Cdd:PLN02246  342 MCLAFAK-EPFPVksgscGTVVRNAELKIVDPeTGASLPRNQPGEICIRGPQIMKGYLNDPEATA--------------- 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  901 qgaatlriyRTGDKARLLNNGDYEY---------CGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKViVAQ----VG 967
Cdd:PLN02246  406 ---------NTIDKDGWLHTGDIGYiddddelfiVDRLKELIKYKGFQVAPAELEALLIS-HPSIADAAV-VPMkdevAG 474

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  968 SRPalVAYaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEAN 1033
Cdd:PLN02246  475 EVP--VAF-VVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAAG 537
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 532-1035 5.10e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 83.29  E-value: 5.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGlGEQSLVGVLAKRDRYFVIALLAIWKAGA 611
Cdd:PRK07638    1 MGITKEYKKHASLQPNKIAIKENDR----VLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  612 AYVPLDPDYPPERLRH---------IITDA-NLSVILGGDGQ--QLAQWSAEQRIDLTDPAVVEQWQDLP---Gdqppai 676
Cdd:PRK07638   76 TCVPLDIKWKQDELKErlaisnadmIVTERyKLNDLPDEEGRviEIDEWKRMIEKYLPTYAPIENVQNAPfymG------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  677 prhaqqlaqviYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMF---NCMSLSFDAGNMTTLLplsSGGTLAFG 753
Cdd:PRK07638  150 -----------FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLiagTLVHSLFLYGAISTLY---VGQTVHLM 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  754 E---PND-RAIMQAEQAGATHLIlPTALMSILD----PEQVNGIQAIGMGGEACPNAVVENWADKVALYNMYGPTECT-V 824
Cdd:PRK07638  216 RkfiPNQvLDKLETENISVMYTV-PTMLESLYKenrvIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSfV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  825 TALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLN----QPQMTASrfEHITLNDVNnag 900
Cdd:PRK07638  295 TALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIggvlARELNAD--GWMTVRDVG--- 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  901 qgaatlRIYRTGdkarllnngdYEYC-GRIDEQIKLRGYRIEPGEIEaQLAAVCPSLKQIKVI-VAQV--GSRPalVAYA 976
Cdd:PRK07638  370 ------YEDEEG----------FIYIvGREKNMILFGGINIFPEEIE-SVLHEHPAVDEIVVIgVPDSywGEKP--VAII 430

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635  977 TVKADSSTPEPAavlidVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEANES 1035
Cdd:PRK07638  431 KGSATKQQLKSF-----CLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1567-1867 5.38e-16

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


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 82.69  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1567 PLSSLQQSMLY-HRLrcpQDDAYHLQTPI--RYAHVLDVEGYRQAWQRQIQRFPALRAALESECA-SIQVIVKQADLPFY 1642
Cdd:cd20483     3 PMSTFQRRLWFlHNF---LEDKTFLNLLLvcHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDfGEQQVLDDPSFHLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1643 YQDLMQDADPLAVIERYRQQDLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQGQ 1722
Cdd:cd20483    80 VIDLSEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1723 VLMHGDAPAIQvdraYVDYA--RHAVAQQSAVD---AFWQQRqslLAQTNDVSML--FAAAGKRAdlsqhLTQIEPQVTS 1795
Cdd:cd20483   160 DLATVPPPPVQ----YIDFTlwHNALLQSPLVQpllDFWKEK---LEGIPDASKLlpFAKAERPP-----VKDYERSTVE 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635 1796 VSLNEKDQATLTAFAREVGITPSIIAQYAWHRLLARSTGDAVSIVGNVLSGRESPveDVASSVGLYINSLPL 1867
Cdd:cd20483   228 ATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHP--DFDDLVGFFVNMLPI 297
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 562-1026 6.14e-16

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 83.53  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITD--ANLSVILg 639
Cdd:PRK07059   49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDsgAEAIVVL- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 gdgQQLAQwSAEQRIDLTD--PAVVEQWQDLPGDQ---------------PP-AIPRH-----------AQQLAQVI--- 687
Cdd:PRK07059  128 ---ENFAT-TVQQVLAKTAvkHVVVASMGDLLGFKghivnfvvrrvkkmvPAwSLPGHvrfndalaegaRQTFKPVKlgp 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  688 -------YTSGSTGLPKGVMIEHGSLI-NLLDDH---------RDRID--FT----PQSTMF----NCMsLSFDAGNMTT 740
Cdd:PRK07059  204 ddvaflqYTGGTTGVSKGATLLHRNIVaNVLQMEawlqpafekKPRPDqlNFvcalPLYHIFaltvCGL-LGMRTGGRNI 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  741 LLPlssggtlafgEPNDRAIMQAEQAGATHLILP------TALMSILDPEQV---NGIQAIGmGGEACPNAVVENWADKV 811
Cdd:PRK07059  283 LIP----------NPRDIPGFIKELKKYQVHIFPavntlyNALLNNPDFDKLdfsKLIVANG-GGMAVQRPVAERWLEMT 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  812 --ALYNMYGPTECTVTALSTRLRKGQ-PVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQ-----M 883
Cdd:PRK07059  352 gcPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDetakvM 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  884 TASRFehitlndvnnagqgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEaQLAAVCPSLKQIKVI- 962
Cdd:PRK07059  432 TADGF--------------------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE-EVVASHPGVLEVAAVg 490

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404635  963 VAQVGSRPALVAYaTVKADSSTPEpAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK07059  491 VPDEHSGEAVKLF-VVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 684-1021 8.14e-16

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: 81.15  E-value: 8.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  684 AQVIYTSGSTGLPKGVMIEHGSLINLLDD-HRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPN--DRAI 760
Cdd:cd17635     4 LAVIFTSGTTGEPKAVLLANKTFFAVPDIlQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENttYKSL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  761 MQAEQ--AGATHLILPTAlMSILDPEQVNGIQA------IGMGGEACPNAVVEN--WADKVALYNMYGPTECT-VTALST 829
Cdd:cd17635    84 FKILTtnAVTTTCLVPTL-LSKLVSELKSANATvpslrlIGYGGSRAIAADVRFieATGLTNTAQVYGLSETGtALCLPT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  830 RLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNdvnnagqgaatlriy 909
Cdd:cd17635   163 DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVN--------------- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  910 rTGDKARlLNNGDYEYC-GRIDEQIKLRGYRIEPGEIEaQLAAVCPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPA 988
Cdd:cd17635   228 -TGDLGE-RREDGFLFItGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAI 304

                         330       340       350
                  ....*....|....*....|....*....|....
gi 499404635  989 AVLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:cd17635   305 RALKHtIRRELEPYARPSTIVIVTDIPRTQSGKV 338
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 562-1026 1.15e-15

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: 81.85  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRhiitdanlsvilggd 641
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLR--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  642 gqqlaqwsaeQRIDLTDPAVVEQWQDLPGDQPpaiprhaqqlAQVIYTSGSTGLPKGVMIEH-----GSLINLLddhrdR 716
Cdd:cd05974    66 ----------DRVDRGGAVYAAVDENTHADDP----------MLLYFTSGTTSKPKLVEHTHrsypvGHLSTMY-----W 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  717 IDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGTL-AFGEP--NDRAIMQA-EQAGATHLILPTALMSILDPEQVNG--- 788
Cdd:cd05974   121 IGLKPGDVHWNISSPGWAKHAWSCFFaPWNAGATVfLFNYArfDAKRVLAAlVRYGVTTLCAPPTVWRMLIQQDLASfdv 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  789 -IQAIGMGGEACPNAVVEN----WAdkVALYNMYGPTECTVTALSTrlrKGQPV---TIGKPLIHIQALILDtagqlcPV 860
Cdd:cd05974   201 kLREVVGAGEPLNPEVIEQvrraWG--LTIRDGYGQTETTALVGNS---PGQPVkagSMGRPLPGYRVALLD------PD 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  861 GVP---GELCLA-----GLGLARGYLNQPQMTASrfehitlndvnnAGQGAatlrIYRTGDKARLLNNGDYEYCGRIDEQ 932
Cdd:cd05974   270 GAPateGEVALDlgdtrPVGLMKGYAGDPDKTAH------------AMRGG----YYRTGDIAMRDEDGYLTYVGRADDV 333

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  933 IKLRGYRIEPGEIEAQL--------AAVCPSLKQIKVIVAQvgsrpalvAYATVKAdSSTPEPAAVLiDVAKYLPEYMVP 1004
Cdd:cd05974   334 FKSSDYRISPFELESVLiehpavaeAAVVPSPDPVRLSVPK--------AFIVLRA-GYEPSPETAL-EIFRFSRERLAP 403

                         490       500
                  ....*....|....*....|....*
gi 499404635 1005 F---RLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05974   404 YkriRRLEFAELPKTISGKIRRVEL 428
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 555-952 1.48e-15

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 82.35  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  555 GEPRT-DTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITD-- 631
Cdd:PRK07768   22 GEPDApVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDtl 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  632 -------ANLsVILGGDGQQLAQWSAEQRIdlTDPAVVEQWQDLPGDqPPAIPRHAQQLAQViyTSGSTGLPKGVMIEHG 704
Cdd:PRK07768  102 rvigmigAKA-VVVGEPFLAAAPVLEEKGI--RVLTVADLLAADPID-PVETGEDDLALMQL--TSGSTGSPKAVQITHG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  705 SLINLLDDHRDRIDFTPQS-TMFNCMSLSFDAGNMTTL-LPLSSGGTLAFGEPND---------------RAIMQAEQAG 767
Cdd:PRK07768  176 NLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVGFLtVPMYFGAELVKVTPMDflrdpllwaeliskyRGTMTAAPNF 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  768 AtHLILPTALMSILDPEQVN--GIQAIGMGGEACPNAVVENWADKVALYNM--------YGPTECTVTA----------- 826
Cdd:PRK07768  256 A-YALLARRLRRQAKPGAFDlsSLRFALNGAEPIDPADVEDLLDAGARFGLrpeailpaYGMAEATLAVsfspcgaglvv 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 ------LSTRLRKGQP---------VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLnqpqmTASRFEhi 891
Cdd:PRK07768  335 devdadLLAALRRAVPatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFI-- 407

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404635  892 tlndvnnAGQGAATLriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAV 952
Cdd:PRK07768  408 -------PAQDADGW--LDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARV 459
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1156-1424 2.02e-15

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: 81.00  E-value: 2.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1156 PEVDTERLVTMLQALMAQHDALRLGCDAEG-QRYLADVPCPALSTLDYRQLGDDGLQQAFTALQSE-----FDPAQGRTM 1229
Cdd:cd19535    35 EDLDPDRLERAWNKLIARHPMLRAVFLDDGtQQILPEVPWYGITVHDLRGLSEEEAEAALEELRERlshrvLDVERGPLF 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1230 ACALVRHhPQADTALFLAFHHLVIDAVSWRILVDDLERLYL--GEPLLPKTSSYRQWGAALQ-HYATQHAEQLTYWQAQE 1306
Cdd:cd19535   115 DIRLSLL-PEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPLPPLELSFRDYLLAEQaLRETAYERARAYWQERL 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1307 DgvDL---TALLAAKDPQGHASAAI----LTLDAKTTGQLVSEAnRAFNTDVSDLLLSALTRTLNdlGWGDKAR--IMLE 1377
Cdd:cd19535   194 P--TLppaPQLPLAKDPEEIKEPRFtrreHRLSAEQWQRLKERA-RQHGVTPSMVLLTAYAEVLA--RWSGQPRflLNLT 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 499404635 1378 GHGREAIDPtlDVSRTVGWFTST--YPVCLQDKPDWASLIQSSKEQLRQ 1424
Cdd:cd19535   269 LFNRLPLHP--DVNDVVGDFTSLllLEVDGSEGQSFLERARRLQQQLWE 315
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 561-1026 2.66e-15

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: 80.97  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLgEQSLVGVLAKRDRYFVIAL-LAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG 639
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGI-RRGMRAVLMVPPGPDFFALtFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 gdgqqlaqwsaeqridltdpavveqwqdlpgdqppaIPRhAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDF 719
Cdd:cd05910    81 ------------------------------------IPK-ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  720 TPQSTMFNCMSLS--FD-AGNMTTLLPlsSGGTLAFGEPNDRAIMQA-EQAGATHLILPTALMSIL------DPEQVNGI 789
Cdd:cd05910   124 RPGEVDLATFPLFalFGpALGLTSVIP--DMDPTRPARADPQKLVGAiRQYGVSIVFGSPALLERVarycaqHGITLPSL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  790 QAIGMGGEACPNAVVENW----ADKVALYNMYGPTEC-TVTALSTR-LR--------KGQPVTIGKPLIHIQALILDT-- 853
Cdd:cd05910   202 RRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEAlPVSSIGSReLLatttaatsGGAGTCVGRPIPGVRVRIIEIdd 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  854 ------AGQLC-PVGVPGELCLAGLGLARGYLNQPQMTAsrfehitLNDVNNAGQGAatlrIYRTGDKARLLNNGDYEYC 926
Cdd:cd05910   282 epiaewDDTLElPRGEIGEITVTGPTVTPTYVNRPVATA-------LAKIDDNSEGF----WHRMGDLGYLDDEGRLWFC 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  927 GRIDEQIKLRGYRIEPGEIEAqLAAVCPSLKQIKV--IVAQVGSRPALVayatVKADSSTPEPAA----VLIDVAKYLPE 1000
Cdd:cd05910   351 GRKAHRVITTGGTLYTEPVER-VFNTHPGVRRSALvgVGKPGCQLPVLC----VEPLPGTITPRArleqELRALAKDYPH 425

                         490       500
                  ....*....|....*....|....*...
gi 499404635 1001 YMVPFRLMLLEDMPLTP--NGKLDMKQL 1026
Cdd:cd05910   426 TQRIGRFLIHPSFPVDIrhNAKIFREKL 453
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 541-1032 4.33e-15

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 80.86  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  541 VAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDY 620
Cdd:PRK07470   16 AARRFPDRIALVWGDR----SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  621 PPERLRHIITDANLSVILG-GDGQQLAQWSAEQRIDLT------DPAVVEQWQDLPGDQPPAIPRHAQ----QLAQVIYT 689
Cdd:PRK07470   92 TPDEVAYLAEASGARAMIChADFPEHAAAVRAASPDLThvvaigGARAGLDYEALVARHLGARVANAAvdhdDPCWFFFT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  690 SGSTGLPKGVMIEHGSLINLLDDHRdrIDFTPQSTMFNC----MSLSFDAGnMTTLLPLSSGGT--LAFGEPNDRAIMQA 763
Cdd:PRK07470  172 SGTTGRPKAAVLTHGQMAFVITNHL--ADLMPGTTEQDAslvvAPLSHGAG-IHQLCQVARGAAtvLLPSERFDPAEVWA 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  764 --EQAGATHLI-LPTAL-MSILDPE-----------------------QVNGIQAIGmggeacpnavvenwadKVaLYNM 816
Cdd:PRK07470  249 lvERHRVTNLFtVPTILkMLVEHPAvdrydhsslryviyagapmyradQKRALAKLG----------------KV-LVQY 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  817 YGPTECT--VTALSTRLRKGQPV------TIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF 888
Cdd:PRK07470  312 FGLGEVTgnITVLPPALHDAEDGpdarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  889 EHitlndvnnaGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI-VA--- 964
Cdd:PRK07470  392 RD---------GW-------FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLT-HPAVSEVAVLgVPdpv 454

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  965 --QVGsrpalVAyATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEA 1032
Cdd:PRK07470  455 wgEVG-----VA-VCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEE 518
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 525-1021 4.91e-15

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 80.85  E-value: 4.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  525 RSYPQ--PQLTVTDV------IEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRD 596
Cdd:PRK06710    9 KSYPEeiPSTISYDIqplhkyVEQMASRYPEKKALHFLGK----DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNC 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  597 RYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGGD--GQQLAQWSAEQRID------------------- 655
Cdd:PRK06710   85 PQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDlvFPRVTNVQSATKIEhvivtriadflpfpknlly 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  656 -------------LTDPAVVEQWQDLPGDQPPAI-----PRHaqQLAQVIYTSGSTGLPKGVMIEHGSLIN--LLDDHrd 715
Cdd:PRK06710  165 pfvqkkqsnlvvkVSESETIHLWNSVEKEVNTGVevpcdPEN--DLALLQYTGGTTGFPKGVMLTHKNLVSntLMGVQ-- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  716 ridftpqsTMFNCMSLS---------FDAGNMTTLLPLS--SGGTLAFGEPND-RAIMQAEQAGATHLI--LPTALMSIL 781
Cdd:PRK06710  241 --------WLYNCKEGEevvlgvlpfFHVYGMTAVMNLSimQGYKMVLIPKFDmKMVFEAIKKHKVTLFpgAPTIYIALL 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  782 DPE-----QVNGIQAIGMGGEACPNAVVENWADKVA--LYNMYGPTECTVTALSTRL-RKGQPVTIGKPLIHIQALILD- 852
Cdd:PRK06710  313 NSPllkeyDISSIRACISGSAPLPVEVQEKFETVTGgkLVEGYGLTESSPVTHSNFLwEKRVPGSIGVPWPDTEAMIMSl 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  853 TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNdvnnagqgaatlriyrTGDKARLLNNGDYEYCGRIDEQ 932
Cdd:PRK06710  393 ETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLH----------------TGDVGYMDEDGFFYVKDRKKDM 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  933 IKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVAQVGSRPALVAYATVKADSSTPEPAAVLIdVAKYLPEYMVPFRLMLLED 1012
Cdd:PRK06710  457 IVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQF-ARKYLAAYKVPKVYEFRDE 535


                  ....*....
gi 499404635 1013 MPLTPNGKL 1021
Cdd:PRK06710  536 LPKTTVGKI 544
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
561-1026 8.96e-15

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 79.92  E-value: 8.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLhrqgLGEQSLvgvlAKRDRY---------FVIALLAIWKAGAAYVPLDPDYPPERLRHIITD 631
Cdd:PRK08751   50 TITYREADQLVEQFAAYL----LGELQL----KKGDRValmmpnclqYPIATFGVLRAGLTVVNVNPLYTPRELKHQLID 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  632 ANLSVILGGDG------QQLAQWSAEQRI-----DLTDPA-------VVEQWQDL-PGDQPPAIPRHAQQLAQ------- 685
Cdd:PRK08751  122 SGASVLVVIDNfgttvqQVIADTPVKQVIttglgDMLGFPkaalvnfVVKYVKKLvPEYRINGAIRFREALALgrkhsmp 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 -----------VIYTSGSTGLPKGVMIEHGSLI-NLLddhrdridftpQSTMFNCMSLSFDAGNMT--TLLPLSSGGTLA 751
Cdd:PRK08751  202 tlqiepddiafLQYTGGTTGVAKGAMLTHRNLVaNMQ-----------QAHQWLAGTGKLEEGCEVviTALPLYHIFALT 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  752 fgePNDRAIMQAeqAGATHLI-----LP-----------TALMSI------------LDPEQVNGIQAIGMGGEACPNAV 803
Cdd:PRK08751  271 ---ANGLVFMKI--GGCNHLIsnprdMPgfvkelkktrfTAFTGVntlfngllntpgFDQIDFSSLKMTLGGGMAVQRSV 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  804 VENW--ADKVALYNMYGPTECTVTALSTRLR-KGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQ 880
Cdd:PRK08751  346 AERWkqVTGLTLVEAYGLTETSPAACINPLTlKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKR 425

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  881 PQMTASRFEhitlndvnnaGQGAatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIE---------AQLAA 951
Cdd:PRK08751  426 PEETAKVMD----------ADGW-----LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEdviammpgvLEVAA 490

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635  952 V-CPSLKQ---IKVIVaqVGSRPALVAyATVKADSSTpepaavliDVAKYLPEYMVPFRlmllEDMPLTPNGKLDMKQL 1026
Cdd:PRK08751  491 VgVPDEKSgeiVKVVI--VKKDPALTA-EDVKAHARA--------NLTGYKQPRIIEFR----KELPKTNVGKILRREL 554
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1157-1425 3.16e-14

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: 77.24  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1157 EVDTERLVTMLQALMAQHDALRLGCDAEG-----QRYLADVPCPaLSTLDYRQLGDDGLQQAFTALQSE-----FDPAQG 1226
Cdd:cd19543    35 PLDPDRFRAAWQAVVDRHPILRTSFVWEGlgeplQVVLKDRKLP-WRELDLSHLSEAEQEAELEALAEEdrergFDLARA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1227 RTMACALVRHHPQADTaLFLAFHHLVIDAVSWRILVDDLERLYLG-----EPLLPKTSSYRQWGAALQHYATQHAEQltY 1301
Cdd:cd19543   114 PLMRLTLIRLGDDRYR-LVWSFHHILLDGWSLPILLKELFAIYAAlgegqPPSLPPVRPYRDYIAWLQRQDKEAAEA--Y 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1302 WQAQEDGVD-----LTALLAAKDPQGHASAAILTLDAKTTGQLVSEANRA---FNTDVS---DLLLSALTRTlNDLGWGd 1370
Cdd:cd19543   191 WREYLAGFEeptplPKELPADADGSYEPGEVSFELSAELTARLQELARQHgvtLNTVVQgawALLLSRYSGR-DDVVFG- 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635 1371 karimLEGHGREAIDPtlDVSRTVGWFTSTYPVCLQDKPDwasliQSSKEQLRQV 1425
Cdd:cd19543   269 -----TTVSGRPAELP--GIETMVGLFINTLPVRVRLDPD-----QTVLELLKDL 311
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 688-1022 5.20e-14

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: 75.52  E-value: 5.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  688 YTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTL----AFGEPNDRAIMQA 763
Cdd:cd17633     7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFigqrKFNPKSWIRKINQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  764 EQAGATHLIlPT---ALMSILDPEqvNGIQAIGMGGEACPN---AVVENWADKVALYNMYGPTECTVTALSTRLRKGQPV 837
Cdd:cd17633    87 YNATVIYLV-PTmlqALARTLEPE--SKIKSIFSSGQKLFEstkKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  838 TIGKPLIHIQALILDTAGqlcpvGVPGELClaglglargyLNQPQMtasrFEHITLNDVNNAGQGaatlriYRTGDKARL 917
Cdd:cd17633   164 SVGRPFPNVEIEIRNADG-----GEIGKIF----------VKSEMV----FSGYVRGGFSNPDGW------MSVGDIGYV 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  918 LNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIkVIVAQVGSRPALVAYATVKADSSTPEpaAVLIDVAKY 997
Cdd:cd17633   219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKA-IPGIEEA-IVVGIPDARFGEIAVALYSGDKLTYK--QLKRFLKQK 294

                         330       340
                  ....*....|....*....|....*
gi 499404635  998 LPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:cd17633   295 LSRYEIPKKIIFVDSLPYTSSGKIA 319
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 561-962 5.41e-14

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: 77.01  E-value: 5.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDAnLSVILgg 640
Cdd:cd17640     5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHS-ESVAL-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 dgqqlaqwsaeqridltdpaVVEQwqdlpgdqppaiprHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFT 720
Cdd:cd17640    82 --------------------VVEN--------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  721 PQSTMfncMSL-----SFDAGNMTTLlpLSSGGTLAFGEPndRAIMQAEQAGATHLILPT-----ALMSILDPEQVN--- 787
Cdd:cd17640   128 PGDRF---LSIlpiwhSYERSAEYFI--FACGCSQAYTSI--RTLKDDLKRVKPHYIVSVprlweSLYSGIQKQVSKssp 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  788 ------------GIQAIGM-GGEACPNAVVENW-ADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILD- 852
Cdd:cd17640   201 ikqflflfflsgGIFKFGIsGGGALPPHVDTFFeAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDp 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  853 TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfEHITLNDVNNagqgaatlriyrTGDKARLLNNGDYEYCGRIDEQ 932
Cdd:cd17640   281 EGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATS---KVLDSDGWFN------------TGDLGWLTCGGELVLTGRAKDT 345

                         410       420       430
                  ....*....|....*....|....*....|.
gi 499404635  933 IKLR-GYRIEPGEIEAQLAAvCPSLKQIKVI 962
Cdd:cd17640   346 IVLSnGENVEPQPIEEALMR-SPFIEQIMVV 375
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 538-965 5.91e-14

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: 77.09  E-value: 5.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  538 IEAVAQRDPQQLAIA-FDGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPL 616
Cdd:cd05921     1 LAHWARQAPDRTWLAeREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  617 DPDYPP-----ERLRHIITDANLSVILGGDGQQLAQwsAEQRIDLTDPAVVEQWQDLPGD----------QPP--AIPRH 679
Cdd:cd05921    81 SPAYSLmsqdlAKLKHLFELLKPGLVFAQDAAPFAR--ALAAIFPLGTPLVVSRNAVAGRgaisfaelaaTPPtaAVDAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  680 AQQ-----LAQVIYTSGSTGLPKGVMIEHGSL---INLLDDHRDRIDFTPqSTMFNCM--SLSFdAGNMTTLLPLSSGGT 749
Cdd:cd05921   159 FAAvgpdtVAKFLFTSGSTGLPKAVINTQRMLcanQAMLEQTYPFFGEEP-PVLVDWLpwNHTF-GGNHNFNLVLYNGGT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  750 LAF--GEPNDRAIMQA-----EQAGATHLILPTA---LMSILDPEQV------NGIQAIGMGGEACPNAV--------VE 805
Cdd:cd05921   237 LYIddGKPMPGGFEETlrnlrEISPTVYFNVPAGwemLVAALEKDEAlrrrffKRLKLMFYAGAGLSQDVwdrlqalaVA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  806 NWADKVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQAlildtagQLCPVGVPGELCLAGLGLARGYLNQPQMTA 885
Cdd:cd05921   317 TVGERIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTA 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  886 SRFEHitlndvnnagQGaatlrIYRTGDKARLLNNGDYE----YCGRIDEQIKLR-GYRIEPGEIEAQLAAVCPSLKQIK 960
Cdd:cd05921   390 QAFDE----------EG-----FYCLGDAAKLADPDDPAkglvFDGRVAEDFKLAsGTWVSVGPLRARAVAACAPLVHDA 454


                  ....*
gi 499404635  961 VIVAQ 965
Cdd:cd05921   455 VVAGE 459
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 529-757 6.36e-14

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: 77.11  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  529 QPQLTVTDVIE----------AVAQRDPQQLAIAFDGE------PRTDTLTYAELNRQANQLAHWLH-RQGLGEQSLVGV 591
Cdd:cd17632    19 RPGLRLAQIIAtvmtgyadrpALGQRATELVTDPATGRttlrllPRFETITYAELWERVGAVAAAHDpEQPVRPGDFVAV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  592 LAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIIT--------------DANLSVILGG---------------DG 642
Cdd:cd17632    99 LGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAeteprllavsaehlDLAVEAVLEGgtpprlvvfdhrpevDA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  643 QQLAQWSAEQRI------DLTDPAVVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDR 716
Cdd:cd17632   179 HRAALESARERLaavgipVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSI 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 499404635  717 IDFTPQ-STMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPND 757
Cdd:cd17632   259 QDIRPPaSITLNFMPMSHIAGRISLYGTLARGGTAYFAAASD 300
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 560-1026 7.49e-14

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: 76.65  E-value: 7.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  560 DTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDyPPERLRHIITDAN---LSV 636
Cdd:cd05929    16 RLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSR-APRAEACAIIEIKaaaLVC 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  637 ILGGDGQQLAQWSaeqridlTDPAVveqwqdlPGDQP-PAIPRHAQQLAqVIYTSGSTGLPKGVMIEH-GSLINllDDHR 714
Cdd:cd05929    95 GLFTGGGALDGLE-------DYEAA-------EGGSPeTPIEDEAAGWK-MLYSGGTTGRPKGIKRGLpGGPPD--NDTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  715 ----DRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPND-----RAImqaEQAGATHL-ILPTALMSILD-P 783
Cdd:cd05929   158 maaaLGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDpeeflRLI---ERYRVTFAqFVPTMFVRLLKlP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  784 EQVNG------IQAIGMGGEACPNAVVENWAD--KVALYNMYGPTECT-VTALSTRLRKGQPVTIGKPL---IHiqalIL 851
Cdd:cd05929   235 EAVRNaydlssLKRVIHAAAPCPPWVKEQWIDwgGPIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAVlgkVH----IL 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  852 DTAGQLCPVGVPGELCLAGlGLARGYLNQPQMTA-SRFEHitlndvnnagqGAATLriyrtGDKARLLNNGDYEYCGRID 930
Cdd:cd05929   311 DEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAaARNEG-----------GWSTL-----GDVGYLDEDGYLYLTDRRS 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  931 EQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVI---VAQVGSRP-ALVayATVKADSSTPEPAAVLIDVAK-YLPEYMVPF 1005
Cdd:cd05929   374 DMIISGGVNIYPQEIENALIA-HPKVLDAAVVgvpDEELGQRVhAVV--QPAPGADAGTALAEELIAFLRdRLSRYKCPR 450

                         490       500
                  ....*....|....*....|.
gi 499404635 1006 RLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05929   451 SIEFVAELPRDDTGKLYRRLL 471
PRK05857 PRK05857
fatty acid--CoA ligase;
533-1021 8.86e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 76.59  E-value: 8.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQqlAIAFDGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK05857   15 TVLDRVFEQARQQPE--AIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPLDPDYPP---ERLRHIITDANLSVILGG--DGQQLAQWSAE---QRIDLTDPAvVEQWQDLPGDQPPAIPRH-AQQL 683
Cdd:PRK05857   93 AVMADGNLPIaaiERFCQITDPAAALVAPGSkmASSAVPEALHSipvIAVDIAAVT-RESEHSLDAASLAGNADQgSEDP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  684 AQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDR----IDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRA 759
Cdd:PRK05857  172 LAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnwVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTS 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  760 IMQA--EQAGATHLILPTaLMSILDPE------QVNGIQAIGMGGEACPNAVVENW-ADKVALYNMYGPTECTVTAL--- 827
Cdd:PRK05857  252 LLEIltTNAVATTCLVPT-LLSKLVSElksanaTVPSLRLVGYGGSRAIAADVRFIeATGVRTAQVYGLSETGCTALclp 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  828 --STRLRKGQPVTIGKPLIHIQALILDT--AGQLCPVGVP----GELCLAGLGLARGYLNQPQMTAsrfEHITLNDVNna 899
Cdd:PRK05857  331 tdDGSIVKIEAGAVGRPYPGVDVYLAATdgIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTA---EVLIDGWVN-- 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  900 gqgaatlriyrTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEaQLAAVCPSLKQ---IKVIVAQVGSRPALVAYA 976
Cdd:PRK05857  406 -----------TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGVSGVREaacYEIPDEEFGALVGLAVVA 473

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635  977 TVKADSSTPEPAAVLIdVAKYL--PEYMV-PFRLMLLEDMPLTPNGKL 1021
Cdd:PRK05857  474 SAELDESAARALKHTI-AARFRreSEPMArPSTIVIVTDIPRTQSGKV 520
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 533-1026 8.86e-14

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 76.64  E-value: 8.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAF-DGEPRTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGA 611
Cdd:PRK08008    8 HLRQMWDDLADVYGHKTALIFeSSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  612 AYVPLDPDYPPERLRHII--TDANLSVI---LGGDGQQLAQWSAEQR-----IDLTDPAV--VEQWQDLPGDQPP----A 675
Cdd:PRK08008   88 IMVPINARLLREESAWILqnSQASLLVTsaqFYPMYRQIQQEDATPLrhiclTRVALPADdgVSSFTQLKAQQPAtlcyA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  676 IPRHAQQLAQVIYTSGSTGLPKGVMIEHGSL----------INLLDDhrDRIdftpQSTM------FNCmslsfdagnmT 739
Cdd:PRK08008  168 PPLSTDDTAEILFTSGTTSRPKGVVITHYNLrfagyysawqCALRDD--DVY----LTVMpafhidCQC----------T 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  740 TLLP-LSSGGTLAFGEP-NDRAI---MQAEQAGATH---LILPTaLMsiLDPEQVNGIQAigmggeaCPNAVV--ENWAD 809
Cdd:PRK08008  232 AAMAaFSAGATFVLLEKySARAFwgqVCKYRATITEcipMMIRT-LM--VQPPSANDRQH-------CLREVMfyLNLSD 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  810 ----------KVALYNMYGPTECTVTALSTRlrKGQP---VTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGL---GL 873
Cdd:PRK08008  302 qekdafeerfGVRLLTSYGMTETIVGIIGDR--PGDKrrwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTI 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  874 ARGYLNQPQMTASRFEhitlndvnnaGQGAatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvC 953
Cdd:PRK08008  380 FKEYYLDPKATAKVLE----------ADGW-----LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIAT-H 443

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499404635  954 PSLKQIKVI-VAQVGSRPALVAYaTVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK08008  444 PKIQDIVVVgIKDSIRDEAIKAF-VVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 551-1026 1.68e-13

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 75.79  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  551 IAFDGEPRTDTLTYAELNRQANQLAHWLHRQGLGE-QSLVGVLAKRDRYFVIALlAIWKAGAAYVPLDPDYPPERLRHII 629
Cdd:PLN02330   45 VAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKgQVVVVVLPNVAEYGIVAL-GIMAAGGVFSGANPTALESEIKKQA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  630 TDANLSVILGGDgqqlAQWSAEQRIDLtdPAVV---------EQWQDL------PGDQPPAIPRHAQQLAQVIYTSGSTG 694
Cdd:PLN02330  124 EAAGAKLIVTND----TNYGKVKGLGL--PVIVlgeekiegaVNWKELleaadrAGDTSDNEEILQTDLCALPFSSGTTG 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  695 LPKGVMIEHGSLI-NLLddhrdridftpqSTMFNCMSLSFdaGNMTTL--LPL---------------SSGGTLAFGEPN 756
Cdd:PLN02330  198 ISKGVMLTHRNLVaNLC------------SSLFSVGPEMI--GQVVTLglIPFfhiygitgiccatlrNKGKVVVMSRFE 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  757 DRAIMQA---EQAGATHLILPTALMSILDP--EQVN----GIQAIGMGgeACPNA-----VVENWADKVALYNMYGPTEC 822
Cdd:PLN02330  264 LRTFLNAlitQEVSFAPIVPPIILNLVKNPivEEFDlsklKLQAIMTA--AAPLApelltAFEAKFPGVQVQEAYGLTEH 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  823 TVTALS-TRLRKGQPV----TIGKPLIHIQALILD-TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHitlndv 896
Cdd:PLN02330  342 SCITLThGDPEKGHGIakknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDE------ 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  897 nnagQGAatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIV---AQVGSRPALV 973
Cdd:PLN02330  416 ----DGW-----LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLT-HPSVEDAAVVPlpdEEAGEIPAAC 485

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499404635  974 AYATVKADSSTPEPAA-VLIDVAKYLPEYMVPFrlmlLEDMPLTPNGKLdMKQL 1026
Cdd:PLN02330  486 VVINPKAKESEEDILNfVAANVAHYKKVRVVQF----VDSIPKSLSGKI-MRRL 534
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 821-1114 2.03e-13

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 73.25  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  821 ECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGElclaGLGLARGYLNQPQMTASRFEHITLNDVNNAG 900
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGG----EGGLLGAGLLLRIRLLAAAARAPFIPVPYPA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  901 QGAATLRiyrtgDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIVAQVGSRPALVAYATVKA 980
Cdd:COG3433    77 QPGRQAD-----DLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  981 DSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEANESDGEAD------NPLEADVLAIWRSV 1054
Cdd:COG3433   152 ALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPapaletALTEEELRADVAEL 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499404635 1055 LNTP---LGVEDDFFRLGGDSILSIQLTTRLRSAGYACTVKDVFEAKSVRRLCRVLAQNNRDT 1114
Cdd:COG3433   232 LGVDpeeIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
536-1026 2.18e-13

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 75.48  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWLhRQGLGeqslvgvLAKRDRY---------FVIALLAI 606
Cdd:PRK08974   27 DMFEQAVARYADQPAFINMGE----VMTFRKLEERSRAFAAYL-QNGLG-------LKKGDRValmmpnllqYPIALFGI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  607 WKAGAAYVPLDPDYPPERLRHIITDA---------NL--------------SVILGGDGQQLaqwSAEQRIdLTDPAV-- 661
Cdd:PRK08974   95 LRAGMIVVNVNPLYTPRELEHQLNDSgakaivivsNFahtlekvvfktpvkHVILTRMGDQL---STAKGT-LVNFVVky 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  662 ----VEQWqDLPGdqppAIP--------RHAQ---------QLAQVIYTSGSTGLPKGVMIEHGSLI-NLLD-------- 711
Cdd:PRK08974  171 ikrlVPKY-HLPD----AISfrsalhkgRRMQyvkpelvpeDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQakaaygpl 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  712 -DHRDRIDFTPQStMFNCMSLSfdagnMTTLLPLSSGGT-LAFGEPNDRAIMQAEQA--------GATHLIlpTALMSIL 781
Cdd:PRK08974  246 lHPGKELVVTALP-LYHIFALT-----VNCLLFIELGGQnLLITNPRDIPGFVKELKkypftaitGVNTLF--NALLNNE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  782 DPEQVNGIQ---AIGmGGEACPNAVVENWAD--KVALYNMYGPTECT--VTALSTRLrKGQPVTIGKPLIHIQALILDTA 854
Cdd:PRK08974  318 EFQELDFSSlklSVG-GGMAVQQAVAERWVKltGQYLLEGYGLTECSplVSVNPYDL-DYYSGSIGLPVPSTEIKLVDDD 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  855 GQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfehitlnDVNNAGQGAatlriyrTGDKARLLNNGDYEYCGRIDEQIK 934
Cdd:PRK08974  396 GNEVPPGEPGELWVKGPQVMLGYWQRPEATD---------EVIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMIL 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  935 LRGYRIEPGEIEAQLAAvcpslkQIKVI-VAQVG----SRPALVAYATVKADSS-TPEpaAVLIDVAKYLPEYMVPFRLM 1008
Cdd:PRK08974  460 VSGFNVYPNEIEDVVML------HPKVLeVAAVGvpseVSGEAVKIFVVKKDPSlTEE--ELITHCRRHLTGYKVPKLVE 531

                         570
                  ....*....|....*...
gi 499404635 1009 LLEDMPLTPNGKLDMKQL 1026
Cdd:PRK08974  532 FRDELPKSNVGKILRREL 549
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
532-1026 2.97e-13

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 75.03  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAvaQRDPQQLAIaFDGEPRtdtLTYAELNRQANQLAHWLHRQGL--GEQSLV--GVLAKrdryFVIALLAIW 607
Cdd:PRK10946   25 LPLTDILTR--HAASDAIAV-ICGERQ---FSYRELNQASDNLACSLRRQGIkpGDTALVqlGNVAE----FYITFFALL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  608 KAGAAyvPLDPDYPPERL-----------RHIITDANLSviLGGDGQQLAQWSAEQR-----IDLTDPA--VVEQWQDLP 669
Cdd:PRK10946   95 KLGVA--PVNALFSHQRSelnayasqiepALLIADRQHA--LFSDDDFLNTLVAEHSslrvvLLLNDDGehSLDDAINHP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  670 GDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHgslinllDDHRDRI-------DFTPQsTMFNC-------MSLS--- 732
Cdd:PRK10946  171 AEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTH-------NDYYYSVrrsveicGFTPQ-TRYLCalpaahnYPMSspg 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  733 ----FDAGNMTTLLPlSSGGTLAFgepndrAIMQAEQAGATHLILPTA---LMSILDP---EQVNGIQAIGMGGEACPNA 802
Cdd:PRK10946  243 algvFLAGGTVVLAP-DPSATLCF------PLIEKHQVNVTALVPPAVslwLQAIAEGgsrAQLASLKLLQVGGARLSET 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  803 VvenwADKVA------LYNMYGPTECTVTalSTRLRKGQPVTI---GKPLIHIQAL-ILDTAGQLCPVGVPGELCLAGLG 872
Cdd:PRK10946  316 L----ARRIPaelgcqLQQVFGMAEGLVN--YTRLDDSDERIFttqGRPMSPDDEVwVADADGNPLPQGEVGRLMTRGPY 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  873 LARGYLNQPQMTASRFehitlnDVNNagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLaav 952
Cdd:PRK10946  390 TFRGYYKSPQHNASAF------DANG---------FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLL--- 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  953 cpsLKQIKVIVAqvgsrpALV------------AYATVKadssTPEPAAVLidvAKYL-----PEYMVPFRLMLLEDMPL 1015
Cdd:PRK10946  452 ---LRHPAVIHA------ALVsmedelmgekscAFLVVK----EPLKAVQL---RRFLreqgiAEFKLPDRVECVDSLPL 515

                         570
                  ....*....|.
gi 499404635 1016 TPNGKLDMKQL 1026
Cdd:PRK10946  516 TAVGKVDKKQL 526
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 524-1026 4.69e-13

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 74.41  E-value: 4.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  524 PRSYPqpqlTVTDVIEAVAQRDPQQLAIAFDGEprtdTLTYAELNRQANQLAHWL-HRQGLGEQSLVGVLAKRDRYFVIA 602
Cdd:PRK05677   20 PDEYP----NIQAVLKQSCQRFADKPAFSNLGK----TLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  603 LLAIWKAGAAYVPLDPDYPPERLRHIITD--ANLSVILGGDGQQLAQWSAEQRI---------DLTDP-------AVVEQ 664
Cdd:PRK05677   92 VFGAMRAGLIVVNTNPLYTAREMEHQFNDsgAKALVCLANMAHLAEKVLPKTGVkhvivtevaDMLPPlkrllinAVVKH 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  665 WQ------DLPG------------DQP--PAIPrHAQQLAQVIYTSGSTGLPKGVMIEHGSLI-----------NLLDDH 713
Cdd:PRK05677  172 VKkmvpayHLPQavkfndalakgaGQPvtEANP-QADDVAVLQYTGGTTGVAKGAMLTHRNLVanmlqcralmgSNLNEG 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  714 RDRIdFTP------QSTMFNCMSLsFDAGNMTTLLPlssggtlafgEPNDRAIMQAE---QAGATHLILPTALMSILDPE 784
Cdd:PRK05677  251 CEIL-IAPlplyhiYAFTFHCMAM-MLIGNHNILIS----------NPRDLPAMVKElgkWKFSGFVGLNTLFVALCNNE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  785 QV-----NGIQAIGMGGEACPNAVVENWAD--KVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQL 857
Cdd:PRK05677  319 AFrkldfSALKLTLSGGMALQLATAERWKEvtGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNE 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  858 CPVGVPGELCLAGLGLARGYLNQPQMTASrfehiTLNDvnnagQGaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRG 937
Cdd:PRK05677  399 LPLGEVGELCVKGPQVMKGYWQRPEATDE-----ILDS-----DG-----WLKTGDIALIQEDGYMRIVDRKKDMILVSG 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  938 YRIEPGEIEAQLAAVcPSLKQIKVI-VAQVGSRPALVAYATVKADSSTPEpAAVLIDVAKYLPEYMVPFRLMLLEDMPLT 1016
Cdd:PRK05677  464 FNVYPNELEDVLAAL-PGVLQCAAIgVPDEKSGEAIKVFVVVKPGETLTK-EQVMEHMRANLTGYKVPKAVEFRDELPTT 541

                         570
                  ....*....|
gi 499404635 1017 PNGKLDMKQL 1026
Cdd:PRK05677  542 NVGKILRREL 551
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 524-706 5.57e-13

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 74.14  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  524 PRSYPQpqlTVTDVIEAVAQRDPQQLAIA---FDGEPRTdtLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRD-RYF 599
Cdd:PRK08180   34 LGDYPR---RLTDRLVHWAQEAPDRVFLAergADGGWRR--LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSiEHA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  600 VIALLAIWkAGAAYVPLDPDY-----PPERLRHIITDANLSVILGGDGQQLAqwSAEQRIDLTDPAVVEQ---------- 664
Cdd:PRK08180  109 LLALAAMY-AGVPYAPVSPAYslvsqDFGKLRHVLELLTPGLVFADDGAAFA--RALAAVVPADVEVVAVrgavpgraat 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 499404635  665 -WQDLPGDQPPAI--PRHAQ----QLAQVIYTSGSTGLPKGVMIEHGSL 706
Cdd:PRK08180  186 pFAALLATPPTAAvdAAHAAvgpdTIAKFLFTSGSTGLPKAVINTHRML 234
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 536-1020 1.51e-12

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 72.60  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  536 DVIEAvAQRDPQQLAIAFDGeprTDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVP 615
Cdd:PRK07514    7 DALRA-AFADRDAPFIETPD---GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  616 LDPDYPPERLRHIITDANLSVILGGDGQQ-----LAQWSAEQRIDLTDPAVVEQWQDLPGDQPPA---IPRHAQQLAQVI 687
Cdd:PRK07514   83 LNTAYTLAELDYFIGDAEPALVVCDPANFawlskIAAAAGAPHVETLDADGTGSLLEAAAAAPDDfetVPRGADDLAAIL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  688 YTSGSTGLPKGVMIEHGsliNLLDDH---RDRIDFTPQSTM------FNCMSLsFDAGNmTTLLplsSGGTLAFGEPNDR 758
Cdd:PRK07514  163 YTSGTTGRSKGAMLSHG---NLLSNAltlVDYWRFTPDDVLihalpiFHTHGL-FVATN-VALL---AGASMIFLPKFDP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  759 AIMQAEQAGATHLI-LPTALMSILDPEQVNGIQAIGM----GGEA--CPNAVVEnWADKV--ALYNMYGPTEctvTALST 829
Cdd:PRK07514  235 DAVLALMPRATVMMgVPTFYTRLLQEPRLTREAAAHMrlfiSGSAplLAETHRE-FQERTghAILERYGMTE---TNMNT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  830 -------RLrkgqPVTIGKPLIHIQALILD-TAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndvNNAGq 901
Cdd:PRK07514  311 snpydgeRR----AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF--------RADG- 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  902 gaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI-VAQVGSRPALVAyATVKA 980
Cdd:PRK07514  378 ------FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDEL-PGVVESAVIgVPHPDFGEGVTA-VVVPK 449

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 499404635  981 DSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGK 1020
Cdd:PRK07514  450 PGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 686-1026 2.28e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 72.11  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 VIYTSGSTGLPKGVMIEHGSL-INLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLL-PLSSGGT-----LAFGEPNdr 758
Cdd:cd05928   179 IYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFePWIQGACvfvhhLPRFDPL-- 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  759 AIMQA-EQAGATHLI-LPTALMSILDPE----QVNGIQAIGMGGEACPNAVVENWADKVAL--YNMYGPTECTVTALSTR 830
Cdd:cd05928   257 VILKTlSSYPITTFCgAPTVYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKAQTGLdiYEGYGQTETGLICANFK 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  831 LRKGQPVTIGKPLIHIQALILDTAGQLCPVGVPGELCL-----AGLGLARGYLNQPQMTAsrfehitlndvnnagqgaAT 905
Cdd:cd05928   337 GMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTA------------------AT 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  906 LR--IYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLA---AVCPSlkqikvivAQVGS----RPALV-AY 975
Cdd:cd05928   399 IRgdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIehpAVVES--------AVVSSpdpiRGEVVkAF 470

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  976 ATVKADSSTPEPAAVLID----VAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:cd05928   471 VVLAPQFLSHDPEQLTKElqqhVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 529-923 3.48e-12

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 71.68  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  529 QPQLTVTDVIEAVAQRDPQQLAIAF-------DGEPRTdtLTYAELNRQANQLAHWLhrQGLGEQ-SLVGVLAKRDRYFV 600
Cdd:PRK07769   18 PPNTNLVRHVERWAKVRGDKLAYRFldfsterDGVARD--LTWSQFGARNRAVGARL--QQVTKPgDRVAILAPQNLDYL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  601 IALLAIWKAGAAYVPL-DPDYP--PERLRHIITDANLSVILGGDG------QQLAQWSAEQR-----IDLTDPAVVEQWQ 666
Cdd:PRK07769   94 IAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDsaegvrKFFRARPAKERprviaVDAVPDEVGATWV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  667 dlpgdqPPAIprHAQQLAQVIYTSGSTGLPKGVMIEHGSL-------INLLD-DHRDR-IDFTPqstMFNCMSLsfdagn 737
Cdd:PRK07769  174 ------PPEA--NEDTIAYLQYTSGSTRIPAGVQITHLNLptnvlqvIDALEgQEGDRgVSWLP---FFHDMGL------ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  738 MTTLLPLSSGGTLAFGEPN------DRAI--MQAEQAGATHLI---------------LPTALMSILDPEQVNGIQAigm 794
Cdd:PRK07769  237 ITVLLPALLGHYITFMSPAafvrrpGRWIreLARKPGGTGGTFsaapnfafehaaargLPKDGEPPLDLSNVKGLLN--- 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 GGEACPNAVVENWADKVALYNM--------YGPTECTVTALSTR--------------LRKGQPVTI------------- 839
Cdd:PRK07769  314 GSEPVSPASMRKFNEAFAPYGLpptaikpsYGMAEATLFVSTTPmdeeptviyvdrdeLNAGRFVEVpadapnavaqvsa 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  840 GKPLIHIQALILD--TAGQLcPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITLNDVNNA-GQGAAtlriyrtgDKAR 916
Cdd:PRK07769  394 GKVGVSEWAVIVDpeTASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSRLSEShAEGAP--------DDAL 464


                  ....*..
gi 499404635  917 LLNNGDY 923
Cdd:PRK07769  465 WVRTGDY 471
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
672-1022 3.71e-12

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 71.92  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  672 QPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGsliNLLDDHRD---RIDFTPQSTMFNCMSL--SF--DAGnmtTLLPL 744
Cdd:PRK06814  784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHR---NLLANRAQvaaRIDFSPEDKVFNALPVfhSFglTGG---LVLPL 857

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  745 SSG-GTLAFGEP-NDRAIMQ-AEQAGATHLI-LPTALMS---ILDPEQVNGIQAIGMGGEACPNAVVENWADK--VALYN 815
Cdd:PRK06814  858 LSGvKVFLYPSPlHYRIIPElIYDTNATILFgTDTFLNGyarYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgIRILE 937

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  816 MYGPTECT-VTALSTRLRKgQPVTIGKPLIHIQAlildtagQLCPV-GVP--GELCLAGLGLARGYLnqpqmtasrfehi 891
Cdd:PRK06814  938 GYGVTETApVIALNTPMHN-KAGTVGRLLPGIEY-------RLEPVpGIDegGRLFVRGPNVMLGYL------------- 996

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  892 tlnDVNNAGqgaaTLRI-----YRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIKVIV--A 964
Cdd:PRK06814  997 ---RAENPG----VLEPpadgwYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIpdA 1069

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  965 QVGSRPALVayaTVKADSStpepAAVLIDVAKY--LPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:PRK06814 1070 RKGERIILL---TTASDAT----RAAFLAHAKAagASELMVPAEIITIDEIPLLGTGKID 1122
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
560-1046 3.71e-12

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 71.60  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  560 DTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDP-----DYP-PERlrhiITDAN 633
Cdd:PRK06060   29 DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPelhrdDHAlAAR----NTEPA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  634 LSVILGGDGQQLAQWSAEQRIDL-TDPAVVEqwqdlPGDQPPAiprHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDD 712
Cdd:PRK06060  105 LVVTSDALRDRFQPSRVAEAAELmSEAARVA-----PGGYEPM---GGDALAYATYTSGTTGPPKAAIHRHADPLTFVDA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  713 H-RDRIDFTPQSTMFNC--MSLSFDAGNmTTLLPLSSGGTLAFGE----PNDRAIMQAEQAGATHLILPTALMSILD--- 782
Cdd:PRK06060  177 McRKALRLTPEDTGLCSarMYFAYGLGN-SVWFPLATGGSAVINSapvtPEAAAILSARFGPSVLYGVPNFFARVIDscs 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  783 PEQVNGIQAIGMGGEACPNAVVENWAD---KVALYNMYGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCP 859
Cdd:PRK06060  256 PDSFRSLRCVVSAGEALELGLAERLMEffgGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAG 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  860 VGVPGELCLAGLGLARGYLNQPQMTasrfehitlndVNNAGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYR 939
Cdd:PRK06060  336 PGVEGDLWVRGPAIAKGYWNRPDSP-----------VANEGW-------LDTRDRVCIDSDGWVTYRCRADDTEVIGGVN 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  940 IEPGEIEaQLAAVCPSLKQIKVI-VAQVGSRPALVAYATVKADSSTPEpaAVLIDVAK----YLPEYMVPFRLMLLEDMP 1014
Cdd:PRK06060  398 VDPREVE-RLIIEDEAVAEAAVVaVRESTGASTLQAFLVATSGATIDG--SVMRDLHRgllnRLSAFKVPHRFAVVDRLP 474

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 499404635 1015 LTPNGKLDMK----QLP--PVLEANESDGEADNPLEAD 1046
Cdd:PRK06060  475 RTPNGKLVRGalrkQSPtkPIWELSLTEPGSGVRAQRD 512
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 533-950 6.89e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 70.48  E-value: 6.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDpqQLAIAFDGEprtdTLTYAELNRQANQLAHWLH-RQGLGEQSLVGVLAKRDRYFVIALLAIWKAGA 611
Cdd:PRK07867    6 TVAELLLPLAEDD--DRGLYFEDS----FTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  612 AYVPLDPDYPPERLRHIITDANLSVILGGDGQQ--LAQWSAEQRIDLTDPAvveQWQDL----PGDQPPAIPRHAQQLAQ 685
Cdd:PRK07867   80 VPVGLNPTRRGAALARDIAHADCQLVLTESAHAelLDGLDPGVRVINVDSP---AWADElaahRDAEPPFRVADPDDLFM 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 VIYTSGSTGLPKGVMIEHGSLI---NLLDDHRdriDFTPQSTMFNCMSLSFDAGNMTTLLP-LSSGGTLAFgepndRAIM 761
Cdd:PRK07867  157 LIFTSGTSGDPKAVRCTHRKVAsagVMLAQRF---GLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIAL-----RRKF 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  762 QAEQ-------AGATHL---------ILPTALMsildPEQVNGIQAIGMGGEACPNAvVENWADK--VALYNMYGPTECT 823
Cdd:PRK07867  229 SASGflpdvrrYGATYAnyvgkplsyVLATPER----PDDADNPLRIVYGNEGAPGD-IARFARRfgCVVVDGFGSTEGG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  824 VTAlsTRLRKGQPVTIGKPLIHIQALILDTaGQLCPVGVP------------GELC-LAGLGLARGYLNQPQMTASRFEH 890
Cdd:PRK07867  304 VAI--TRTPDTPPGALGPLPPGVAIVDPDT-GTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRG 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  891 itlndvnnagqgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLA 950
Cdd:PRK07867  381 ----------------GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL 424
PRK05691 PRK05691
peptide synthase; Validated
 68-496 7.68e-12

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 71.35  E-value: 7.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   68 NATSGPLSSsQSGL-----WFIEQYEEQSHLYNMPVYFRLTGPLDVAALEFAFDALAQRHASLRTRFV-VNEQGKGEQRI 141
Cdd:PRK05691 2782 QAEQGPLQG-ASGLtpiqhWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSqADGRWQAEYRA 2860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  142 DAYQPFVIQHDDFSLlpeAERegrlqQQVKAEISRPFDLTAGDLTRVRLVKMSERTHVLMITQHHIISDGWSVKNLFADF 221
Cdd:PRK05691 2861 VTAQELLWQVTVADF---AEC-----AALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDL 2932

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  222 KPAF--LACQNCQPYPVETTQLNyiDYAHWFNSDSFLDYHNEFKPFWVERLTGIPevHSLPLDKPRPAHQNSGGEVIfsA 299
Cdd:PRK05691 2933 QALYrqLSAGAEPALPAKTSAFR--DWAARLQAYAGSESLREELGWWQAQLGGPR--AELPCDRPQGGNLNRHAQTV--S 3006

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  300 INNDLwDKFKRLCQR----YNTSNFIGLHAVFSLMLARISGEKDIVIGSPLAYRERP----DIEDVVGFFVNTIVLRTQ- 370
Cdd:PRK05691 3007 VRLDA-ERTRQLLQQapaaYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALfddiDLTRSVGWFTSAYPLRLTp 3085

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  371 -LQDSQNFVDYLQYCREQdLSAFDHQLYRFEALSE-AIGSDRTT-AINPIFQVMLVYQAKVD--------FNDLIPGCDA 439
Cdd:PRK05691 3086 aPGDDAARGESIKAIKEQ-LRAVPHKGLGYGVLRYlADAAVREAmAALPQAPITFNYLGQFDqsfasdalFRPLDEPAGP 3164

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 499404635  440 AEETSPVLPakTDISVKVTELMGEVRLDWLFATALFERQTIQYYADRFIRLIEAVVE 496
Cdd:PRK05691 3165 AHDPDAPLP--NELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIA 3219
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 546-951 8.49e-12

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: 70.42  E-value: 8.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  546 PQQLAIAFDG--EPRTDTLTYAELNRQANQLAHWLHRQGLgeqslvgvlAKRDR---YF------VIALLAIWKAGAAYV 614
Cdd:cd05967    65 GDQIALIYDSpvTGTERTYTYAELLDEVSRLAGVLRKLGV---------VKGDRviiYMpmipeaAIAMLACARIGAIHS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  615 PLDPDYPPERLRHIITDANLSVILGGD-----GQ------------QLAQWSAE-----QR----IDLTDPAVVEQWQDL 668
Cdd:cd05967   136 VVFGGFAAKELASRIDDAKPKLIVTAScgiepGKvvpykplldkalELSGHKPHhvlvlNRpqvpADLTKPGRDLDWSEL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  669 PGDQPPA--IPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSlsfDAG-----NMTTL 741
Cdd:cd05967   216 LAKAEPVdcVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAAS---DVGwvvghSYIVY 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  742 LPLSSGGTLAF--GEPND--------RAImqaEQAGATHLI-LPTALMSI--LDPE-------QVNGIQAIGMGGEACPN 801
Cdd:cd05967   293 GPLLHGATTVLyeGKPVGtpdpgafwRVI---EKYQVNALFtAPTAIRAIrkEDPDgkyikkyDLSSLRTLFLAGERLDP 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  802 AVVEnWADK---VALYNMYGPTE------CTVTALSTR-LRKGQPvtiGKPLIHIQALILDTAGQLCPVGVPGELCLaGL 871
Cdd:cd05967   370 PTLE-WAENtlgVPVIDHWWQTEtgwpitANPVGLEPLpIKAGSP---GKPVPGYQVQVLDEDGEPVGPNELGNIVI-KL 444

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  872 GLARGYLNQPQMTASRFEHITLNDVNNagqgaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAA 951
Cdd:cd05967   445 PLPPGCLLTLWKNDERFKKLYLSKFPG---------YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLS 515
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1566-1985 1.05e-11

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: 69.60  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSMLY-HRLRCPQDdAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIV--KQADLPF 1641
Cdd:cd19538     2 IPLSFAQRRLWFlHQLEGPSA-TYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFpEEDGVPYQLILeeDEATPKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1642 YyqdlMQDADPLAVIERYRQQdLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQTLMQG 1721
Cdd:cd19538    81 E----IKEVDEEELESEINEA-VRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 QvlMHGDAP-AIQvdraYVDYA-------RHAVAQQSAVD---AFW-QQRQSLLAQTN---DVsmlfaaagKRADLSQHl 1786
Cdd:cd19538   156 E--APELAPlPVQ----YADYAlwqqellGDESDPDSLIArqlAYWkKQLAGLPDEIElptDY--------PRPAESSY- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1787 tqiEPQVTSVSLNEKDQATLTAFAREVGITPSIIAQYAWHRLLARsTGDAVSIV-GNVLSGRESpvEDVASSVGLYINSL 1865
Cdd:cd19538   221 ---EGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTR-LGAGTDIPiGSPVAGRND--DSLEDLVGFFVNTL 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1866 PLALSWQQPVSLQQHL--VQLQNeLMAM-NQHATQSLI--ALTAGRSR----LFNSLFIYENYPDAKAEQGQRADDPhRL 1936
Cdd:cd19538   295 VLRTDTSGNPSFRELLerVKETN-LEAYeHQDIPFERLveALNPTRSRsrhpLFQIMLALQNTPQPSLDLPGLEAKL-EL 372

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 499404635 1937 YPEFSAAYEkvempLNLVVREQSGC-----MLLRFEFDADALDSAQARRVLMRW 1985
Cdd:cd19538   373 RTVGSAKFD-----LTFELREQYNDgtpngIEGFIEYRTDLFDHETIEALAQRY 421
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1566-1867 1.08e-11

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: 69.37  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1566 LPLSSLQQSM-LYHRLRcPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIV--KQADLPF 1641
Cdd:cd19540     2 IPLSFAQQRLwFLNRLD-GPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFpEDDGGPYQVVLpaAEARPDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1642 YYQDLMQDADPLAVIERyrqqdLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLgavhRDyqtlmqg 1721
Cdd:cd19540    81 TVVDVTEDELAARLAEA-----ARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLA----RD------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1722 qvLM-------HGDAP-----AIQvdraYVDYA--RHAV-----------AQQSavdAFWQQRqslLAQTNDVSML---- 1772
Cdd:cd19540   145 --LAtayaarrAGRAPdwaplPVQ----YADYAlwQRELlgdeddpdslaARQL---AYWRET---LAGLPEELELptdr 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1773 --FAAAGKRADlsQHLTQIEPQVTsvslnekdqATLTAFAREVGITPSIIAQYAWHRLLAR-STGDAVSIvGNVLSGR-E 1848
Cdd:cd19540   213 prPAVASYRGG--TVEFTIDAELH---------ARLAALAREHGATLFMVLHAALAVLLSRlGAGDDIPI-GTPVAGRgD 280

                         330
                  ....*....|....*....
gi 499404635 1849 SPVEDVassVGLYINSLPL 1867
Cdd:cd19540   281 EALDDL---VGMFVNTLVL 296
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 542-1021 1.36e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 69.27  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  542 AQRDPQQLAI--AFDGEprtdTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPD 619
Cdd:PRK13390    7 AQIAPDRPAVivAETGE----QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  620 YPPERLRHIITDANLSVILGG---DGQqLAQWSAEQRIDLTDPAVVEQWQDLPGDQPPAIPRHAQQL--AQVIYTSGSTG 694
Cdd:PRK13390   83 LTAPEADYIVGDSGARVLVASaalDGL-AAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLTEQPcgAVMLYSSGTTG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  695 LPKGVMIE-HGSLINLLDD-----HRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLAFGEPNDRAI----MQAE 764
Cdd:PRK13390  162 FPKGIQPDlPGRDVDAPGDpivaiARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQAtlghVERY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  765 QAGATHLIlPTALMSI--LDPE-----QVNGIQAIGMGGEACPNAVVENWADKVA--LYNMYGPTEC-TVTALSTRLRKG 834
Cdd:PRK13390  242 RITVTQMV-PTMFVRLlkLDADvrtryDVSSLRAVIHAAAPCPVDVKHAMIDWLGpiVYEYYSSTEAhGMTFIDSPDWLA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  835 QPVTIGKPL---IHiqalILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTAsrfehitlndvnnAGQGAATLRIYRT 911
Cdd:PRK13390  321 HPGSVGRSVlgdLH----ICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA-------------AAQHPAHPFWTTV 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  912 GDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLaAVCPSLKQIKVIVA---QVGSRPALVAYATVKADSSTpEPA 988
Cdd:PRK13390  384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENAL-TMHPAVHDVAVIGVpdpEMGEQVKAVIQLVEGIRGSD-ELA 461

                         490       500       510
                  ....*....|....*....|....*....|....
gi 499404635  989 AVLIDVAK-YLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:PRK13390  462 RELIDYTRsRIAHYKAPRSVEFVDELPRTPTGKL 495
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 533-888 8.74e-11

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 66.89  E-value: 8.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  533 TVTDVIEAVAQRDPQQLAIAF-----DGEPRTDTLTYAELNRQANQLAHWLHRQGL-GEQSLVgvLAKRDRYFVIALLAI 606
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTFidyeqDPAGVAETLTWSQLYRRTLNVAEELRRHGStGDRAVI--LAPQGLEYIVAFLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  607 WKAGAAYVPLDPDYP---PERLRHIITDANLSVIL--GGDGQQLAQWSAEQRIDlTDPAVVE-QWQDLPGDQPPAIPRH- 679
Cdd:PRK05850   80 LQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLttSAVVDDVTEYVAPQPGQ-SAPPVIEvDLLDLDSPRGSDARPRd 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  680 AQQLAQVIYTSGSTGLPKGVMIEHGSLI----NLLDD---HRDRIdFTPQSTMFNCMSLSFDAGNMTTL-LPLSSGGT-- 749
Cdd:PRK05850  159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIanfeQLMSDyfgDTGGV-PPPDTTVVSWLPFYHDMGLVLGVcAPILGGCPav 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  750 ----LAFGEPNDRAImqaeQAGATHLILPTAL----------------MSILDPEQVNGIQAigmGGEACPNAVVENWAD 809
Cdd:PRK05850  238 ltspVAFLQRPARWM----QLLASNPHAFSAApnfafelavrktsdddMAGLDLGGVLGIIS---GSERVHPATLKRFAD 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  810 KVALYNM--------YGPTECTVTALSTrlRKGQPVTI--------------------GKPLIHIQA------LILDT-A 854
Cdd:PRK05850  311 RFAPFNLretairpsYGLAEATVYVATR--EPGQPPESvrfdyeklsaghakrcetggGTPLVSYGSprsptvRIVDPdT 388

                         410       420       430
                  ....*....|....*....|....*....|....
gi 499404635  855 GQLCPVGVPGELCLAGLGLARGYLNQPQMTASRF 888
Cdd:PRK05850  389 CIECPAGTVGEIWVHGDNVAAGYWQKPEETERTF 422
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 534-1021 8.90e-11

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 67.07  E-value: 8.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  534 VTDVIEAVAQRdpqQLAIAFDGEPRTDTLTYAELNRQANQLAHWLHR-QGLGEQslVGVLAKRDRYFVIALLAIWKAGAA 612
Cdd:PRK12476   44 IANVGDTVAYR---YLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQvAGPGDR--VAILAPQGIDYVAGFFAAIKAGTI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  613 YVPL-DPDYP--PERLRHIITDANLSVILGgdgQQLAQWSAEQRID----LTDPAV--VEQWQDLPGDQPPAIPRHAQQL 683
Cdd:PRK12476  119 AVPLfAPELPghAERLDTALRDAEPTVVLT---TTAAAEAVEGFLRnlprLRRPRViaIDAIPDSAGESFVPVELDTDDV 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  684 AQVIYTSGSTGLPKGVMIEHGSL----------INLLDDHRDRIDFTPqstMFNCMSLS---FDA---GNMTTLLPlssg 747
Cdd:PRK12476  196 SHLQYTSGSTRPPVGVEITHRAVgtnlvqmilsIDLLDRNTHGVSWLP---LYHDMGLSmigFPAvygGHSTLMSP---- 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  748 gtLAFGEPNDRAImQAEQAGATHLILPTALMSILD--------PEQVNGIQ----AIGMGGEACPNAVVENWADKVALYN 815
Cdd:PRK12476  269 --TAFVRRPQRWI-KALSEGSRTGRVVTAAPNFAYewaaqrglPAEGDDIDlsnvVLIIGSEPVSIDAVTTFNKAFAPYG 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  816 M--------YGPTECT-------------VTAL---------STRLRKGQP-----VTIGKPLIHIQALILD-TAGQLCP 859
Cdd:PRK12476  346 LprtafkpsYGIAEATlfvatiapdaepsVVYLdreqlgagrAVRVAADAPnavahVSCGQVARSQWAVIVDpDTGAELP 425

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  860 VGVPGELCLAGLGLARGYLNQPQMTASRFE---HITLNDVNNAGQGAATLRIYRTGDKARLLnNGDYEYCGRIDEQIKLR 936
Cdd:PRK12476  426 DGEVGEIWLHGDNIGRGYWGRPEETERTFGaklQSRLAEGSHADGAADDGTWLRTGDLGVYL-DGELYITGRIADLIVID 504

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  937 GYRIEPGEIEAQLAAVCPSLKQIKV----IVAQVGSRPALVAYATVKADSSTPEPA--AVLIDVAKylpEYMVP---FRL 1007
Cdd:PRK12476  505 GRNHYPQDIEATVAEASPMVRRGYVtaftVPAEDNERLVIVAERAAGTSRADPAPAidAIRAAVSR---RHGLAvadVRL 581

                         570
                  ....*....|....
gi 499404635 1008 MLLEDMPLTPNGKL 1021
Cdd:PRK12476  582 VPAGAIPRTTSGKL 595
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 683-1024 1.17e-10

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: 65.21  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  683 LAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQST------MFNcmSLSFDAGNMTTLLplsSGGTLAFGEPN 756
Cdd:cd17638     2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRyliinpFFH--TFGYKAGIVACLL---TGATVVPVAVF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  757 D-RAIMQAEqagATHLIL-----PTALMSILD-PEQVNG----IQAIGMGGEACPNAVVENWADKVALYNM---YGPTEC 822
Cdd:cd17638    77 DvDAILEAI---ERERITvlpgpPTLFQSLLDhPGRKKFdlssLRAAVTGAATVPVELVRRMRSELGFETVltaYGLTEA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  823 TVTALStrlRKGQPVTigkplihiqaLILDTAGQLCP-----VGVPGELCLAGLGLARGYLNQPQMTASRfehitlndVN 897
Cdd:cd17638   154 GVATMC---RPGDDAE----------TVATTCGRACPgfevrIADDGEVLVRGYNVMQGYLDDPEATAEA--------ID 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  898 NAGQgaatlriYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI------VAQVGSrpA 971
Cdd:cd17638   213 ADGW-------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEH-PGVAQVAVIgvpderMGEVGK--A 282

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499404635  972 LVayatVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLdMK 1024
Cdd:cd17638   283 FV----VARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV-MK 330
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 561-1020 1.42e-10

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 65.92  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQ-GLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIItdaNLSvilg 639
Cdd:cd05937     5 TWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCL---KLS---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 gdgqqlaqwsaEQRIDLTDPAVVeqwqdlpgdqppaiprhaqqlAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDF 719
Cdd:cd05937    78 -----------GSRFVIVDPDDP---------------------AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNL 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  720 TPQSTMFNCMSLSFDAGNMTTLLP-LSSGGTLAFGE--PNDRAIMQAEQAGATHLI--------LPTALMSILDpeQVNG 788
Cdd:cd05937   126 KNGDRTYTCMPLYHGTAAFLGACNcLMSGGTLALSRkfSASQFWKDVRDSGATIIQyvgelcryLLSTPPSPYD--RDHK 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  789 IQAI---GMGGEacpnaVVENWADKVA---LYNMYGPTECTVTalSTRLRKGqPVTIGK-----PLIHI-----QALI-L 851
Cdd:cd05937   204 VRVAwgnGLRPD-----IWERFRERFNvpeIGEFYAATEGVFA--LTNHNVG-DFGAGAighhgLIRRWkfenqVVLVkM 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  852 DTAGQL------------CPVGVPGELCLA----GLGLARGYLNQPQMTASRFehitLNDVNNAGQGaatlrIYRTGDKA 915
Cdd:cd05937   276 DPETDDpirdpktgfcvrAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKL----VRDVFRKGDI-----YFRTGDLL 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  916 RLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVIVAQVGSRPALVAYATVK-ADSSTPEPAAVLIDV 994
Cdd:cd05937   347 RQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAH-PDIAEANVYGVKVPGHDGRAGCAAITlEESSAVPTEFTKSLL 425

                         490       500       510
                  ....*....|....*....|....*....|
gi 499404635  995 AKY----LPEYMVPFRLMLLEDMPLTPNGK 1020
Cdd:cd05937   426 ASLarknLPSYAVPLFLRLTEEVATTDNHK 455
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1133-1305 1.61e-10

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: 65.45  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1133 QR-WFMEQSLARPEHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLGCDAEG----QRYLADVPCPaLSTLDYRQLG 1206
Cdd:cd19531     9 QRlWFLDQLEPGSAAYNIPGALRLRgPLDVAALERALNELVARHEALRTTFVEVDgepvQVILPPLPLP-LPVVDLSGLP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1207 DDGLQQAFTALQSE-----FDPAQGRTMACALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERLYLGE------PLL 1275
Cdd:cd19531    88 EAEREAEAQRLAREearrpFDLARGPLLRATLLRLGED-EHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlagrpsPLP 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 499404635 1276 PKTSSY-------RQW--GAALQhyatqhaEQLTYWQAQ 1305
Cdd:cd19531   167 PLPIQYadyavwqREWlqGEVLE-------RQLAYWREQ 198
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 678-946 2.14e-10

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: 65.59  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  678 RHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTT-LLPLSSGG------TL 750
Cdd:cd05908   103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMnqylmpTR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  751 AFGEPNDRAIMQAEQAGATHLILPT----ALMSILDPEQVN-----GIQAIGMGGEACPNAVVENWADKVALYNM----- 816
Cdd:cd05908   183 LFIRRPILWLKKASEHKATIVSSPNfgykYFLKTLKPEKANdwdlsSIRMILNGAEPIDYELCHEFLDHMSKYGLkrnai 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  817 ---YGPTECTVTALSTRLRK--------------GQP--------------VTIGKPLIHIQALILDTAGQLCPVGVPGE 865
Cdd:cd05908   263 lpvYGLAEASVGASLPKAQSpfktitlgrrhvthGEPepevdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGH 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  866 LCLAGLGLARGYLNQPQMTASRFehitlndvnnAGQGAatlriYRTGDKArLLNNGDYEYCGRIDEQIKLRGYRIEPGEI 945
Cdd:cd05908   343 IQIRGKNVTPGYYNNPEATAKVF----------TDDGW-----LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDI 406


                  .
gi 499404635  946 E 946
Cdd:cd05908   407 E 407
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 562-761 2.62e-10

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: 65.31  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGL--GEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILG 639
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  640 GDGQQLaqWSAEQRIDLTDpavveqwqdlpGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLIN----LLDDHRD 715
Cdd:cd05927    86 DAGVKV--YSLEEFEKLGK-----------KNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILEI 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635  716 RIDFTPQSTMFNCMSLS--FDAgnMTTLLPLSSGGTLAFGEPNDRAIM 761
Cdd:cd05927   153 LNKINPTDVYISYLPLAhiFER--VVEALFLYHGAKIGFYSGDIRLLL 198
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1161-1471 3.68e-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: 64.39  E-value: 3.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1161 ERLVTMLQALMAQHDALRLGCDAEGQRYLADVPCPALStLDYRQLGDDGLQQAFTALQSEFDPAQGRT--------MACA 1232
Cdd:cd19536    39 DLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQ-VPVTELDLTPLEEQLDPLRAYKEETKIRRfdlgraplVRAA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1233 LVRHHPQADTALFLAFHHLVIDAVSWRILVDDLERLYLGEP-----LLPKTSSYRQWgAALQHYATQHAEQLTYWQAQED 1307
Cdd:cd19536   118 LVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLeykplSLPPAQPYRDF-VAHERASIQQAASERYWREYLA 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1308 GVDLTAL----LAAKDPQGHASAAILTLDAKTTGQlvsEANRAFNTDVSDLLLSALTRTLNDLGWGDKARIMLEGHGREA 1383
Cdd:cd19536   197 GATLATLpalsEAVGGGPEQDSELLVSVPLPVRSR---SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSE 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1384 idPTLDVSRTVGWFTSTYP--VCLQDKPdWASLIQSSKEQLRQVPDKGVGfnPLRYHHPQGNSLTLSPIVFNYLGLSVQA 1461
Cdd:cd19536   274 --ETTGAERLLGLFLNTLPlrVTLSEET-VEDLLKRAQEQELESLSHEQV--PLADIQRCSEGEPLFDSIVNFRHFDLDF 348

                         330
                  ....*....|
gi 499404635 1462 AGTWRPVDVA 1471
Cdd:cd19536   349 GLPEWGSDEG 358
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 561-987 4.03e-10

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: 65.07  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVILGG 640
Cdd:cd05933     8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 DGQQLAQWSAEQR--------IDLTDP-----AVVEQWQDLPgDQPPAIPRH----------AQQLAQVIYTSGSTGLPK 697
Cdd:cd05933    88 NQKQLQKILQIQDklphlkaiIQYKEPlkekePNLYSWDEFM-ELGRSIPDEqldaiissqkPNQCCTLIYTSGTTGMPK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  698 GVMIEHgslinllddhrDRIDFTP----QSTMFNC-----------MSLSFDAGNMTTL-LPLSSGGTLAFGEPN----D 757
Cdd:cd05933   167 GVMLSH-----------DNITWTAkaasQHMDLRPatvgqesvvsyLPLSHIAAQILDIwLPIKVGGQVYFAQPDalkgT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  758 RAIMQAEQAGATHLILPTALMSILDPEQVNGIQAIG--------------------MGGEAcPNAVVENWADK------- 810
Cdd:cd05933   236 LVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTlkrkiaswakgvgletnlklMGGES-PSPLFYRLAKKlvfkkvr 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  811 ------------------------------VALYNMYGPTECTvtalstrlrkgQPVTIGKPlihiQALILDTAGQLCPv 860
Cdd:cd05933   315 kalgldrcqkfftgaapisretlefflslnIPIMELYGMSETS-----------GPHTISNP----QAYRLLSCGKALP- 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  861 GVP-----------GELCLAGLGLARGYLNQPQMTASRF-EHITLndvnnagqgaatlriyRTGDKARLLNNGDYEYCGR 928
Cdd:cd05933   379 GCKtkihnpdadgiGEICFWGRHVFMGYLNMEDKTEEAIdEDGWL----------------HSGDLGKLDEDGFLYITGR 442

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499404635  929 IDEQIKLR-GYRIEPGEIEAQLAAVCPSLKQIKVIVAQvgsRPALVAYATVKA--DSSTPEP 987
Cdd:cd05933   443 IKELIITAgGENVPPVPIEDAVKKELPIISNAMLIGDK---RKFLSMLLTLKCevNPETGEP 501
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 589-1026 4.44e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 64.66  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  589 VGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERL----RH-----IITDANLSVILggDGQQLaqwSAEQRIDLTDP 659
Cdd:PRK13388   55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALaadiRRadcqlLVTDAEHRPLL--DGLDL---PGVRVLDVDTP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  660 AvveqWQDL---PGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAG 736
Cdd:PRK13388  130 A----YAELvaaAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNA 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  737 NMTTLLP-LSSGGTLAFgepndRAIMQA-------EQAGATHL-ILPTALMSIL-DPEQVNGIQ---AIGMGGEACPNAV 803
Cdd:PRK13388  206 VMAGWAPaVASGAAVAL-----PAKFSAsgflddvRRYGATYFnYVGKPLAYILaTPERPDDADnplRVAFGNEASPRDI 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  804 VEnWADK--VALYNMYGPTECTVTAlsTRLRKGQPVTIGKPLIHIQALILDTaGQLCPVGV-------------PGELC- 867
Cdd:PRK13388  281 AE-FSRRfgCQVEDGYGSSEGAVIV--VREPGTPPGSIGRGAPGVAIYNPET-LTECAVARfdahgallnadeaIGELVn 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  868 LAGLGLARGYLNQPQMTASRFEHitlndvnnagqgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEA 947
Cdd:PRK13388  357 TAGAGFFEGYYNNPEATAERMRH----------------GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  948 QLAavcpslKQIKVIVAQVGSRP-----ALVAYATVKADSSTPEPA--AVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGK 1020
Cdd:PRK13388  421 ILL------RHPAINRVAVYAVPdervgDQVMAALVLRDGATFDPDafAAFLAAQPDLGTKAWPRYVRIAADLPSTATNK 494


                  ....*.
gi 499404635 1021 LDMKQL 1026
Cdd:PRK13388  495 VLKREL 500
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 686-1024 8.99e-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: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 62.78  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 VIYTSGSTGLPKGVMIEHGSLINLLDDHRD--RIDFTPQ------------STMFNCMSLSFDAGNMTTLLPLSSGGTLA 751
Cdd:cd05924     8 ILYTGGTTGMPKGVMWRQEDIFRMLMGGADfgTGEFTPSedahkaaaaaagTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  752 FgePNDR-----AIMQAEQAGATHLILPTALMS--ILD------PEQVNGIQAIGMGG------------EACPNAVven 806
Cdd:cd05924    88 L--PDDRfdpeeVWRTIEKHKVTSMTIVGDAMArpLIDalrdagPYDLSSLFAISSGGallspevkqgllELVPNIT--- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  807 wadkvaLYNMYGPTEctVTALSTRLRKGQPVTIGkPLIHIQ--ALILDTAGQLCPVGVPGELCLAGLGL-ARGYLNQPQM 883
Cdd:cd05924   163 ------LVDAFGSSE--TGFTGSGHSAGSGPETG-PFTRANpdTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  884 TASRFehITLNDVnnagqgaatlRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQikVIV 963
Cdd:cd05924   234 TAETF--PEVDGV----------RYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS-HPAVYD--VLV 298

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  964 AQV-----GSRPALVAYAtvkADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMK 1024
Cdd:cd05924   299 VGRpderwGQEVVAVVQL---REGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 686-1022 1.33e-09

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: 61.90  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 VIYTSGSTGLPKGVMIEHGSLI--NL-------LDDHRDRIDFTPqstMFNCMSLS-----FDAGNMTTLLPlssggtlA 751
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIaaNLqlihamgLTEADVYLNMLP---LFHIAGLNlalatFHAGGANVVME-------K 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  752 FGEPNDRAIMQAEqaGATHLI-LPTALMSILDPEQVNGIQAIGM---GGEACPnAVVENWADKVA--LYNMYGPTE--CT 823
Cdd:cd17637    75 FDPAEALELIEEE--KVTLMGsFPPILSNLLDAAEKSGVDLSSLrhvLGLDAP-ETIQRFEETTGatFWSLYGQTEtsGL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  824 VTALSTRLRKGqpvTIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFE---Hitlndvnnag 900
Cdd:cd17637   152 VTLSPYRERPG---SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRngwH---------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  901 qgaatlriyRTGDKARLLNNGDYEYCGRIDEQ--IKLRGYRIEPGEIEAQLAAVcPSLKQIKVI-VAQVGSRPALVAYAT 977
Cdd:cd17637   219 ---------HTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEH-PAIAEVCVIgVPDPKWGEGIKAVCV 288

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 499404635  978 VKAdSSTPEPAAvLID-VAKYLPEYMVPFRLMLLEDMPLTPNGKLD 1022
Cdd:cd17637   289 LKP-GATLTADE-LIEfVGSRIARYKKPRYVVFVEALPKTADGSID 332
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1560-1914 1.98e-09

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 63.14  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1560 YDIDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAAL-ESECASIQVIVKQAD 1638
Cdd:PRK10252    2 EPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFtEDNGEVWQWVDPALT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1639 LPFY-YQDLMQDADPLAVIERYRQQDLRTGFDLSQ-PPLLRIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLGAVHRDYQ 1716
Cdd:PRK10252   82 FPLPeIIDLRTQPDPHAAAQALMQADLQQDLRVDSgKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1717 TLMQGQvlmhgDAPAIQ-VDRAYV--DYARHAVAQQSAVD-AFW-QQRQSLLAQTNDVSMLFAAAGKRADLsqhltqiep 1791
Cdd:PRK10252  162 AWLRGE-----PTPASPfTPFADVveEYQRYRASEAWQRDaAFWaEQRRQLPPPASLSPAPLPGRSASADI--------- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1792 qvtsvsLNEKDQATLTAFAREVGITPSI---------IAQYawhrlLARSTGDAVSIVGNVLSGRESPVedVASSVGLYI 1862
Cdd:PRK10252  228 ------LRLKLEFTDGAFRQLAAQASGVqrpdlalalVALW-----LGRLCGRMDYAAGFIFMRRLGSA--ALTATGPVL 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499404635 1863 NSLPLALSWQQPVSLQQHLVQLQNELMAMNQH----ATQSL--IALTAGRSRLFNSLF 1914
Cdd:PRK10252  295 NVLPLRVHIAAQETLPELATRLAAQLKKMRRHqrydAEQIVrdSGRAAGDEPLFGPVL 352
PRK05691 PRK05691
peptide synthase; Validated
 1559-1703 6.06e-09

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 61.72  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1559 RYDIDTLLPLSSLQQSMLYHRLRCPQDDAYHLQTPIRYAHVLDVEGYRQAWQRQIQRFPALRAALES-ECASIQVIVKQA 1637
Cdd:PRK05691 1722 RVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSvDGVPVQQVAEDS 1801

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1638 DLPFYYQDLmqDADPLAVIERYRQQ----DLRTGFDLSQPPLLRIACFRLGEQDYRVLLSCHHSVIDGWS 1703
Cdd:PRK05691 1802 GLRMDWQDF--SALPADARQQRLQQladsEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWA 1869
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 559-1021 6.18e-09

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: 60.90  E-value: 6.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  559 TDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLDPDYPPERLRHIITDANLSVIL 638
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  639 ggdgqqlaqwsaeqrIDLTDPAVveqwQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRID 718
Cdd:cd05939    81 ---------------FNLLDPLL----TQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  719 FTPQSTMFNCMSLSFDAGNMttllpLSSGGTLAFgepndraimqaeqaGATHLILP--TALMSILDPEQVNG--IQAIgm 794
Cdd:cd05939   142 MRPEDVVYDCLPLYHSAGGI-----MGVGQALLH--------------GSTVVIRKkfSASNFWDDCVKYNCtiVQYI-- 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  795 gGEAC------PNAVVEN----------------WADKVALYNM------YGPTECT---------VTA---LSTRLRKG 834
Cdd:cd05939   201 -GEICryllaqPPSEEEQkhnvrlavgnglrpqiWEQFVRRFGIpqigefYGATEGNsslvnidnhVGAcgfNSRILPSV 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  835 QPVTIGKPLIHIQALILDTAGqLCPVGVPGElclAGLGLARGYLNQPqmtASRFEhitlndvNNAGQGAATLRIYR---- 910
Cdd:cd05939   280 YPIRLIKVDEDTGELIRDSDG-LCIPCQPGE---PGLLVGKIIQNDP---LRRFD-------GYVNEGATNKKIARdvfk 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  911 TGDKArlLNNGD--------YEYC-GRIDEQIKLRGYRIEPGEIEAQLAAvCPSLKQIKVIVAQVGSRPALVAYATVKAD 981
Cdd:cd05939   346 KGDSA--FLSGDvlvmdelgYLYFkDRTGDTFRWKGENVSTTEVEGILSN-VLGLEDVVVYGVEVPGVEGRAGMAAIVDP 422

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 499404635  982 SSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKL 1021
Cdd:cd05939   423 ERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKL 462
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
673-1026 1.26e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 59.29  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  673 PPAIPRHAQQL--------------AQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTM---------FNCM 729
Cdd:PRK07824   13 PAQDERRAALLrdalrvgepidddvALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQWLLalpahhiagLQVL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  730 SLSFDAGNMTTLLPLSSGgtlaFGEPNDRAIMQAEQAGATHLIL-PTALMSIL-DPEQVNGIQ---AIGMGGEACPNAVV 804
Cdd:PRK07824   93 VRSVIAGSEPVELDVSAG----FDPTALPRAVAELGGGRRYTSLvPMQLAKALdDPAATAALAeldAVLVGGGPAPAPVL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  805 ENWAD-KVALYNMYGPTEctvTAlstrlrkGQPVTIGKPLIHIQALILDtagqlcpvgvpGELCLAGLGLARGYLNQPqm 883
Cdd:PRK07824  169 DAAAAaGINVVRTYGMSE---TS-------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV-- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  884 tasrfEHitlNDVNNAGQgaatlriYRTGDkARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI- 962
Cdd:PRK07824  226 -----DP---DPFAEPGW-------FRTDD-LGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATH-PAVADCAVFg 288

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  963 VA--QVGSRpalVAYATVKADSSTPEPAAVLIDVAKYLPEYMVPFRLMLLEDMPLTPNGKLDMKQL 1026
Cdd:PRK07824  289 LPddRLGQR---VVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 686-962 1.48e-08

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: 58.85  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  686 VIYTSGSTGLPKGVMIEHGSLI----NLLDDHrdriDFTPQSTMFNCMSLsFDAGN-MTTLLPLSSGGTLAFGEPND--- 757
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLaqalVLAVLQ----AIDEGTVFLNSGPL-FHIGTlMFTLATFHAGGTNVFVRRVDaee 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  758 -RAIMQAEQAGATHLILPTaLMSIL-----DPEQVNGIQAIGMGGEACPNAVVENWADKVALYNmYGPTEctVTALSTRL 831
Cdd:cd17636    80 vLELIEAERCTHAFLLPPT-IDQIVelnadGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG-YGQTE--VMGLATFA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  832 RKGQPV--TIGKPLIHIQALILDTAGQLCPVGVPGELCLAGLGLARGYLNQPQMTASRFehitlndvnnAGQGaatlriY 909
Cdd:cd17636   156 ALGGGAigGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT----------RGGW------H 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499404635  910 RTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLAAVcPSLKQIKVI 962
Cdd:cd17636   220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQH-PAVADAAVI 271
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1600-1867 1.49e-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, 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: 59.39  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1600 LDVEGYRQAWQRQIQRFPALRAALESECAS---IQVIVKQADLPFYYQDLMQDADPLAVIERYRQQDlrtgFDLSQPPLL 1676
Cdd:cd19532    36 LDVARLERAVRAVGQRHEALRTCFFTDPEDgepMQGVLASSPLRLEHVQISDEAEVEEEFERLKNHV----YDLESGETM 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1677 RIACFRLGEQDYRVLLSCHHSVIDGWSGPQLLgavhRDYQTLMQGQVLMHgdaPAIQvdraYVDYARHavaQQSAVD--- 1753
Cdd:cd19532   112 RIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFL----RDLERAYNGQPLLP---PPLQ----YLDFAAR---QRQDYEsga 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1754 -----AFWQqrqSLLAQTNDVSML--FAAAGKRADLSQHLTQIepqvTSVSLNEKDQATLTAFAREVGITPSIIaqY--A 1824
Cdd:cd19532   178 ldedlAYWK---SEFSTLPEPLPLlpFAKVKSRPPLTRYDTHT----AERRLDAALAARIKEASRKLRVTPFHF--YlaA 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 499404635 1825 WHRLLARSTG-DAVSIvGNVLSGRESpvEDVASSVGLYINSLPL 1867
Cdd:cd19532   249 LQVLLARLLDvDDICI-GIADANRTD--EDFMETIGFFLNLLPL 289
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1047-1101 4.54e-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: 51.41  E-value: 4.54e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635  1047 VLAIWRSVLNTP---LGVEDDFFRLGGDSILSIQLTTRLRSA-GYACTVKDVFEAKSVR 1101
Cdd:pfam00550    3 LRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
PRK09192 PRK09192
fatty acyl-AMP ligase;
559-721 4.56e-08

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 58.09  E-value: 4.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  559 TDTLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGAAYVPLdpdypP------------ERLR 626
Cdd:PRK09192   47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-----PlpmgfggresyiAQLR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  627 HIITDANLSVILGGDGqqLAQWSAEQRIDLTDPAVVE-QWQDLPGDQPPAIPR-HAQQLAQVIYTSGSTGLPKGVMIEHG 704
Cdd:PRK09192  122 GMLASAQPAAIITPDE--LLPWVNEATHGNPLLHVLShAWFKALPEADVALPRpTPDDIAYLQYSSGSTRFPRGVIITHR 199

                         170
                  ....*....|....*...
gi 499404635  705 SLINLLDDH-RDRIDFTP 721
Cdd:PRK09192  200 ALMANLRAIsHDGLKVRP 217
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 561-973 2.35e-07

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: 55.68  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  561 TLTYAELNRQANQLAHWLHRQGLGEQSLVGVLAKRDRYFVIALLAIWKAGaayvpldpdypperlrhiITDANLSVILGG 640
Cdd:cd17639     5 YMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN------------------IPIVTVYATLGE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  641 DGQQLAQWSAEQRIDLTDPAvveqwqdlPGDqppaiprhaqqLAQVIYTSGSTGLPKGVMIEHGSLI--------NLLDD 712
Cdd:cd17639    67 DALIHSLNETECSAIFTDGK--------PDD-----------LACIMYTSGSTGNPKGVMLTHGNLVagiaglgdRVPEL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  713 HR--DR-IDFTPQSTMFncmSLSFdagnmtTLLPLSSGGTLAFGEPndRAIMQAEQAGaTHLIL----PTaLMS----IL 781
Cdd:cd17639   128 LGpdDRyLAYLPLAHIF---ELAA------ENVCLYRGGTIGYGSP--RTLTDKSKRG-CKGDLtefkPT-LMVgvpaIW 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  782 DP---------EQVNGIQ-------------AIGMGGEACP-NAVVENwadKVA------LYNM---------------- 816
Cdd:cd17639   195 DTirkgvlaklNPMGGLKrtlfwtayqsklkALKEGPGTPLlDELVFK---KVRaalggrLRYMlsggaplsadtqefln 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  817 ---------YGPTECTVTALSTRLRKGQPVTIGKPLIHIQALILDT--AGQLCPVGVP-GELCLAGLGLARGYLNQPQMT 884
Cdd:cd17639   272 ivlcpviqgYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWeeGGYSTDKPPPrGEILIRGPNVFKGYYKNPEKT 351

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  885 ASRFehitlndvnnAGQGaatlrIYRTGDKARLLNNGDYEYCGRIDEQIKLR-GYRIEPGEIEAQLAAvCPSLKQIKVIV 963
Cdd:cd17639   352 KEAF----------DGDG-----WFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRS-NPLVNNICVYA 415

                         490
                  ....*....|.
gi 499404635  964 AQVGSRP-ALV 973
Cdd:cd17639   416 DPDKSYPvAIV 426
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1041-1110 6.11e-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: 49.08  E-value: 6.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499404635 1041 NPLEADVLAIWRSVLNTP---LGVEDDFFR-LGGDSILSIQLTTRLRSA-GYACTVKDVFEAKSVRRLCRVLAQN 1110
Cdd:COG0236     4 EELEERLAEIIAEVLGVDpeeITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEEK 78
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1131-1425 6.78e-07

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: 53.85  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1131 PIQRWFMEQSLARPEHWNQAAMIQL-PEVDTERLVTMLQALMAQHDALR---LGCDAEGQRY---LADVPCPALSTldyr 1203
Cdd:cd19542     6 PMQEGMLLSQLRSPGLYFNHFVFDLdSSVDVERLRNAWRQLVQRHDILRtvfVESSAEGTFLqvvLKSLDPPIEEV---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1204 QLGDDGLQQAFTALQSEFDPAQGRTMACALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERLYLGEPLLPKTSSYRQ 1283
Cdd:cd19542    82 ETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSG-EVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPPFSDY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1284 wgaALQHYATQHAEQLTYWQAQEDGVDLTAL-----LAAKDPQGHASAAIL-TLDA--KTTGqlVSEANrAFNTDVSdLL 1355
Cdd:cd19542   161 ---ISYLQSQSQEESLQYWRKYLQGASPCAFpslspKRPAERSLSSTRRSLaKLEAfcASLG--VTLAS-LFQAAWA-LV 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1356 LSALTRTlNDLGWGDkariMLegHGREAIDPTLDvsRTVGWFTSTYPVCLQDKPDWasliqSSKEQLRQV 1425
Cdd:cd19542   234 LARYTGS-RDVVFGY----VV--SGRDLPVPGID--DIVGPCINTLPVRVKLDPDW-----TVLDLLRQL 289
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1133-1469 7.76e-07

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: 53.80  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1133 QR--WFMEQSLARPEHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLGC---DAEGQRYLADVPCPALSTLDYRQLG 1206
Cdd:cd20483     8 QRrlWFLHNFLEDKTFLNLLLVCHIKgKPDVNLLQKALSELVRRHEVLRTAYfegDDFGEQQVLDDPSFHLIVIDLSEAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1207 D--DGLQQAFTALQS-EFDPAQGRTMACALVRHHPqADTALFLAFHHLVIDAVSWRILVDDLERLY----LGEPL---LP 1276
Cdd:cd20483    88 DpeAALDQLVRNLRRqELDIEEGEVIRGWLVKLPD-EEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLatvPP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1277 KTSSYRQ---WGAALQHYATQHAEqLTYWQAQEDGV-DLTALL----AAKDP--QGHASAAILTLDAKTTGQLVSEANRA 1346
Cdd:cd20483   167 PPVQYIDftlWHNALLQSPLVQPL-LDFWKEKLEGIpDASKLLpfakAERPPvkDYERSTVEATLDKELLARMKRICAQH 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1347 FNTDVSdLLLSALTRTLNDLGwGDKARIMLEGHGREaidPTLDVSRTVGWFTSTYPVCLQDKPDWA--SLIQSSKEQL-- 1422
Cdd:cd20483   246 AVTPFM-FLLAAFRAFLYRYT-EDEDLTIGMVDGDR---PHPDFDDLVGFFVNMLPIRCRMDCDMSfdDLLESTKTTCle 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635 1423 ----RQVP-----DKgVGFNPLRYHHPqgnsltLSPIVFNYlglsvQAAGTWRPVD 1469
Cdd:cd20483   321 ayehSAVPfdyivDA-LDVPRSTSHFP------IGQIAVNY-----QVHGKFPEYD 364
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
676-1035 7.97e-07

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 54.33  E-value: 7.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  676 IPRHAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLsFDAGNMTT--LLPLSSggtlafg 753
Cdd:PRK08043  360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPL-FHSFGLTVglFTPLLT------- 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  754 epndraimqaeqaGATHLILPTALMSILDPEQV---NGIQAIGM------------------------GGEACPNAVVEN 806
Cdd:PRK08043  432 -------------GAEVFLYPSPLHYRIVPELVydrNCTVLFGTstflgnyarfanpydfarlryvvaGAEKLQESTKQL 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  807 WADKVALYNM--YGPTECT-VTALSTRLrKGQPVTIGKPLIHIQALILDTAGqlcpVGVPGELCLAGLGLARGYLnqpqm 883
Cdd:PRK08043  499 WQDKFGLRILegYGVTECApVVSINVPM-AAKPGTVGRILPGMDARLLSVPG----IEQGGRLQLKGPNIMNGYL----- 568

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  884 tasRFEHITLNDVNNA--GQGAATLRIYRTGDKARLLNNGdyeYCgrideQIKLRGYRIepgeieAQLAAVCPSLKQIKV 961
Cdd:PRK08043  569 ---RVEKPGVLEVPTAenARGEMERGWYDTGDIVRFDEQG---FV-----QIQGRAKRF------AKIAGEMVSLEMVEQ 631

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  962 IVAQVGsrPALVAYATVKADSSTPEpAAVLIDVAKYL--------------PEYMVPFRLMLLEDMPLTPNGKLDMKQLP 1027
Cdd:PRK08043  632 LALGVS--PDKQHATAIKSDASKGE-ALVLFTTDSELtreklqqyarehgvPELAVPRDIRYLKQLPLLGSGKPDFVTLK 708


                  ....*...
gi 499404635 1028 PVLEANES 1035
Cdd:PRK08043  709 SMVDEPEQ 716
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1135-1422 1.12e-06

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: 53.54  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1135 WFMEQSLARPEHWNQAAMIQLPE-VDTERLVTMLQALMAQHDALRLGCDAEGQrylaDVPCPALST-----LDYRQLGDD 1208
Cdd:cd19539    12 WFIDQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDG----GVPRQEILPpgpapLEVRDLSDP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1209 G--LQQAFTALQSE-----FDPAQGRTMACALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERLYLG-----EPLLP 1276
Cdd:cd19539    88 DsdRERRLEELLREresrgFDLDEEPPIRAVLGRFDPD-DHVLVLVAHHTAFDAWSLDVFARDLAALYAArrkgpAAPLP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1277 KT-SSYRQWGAALQHYAT--QHAEQLTYWQAQEDGVDLTALLAA--KDPQGHASAAILT--LDAKTTGQLVSEANRAFNT 1349
Cdd:cd19539   167 ELrQQYKEYAAWQREALAapRAAELLDFWRRRLRGAEPTALPTDrpRPAGFPYPGADLRfeLDAELVAALRELAKRARSS 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499404635 1350 DVSdLLLSALTRTLNDlgWGDKARIML----EGHGREAIDptldvsRTVGWFTSTYPVCLQ--DKPDWASLIQSSKEQL 1422
Cdd:cd19539   247 LFM-VLLAAYCVLLRR--YTGQTDIVVgtpvAGRNHPRFE------STVGFFVNLLPLRVDvsDCATFRDLIARVRKAL 316
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1600-1703 4.42e-06

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: 51.48  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1600 LDVEGYRQAWQRQIQRFPALRAALESECASIQVIVK---QADLPFYYQDLMQDADPLAVieRYRQQDLRTGFDLSQPPLL 1676
Cdd:cd19534    34 LDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRgdvEELFRLEVVDLSSLAQAAAI--EALAAEAQSSLDLEEGPLL 111

                          90       100
                  ....*....|....*....|....*..
gi 499404635 1677 RIACFRLGEQDYRVLLSCHHSVIDGWS 1703
Cdd:cd19534   112 AAALFDGTDGGDRLLLVIHHLVVDGVS 138
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 661-712 5.50e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 51.52  E-value: 5.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499404635  661 VVEQWQDLPGDQPPAIPRHAQQLAQVIYTSGSTGLPKGVMIEHGSL---INLLDD 712
Cdd:PTZ00216  244 VVAKGHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLtagILALED 298
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 670-707 6.05e-06

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


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 51.66  E-value: 6.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499404635  670 GDQPPAIPR--HAQQLAQVIYTSGSTGLPKGVMIEHGSLI 707
Cdd:PLN02387  237 GKENPVDPDlpSPNDIAVIMYTSGSTGLPKGVMMTHGNIV 276
TubC_N pfam18563
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ...
 4-54 1.28e-05

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: 44.43  E-value: 1.28e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 499404635     4 IVTLLKQLERQGVRLALNaQGQLISQSNKEAITAEIGRTIKENKDAIVRCL 54
Cdd:pfam18563    1 IVELLAELYALGIKLWLE-GGRLRFRAPKGVLTPELREKLKERKAEIIAFL 50
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 688-1032 1.72e-05

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 50.02  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  688 YTSGSTGLPKGVMIEH-GSLINLLDDHRD-RIDFTP----QSTMFNCMSLSFDAGNMttllplSSGGT-LAFGEPNDRAI 760
Cdd:PLN03102  193 YTSGTTADPKGVVISHrGAYLSTLSAIIGwEMGTCPvylwTLPMFHCNGWTFTWGTA------ARGGTsVCMRHVTAPEI 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  761 MQ-AEQAGATHL-ILPTALMSILDPEQVN-----GIQAIGMGGEACPNAVVENwADKVALYNM--YGPTECTVTALS--- 828
Cdd:PLN03102  267 YKnIEMHNVTHMcCVPTVFNILLKGNSLDlsprsGPVHVLTGGSPPPAALVKK-VQRLGFQVMhaYGLTEATGPVLFcew 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  829 ----TRLRKGQPVTIG--KPLIHIQALILDTAGQLCPVGVP------GELCLAGLGLARGYLNQPQMTASRFEHITLNdv 896
Cdd:PLN03102  346 qdewNRLPENQQMELKarQGVSILGLADVDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLN-- 423

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  897 nnagqgaatlriyrTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIEAQLaavcpsLKQIKVIVAQVGSRP------ 970
Cdd:PLN03102  424 --------------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL------YKYPKVLETAVVAMPhptwge 483

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404635  971 ALVAYATVKADSSTPEPAAVLI-----DVAKY----LPEYMVPFRLMLLEDMPLTPNGKLDMKQLPPVLEA 1032
Cdd:PLN03102  484 TPCAFVVLEKGETTKEDRVDKLvtrerDLIEYcrenLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 2033-2098 2.53e-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: 43.71  E-value: 2.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499404635  2033 QTLLRAWAQTLHLGEPGLGESDlwsrTLCESGVDSLQRIALAQALSRTLAHPVSVALLQHYPSPQA 2098
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDT----DLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 2035-2105 4.25e-05

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


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.78  E-value: 4.25e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499404635   2035 LLRAWAQTLHLGEPGLGESDlwsRTLCESGVDSLQRIALAQALSRTLAHPVSVALLQHYPSPQALSGHLAQ 2105
Cdd:smart00823   17 VREQVAAVLGHAAAEAIDPD---RPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1156-1312 4.96e-05

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: 47.95  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1156 PEVDTERLVTMLQALMAQHDALR---LGCDAEGQRYLADVPcP---ALSTLDYRqlgddglqqafTALQSEFDPAQGrtm 1229
Cdd:cd19537    34 GDVDRDRLASAWNTVLARHRILRsryVPRDGGLRRSYSSSP-PrvqRVDTLDVW-----------KEINRPFDLERE--- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1230 acALVRHHPQADTaLFLAFHHLVIDAVSWRILVDDLERLYLGEPLLPKTSSYRQWgAALQHYATQhaEQLTYWQAQEDGV 1309
Cdd:cd19537    99 --DPIRVFISPDT-LLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDS-TAWSRPASP--EDLDFWSEYLSGL 172


                  ...
gi 499404635 1310 DLT 1312
Cdd:cd19537   173 PLL 175
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1131-1310 5.46e-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: 48.06  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1131 PIQRWFMEQSLARPEHWNQAAMIQLPE-VDTERLVTMLQALMAQHDALRlgcdaegqryladvpcpalSTLDyrQLGDDG 1209
Cdd:cd19545     6 PLQEGLMALTARQPGAYVGQRVFELPPdIDLARLQAAWEQVVQANPILR-------------------TRIV--QSDSGG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1210 LQQA-----------FTALQS--EFDPAQG-----RTMACALVRHhPQADTALFLAFHHLVIDAVSWRILVDDLERLYLG 1271
Cdd:cd19545    65 LLQVvvkespiswteSTSLDEylEEDRAAPmglggPLVRLALVED-PDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG 143

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 499404635 1272 EPlLPKTSSYRQWGAALQHyaTQHAEQLTYWQAQEDGVD 1310
Cdd:cd19545   144 EP-VPQPPPFSRFVKYLRQ--LDDEAAAEFWRSYLAGLD 179
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
532-823 6.01e-05

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 48.24  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  532 LTVTDVIEAVAQRDPQQLAIAFDGEPRTDTlTYAELNRQANQLAHWLHRQ-GLGEQSLVGVLAKRDRYFVIALLAIWKAG 610
Cdd:PRK05620   10 LSLTRILEYGSTVHGDTTVTTWGGAEQEQT-TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  611 AAYVPLDPDYPPERLRHIITDANLSVILGG--DGQQLAQWSAE----------QRIDLTDPAV----------------- 661
Cdd:PRK05620   89 AVFNPLNKQLMNDQIVHIINHAEDEVIVADprLAEQLGEILKEcpcvravvfiGPSDADSAAAhmpegikvysyealldg 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  662 ---VEQWQDLPGDQPPAIprhaqqlaqvIYTSGSTGLPKGVMIEHGSLinllddhrdridftpqstMFNCMSL----SFD 734
Cdd:PRK05620  169 rstVYDWPELDETTAAAI----------CYSTGTTGAPKGVVYSHRSL------------------YLQSLSLrttdSLA 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  735 AGNMTTLL---P----LSSGGTLAF---GEPndrAIMQAEQAGATHLI-------------LPTALMSIL------DPEQ 785
Cdd:PRK05620  221 VTHGESFLccvPiyhvLSWGVPLAAfmsGTP---LVFPGPDLSAPTLAkiiatamprvahgVPTLWIQLMvhylknPPER 297

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 499404635  786 VNgIQAIGMGGEACPNAVVENWADK--VALYNMYGPTECT 823
Cdd:PRK05620  298 MS-LQEIYVGGSAVPPILIKAWEERygVDVVHVWGMTETS 336
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 562-721 7.50e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 47.79  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  562 LTYAELNRQANQLAHWLHRQGLGEQSLVGVlakrdrYFV--IALLAIWKAGAAY----VPLDPDYPPERLRHIITDANLS 635
Cdd:PLN02736   79 MTYGEAGTARTAIGSGLVQHGIPKGACVGL------YFInrPEWLIVDHACSAYsyvsVPLYDTLGPDAVKFIVNHAEVA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  636 -------------------------VILGGDGQQLAQWSAEQRIDLTDPAVVEQwQDLPGDQPPAIPRhAQQLAQVIYTS 690
Cdd:PLN02736  153 aifcvpqtlntllsclseipsvrliVVVGGADEPLPSLPSGTGVEIVTYSKLLA-QGRSSPQPFRPPK-PEDVATICYTS 230

                         170       180       190
                  ....*....|....*....|....*....|.
gi 499404635  691 GSTGLPKGVMIEHGSLINLLDDHRDRIDFTP 721
Cdd:PLN02736  231 GTTGTPKGVVLTHGNLIANVAGSSLSTKFYP 261
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 684-935 7.85e-05

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 47.50  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  684 AQVIYTSGSTGLPKGVMIEHGsliNLLDDHRDRIDFTPQSTMFNCMSL--SFDAG--NMTTLLPLSSGGTLAFGEPNDRA 759
Cdd:PRK06334  186 AVILFTSGTEKLPKGVPLTHA---NLLANQRACLKFFSPKEDDVMMSFlpPFHAYgfNSCTLFPLLSGVPVVFAYNPLYP 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  760 IMQAEQAGATHLIL----PTALMSILDPEQ-----VNGIQAIGMGGEACPNAV---VENWADKVALYNMYGPTECT-VTA 826
Cdd:PRK06334  263 KKIVEMIDEAKVTFlgstPVFFDYILKTAKkqescLPSLRFVVIGGDAFKDSLyqeALKTFPHIQLRQGYGTTECSpVIT 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  827 LSTRLRKGQPVTIGKPLIHIQALILDTAGQLcPV--GVPGELCLAGLGLARGYLNqpqmtasrfehitlndvNNAGQGAA 904
Cdd:PRK06334  343 INTVNSPKHESCVGMPIRGMDVLIVSEETKV-PVssGETGLVLTRGTSLFSGYLG-----------------EDFGQGFV 404

                         250       260       270
                  ....*....|....*....|....*....|....
gi 499404635  905 TL---RIYRTGDKARLLNNGDYEYCGRIDEQIKL 935
Cdd:PRK06334  405 ELggeTWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 944-1020 1.43e-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: 42.15  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   944 EIEAQLAAvCPSLKQIKVI---VAQVGSRPalVAYATVKADssTPEPAAVLID-VAKYLPEYMVPFRLMLLEDMPLTPNG 1019
Cdd:pfam13193    1 EVESALVS-HPAVAEAAVVgvpDELKGEAP--VAFVVLKPG--VELLEEELVAhVREELGPYAVPKEVVFVDELPKTRSG 75


                   .
gi 499404635  1020 K 1020
Cdd:pfam13193   76 K 76
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1035-1109 1.56e-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: 42.24  E-value: 1.56e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635   1035 SDGEADNPLEADVLAIWRSVLNTP----LGVEDDFFRLGGDSILSIQLTTRLRSA-GYACTVKDVFEAKSVRRLCRVLAQ 1109
Cdd:smart00823    5 PPAERRRLLLDLVREQVAAVLGHAaaeaIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAA 84
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1129-1359 2.25e-04

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: 45.82  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1129 LLPIQR--WFMEQSLARPEHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLG-CDAEG---QRYLADVPCPaLSTLD 1201
Cdd:cd19533     4 LTSAQRgvWFAEQLDPEGSIYNLAEYLEITgPVDLAVLERALRQVIAEAETLRLRfTEEEGepyQWIDPYTPVP-IRHID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1202 YRQLGD-DGLQQAF--TALQSEFDPAQGRTMACALVRHHPQAdTALFLAFHHLVIDAVSWRILVDDLERLYL----GEPL 1274
Cdd:cd19533    83 LSGDPDpEGAAQQWmqEDLRKPLPLDNDPLFRHALFTLGDNR-HFWYQRVHHIVMDGFSFALFGQRVAEIYTallkGRPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1275 LPKTS-SYRQWGAALQHYAT--QHAEQLTYWQAQEDGVDLTALLAAKDPQGHASAAILTLD-AKTTGQLVSEANRAFNTD 1350
Cdd:cd19533   162 PPAPFgSFLDLVEEEQAYRQseRFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAElPPELTRTLLEAAEAHGAS 241


                  ....*....
gi 499404635 1351 VSDLLLSAL 1359
Cdd:cd19533   242 WPSFFIALV 250
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1161-1339 2.89e-04

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: 45.51  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1161 ERLVTMLQALMAQHDALRLGCDAEG-----QRYLADVPCPaLSTLDYRQlGDDGLQQaftaLQSEFDPAQGRT------- 1228
Cdd:cd19544    39 DAFLAALQQVIDRHDILRTAILWEGlsepvQVVWRQAELP-VEELTLDP-GDDALAQ----LRARFDPRRYRLdlrqapl 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1229 MACALVRHHPQADTALFLAFHHLVIDAVSWRILVDDLERLYLGEP-LLPKTSSYRQWGAALQHyATQHAEQLTYWQAQED 1307
Cdd:cd19544   113 LRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRAaALPPPVPYRNFVAQARL-GASQAEHEAFFREMLG 191

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 499404635 1308 GVD-LTALLAAKDPQGHASA---AILTLDAKTTGQL 1339
Cdd:cd19544   192 DVDePTAPFGLLDVQGDGSDiteARLALDAELAQRL 227
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1121-1359 3.23e-04

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 46.19  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1121 GTLEGEFALLPIQR--WFMEQSLARPEHWNQAAMIQLP-EVDTERLVTMLQALMAQHDALRLG-CDAEG---QRYLADVP 1193
Cdd:PRK10252    2 EPMSQHLPLVAAQPgiWMAEKLSPLPSAWSVAHYVELTgELDAPLLARAVVAGLAEADTLRMRfTEDNGevwQWVDPALT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1194 CPALSTLDYRQlGDDGLQQAFTA----LQSEFDPAQGRTMAC-ALVRHHPQaDTALFLAFHHLVIDAVSWRILVDDLERL 1268
Cdd:PRK10252   82 FPLPEIIDLRT-QPDPHAAAQALmqadLQQDLRVDSGKPLVFhQLIQLGDN-RWYWYQRYHHLLVDGFSFPAITRRIAAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635 1269 Y----LGEPllPKTSSYRQWGAAL---QHYATQHAEQL--TYWQAQEDGVDLTALLAAKDPQGHASAA-----ILTLDAK 1334
Cdd:PRK10252  160 YcawlRGEP--TPASPFTPFADVVeeyQRYRASEAWQRdaAFWAEQRRQLPPPASLSPAPLPGRSASAdilrlKLEFTDG 237

                         250       260
                  ....*....|....*....|....*
gi 499404635 1335 TTGQLVSEANRAFNTDVSdLLLSAL 1359
Cdd:PRK10252  238 AFRQLAAQASGVQRPDLA-LALVAL 261
PLN03051 PLN03051
acyl-activating enzyme; Provisional
 672-973 5.34e-04

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 44.81  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  672 QPPAIPrhAQQLAQVIYTSGSTGLPKGVMIEHGSLINLLDDHRDRIDFTPQSTMFNCMSLSFDAGNMTTLLPLSSGGTLA 751
Cdd:PLN03051  112 SPVYAP--VESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLA 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  752 F--GEPNDRAIMQ-AEQAGATHL-ILPT----------ALMSILDpeqVNGIQAIGMGGEAcpnAVVENWADKVALYNMY 817
Cdd:PLN03051  190 LygGAPLGRGFGKfVQDAGVTVLgLVPSivkawrhtgaFAMEGLD---WSKLRVFASTGEA---SAVDDVLWLSSVRGYY 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  818 GPT-EC-------TVTALSTRLRKGQPVTIGKPLIHIQALILDTAGQLCPVGVP--GELCLAG--LGLARGYLNQPQmTA 885
Cdd:PLN03051  264 KPViEYcggtelaSGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPcvGEVALAPpmLGASDRLLNADH-DK 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  886 SRFEHITLNDVNNagqgaatLRIYRTGDKARLLNNGDYEYCGRIDEQIKLRGYRIEPGEIE-AQLAAVCPSLKQIKVIVA 964
Cdd:PLN03051  343 VYYKGMPMYGSKG-------MPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIErACDRAVAGIAETAAVGVA 415


                  ....*....
gi 499404635  965 QVGSRPALV 973
Cdd:PLN03051  416 PPDGGPELL 424
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 857-974 6.70e-04

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


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 44.65  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  857 LCPVGVPGELCLAGLGLARGYLNQPQMTASRFEHITlndVNNAGQGAATLRIYRTGDKA-----RLLNNGDYEY-----C 926
Cdd:cd05905   382 LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFP---STRLSTGITNNSYARTGLLGflrptKCTDLNVEEHdllfvV 458

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499404635  927 GRIDEQIKLRGYRIEPGEIEAQLAAVCPSLKQIkvIVAQVGSRPALVA 974
Cdd:cd05905   459 GSIDETLEVRGLRHHPSDIEATVMRVHPYRGRC--AVFSITGLVVVVA 504
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
101-211 6.50e-03

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 41.23  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404635  101 RLTGPLDVAALEFAFDALAQRHASLRTRFvvneqgkgEQRIDAYQPFVIQHDdfsLLPEAEregrlqqQVKAEISRP--- 177
Cdd:PRK09294   29 HLRGVLDIDALSDAFDALLRAHPVLAAHL--------EQDSDGGWELVADDL---LHPGIV-------VVDGDAARPlpe 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499404635  178 FDLTAGD-LTRVRLVKMSERTHVLMITqHHIISDG 211
Cdd:PRK09294   91 LQLDQGVsLLALDVVPDDGGARVTLYI-HHSIADA 124
 
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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