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Conserved domains on  [gi|1698252301|ref|WP_141546162.1|]
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amino acid adenylation domain-containing protein

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 1002729)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products; may contain C-terminal alpha/beta hydrolase domain

EC:  6.2.1.-
Gene Ontology:  GO:0019184|GO:0016874
PubMed:  11342140|15582399|14529378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12467 super family cl36129
peptide synthase; Provisional
 1-1244 0e+00

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1164.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVrEDRPNDKRIIAYIV----AEEKEP-INLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:PRK12467   932 LLAQPGVREAVVLA-QPGDAGLQLVAYLVpaavADGAEHqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   76 KLPAPDFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTV 154
Cdd:PRK12467  1011 ALPKPDASAVQATFVApQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTL 1090

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  155 AELAKQLN-HAKSARPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETL 233
Cdd:PRK12467  1091 AGFAQAVAaQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESL 1170

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  234 RTIFPNVLGSSYQKILDMENLNLE---MVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIV 310
Cdd:PRK12467  1171 RTTFVQEDGRTRQVIHPVGSLTLEeplLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIV 1250

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  311 GDGWSLQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLL--GDEttpesliSTQLDFWKEELKGLPDQMELPT 388
Cdd:PRK12467  1251 SDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMdaGER-------ARQLAYWKAQLGGEQPVLELPT 1323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  389 DYQRPVETSYRGETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLF 468
Cdd:PRK12467  1324 DRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFF 1403

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  469 VNTLVLRTNTSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPdleASL 548
Cdd:PRK12467  1404 VNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQL---PGL 1480

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  549 EIQSVG----SAKFDLTFEISESnevdgtPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVA 624
Cdd:PRK12467  1481 SVESLSwesqTAQFDLTLDTYES------SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEA 1554

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  625 EKNTVLEKWNG-GFQIAPEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRS 703
Cdd:PRK12467  1555 ERRQILEGWNAtHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERS 1634

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  704 LNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSV--EIECDESLKILVDDvNVMEEIEKYSEENIDE 781
Cdd:PRK12467  1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLqaRLPLPDGLRSLVLD-QEDDWLEGYSDSNPAV 1713

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  782 MeclkpLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLV 861
Cdd:PRK12467  1714 N-----LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLV 1788

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHNApkV 941
Cdd:PRK12467  1789 IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD---EQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG--L 1863

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERF 1021
Cdd:PRK12467  1864 FNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERF 1943

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1022 IADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVrEDQPGDKRLVAYI 1101
Cdd:PRK12467  1944 VADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYV 2022

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1102 VASNNETIDTNE--------MRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEfiASSSSRGPRTPQEEM-- 1171
Cdd:PRK12467  2023 VPTDPGLVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD--ASELQQAYVAPQSELeq 2100

                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1172 -LCDLFTEVLSVSQIGIDDGFFDLGGHSLLAVQLMSRMKEAlGVELNIGTLFAAPTVAGLAERLEIGNGQSALD 1244
Cdd:PRK12467  2101 rLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDGTVSID 2173
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 1257-1411 5.50e-31

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00975:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 223  Bit Score: 122.11  E-value: 5.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1257 PLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHA 1336
Cdd:pfam00975    2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFE 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1337 MAAQLQNEGEEVELLVMLDSYPGHFLPNT-EAPTEEEALIALLALGGYDPDNMDGKPLTMESAVEILRKDGSALAS 1411
Cdd:pfam00975   82 VARRLERQGEAVRSLFLSDASAPHTVRYEaSRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALES 157
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 1-1244 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1164.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVrEDRPNDKRIIAYIV----AEEKEP-INLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:PRK12467   932 LLAQPGVREAVVLA-QPGDAGLQLVAYLVpaavADGAEHqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   76 KLPAPDFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTV 154
Cdd:PRK12467  1011 ALPKPDASAVQATFVApQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTL 1090

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  155 AELAKQLN-HAKSARPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETL 233
Cdd:PRK12467  1091 AGFAQAVAaQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESL 1170

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  234 RTIFPNVLGSSYQKILDMENLNLE---MVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIV 310
Cdd:PRK12467  1171 RTTFVQEDGRTRQVIHPVGSLTLEeplLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIV 1250

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  311 GDGWSLQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLL--GDEttpesliSTQLDFWKEELKGLPDQMELPT 388
Cdd:PRK12467  1251 SDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMdaGER-------ARQLAYWKAQLGGEQPVLELPT 1323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  389 DYQRPVETSYRGETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLF 468
Cdd:PRK12467  1324 DRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFF 1403

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  469 VNTLVLRTNTSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPdleASL 548
Cdd:PRK12467  1404 VNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQL---PGL 1480

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  549 EIQSVG----SAKFDLTFEISESnevdgtPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVA 624
Cdd:PRK12467  1481 SVESLSwesqTAQFDLTLDTYES------SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEA 1554

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  625 EKNTVLEKWNG-GFQIAPEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRS 703
Cdd:PRK12467  1555 ERRQILEGWNAtHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERS 1634

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  704 LNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSV--EIECDESLKILVDDvNVMEEIEKYSEENIDE 781
Cdd:PRK12467  1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLqaRLPLPDGLRSLVLD-QEDDWLEGYSDSNPAV 1713

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  782 MeclkpLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLV 861
Cdd:PRK12467  1714 N-----LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLV 1788

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHNApkV 941
Cdd:PRK12467  1789 IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD---EQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG--L 1863

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERF 1021
Cdd:PRK12467  1864 FNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERF 1943

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1022 IADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVrEDQPGDKRLVAYI 1101
Cdd:PRK12467  1944 VADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYV 2022

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1102 VASNNETIDTNE--------MRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEfiASSSSRGPRTPQEEM-- 1171
Cdd:PRK12467  2023 VPTDPGLVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD--ASELQQAYVAPQSELeq 2100

                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1172 -LCDLFTEVLSVSQIGIDDGFFDLGGHSLLAVQLMSRMKEAlGVELNIGTLFAAPTVAGLAERLEIGNGQSALD 1244
Cdd:PRK12467  2101 rLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDGTVSID 2173
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 166-1389 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: 1149.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  166 SARPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSY 245
Cdd:COG1020      4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  246 QKILDMENLNLEMVI-----TNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLT 320
Cdd:COG1020     84 QVIQPVVAAPLPVVVllvdlEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  321 RDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLLGDETTPEslistQLDFWKEELKGLPDQMELPTDYQRPVETSYRG 400
Cdd:COG1020    164 AELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELAR-----QLAYWRQQLAGLPPLLELPTDRPRPAVQSYRG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  401 ETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSG 480
Cdd:COG1020    239 ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  481 DPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSAKFDL 560
Cdd:COG1020    319 DPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  561 TFEISEsnevdgTPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGFQIA 640
Cdd:COG1020    399 TLTVVE------TGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPY 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  641 P-EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAG 719
Cdd:COG1020    473 PaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  720 YLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEIEC-DESLKILVDDVnvmEEIEKYSEENIDEmeclkPLAPSHIAYVIY 798
Cdd:COG1020    553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGVPVLALDA---LALAAEPATNPPV-----PVTPDDLAYVIY 624

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLL 878
Cdd:COG1020    625 TSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELL 704

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSAFYQLMQADREneevgQKLSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVHVSYIE 958
Cdd:COG1020    705 ARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLPG--ARLVNLYGPTETTVDSTYYE 777

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  959 LDESIVSlRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGD 1038
Cdd:COG1020    778 VTPPDAD-GGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGD 856

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1039 LARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHA 1118
Cdd:COG1020    857 LARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL 936

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1119 SGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSSRGPRTPQEEMLCDLFTEVLSVSQIGIDDGFFDLGGHS 1198
Cdd:COG1020    937 ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLG 1016

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1199 LLAVQLMsRMKEALGVELNIGTLFAAPTVAGLAERLEIGNGQSALDVLLPLRASGDQLPLFCVHPAGGLSWCYAGLMKSL 1278
Cdd:COG1020   1017 LLLLLAL-ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLAL 1095

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1279 GTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHAMAAQLQNEGEEVELLVMLDSYP 1358
Cdd:COG1020   1096 LALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLL 1175

                         1210      1220      1230
                   ....*....|....*....|....*....|.
gi 1698252301 1359 GHFLPNTEAPTEEEALIALLALGGYDPDNMD 1389
Cdd:COG1020   1176 LLALLLLALLLLLLLLLLLLLLLLLLLLLLL 1206
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 657-1150 0e+00

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


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 765.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd17643     81 ADSGPSLLLTD------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANV 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd17643    119 LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQL 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 MQADRENEEvgQKLSLRYVVFGGEALELSRLEDWYSRHPHNAPKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSI 976
Cdd:cd17643    199 VEAADRDGR--DPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPL 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADH 1056
Cdd:cd17643    277 PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADE 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1057 QIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNE 1136
Cdd:cd17643    357 QVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDA 436

                          490
                   ....*....|....
gi 1698252301 1137 LPLTPNGKLDRKAL 1150
Cdd:cd17643    437 LPLTVNGKLDRAAL 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 670-1085 1.87e-169

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: 514.51  E-value: 1.87e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  670 TYEKLNRKANKIARFLIA-KGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SVEIECDESLKILVDDVNVMEEiekYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ 828
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELA---ALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKE-KVTVLNQTPSAFYQLMQADREneevg 907
Cdd:TIGR01733  158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEhPVTVLNLTPSLLALLAAALPP----- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  908 QKLSLRYVVFGGEALELSRLEDWYSRHPhnAPKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNY 987
Cdd:TIGR01733  233 ALASLRLVILGGEALTPALVDRWRARGP--GARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDD 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  988 LQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPF-GKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIE 1066
Cdd:TIGR01733  311 LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390

                          410
                   ....*....|....*....
gi 1698252301 1067 LGEIEAVIMKHDKVEQVAV 1085
Cdd:TIGR01733  391 LGEIEAALLRHPGVREAVV 409
AMP-binding pfam00501
AMP-binding enzyme;
649-1061 4.32e-123

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 390.91  E-value: 4.32e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  649 FEKQAHINPNSIAV-VFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDY 727
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  728 PSDRISFMLHDAKPSCVLTNSSVEIE---------CDESLKILVDDVNVMEEIEKYSEENIDEM--ECLKPLAPSHIAYV 796
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgklEVVKLVLVLDRDPVLKEEPLPEEAKPADVppPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  797 IYTSGSTGRPKGVMIPHQNVVRLLGA----TDHWFQFDADDVWTMFHSYAFDFSV-WEIWGPLLYGGRLVVVPHTVSRSP 871
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 KEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgQKLSLRYVVFGGEALELSRLEDWYSRHPhnaPKVINMYGITETT 951
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA--LLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  952 VHVSYIELDEsiVSLRANSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgkpg 1030
Cdd:pfam00501  316 GVVTTPLPLD--EDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------ 387

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1698252301 1031 tRMYRTGDLARWRQDGTLDYIGRADHQIKIR 1061
Cdd:pfam00501  388 -GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 1257-1411 5.50e-31

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 122.11  E-value: 5.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1257 PLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHA 1336
Cdd:pfam00975    2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFE 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1337 MAAQLQNEGEEVELLVMLDSYPGHFLPNT-EAPTEEEALIALLALGGYDPDNMDGKPLTMESAVEILRKDGSALAS 1411
Cdd:pfam00975   82 VARRLERQGEAVRSLFLSDASAPHTVRYEaSRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALES 157
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1250-1405 1.83e-13

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 71.81  E-value: 1.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1250 RASGDQLPLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQ--ARGIAENEELPKSLEEMAADYlkhVREIQPH--GPYRLL 1325
Cdd:COG3208      1 PRPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQlpGRGDRLGEPPLTSLEELADDL---AEELAPLldRPFALF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1326 GWSLGGNVVHAMAAQLQNEGEEVELLVMLDSYPGHFLPNTEAPT---EEEALIALL-ALGGYDPDNMDGKPLtMESAVEI 1401
Cdd:COG3208     78 GHSMGALLAFELARRLERRGRPLPAHLFVSGRRAPHLPRRRRPLhdlSDAELLAELrRLGGTPEEVLADPEL-LELFLPI 156


                   ....
gi 1698252301 1402 LRKD 1405
Cdd:COG3208    157 LRAD 160
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1164-1234 3.18e-10

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: 58.03  E-value: 3.18e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301  1164 PRTPQEEMLCDLF-TEVLSV------SQIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERL 1234
Cdd:smart00823    5 PPAERRRLLLDLVrEQVAAVlghaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 1271-1384 1.46e-09

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 59.55  E-value: 1.46e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  1271 YAGLMKSLGTDYPIYGVQARGIAENEELPKSLEeMAADYLKH-VREIQPHGPYRLLGWSLGGNVVHAMAAQLQNEGEEVE 1349
Cdd:smart00824   15 YARLAAALRGRRDVSALPLPGFGPGEPLPASAD-ALVEAQAEaVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPA 93

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1698252301  1350 LLVMLDSY-PGHFLPNTEAPTEEEALIA------------LLALGGYD 1384
Cdd:smart00824   94 AVVLLDTYpPGDPAPEGWLPELLRGVFEredsfvpmddarLTAMGAYL 141
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 1258-1358 2.61e-03

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 41.34  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1258 LFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEEL-PKSLEEMAADYLKHVREiqphgPYRLLGWSLGGNVVHA 1336
Cdd:TIGR01738    7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFgPLSLADMAEAIAAQAPD-----PAIWLGWSLGGLVALH 81

                           90       100
                   ....*....|....*....|..
gi 1698252301 1337 MAAQLQnegEEVELLVMLDSYP 1358
Cdd:TIGR01738   82 IAATHP---DRVRALVTVASSP 100
 
Name Accession Description Interval E-value
PRK12467 PRK12467
peptide synthase; Provisional
 1-1244 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1164.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVrEDRPNDKRIIAYIV----AEEKEP-INLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:PRK12467   932 LLAQPGVREAVVLA-QPGDAGLQLVAYLVpaavADGAEHqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   76 KLPAPDFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTV 154
Cdd:PRK12467  1011 ALPKPDASAVQATFVApQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTL 1090

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  155 AELAKQLN-HAKSARPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETL 233
Cdd:PRK12467  1091 AGFAQAVAaQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESL 1170

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  234 RTIFPNVLGSSYQKILDMENLNLE---MVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIV 310
Cdd:PRK12467  1171 RTTFVQEDGRTRQVIHPVGSLTLEeplLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIV 1250

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  311 GDGWSLQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLL--GDEttpesliSTQLDFWKEELKGLPDQMELPT 388
Cdd:PRK12467  1251 SDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMdaGER-------ARQLAYWKAQLGGEQPVLELPT 1323

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  389 DYQRPVETSYRGETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLF 468
Cdd:PRK12467  1324 DRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFF 1403

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  469 VNTLVLRTNTSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPdleASL 548
Cdd:PRK12467  1404 VNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQL---PGL 1480

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  549 EIQSVG----SAKFDLTFEISESnevdgtPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVA 624
Cdd:PRK12467  1481 SVESLSwesqTAQFDLTLDTYES------SEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEA 1554

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  625 EKNTVLEKWNG-GFQIAPEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRS 703
Cdd:PRK12467  1555 ERRQILEGWNAtHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERS 1634

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  704 LNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSV--EIECDESLKILVDDvNVMEEIEKYSEENIDE 781
Cdd:PRK12467  1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLqaRLPLPDGLRSLVLD-QEDDWLEGYSDSNPAV 1713

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  782 MeclkpLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLV 861
Cdd:PRK12467  1714 N-----LAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLV 1788

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHNApkV 941
Cdd:PRK12467  1789 IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD---EQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTG--L 1863

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERF 1021
Cdd:PRK12467  1864 FNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERF 1943

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1022 IADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVrEDQPGDKRLVAYI 1101
Cdd:PRK12467  1944 VADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYV 2022

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1102 VASNNETIDTNE--------MRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEfiASSSSRGPRTPQEEM-- 1171
Cdd:PRK12467  2023 VPTDPGLVDDDEaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD--ASELQQAYVAPQSELeq 2100

                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1172 -LCDLFTEVLSVSQIGIDDGFFDLGGHSLLAVQLMSRMKEAlGVELNIGTLFAAPTVAGLAERLEIGNGQSALD 1244
Cdd:PRK12467  2101 rLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDGTVSID 2173
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 166-1389 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: 1149.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  166 SARPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSY 245
Cdd:COG1020      4 AAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  246 QKILDMENLNLEMVI-----TNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLT 320
Cdd:COG1020     84 QVIQPVVAAPLPVVVllvdlEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  321 RDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLLGDETTPEslistQLDFWKEELKGLPDQMELPTDYQRPVETSYRG 400
Cdd:COG1020    164 AELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELAR-----QLAYWRQQLAGLPPLLELPTDRPRPAVQSYRG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  401 ETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSG 480
Cdd:COG1020    239 ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  481 DPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSAKFDL 560
Cdd:COG1020    319 DPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  561 TFEISEsnevdgTPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGFQIA 640
Cdd:COG1020    399 TLTVVE------TGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPY 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  641 P-EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAG 719
Cdd:COG1020    473 PaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  720 YLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEIEC-DESLKILVDDVnvmEEIEKYSEENIDEmeclkPLAPSHIAYVIY 798
Cdd:COG1020    553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLpELGVPVLALDA---LALAAEPATNPPV-----PVTPDDLAYVIY 624

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLL 878
Cdd:COG1020    625 TSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELL 704

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSAFYQLMQADREneevgQKLSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVHVSYIE 958
Cdd:COG1020    705 ARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLPG--ARLVNLYGPTETTVDSTYYE 777

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  959 LDESIVSlRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGD 1038
Cdd:COG1020    778 VTPPDAD-GGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGD 856

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1039 LARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHA 1118
Cdd:COG1020    857 LARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL 936

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1119 SGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSSRGPRTPQEEMLCDLFTEVLSVSQIGIDDGFFDLGGHS 1198
Cdd:COG1020    937 ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLG 1016

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1199 LLAVQLMsRMKEALGVELNIGTLFAAPTVAGLAERLEIGNGQSALDVLLPLRASGDQLPLFCVHPAGGLSWCYAGLMKSL 1278
Cdd:COG1020   1017 LLLLLAL-ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLAL 1095

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1279 GTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHAMAAQLQNEGEEVELLVMLDSYP 1358
Cdd:COG1020   1096 LALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLL 1175

                         1210      1220      1230
                   ....*....|....*....|....*....|.
gi 1698252301 1359 GHFLPNTEAPTEEEALIALLALGGYDPDNMD 1389
Cdd:COG1020   1176 LLALLLLALLLLLLLLLLLLLLLLLLLLLLL 1206
PRK12467 PRK12467
peptide synthase; Provisional
 169-1258 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 997.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  169 PAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKI 248
Cdd:PRK12467    39 PIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVI 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  249 LDMENLNLEMVITNTCKDE-----LESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDF 323
Cdd:PRK12467   119 DASLSLTIPLDDLANEQGRaresqIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEEL 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  324 TAAYKARCQGDRVQLETLPVQYADYALWQQQLL--GDEttpesliSTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGE 401
Cdd:PRK12467   199 VQLYSAYSQGREPSLPALPIQYADYAIWQRSWLeaGER-------ERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGA 271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  402 TIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGD 481
Cdd:PRK12467   272 RLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQ 351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  482 PSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFN--APDLEAsLEIQSVG----S 555
Cdd:PRK12467   352 ASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATGGRDreGAQLPG-LTVEELSwarhT 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  556 AKFDLTFEISESnevdgtPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNG 635
Cdd:PRK12467   431 AQFDLALDTYES------AQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNA 504

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  636 GFQIAPEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLK 715
Cdd:PRK12467   505 PATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLK 584

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  716 AGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEIECD--ESLKILVDDvNVMEEIEKYSEENIDemeclKPLAPSHI 793
Cdd:PRK12467   585 AGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpAGLRSLCLD-EPADLLCGYSGHNPE-----VALDPDNL 658

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  794 AYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKE 873
Cdd:PRK12467   659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEA 738

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  874 FLQLLVKEKVTVLNQTPSAFYQLMQADReneeVGQKLSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVH 953
Cdd:PRK12467   739 FAALMADQGVTVLKIVPSHLQALLQASR----VALPRPQRALVCGGEALQVDLLARVRALGPG--ARLINHYGPTETTVG 812

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  954 VSYIEL-DESIVSlrANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTR 1032
Cdd:PRK12467   813 VSTYELsDEERDF--GNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGR 890

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1033 MYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQvAVIVREDQPGDKRLVAYIVA-----SNNE 1107
Cdd:PRK12467   891 LYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE-AVVLAQPGDAGLQLVAYLVPaavadGAEH 969

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1108 TIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSS-RGPRTPQEEMLCDLFTEVLSVSQIG 1186
Cdd:PRK12467   970 QATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATfVAPQTELEKRLAAIWADVLKVERVG 1049

                         1050      1060      1070      1080      1090      1100      1110
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1187 IDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLeiGNGQSALDVLLPLRASGDQLPL 1258
Cdd:PRK12467  1050 LTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAV--AAQQQGAQPALPDVDRDQPLPL 1119
PRK12316 PRK12316
peptide synthase; Provisional
 169-1231 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 909.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  169 PAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKI 248
Cdd:PRK12316    39 PIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQV 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  249 LDMENLNLEMV-ITNTCKDELESVLSEAVRYS----FNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDF 323
Cdd:PRK12316   119 PLDRPLEVEFEdCSGLPEAEQEARLRDEAQREslqpFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEF 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  324 TAAYKARCQGDRVQLETLPVQYADYALWQQQLL--GDEttpesliSTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGE 401
Cdd:PRK12316   199 SRFYSAYATGAEPGLPALPIQYADYALWQRSWLeaGEQ-------ERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGS 271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  402 TIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGD 481
Cdd:PRK12316   272 RYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGR 351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  482 PSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTP---EATFNAPDLE-ASLEIQSvGSAK 557
Cdd:PRK12316   352 TRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVadiEALDTVAGLEfGQLEWKS-RTTQ 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  558 FDLTFEISEsnevdgTPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGF 637
Cdd:PRK12316   431 FDLTLDTYE------KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATA 504

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  638 QIAPEMT-LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKA 716
Cdd:PRK12316   505 AEYPLQRgVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKA 584

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  717 GAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEIECDESLKILVDDVN-VMEEIEKYSEENIDEMeclkpLAPSHIAY 795
Cdd:PRK12316   585 GGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDrPAAWLEGYSEENPGTE-----LNPENLAY 659

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  796 VIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFL 875
Cdd:PRK12316   660 VIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLV 739

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  876 QLLVKEKVTVLNQTPSafyqLMQADRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHNapKVINMYGITETTVHVS 955
Cdd:PRK12316   740 ELINREGVDTLHFVPS----MLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQA--GLYNLYGPTEAAIDVT 813

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  956 YieldESIVSLRANSL-IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKpGTRMY 1034
Cdd:PRK12316   814 H----WTCVEEGGDSVpIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMY 888

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1035 RTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQpgdkRLVAYIVASNNETIDTNEM 1114
Cdd:PRK12316   889 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGK----QLVGYVVLESEGGDWREAL 964

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1115 RQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEfiASSSSRG---PRTPQEEMLCDLFTEVLSVSQIGIDDGF 1191
Cdd:PRK12316   965 KAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPE--ASVAQQGyvaPRNALERTLAAIWQDVLGVERVGLDDNF 1042

                         1050      1060      1070      1080
                   ....*....|....*....|....*....|....*....|
gi 1698252301 1192 FDLGGHSLLAVQLMSRMKEAlGVELNIGTLFAAPTVAGLA 1231
Cdd:PRK12316  1043 FELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLA 1081
PRK12316 PRK12316
peptide synthase; Provisional
 1-1250 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 904.33  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVmVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:PRK12316  2423 LQAHPAVREAVV-VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKP 2501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   81 DFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAK 159
Cdd:PRK12316  2502 DVSQLRQAYVApQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAA 2581

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  160 QLNHAKSAR-PAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFP 238
Cdd:PRK12316  2582 SLESGQTSRaPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFV 2661

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  239 NVLGSSYQKILDMENLNLEMVITNTCKDE-LESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQ 317
Cdd:PRK12316  2662 EVGEQTRQVILPNMSLRIVLEDCAGVADAaIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQ 2741

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  318 PLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLLgdettPESLISTQLDFWKEELKGLPDQMELPTDYQRPVETS 397
Cdd:PRK12316  2742 VMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWM-----DSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQS 2816

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  398 YRGETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTN 477
Cdd:PRK12316  2817 HRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQ 2896

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  478 TSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSAK 557
Cdd:PRK12316  2897 VDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQ 2976

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  558 FDLTFEISESnevdgtPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGF 637
Cdd:PRK12316  2977 FDLALDTWES------AEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATA 3050

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  638 QIAP-EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKA 716
Cdd:PRK12316  3051 AEYPlERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKA 3130

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  717 GAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEIECDESLKILVDDvnvmEEIEKYSEENIDEMeclkpLAPSHIAYV 796
Cdd:PRK12316  3131 GGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLD----RGDENYAEANPAIR-----TMPENLAYV 3201

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  797 IYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQ 876
Cdd:PRK12316  3202 IYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVE 3281

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  877 LLVKEKVTVLNQTPSafyqLMQADRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPhnapkVINMYGITETTVHVSY 956
Cdd:PRK12316  3282 LINSEGVDVLHAYPS----MLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP-----LYNLYGPTEATITVTH 3352

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  957 IELDESIVslrANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgKPGTRMYRT 1036
Cdd:PRK12316  3353 WQCVEEGK---DAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRT 3428

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1037 GDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQpgdkRLVAYIVASNNETIDTNEMRQ 1116
Cdd:PRK12316  3429 GDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREALKA 3504

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1117 HASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEfiASSSSRG---PRTPQEEMLCDLFTEVLSVSQIGIDDGFFD 1193
Cdd:PRK12316  3505 HLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPD--AALLQQDyvaPVNELERRLAAIWADVLKLEQVGLTDNFFE 3582

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1194 LGGHSLLAVQLMSRMKEAlGVELNIGTLFAAPTVAGLAERLEIGNGQ-------SALDVLLPLR 1250
Cdd:PRK12316  3583 LGGDSIISLQVVSRARQA-GIRFTPKDLFQHQTIQGLARVARVGGGVavdqgpvSGETLLLPIQ 3645
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
178-1502 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 869.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  178 NEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKI--------L 249
Cdd:PRK10252     6 QHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVdpaltfplP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  250 DMENLNLEMVITNTCKDELESVLSEAVRysfnLD-FEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYK 328
Cdd:PRK10252    86 EIIDLRTQPDPHAAAQALMQADLQQDLR----VDsGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYC 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  329 ARCQGDRVQLETLPVQ---YADYALWQQqllgDETTpeslistQLD--FWKEELKGLPDQMELPtdyqrPVETSYRGETI 403
Cdd:PRK10252   162 AWLRGEPTPASPFTPFadvVEEYQRYRA----SEAW-------QRDaaFWAEQRRQLPPPASLS-----PAPLPGRSASA 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  404 HFH-----IDEGMHSRLVelGRKNGVSLFMVLQAgLSALF-TRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTN 477
Cdd:PRK10252   226 DILrlkleFTDGAFRQLA--AQASGVQRPDLALA-LVALWlGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVH 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  478 TSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVR-TRNSH-PLFQVMLaFQNTPEAtfnaPDLEASLEIQSVGS 555
Cdd:PRK10252   303 IAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAgDEPLFgPVLNIKV-FDYQLDF----PGVQAQTHTLATGP 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  556 AKfDLTFEISesneVDGtPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKnTVLEKWNG 635
Cdd:PRK10252   378 VN-DLELALF----PDE-HGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNA 450

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  636 GFQIAPEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLK 715
Cdd:PRK10252   451 TAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  716 AGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSveiecdesLKILVDDVNVMEEIEKYSEENIDEMECLKPLAPSHIAY 795
Cdd:PRK10252   531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD--------QLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAY 602

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  796 VIYTSGSTGRPKGVMIPHQNVV-RLLGATDHwFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEF 874
Cdd:PRK10252   603 IIFTSGSTGRPKGVMVGQTAIVnRLLWMQNH-YPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAM 681

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  875 LQLLVKEKVTVLNQTPS---AFyqLMQADRENEeVGQKLSLRYVVFGGEALELSRLEDWYSRHphNAPkVINMYGITETT 951
Cdd:PRK10252   682 QQFFAEYGVTTTHFVPSmlaAF--VASLTPEGA-RQSCASLRQVFCSGEALPADLCREWQQLT--GAP-LHNLYGPTEAA 755

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  952 VHVSYIELD-ESIVSLRANSL-IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkP 1029
Cdd:PRK10252   756 VDVSWYPAFgEELAAVRGSSVpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-P 834

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1030 GTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAV-----IVREDQPGD-KRLVAYIVA 1103
Cdd:PRK10252   835 GERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacviNQAAATGGDaRQLVGYLVS 914

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1104 SNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSSRGPRTPQEEMLCDLFTEVLSVS 1183
Cdd:PRK10252   915 QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCD 994

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1184 QIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERL---EIGNGQSALDVLLPLRaSGDQLPLFC 1260
Cdd:PRK10252   995 VVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLdaeEDESRRLGFGTILPLR-EGDGPTLFC 1073

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1261 VHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHAMAAQ 1340
Cdd:PRK10252  1074 FHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAAR 1153

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1341 LQNEGEEVELLVMLDSYPghflPNTEAPTEEEAliallalGGYDPDNMDGKPLTMESAVEILRkdgsalASLEEETILNL 1420
Cdd:PRK10252  1154 LRARGEEVAFLGLLDTWP----PETQNWREKEA-------NGLDPEVLAEIDREREAFLAAQQ------GSLSTELFTTI 1216

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1421 KETYVNSVGLLGKYVPKVYNGDILFFRST-VIPDWFDPisPNTWLNYLdGDIVQHDIDCRHKDLCQPGPLTEIGQVLAKY 1499
Cdd:PRK10252  1217 EGNYADAVRLLTTAHSVPFDGKATLFVAErTLQEGMSP--EQAWSPWI-AELDVYRQDCAHVDIISPEAFEKIGPILRAT 1293


                   ...
gi 1698252301 1500 LQN 1502
Cdd:PRK10252  1294 LNE 1296
PRK05691 PRK05691
peptide synthase; Validated
 7-1231 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 841.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    7 IQQAVVMVREDrPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAPDFNgmN 86
Cdd:PRK05691  1553 VAQAAVLVREG-AAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ--Q 1629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   87 NERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAKQLNHAK 165
Cdd:PRK05691  1630 REHVEpRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQ 1709

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  166 SA-----RPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNV 240
Cdd:PRK05691  1710 AAgernsQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSV 1789

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  241 LGSSYQKI-----LDMENLNLEMVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWS 315
Cdd:PRK05691  1790 DGVPVQQVaedsgLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWA 1869

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  316 LQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLL-GDETtpesliSTQLDFWKEELKGLPDQMELPTDYQRPV 394
Cdd:PRK05691  1870 MDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLeSGER------QRQLDYWKAQLGNEHPLLELPADRPRPP 1943

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  395 ETSYRGETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVL 474
Cdd:PRK05691  1944 VQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVL 2023

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  475 RTNTSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVML-----AFQNTPEATfnapDLEASLE 549
Cdd:PRK05691  2024 RCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCnvqrwEFQQSRQLA----GMTVEYL 2099

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  550 IQSVGSAKFDLTFEISEsneVDGTpngLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTV 629
Cdd:PRK05691  2100 VNDARATKFDLNLEVTD---LDGR---LGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQL 2173

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  630 LEKWNG-GFQIAPEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVV 708
Cdd:PRK05691  2174 LDSLAGeAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVV 2253

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  709 SLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEiecdESLKILVDDVN--VMEE----IEKYSEENIDEM 782
Cdd:PRK05691  2254 GLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALF----EALGELPAGVArwCLEDdaaaLAAYSDAPLPFL 2329

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  783 EclkplAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRlVV 862
Cdd:PRK05691  2330 S-----LPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGAR-VV 2403

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  863 VPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQ--ADReneevGQKLSLRYVVFGGEAL---ELSRLEDWYsrhphn 937
Cdd:PRK05691  2404 LRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQwlAGQ-----GEQLPVRMCITGGEALtgeHLQRIRQAF------ 2472

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  938 APKVI-NMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGL 1016
Cdd:PRK05691  2473 APQLFfNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGL 2552

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1017 TAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQvAVIVREDQPGDKR 1096
Cdd:PRK05691  2553 TAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQ 2631

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1097 LVAYIV----ASNNETIDT--NEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEF-IASSSSRGPRTPQE 1169
Cdd:PRK05691  2632 LAGYLVsavaGQDDEAQAAlrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPeLNRQAYQAPRSELE 2711

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1170 EMLCDLFTEVLSVSQIGIDDGFFDLGGHSLLAVQLMSRMKEaLGVELNIGTLFAAPTVAGLA 1231
Cdd:PRK05691  2712 QQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQTLA 2772
PRK05691 PRK05691
peptide synthase; Validated
 41-1235 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 815.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   41 IRSYVSEslANYMIPSAFVVLE--ELPLTPNGKVDRK---------------KLPAPDFNGMNNERVARNPKEEILCDLF 103
Cdd:PRK05691   518 IRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKLQRSacrlrladgsldsyaLFPALQAVEAAQTAASGDELQARIAAIW 595

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  104 AEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTV----AELAKQLNHAKSARPAIQKASRPNE 179
Cdd:PRK05691   596 CEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLaafsAAVARQLAGGGAAQAAIARLPRGQA 675

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  180 VPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEMV 259
Cdd:PRK05691   676 LPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRI 755

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  260 -ITNTCKDELES----VLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGD 334
Cdd:PRK05691   756 dLSDLPEAEREAraaqIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQ 835

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  335 RVQLETLPVQYADYALWQQQLLGDETTpesliSTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSR 414
Cdd:PRK05691   836 TAELAPLPLGYADYGAWQRQWLAQGEA-----ARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEA 910

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  415 LVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQV 494
Cdd:PRK05691   911 LRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQA 990

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  495 NLAAYENQDVPFERLVEVLNPVRtrnSHPLFQVMLAFQN-TPEATFNAPDLEASLEIQSVGSAKFDLTFEISESNevdgt 573
Cdd:PRK05691   991 TLGAQAHQDLPFEQLVEALPQAR---EQGLFQVMFNHQQrDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDR----- 1062

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  574 pNGLHGL-LEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEkWNGGFQIAPEMTLPQLFEKQ 652
Cdd:PRK05691  1063 -NGRLTLsFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQ-WGQAPCAPAQAWLPELLNEQ 1140

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRI 732
Cdd:PRK05691  1141 ARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERL 1220

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  733 SFMLHDAKPSCVLTNSSveiecdeslkiLVDDvnvMEEIEKYSEENIDEMECLK-PLAP-------SHIAYVIYTSGSTG 804
Cdd:PRK05691  1221 AYMLADSGVELLLTQSH-----------LLER---LPQAEGVSAIALDSLHLDSwPSQApglhlhgDNLAYVIYTSGSTG 1286

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNVVRLLgatdHWFQ----FDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVK 880
Cdd:PRK05691  1287 QPKGVGNTHAALAERL----QWMQatyaLDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQ 1362

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  881 EKVTVLNQTPSafyqLMQADRENEEVGQKLSLRYVVFGGEALElSRLEDwysRHPHNAPKVI--NMYGITETTVHVSYIE 958
Cdd:PRK05691  1363 YGVTTLHFVPP----LLQLFIDEPLAAACTSLRRLFSGGEALP-AELRN---RVLQRLPQVQlhNRYGPTETAINVTHWQ 1434

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  959 LDesiVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGD 1038
Cdd:PRK05691  1435 CQ---AEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGD 1511

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1039 LARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGdKRLVAYIVASNNETIDTNEMRQHA 1118
Cdd:PRK05691  1512 RARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTGEAGQEAEAERLKAAL 1590

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1119 SGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAP-----EFIAssssrgPRTPQEEMLCDLFTEVLSVSQIGIDDGFFD 1193
Cdd:PRK05691  1591 AAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPvwqqrEHVE------PRTELQQQIAAIWREVLGLPRVGLRDDFFA 1664

                         1210      1220      1230      1240
                   ....*....|....*....|....*....|....*....|..
gi 1698252301 1194 LGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLE 1235
Cdd:PRK05691  1665 LGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVA 1706
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 657-1150 0e+00

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


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 765.70  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd17643     81 ADSGPSLLLTD------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANV 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd17643    119 LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQL 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 MQADRENEEvgQKLSLRYVVFGGEALELSRLEDWYSRHPHNAPKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSI 976
Cdd:cd17643    199 VEAADRDGR--DPLALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPL 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADH 1056
Cdd:cd17643    277 PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADE 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1057 QIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNE 1136
Cdd:cd17643    357 QVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDA 436

                          490
                   ....*....|....
gi 1698252301 1137 LPLTPNGKLDRKAL 1150
Cdd:cd17643    437 LPLTVNGKLDRAAL 450
PRK12467 PRK12467
peptide synthase; Provisional
 181-1358 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 763.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGiLNRQALQGAFYDVVEKHETLRTIFpnVLGSSYQKILDMENLNLEMVI 260
Cdd:PRK12467  2648 PLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGF--LWDGELEEPLQVVYKQARLPF 2724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  261 TN-------TCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQG 333
Cdd:PRK12467  2725 SRldwrdraDLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQPPP 2804

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 DRVQLetlpvqYADYALWQQQLLGDETTPeslistqldFWKEELKGLPDQMEL-PTDYQRPVETSYRGETIHFHIDEGMH 412
Cdd:PRK12467  2805 AREGR------YRDYIAWLQAQDAEASEA---------FWKEQLAALEEPTRLaRALYPAPAEAVAGHGAHYLHLDATQT 2869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  413 SRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDV--LSDIVGLFVNTLVLRTNTSGDPSFKELLNR 490
Cdd:PRK12467  2870 RQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLrgAEQQLGLFINTLPVIASPRAEQTVSDWLQQ 2949

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  491 VKQVNLAAYENQDVPferLVEVlNPVRTRNSHPLFQVMLAFQNTPeatfnapdLEASLEiqsvGSAKFDLTFEISESNEV 570
Cdd:PRK12467  2950 VQAQNLALREFEHTP---LADI-QRWAGQGGEALFDSILVFENYP--------ISEALK----QGAPSGLRFGAVSSREQ 3013

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  571 DGTPNGLH-GL-----LEFSTD--LYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGFQIAP- 641
Cdd:PRK12467  3014 TNYPLTLAvGLgdtleLEFSYDrqHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPs 3093

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PRK12467  3094 ERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFMLHDAKPSCVLTNSSVEiecdESLKILVDDVNVMEE---IEKYSEENIDEMeclkpLAPSHIAYVIY 798
Cdd:PRK12467  3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLL----EQLPAPAGDTALTLDrldLNGYSENNPSTR-----VMGENLAYVIY 3244

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVsRSPKEFLQLL 878
Cdd:PRK12467  3245 TSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAI 3323

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSAfyqlMQADRENEEVGQKLSLRYVVFGGEALELSRLEDwYSRHPHNApKVINMYGITETTVHVSYIE 958
Cdd:PRK12467  3324 HAHRISIACFPPAY----LQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQ-VKRKLKPR-GLTNGYGPTEAVVTVTLWK 3397

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  959 LDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGD 1038
Cdd:PRK12467  3398 CGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGD 3477

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1039 LARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGdKRLVAYIVASNNETIDTNEMRQHA 1118
Cdd:PRK12467  3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQGDWRETLRDHL 3556

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1119 SGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSSRGPRTPQEEMLCDLFTEVLSVSQIGIDDGFFDLGGHS 1198
Cdd:PRK12467  3557 AASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDS 3636

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1199 LLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLeiGNGQSALDVLLPLRASGDQLP-LFCVHPAGGLSWCYAGLMKS 1277
Cdd:PRK12467  3637 LLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS--PLGDVPVNLLLDLNRLETGFPaLFCRHEGLGTVFDYEPLAVI 3714

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1278 LGTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHAMAAQLQNEGEEVELLVMLDSY 1357
Cdd:PRK12467  3715 LEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNT 3794


                   .
gi 1698252301 1358 P 1358
Cdd:PRK12467  3795 L 3795
PRK12316 PRK12316
peptide synthase; Provisional
 181-1244 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 723.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGiLNRQALQGAFYDVVEKHETLRTIF--PNVLGSSYQ---KILDMENLN 255
Cdd:PRK12316  4104 PLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvwQGELGRPLQvvhKQVSLPFAE 4182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  256 LEMVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARcqgdr 335
Cdd:PRK12316  4183 LDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGR----- 4257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  336 vQLETLPVQYADYALWQQQllGDETTPESlistqldFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFH-IDEGMHSR 414
Cdd:PRK12316  4258 -PPAQPGGRYRDYIAWLQR--QDAAASEA-------FWREQLAALDEPTRLAQAIARADLRSANGYGEHVReLDATATAR 4327

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  415 LVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVL--SDIVGLFVNTLVLRTNTSGDPSFKELLNRVK 492
Cdd:PRK12316  4328 LREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPgiEGQIGLFINTLPVIATPRAQQSVVEWLQQVQ 4407

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  493 QVNLAAYENQDVPFERLvevlNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGS-----AKFDLTFEISES 567
Cdd:PRK12316  4408 RQNLALREHEHTPLYEI----QRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNheqtnYPLTLAVGLGET 4483

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  568 NEVDgtpnglhglLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWN---GGFQIAPemT 644
Cdd:PRK12316  4484 LSLQ---------FSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNrtdAGYPATR--C 4552

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:PRK12316  4553 VHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLD 4632

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVLTNS--SVEIECDESLKILVDDVNvmEEIEKYSEENIdemecLKPLAPSHIAYVIYTSGS 802
Cdd:PRK12316  4633 PEYPRERLAYMMEDSGAALLLTQShlLQRLPIPDGLASLALDRD--EDWEGFPAHDP-----AVRLHPDNLAYVIYTSGS 4705

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  803 TGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSrSPKEFLQLLVKEK 882
Cdd:PRK12316  4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHR 4784

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  883 VTVLNQTPSAFYQLMQADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRHPHNApkVINMYGITETTVHVSYIELDES 962
Cdd:PRK12316  4785 VTVLVFPPVYLQQLAEHAERDGEPP---SLRVYCFGGEAVAQASYDLAWRALKPVY--LFNGYGPTETTVTVLLWKARDG 4859

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  963 IVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARW 1042
Cdd:PRK12316  4860 DACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARY 4939

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQvAVIVREDQPGDKRLVAYIVASNNETIDT--------NEM 1114
Cdd:PRK12316  4940 RADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE-AVVIAQEGAVGKQLVGYVVPQDPALADAdeaqaelrDEL 5018

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1115 RQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEfiASSSSRG---PRTPQEEMLCDLFTEVLSVSQIGIDDGF 1191
Cdd:PRK12316  5019 KAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPD--ASLLQQAyvaPRSELEQQVAAIWAEVLQLERVGLDDNF 5096

                         1050      1060      1070      1080      1090
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1192 FDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLEIGNGQSALD 1244
Cdd:PRK12316  5097 FELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK 5149
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 179-611 0e+00

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: 713.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEM 258
Cdd:cd19538      1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  259 VITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDRVQL 338
Cdd:cd19538     81 EIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPEL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  339 ETLPVQYADYALWQQQLLGDETTPESLISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSRLVEL 418
Cdd:cd19538    161 APLPVQYADYALWQQELLGDESDPDSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  419 GRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVNLAA 498
Cdd:cd19538    241 AKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  499 YENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSAKFDLTFEISESNEvDGTPNGLH 578
Cdd:cd19538    321 YEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREQYN-DGTPNGIE 399

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1698252301  579 GLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19538    400 GFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 180-611 0e+00

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: 647.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  180 VPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEMV 259
Cdd:cd19540      2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  260 ITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDRVQLE 339
Cdd:cd19540     82 VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  340 TLPVQYADYALWQQQLLGDETTPESLISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSRLVELG 419
Cdd:cd19540    162 PLPVQYADYALWQRELLGDEDDPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  420 RKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVNLAAY 499
Cdd:cd19540    242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  500 ENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSAKFDLTFEISESNEVDGTPNGLHG 579
Cdd:cd19540    322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDADGAPAGLTG 401

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1698252301  580 LLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19540    402 ELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
PRK12316 PRK12316
peptide synthase; Provisional
 181-1255 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 635.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGiLNRQALQGAFYDVVEKHETLRTIFPNV--LGSSYQKILDMENLNLEM 258
Cdd:PRK12316  1558 PLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQdgLEQPLQVIHKQVELPFAE 1636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  259 VITNTCKDELESV--LSEAVRYS-FNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDR 335
Cdd:PRK12316  1637 LDWRGREDLGQALdaLAQAERQKgFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAP 1716

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  336 VQletlpvQYADYALWQQQllGDETTPESlistqldFWKEELKGLPDQMELPTDYQRPVETSYRGEtiHFH-IDEGMHSR 414
Cdd:PRK12316  1717 GG------RYRDYIAWLQR--QDAAASEA-------FWKEQLAALEEPTRLAQAARTEDGQVGYGD--HQQlLDPAQTRA 1779

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  415 LVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDvLSDI---VGLFVNTLVLRTNTSGDPSFKELLNRV 491
Cdd:PRK12316  1780 LAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAE-LPGIeqqIGLFINTLPVIAAPRPDQSVADWLQEV 1858

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  492 KQVNLAAYENQDVPferLVEVlNPVRTRNSHPLFQVMLAFQNTPEAtfnapdlEAsLEiqsvGSAKFDLTFEISESNEVD 571
Cdd:PRK12316  1859 QALNLALREHEHTP---LYDI-QRWAGQGGEALFDSLLVFENYPVA-------EA-LK----QGAPAGLVFGRVSNHEQT 1922

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  572 GTPNGLH-GL-----LEFSTDL--YKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGFQIAP-E 642
Cdd:PRK12316  1923 NYPLTLAvTLgetlsLQYSYDRghFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPrG 2002

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK12316  2003 PGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNSSV--EIECDESLKILvdDVNVMEEIEKYSEENIdemecLKPLAPSHIAYVIYTS 800
Cdd:PRK12316  2083 LDPNYPAERLAYMLEDSGAALLLTQRHLleRLPLPAGVARL--PLDRDAEWADYPDTAP-----AVQLAGENLAYVIYTS 2155

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  801 GSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVsRSPKEFLQLLVK 880
Cdd:PRK12316  2156 GSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDEL-WDPEQLYDEMER 2234

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  881 EKVTVLNQTPSAFYQLMQadrENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPhnAPKVINMYGITETTVHVSYIELD 960
Cdd:PRK12316  2235 HGVTILDFPPVYLQQLAE---HAERDGRPPAVRVYCFGGEAVPAASLRLAWEALR--PVYLFNGYGPTEAVVTPLLWKCR 2309

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  961 ESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLA 1040
Cdd:PRK12316  2310 PQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLA 2389

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1041 RWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQvAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASG 1120
Cdd:PRK12316  2390 RYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE-AVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAA 2468

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1121 SLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEF-IASSSSRGPRTPQEEMLCDLFTEVLSVSQIGIDDGFFDLGGHSL 1199
Cdd:PRK12316  2469 RLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVsQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSL 2548

                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1200 LAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLEIGNGQSALDVL-----LPLRASGDQ 1255
Cdd:PRK12316  2549 LATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQkvtrvQPLPLSHAQ 2609
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 657-1150 0e+00

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


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 629.56  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd05930     81 EDSGAKLVLTD------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGL 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd05930    119 VNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLL 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 MQADreneEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVHVSYIELDESIVSLRANSlIGCSI 976
Cdd:cd05930    199 LQEL----ELAALPSLRLVLVGGEALPPDLVRRWRELLPG--ARLVNLYGPTEATVDATYYRVPPDDEEDGRVP-IGRPI 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARWRQDGTLDYIGRADH 1056
Cdd:cd05930    272 PNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDD 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1057 QIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNE 1136
Cdd:cd05930    351 QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDA 430

                          490
                   ....*....|....
gi 1698252301 1137 LPLTPNGKLDRKAL 1150
Cdd:cd05930    431 LPLTPNGKVDRKAL 444
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 647-1150 0e+00

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: 583.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  647 QLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPD 726
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  727 YPSDRISFMLHDAKPSCVLTNSSVEiecdESLKILVDDVNVMEEIEKYSEENIDEmeclkPLAPSHIAYVIYTSGSTGRP 806
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLA----GRAGGLEVAVVIDEALDAGPAGNPAV-----PVSPDDLAYVMYTSGSTGRP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  807 KGVMIPHQNVVRLLGATDhWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVL 886
Cdd:cd12117    152 KGVAVTHRGVVRLVKNTN-YVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  887 NQTPSAFYQLMQADRENEEvgqklSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVHVSYIELDEsiVSL 966
Cdd:cd12117    231 WLTAALFNQLADEDPECFA-----GLRELLTGGEVVSPPHVRRVLAACPG--LRLVNGYGPTENTTFTTSHVVTE--LDE 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  967 RANSL-IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARWRQD 1045
Cdd:cd12117    302 VAGSIpIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPD 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1046 GTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsnNETIDTNEMRQHASGSLPDY 1125
Cdd:cd12117    381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA--EGALDAAELRAFLRERLPAY 458

                          490       500
                   ....*....|....*....|....*
gi 1698252301 1126 MVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd12117    459 MVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 657-1151 0e+00

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: 569.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd17652     81 ADARPALLLTT------------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGL 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd17652    119 ANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 mqadreneEVGQKLSLRYVVFGGEALELSRLEDWYSRHphnapKVINMYGITETTVHVSYIELDESivslRANSLIGCSI 976
Cdd:cd17652    199 --------PPDDLPDLRTLVVAGEACPAELVDRWAPGR-----RMINAYGPTETTVCATMAGPLPG----GGVPPIGRPV 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADH 1056
Cdd:cd17652    262 PGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADD 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1057 QIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNE 1136
Cdd:cd17652    342 QVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDA 421

                          490
                   ....*....|....*
gi 1698252301 1137 LPLTPNGKLDRKALP 1151
Cdd:cd17652    422 LPLTPNGKLDRRALP 436
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 649-1151 0e+00

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: 563.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  649 FEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYP 728
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  729 SDRISFMLHDAKPSCVLTNSsveiecDESLKILVDDVNVMEeIEKYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKG 808
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHP------ALAGELAVELVAVTL-LDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKG 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  809 VMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQ 888
Cdd:cd17651    154 VVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFL 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  889 TPSAFYQLMQADRENEEVGQklSLRYVVFGGEALEL-SRLEDWYSRHPHnaPKVINMYGITETTVhVSYIELDESIVSLR 967
Cdd:cd17651    234 PTVALRALAEHGRPLGVRLA--ALRYLLTGGEQLVLtEDLREFCAGLPG--LRLHNHYGPTETHV-VTALSLPGDPAAWP 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  968 ANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARWRQDGT 1047
Cdd:cd17651    309 APPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGE 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1048 LDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMV 1127
Cdd:cd17651    388 LEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMV 467

                          490       500
                   ....*....|....*....|....
gi 1698252301 1128 PYAFVVVNELPLTPNGKLDRKALP 1151
Cdd:cd17651    468 PSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 647-1154 3.00e-179

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: 543.46  E-value: 3.00e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  647 QLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPD 726
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  727 YPSDRISFMLHDAKPSCVLTNSSVEI-ECDESLKILVDDvnvmEEIEKYSEENIDemeclKPLAPSHIAYVIYTSGSTGR 805
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQSHLQPpIAFIGLIDLLDE----DTIYHEESENLE-----PVSKSDDLAYVIYTSGSTGK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  806 PKGVMIPHQNVVRL-LGATDHWFQFDADDVwTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVT 884
Cdd:cd17655    152 PKGVMIEHRGVVNLvEWANKVIYQGEHLRV-ALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRIT 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  885 VLNQTPSAFYQLMQADreneeVGQKLSLRYVVFGGEALELSRLEDWYSRHPHNaPKVINMYGITETTVHVSYIELDESIV 964
Cdd:cd17655    231 IIDLTPAHLKLLDAAD-----DSEGLSLKHLIVGGEALSTELAKKIIELFGTN-PTITNAYGPTETTVDASIYQYEPETD 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  965 SlRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgKPGTRMYRTGDLARWRQ 1044
Cdd:cd17655    305 Q-QVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLP 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1045 DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNetIDTNEMRQHASGSLPD 1124
Cdd:cd17655    383 DGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQLREFLARELPD 460

                          490       500       510
                   ....*....|....*....|....*....|
gi 1698252301 1125 YMVPYAFVVVNELPLTPNGKLDRKALPAPE 1154
Cdd:cd17655    461 YMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 646-1150 2.47e-178

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: 541.10  E-value: 2.47e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  646 PQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDP 725
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  726 DYPSDRISFMLHDAKPSCVLTNSsveiecDESLKILVDDVNVMEEIEKYSEENIDEMEclKPLAPSHIAYVIYTSGSTGR 805
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPL--VPPRPDNLAYVIYTSGSTGR 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  806 PKGVMIPHQNVV-RLLGATDHwFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVT 884
Cdd:cd17646    153 PKGVMVTHAGIVnRLLWMQDE-YPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVT 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  885 VLNQTPSAFYQLMQADReneeVGQKLSLRYVVFGGEALELSRLEDWYSRhPHnAPKViNMYGITETTVHVSYIELDESIV 964
Cdd:cd17646    232 TCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARFLAL-PG-AELH-NLYGPTEAAIDVTHWPVRGPAE 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  965 SLRAnsLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARWRQ 1044
Cdd:cd17646    305 TPSV--PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRP 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1045 DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASN-NETIDTNEMRQHASGSLP 1123
Cdd:cd17646    382 DGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgAAGPDTAALRAHLAERLP 461

                          490       500
                   ....*....|....*....|....*..
gi 1698252301 1124 DYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd17646    462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 657-1150 3.74e-176

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: 534.56  E-value: 3.74e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNSsveiECDESLKILVDDVNVMEEIEKYSEENIDEmeclkPLAPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd12116     81 EDAEPALVLTDD----ALPDRLPAGLPVLLLALAAAAAAPAAPRT-----PVSPDDLAYVIYTSGSTGRPKGVVVSHRNL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd12116    152 VNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRML 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 MQADRENEEvgqklSLRYVVfGGEALELSRLEDWYSRhphnAPKVINMYGITETTVHVSYIELDESIVSLRanslIGCSI 976
Cdd:cd12116    232 LDAGWQGRA-----GLTALC-GGEALPPDLAARLLSR----VGSLWNLYGPTETTIWSTAARVTAAAGPIP----IGRPL 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADH 1056
Cdd:cd12116    298 ANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADG 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1057 QIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDqPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNE 1136
Cdd:cd12116    378 QVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDA 456

                          490
                   ....*....|....
gi 1698252301 1137 LPLTPNGKLDRKAL 1150
Cdd:cd12116    457 LPLTANGKLDRKAL 470
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 179-611 1.29e-172

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: 523.46  E-value: 1.29e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEM 258
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  259 V-----ITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQG 333
Cdd:cd19531     81 VdlsglPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 DRVQLETLPVQYADYALWQQQLLGDETtpeslISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHS 413
Cdd:cd19531    161 RPSPLPPLPIQYADYAVWQREWLQGEV-----LERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  414 RLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQ 493
Cdd:cd19531    236 ALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRE 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  494 VNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSAKFDLTFEISEsnevdgT 573
Cdd:cd19531    316 TALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTE------T 389

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1698252301  574 PNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19531    390 DGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 644-1151 3.49e-170

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: 518.91  E-value: 3.49e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPL 723
Cdd:cd17644      1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 DPDYPSDRISFMLHDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGST 803
Cdd:cd17644     81 DPNYPQERLTYILEDAQISVLLTQ------------------------------------------PENLAYVIYTSGST 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  804 GRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKV 883
Cdd:cd17644    119 GKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQL 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  884 TVLNQTPsAFYQLMQADRENEEVGQKLSLRYVVFGGEALELSRLEDWYsRHPHNAPKVINMYGITETTVHVSYIELDESI 963
Cdd:cd17644    199 TVLSLPP-AYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQ-KNVGNFIQLINVYGPTEATIAATVCRLTQLT 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  964 VSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPF-GKPGTRMYRTGDLARW 1042
Cdd:cd17644    277 ERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARY 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSL 1122
Cdd:cd17644    357 LPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKL 436

                          490       500
                   ....*....|....*....|....*....
gi 1698252301 1123 PDYMVPYAFVVVNELPLTPNGKLDRKALP 1151
Cdd:cd17644    437 PDYMIPSAFVVLEELPLTPNGKIDRRALP 465
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 670-1085 1.87e-169

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: 514.51  E-value: 1.87e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  670 TYEKLNRKANKIARFLIA-KGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:TIGR01733    1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SVEIECDESLKILVDDVNVMEEiekYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ 828
Cdd:TIGR01733   81 ALASRLAGLVLPVILLDPLELA---ALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKE-KVTVLNQTPSAFYQLMQADREneevg 907
Cdd:TIGR01733  158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEhPVTVLNLTPSLLALLAAALPP----- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  908 QKLSLRYVVFGGEALELSRLEDWYSRHPhnAPKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNY 987
Cdd:TIGR01733  233 ALASLRLVILGGEALTPALVDRWRARGP--GARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDD 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  988 LQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPF-GKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIE 1066
Cdd:TIGR01733  311 LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIE 390

                          410
                   ....*....|....*....
gi 1698252301 1067 LGEIEAVIMKHDKVEQVAV 1085
Cdd:TIGR01733  391 LGEIEAALLRHPGVREAVV 409
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 657-1151 3.82e-158

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: 486.49  E-value: 3.82e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplAPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd17649     81 EDSGAGLLLTH-----------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPL 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd17649    120 AAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 MQaDRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPhnapKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSI 976
Cdd:cd17649    200 AE-EADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPV----RLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPL 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADH 1056
Cdd:cd17649    275 GGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDH 354

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1057 QIKIRGFRIELGEIEAVIMKHDKVEQVAVIVReDQPGDKRLVAYIV--ASNNETIDTNEMRQHASGSLPDYMVPYAFVVV 1134
Cdd:cd17649    355 QVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVlrAAAAQPELRAQLRTALRASLPDYMVPAHLVFL 433

                          490
                   ....*....|....*..
gi 1698252301 1135 NELPLTPNGKLDRKALP 1151
Cdd:cd17649    434 ARLPLTPNGKLDRKALP 450
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 645-1150 7.34e-156

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: 480.28  E-value: 7.34e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTG 804
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTD------------------------------------------PDDLAYVIYTSGSTG 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNVVRLLGATDHwfQFDADDVWTMFH--SYAFDFSVWEIWGPLLYGGRLVVVphtvsRSPKEFLQLLVKEK 882
Cdd:cd12115    119 RPKGVAIEHRNAAAFLQWAAA--AFSAEELAGVLAstSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAE 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  883 VTVLNQTPSAFYQLMQADreneevGQKLSLRYVVFGGEALELSRLEDWYSRHPhnAPKVINMYGITETTVHVSYIELDES 962
Cdd:cd12115    192 VTLINTVPSAAAELLRHD------ALPASVRVVNLAGEPLPRDLVQRLYARLQ--VERVVNLYGPSEDTTYSTVAPVPPG 263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  963 ivSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARW 1042
Cdd:cd12115    264 --ASGEVS-IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRW 339

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSL 1122
Cdd:cd12115    340 RPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRL 419

                          490       500
                   ....*....|....*....|....*...
gi 1698252301 1123 PDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd12115    420 PAYMVPSRFVRLDALPLTPNGKIDRSAL 447
PRK05691 PRK05691
peptide synthase; Validated
 181-1244 2.94e-153

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 518.95  E-value: 2.94e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILD------MENL 254
Cdd:PRK05691  3259 PLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHkpgrtpIDYL 3338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  255 NLEMVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGD 334
Cdd:PRK05691  3339 DWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGR 3418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  335 RVQLETLPvQYADYALW-QQQLLGDETtpeslistqlDFWKEELKGLPDQMELPTDyqRPVETSYRGETI-------HFH 406
Cdd:PRK05691  3419 EAQLPVPP-RYRDYIGWlQRQDLAQAR----------QWWQDNLRGFERPTPIPSD--RPFLREHAGDSGgmvvgdcYTR 3485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  407 IDEGMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDV--LSDIVGLFVNTLVLRTNTSGDP-- 482
Cdd:PRK05691  3486 LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMpqMQRTVGLFINSIALRVQLPAAGqr 3565

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  483 -SFKELLNRVKQVNLAAYENQDVPferLVEVLNPVRTRNSHPLFQVMLAFQNTPEATF---NAPDLEASLEiQSVGSAKF 558
Cdd:PRK05691  3566 cSVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSvldRAQSLNASSD-SGRTHTNF 3641

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  559 DLTFEISESNEVdgtpnGLHglLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEKNTVLEKWNGGFQ 638
Cdd:PRK05691  3642 PLTAVCYPGDDL-----GLH--LSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSER 3714

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  639 IAP-EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAG 717
Cdd:PRK05691  3715 DYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAG 3794

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  718 AGYLPLDPDYPSDRISFMLHDAK-PSCVLTNSsveieCDESLKILVDDVN--------VMEEIEkysEENIDEMECLKPL 788
Cdd:PRK05691  3795 AGYLPLDPGLPAQRLQRIIELSRtPVLVCSAA-----CREQARALLDELGcanrprllVWEEVQ---AGEVASHNPGIYS 3866

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 APSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVS 868
Cdd:PRK05691  3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIA 3946

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  869 RSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADReneevgQKL-SLRYVVFGGEAL--ELSRleDWYSRHPHNApkVINMY 945
Cdd:PRK05691  3947 HDPQGLLAHVQAQGITVLESVPSLIQGMLAEDR------QALdGLRWMLPTGEAMppELAR--QWLQRYPQIG--LVNAY 4016

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  946 GITETTVHVSYIELDESivSLRANSL-IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIAD 1024
Cdd:PRK05691  4017 GPAECSDDVAFFRVDLA--STRGSYLpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPH 4094

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1025 PFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGdKRLVAYIVAS 1104
Cdd:PRK05691  4095 PFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVPH 4173

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1105 NNETIDT---NEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEF--IASSSSRGPRTPQEEMLCDLFTEV 1179
Cdd:PRK05691  4174 QTVLAQGallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIgqLQSQAYLAPRNELEQTLATIWADV 4253

                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301 1180 LSVSQIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLEiGNGQSALD 1244
Cdd:PRK05691  4254 LKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE-GLAGSAID 4317
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 657-1150 1.03e-142

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: 444.99  E-value: 1.03e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd17650     81 EDSGAKLLLTQ------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNV 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTM-FHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQ 895
Cdd:cd17650    119 AHAAHAWRREYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRP 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  896 LMQADRENEEvgqKLS-LRYVVFGGEALELSRLEDWYSRHPHNApKVINMYGITETTVHVSYIELDESIVSLRANSLIGC 974
Cdd:cd17650    199 VMAYVYRNGL---DLSaMRLLIVGSDGCKAQDFKTLAARFGQGM-RIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGR 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  975 SIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARWRQDGTLDYIGRA 1054
Cdd:cd17650    275 PLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARWRADGNVELLGRV 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 DHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASnnETIDTNEMRQHASGSLPDYMVPYAFVVV 1134
Cdd:cd17650    354 DHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQL 431

                          490
                   ....*....|....*.
gi 1698252301 1135 NELPLTPNGKLDRKAL 1150
Cdd:cd17650    432 DALPLTPNGKVDRRAL 447
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 645-1150 6.78e-131

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: 414.63  E-value: 6.78e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVLTNSsveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTG 804
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSS-----------------------------------------PSDAAYVIFTSGSTG 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNVV-------RLLGATDH--WFQFdAddvwtmfhSYAFDFSVWEIWGPLLYGGrLVVVPHTVSRspKEFL 875
Cdd:cd05918    120 KPKGVVIEHRALStsalahgRALGLTSEsrVLQF-A--------SYTFDVSILEIFTTLAAGG-CLCIPSEEDR--LNDL 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  876 Q-LLVKEKVTVLNQTPSAFYQLmqadrENEEVgqkLSLRYVVFGGEALELSRLEDWYSRhphnaPKVINMYGITETTVHV 954
Cdd:cd05918    188 AgFINRLRVTWAFLTPSVARLL-----DPEDV---PSLRTLVLGGEALTQSDVDTWADR-----VRLINAYGPAECTIAA 254

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  955 SYieldeSIVSLRAN-SLIGCSIPDLkVYVLD--NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPF----- 1026
Cdd:cd05918    255 TV-----SPVVPSTDpRNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqe 328

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1027 -GKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKH---DKVEQVAVIVREDQPGDKRLVAYIV 1102
Cdd:cd05918    329 gSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlpgAKEVVVEVVKPKDGSSSPQLVAFVV 408

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301 1103 ASNNETIDTN-----------------EMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05918    409 LDGSSSGSGDgdslflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 657-1151 9.54e-130

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: 411.48  E-value: 9.54e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNSS--VEIECDESLKILVDDVnvmeeIEKYSEENIDEMeclkpLAPSHIAYVIYTSGSTGRPKGVMIPHQ 814
Cdd:cd17656     82 LDSGVRVVLTQRHlkSKLSFNKSTILLEDPS-----ISQEDTSNIDYI-----NNSDDLLYIIYTSGTTGKPKGVQLEHK 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  815 NVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNqTPSAFY 894
Cdd:cd17656    152 NMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF-LPVAFL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  895 QLMQADRENEEVGQKlSLRYVVFGGEALELSRLEDWYsRHPHNApKVINMYGITETTVHVSY-IELDESIVSLRAnslIG 973
Cdd:cd17656    231 KFIFSEREFINRFPT-CVKHIITAGEQLVITNEFKEM-LHEHNV-HLHNHYGPSETHVVTTYtINPEAEIPELPP---IG 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  974 CSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgKPGTRMYRTGDLARWRQDGTLDYIGR 1053
Cdd:cd17656    305 KPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGR 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1054 ADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASnnETIDTNEMRQHASGSLPDYMVPYAFVV 1133
Cdd:cd17656    384 ADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVP 461

                          490
                   ....*....|....*...
gi 1698252301 1134 VNELPLTPNGKLDRKALP 1151
Cdd:cd17656    462 LDQLPLTPNGKVDRKALP 479
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 657-1150 9.58e-130

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: 411.28  E-value: 9.58e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNSSVEIECDESLKILVDDVnvmeeiekySEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDL---------DALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQL 896
Cdd:cd12114    152 LNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEML 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  897 MQADRENEEVGQklSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVHVSYIELDESIVSLRansligcSI 976
Cdd:cd12114    232 LDVLEAAQALLP--SLRLVLLSGDWIPLDLPARLRALAPD--ARLISLGGATEASIWSIYHPIDEVPPDWR-------SI 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 P------DLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPfgkPGTRMYRTGDLARWRQDGTLDY 1050
Cdd:cd12114    301 PygrplaNQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEF 377

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1051 IGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVReDQPGDKRLVAYIVASN-NETIDTNEMRQHASGSLPDYMVPY 1129
Cdd:cd12114    378 LGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNdGTPIAPDALRAFLAQTLPAYMIPS 456

                          490       500
                   ....*....|....*....|.
gi 1698252301 1130 AFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd12114    457 RVIALEALPLTANGKVDRAAL 477
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 647-1151 5.39e-129

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: 408.10  E-value: 5.39e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  647 QLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPD 726
Cdd:cd17645      2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  727 YPSDRISFMLHDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRP 806
Cdd:cd17645     82 YPGERIAYMLADSSAKILLTN------------------------------------------PDDLAYVIYTSGSTGLP 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  807 KGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVL 886
Cdd:cd17645    120 KGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIS 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  887 NQTPSAFYQLMQADREneevgqklSLRYVVFGGEALElsrledwysRHPHNAPKVINMYGITETTVHVSYIELDESivsl 966
Cdd:cd17645    200 FLPTGAAEQFMQLDNQ--------SLRVLLTGGDKLK---------KIERKGYKLVNNYGPTENTVVATSFEIDKP---- 258

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  967 RANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgKPGTRMYRTGDLARWRQDG 1046
Cdd:cd17645    259 YANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDG 337

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1047 TLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASnnETIDTNEMRQHASGSLPDYM 1126
Cdd:cd17645    338 NIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAP--EEIPHEELREWLKNDLPDYM 415

                          490       500
                   ....*....|....*....|....*
gi 1698252301 1127 VPYAFVVVNELPLTPNGKLDRKALP 1151
Cdd:cd17645    416 IPTYFVHLKALPLTANGKVDRKALP 440
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 647-1150 2.74e-128

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: 405.54  E-value: 2.74e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  647 QLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPD 726
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  727 YPSDRISFMLHDAKPSCVLTNSSVeiecdeslkilvDDVnvmeeiekyseenidemeclkplapshiAYVIYTSGSTGRP 806
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTDSP------------DDL----------------------------AYIIFTSGSTGIP 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  807 KGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVvphtvsRSPKEFLQLLVKEkVTVL 886
Cdd:cd17653    121 KGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDAL 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  887 NQTPSAFYQLMQADRENeevgqklsLRYVVFGGEALELSRLEDWYSRhphnaPKVINMYGITETTVHVSYIELdesivSL 966
Cdd:cd17653    194 MSTPSILSTLSPQDFPN--------LKTIFLGGEAVPPSLLDRWSPG-----RRLYNAYGPTECTISSTMTEL-----LP 255

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  967 RANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGkPGTRMYRTGDLARWRQDG 1046
Cdd:cd17653    256 GQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDG 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1047 TLDYIGRADHQIKIRGFRIELGEIEAVIMKHD-KVEQVAVIVREDqpgdkRLVAYIVAsnnETIDTNEMRQHASGSLPDY 1125
Cdd:cd17653    335 GLEFLGREDNQVKVRGFRINLEEIEEVVLQSQpEVTQAAAIVVNG-----RLVAFVTP---ETVDVDGLRSELAKHLPSY 406

                          490       500
                   ....*....|....*....|....*
gi 1698252301 1126 MVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd17653    407 AVPDRIIALDSFPLTANGKVDRKAL 431
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 657-1151 6.42e-127

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: 402.93  E-value: 6.42e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVG-PDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFM 735
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  736 LHDAKPSCVLTNssveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQN 815
Cdd:cd17648     81 LEDTGARVVITN------------------------------------------STDLAYAIYTSGTTGKPKGVLVEHGS 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  816 VVRLLGATDHWFQFDA--DDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAF 893
Cdd:cd17648    119 VVNLRTSLSERYFGRDngDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL 198

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  894 YQLmqadreneEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHnapKVINMYGITETTV--HVSYIELDEsivslRANSL 971
Cdd:cd17648    199 QQY--------DLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG---LIINAYGPTETTVtnHKRFFPGDQ-----RFDKS 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  972 IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPG-------TRMYRTGDLARWRQ 1044
Cdd:cd17648    263 LGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLP 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1045 DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVRED-----QPGDKRLVAYIVaSNNETIDTNEMRQHAS 1119
Cdd:cd17648    343 SGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYL-PEPGHVPESDLLSFLR 421

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1698252301 1120 GSLPDYMVPYAFVVVNELPLTPNGKLDRKALP 1151
Cdd:cd17648    422 AKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 656-1150 2.40e-124

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: 395.46  E-value: 2.40e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  656 NPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFM 735
Cdd:cd05945      4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  736 LHDAKPSCVLTnssveiecdeslkilvddvnvmeeiekyseenidemeclkplAPSHIAYVIYTSGSTGRPKGVMIPHQN 815
Cdd:cd05945     84 LDAAKPALLIA------------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDN 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  816 VVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQ 895
Cdd:cd05945    122 LVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAM 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  896 LMQADRENEEVGQklSLRYVVFGGEALELSRLEDWYSRHPhnAPKVINMYGITETTVHVSYIELDESIVSlRANSL-IGC 974
Cdd:cd05945    202 CLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRFP--DARIYNTYGPTEATVAVTYIEVTPEVLD-GYDRLpIGY 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  975 SIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFiadpFGKPGTRMYRTGDLARWRQDGTLDYIGRA 1054
Cdd:cd05945    277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEADGLLFYRGRL 352

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 DHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNN-ETIDTNEMRQHASGSLPDYMVPYAFVV 1133
Cdd:cd05945    353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGaEAGLTKAIKAELAERLPPYMIPRRFVY 432

                          490
                   ....*....|....*..
gi 1698252301 1134 VNELPLTPNGKLDRKAL 1150
Cdd:cd05945    433 LDELPLNANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
649-1061 4.32e-123

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 390.91  E-value: 4.32e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  649 FEKQAHINPNSIAV-VFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDY 727
Cdd:pfam00501    1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  728 PSDRISFMLHDAKPSCVLTNSSVEIE---------CDESLKILVDDVNVMEEIEKYSEENIDEM--ECLKPLAPSHIAYV 796
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgklEVVKLVLVLDRDPVLKEEPLPEEAKPADVppPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  797 IYTSGSTGRPKGVMIPHQNVVRLLGA----TDHWFQFDADDVWTMFHSYAFDFSV-WEIWGPLLYGGRLVVVPHTVSRSP 871
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 KEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgQKLSLRYVVFGGEALELSRLEDWYSRHPhnaPKVINMYGITETT 951
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA--LLSSLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  952 VHVSYIELDEsiVSLRANSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgkpg 1030
Cdd:pfam00501  316 GVVTTPLPLD--EDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------ 387

                          410       420       430
                   ....*....|....*....|....*....|.
gi 1698252301 1031 tRMYRTGDLARWRQDGTLDYIGRADHQIKIR 1061
Cdd:pfam00501  388 -GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 645-1152 2.02e-119

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: 382.24  E-value: 2.02e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVLTnssveiecdeslkilvddvnvmeeiekyseenidemeclkplapshiAYVIYTSGSTG 804
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT-----------------------------------------------ALILYTSGTTG 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFHSYAFdfsVWEIWGPLLYGGRLVVVPHtvsRSPKEFLQLLVK 880
Cdd:COG0318    114 RPKGVMLTHRNLLANAAAIAAALGLTPGDVVlvalPLFHVFGL---TVGLLAPLLAGATLVLLPR---FDPERVLELIER 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  881 EKVTVLNQTPSAFYQLMQADRENEEvgqKLS-LRYVVFGGEALELSRLEDWYSRHphnAPKVINMYGITETTVHVSYIEL 959
Cdd:COG0318    188 ERVTVLFGVPTMLARLLRHPEFARY---DLSsLRLVVSGGAPLPPELLERFEERF---GVRIVEGYGLTETSPVVTVNPE 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  960 DESivsLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFiADPFgkpgtrmYRTGDL 1039
Cdd:COG0318    262 DPG---ERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDL 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1040 ARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHAS 1119
Cdd:COG0318    331 GRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLR 410

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1698252301 1120 GSLPDYMVPYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:COG0318    411 ERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 689-1501 2.55e-118

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


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 392.91  E-value: 2.55e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  689 GVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTnssVEIECDESLKILVDDVNVM 768
Cdd:COG3319     47 LVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALALLL---ALLAALALALLALLLAALL 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  769 EEIEKYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVW 848
Cdd:COG3319    124 LALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALL 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  849 EIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVkekvtvlnqTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELSRLE 928
Cdd:COG3319    204 LLLALLLLLLLLLALLLLLLLALLAAAALLA---------LLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLAL 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  929 DWYSRHPHNAPKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLAR 1008
Cdd:COG3319    275 LLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGA 354

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1009 GYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVR 1088
Cdd:COG3319    355 GGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAA 434

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1089 EDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFIASSSSRGPRTPQ 1168
Cdd:COG3319    435 AAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAAL 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1169 EEMLCDLFTEVLSVSQIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLEIGNGQSALDVLLP 1248
Cdd:COG3319    515 ELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVP 594

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1249 LRASGDQLPLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWS 1328
Cdd:COG3319    595 LRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWS 674

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1329 LGGNVVHAMAAQLQNEGEEVELLVMLDSY-PGHFLPNTEAPTEEEALIALLALGGYDPDNMDGKPLT----MESAVEILR 1403
Cdd:COG3319    675 FGGLVAYEMARQLEAQGEEVALLVLLDSYaPGALARLDEAELLAALLRDLARGVDLPLDAEELRALDpeerLARLLERLR 754

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1404 KDGsALASLEEETILNLKETYVNSVGLLGKYVPKVYNGDILFFRSTVIPDWFDPISPNTWLNYLDGDIVQHDIDCRHKDL 1483
Cdd:COG3319    755 EAG-LPAGLDAERLRRLLRVFRANLRALRRYRPRPYDGPVLLFRAEEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSM 833

                          810
                   ....*....|....*...
gi 1698252301 1484 CQPGPLTEIGQVLAKYLQ 1501
Cdd:COG3319    834 LREPHVAELAAALRAALA 851
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 176-611 5.82e-118

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: 377.98  E-value: 5.82e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  176 RPNEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLN 255
Cdd:cd19546      1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  256 LEMVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDR 335
Cdd:cd19546     81 PELPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  336 VQLETLPVQYADYALWQQQLLGDETTPESLISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSRL 415
Cdd:cd19546    161 PERAPLPLQFADYALWERELLAGEDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARL 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  416 VELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDV-LSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQV 494
Cdd:cd19546    241 MEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGdLEGMVGPFARPLALRTDLSGDPTFRELLGRVREA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  495 NLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQ---NTPEATFNAPDLEASLEIQSVGSAKFDLTFEISESNEVD 571
Cdd:cd19546    321 VREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRdddNDPWDAPELPGLRTSPVPLGTEAMELDLSLALTERRNDD 400

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1698252301  572 GTPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19546    401 GDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 179-611 8.23e-107

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: 346.67  E-value: 8.23e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIF-PNVLGSSYQKILDMENLNLE 257
Cdd:cd19539      1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLvRDDGGVPRQEILPPGPAPLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  258 MVITNTCKDELES----VLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQG 333
Cdd:cd19539     81 VRDLSDPDSDRERrleeLLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 DRVQLETLPVQYADYALWQQQLLGDETTPESListqlDFWKEELKGLpDQMELPTDYQRPVETSYRGETIHFHIDEGMHS 413
Cdd:cd19539    161 PAAPLPELRQQYKEYAAWQREALAAPRAAELL-----DFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  414 RLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQ 493
Cdd:cd19539    235 ALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  494 VNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEASLEIQSV-GSAKFDLTFEISEsnevdg 572
Cdd:cd19539    315 ALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIpDGAKFDLNLTVTE------ 388

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1698252301  573 TPNGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19539    389 EGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 372-1235 1.93e-106

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: 370.93  E-value: 1.93e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  372 FWKEELKGLPDQMeLPTDYQRPVETSYRGETIHFHIDEgmhsrlVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGS 451
Cdd:TIGR03443    1 RWSERLDNPTLSV-LPHDYLRPANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  452 piAGRNDDvlsdivglfvNTLVLRTNTSGDPSFKELLNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHP-LFQvmLA 530
Cdd:TIGR03443   74 --SSNKSG----------RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFR--LA 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  531 FQNTPEAtfnapdleaSLEIQSVGSAKfDLTFEISESN---EVDGTPNGLhgllefstdLYKRETVQKLIERFILLLDDA 607
Cdd:TIGR03443  140 FQDAPDN---------QQTTYSTGSTT-DLTVFLTPSSpelELSIYYNSL---------LFSSDRITIVADQLAQLLSAA 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  608 ATNPNQSIGRLEILTVAEKN-----TVLEKWnGGFQIApemtLPQLFEKQAHINPNSIAVV----FED-----KKLTYEK 673
Cdd:TIGR03443  201 SSNPDEPIGKVSLITPSQKSllpdpTKDLDW-SGFRGA----IHDIFADNAEKHPDRTCVVetpsFLDpssktRSFTYKQ 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  674 LNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLT------- 746
Cdd:TIGR03443  276 INEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViekagtl 355

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 NSSVEIECDESLKI--------LVDDVNVMEeiekySEENIDEMECLKP------------LAPSHIAYVIYTSGSTGRP 806
Cdd:TIGR03443  356 DQLVRDYIDKELELrteipalaLQDDGSLVG-----GSLEGGETDVLAPyqalkdtptgvvVGPDSNPTLSFTSGSEGIP 430

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  807 KGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVL 886
Cdd:TIGR03443  431 KGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVT 510

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  887 NQTPsAFYQLMQAdrenEEVGQKLSLRYVVFGGEAL---ELSRLEDWysrhphnAPKV--INMYGITETTVHVSYIElde 961
Cdd:TIGR03443  511 HLTP-AMGQLLSA----QATTPIPSLHHAFFVGDILtkrDCLRLQTL-------AENVciVNMYGTTETQRAVSYFE--- 575

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  962 sIVSLRANSLI----------GCSIPDLKVYVLDNY--LQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKP 1029
Cdd:TIGR03443  576 -IPSRSSDSTFlknlkdvmpaGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDP 654

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1030 GT---------------------RMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVR 1088
Cdd:TIGR03443  655 SHwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVR 734

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1089 EDQPGDKRLVAYIVASNN------------ETIDTNEM--------------RQHASGSLPDYMVPYAFVVVNELPLTPN 1142
Cdd:TIGR03443  735 RDKDEEPTLVSYIVPQDKsdeleefksevdDEESSDPVvkglikyrklikdiREYLKKKLPSYAIPTVIVPLKKLPLNPN 814

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1143 GKLDRKALPAP-----EFIASSSSRGPR----TPQEEMLCDLFTEVL--SVSQIGIDDGFFDLGGHSLLAVQLMSRMKEA 1211
Cdd:TIGR03443  815 GKVDKPALPFPdtaqlAAVAKNRSASAAdeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKK 894

                          970       980
                   ....*....|....*....|....
gi 1698252301 1212 LGVELNIGTLFAAPTVAGLAERLE 1235
Cdd:TIGR03443  895 LNVELPLGLIFKSPTIKGFAKEVD 918
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 179-611 7.48e-105

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: 341.31  E-value: 7.48e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEM 258
Cdd:cd19066      1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  259 VI----TNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGD 334
Cdd:cd19066     81 IIdlrnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  335 RVqLETLPVQYADYALWQQQLLGDEttpesLISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSR 414
Cdd:cd19066    161 PT-LPPPVGSYADYAAWLEKQLESE-----AAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  415 LVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQV 494
Cdd:cd19066    235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  495 NLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEATFNAPDLEAS-LEIQSVGSAKFDLTFEISEsnEVDGt 573
Cdd:cd19066    315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTtPVYTSSEGTVFDLDLEASE--DPDG- 391

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1698252301  574 pnGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19066    392 --DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 178-626 2.02e-104

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: 340.85  E-value: 2.02e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  178 NEVPLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFP-NVLGSSYQKILDMENLNL 256
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPFEL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  257 EMV-ITNTCKDELESVLSEAVR----YSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARC 331
Cdd:pfam00668   83 EIIdISDLSESEEEEAIEAFIQrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  332 QGDrvQLETLPVQ-YADYALWQQQLLGDEttpesLISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEG 410
Cdd:pfam00668  163 KGE--PLPLPPKTpYKDYAEWLQQYLQSE-----DYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDED 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  411 MHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNR 490
Cdd:pfam00668  236 TEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKR 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  491 VKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTP----EATFNAPD-LEASLEIQSVGSAKFDLTFEIS 565
Cdd:pfam00668  316 VQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLgqdsQEEEFQLSeLDLSVSSVIEEEAKYDLSLTAS 395

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301  566 ESNEvdgtpnGLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNPNQSIGRLEILTVAEK 626
Cdd:pfam00668  396 ERGG------GLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEK 450
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
643-1150 5.72e-86

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 290.64  E-value: 5.72e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK04813     2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNSSVEIEcDESLKILVDDvNVMEEIEKYSEENIDemeclKPLAPSHIAYVIYTSGS 802
Cdd:PRK04813    82 VDVSSPAERIEMIIEVAKPSLIIATEELPLE-ILGIPVITLD-ELKDIFATGNPYDFD-----HAVKGDDNYYIIFTSGT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  803 TGRPKGVMIPHQNvvrLLGATDhW----FQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLL 878
Cdd:PRK04813   155 TGKPKGVQISHDN---LVSFTN-WmledFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETL 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSaFYQLMQADRE-NEEvgQKLSLRYVVFGGEALELSRLEDWYSRHPhNApKVINMYGITETTVHVSYI 957
Cdd:PRK04813   231 PQLPINVWVSTPS-FADMCLLDPSfNEE--HLPNLTHFLFCGEELPHKTAKKLLERFP-SA-TIYNTYGPTEATVAVTSI 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  958 ELDESIVSlRANSL-IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFiadpFGKPGTRMYRT 1036
Cdd:PRK04813   306 EITDEMLD-QYKRLpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHT 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1037 GDLARWrQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQvAVIVredqPGDK-----RLVAYIVASNNETID- 1110
Cdd:PRK04813   381 GDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVES-AVVV----PYNKdhkvqYLIAYVVPKEEDFERe 454

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1698252301 1111 ---TNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK04813   455 felTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 792-1146 3.61e-81

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: 270.70  E-value: 3.61e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  792 HIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPhtvSRSP 871
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 KEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgQKLSLRYVVFGGEALELSRLEDWYSRHPhnaPKVINMYGITETT 951
Cdd:cd04433     78 EAALELIEREKVTILLGVPTLLARLLKAPESAGY--DLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLTETG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  952 VHVSYIELDEsiVSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFiadpfgkpGT 1031
Cdd:cd04433    153 GTVATGPPDD--DARKPGS-VGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------ED 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1032 RMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDT 1111
Cdd:cd04433    222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA 301

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1698252301 1112 NEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLD 1146
Cdd:cd04433    302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 179-611 2.99e-76

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: 259.70  E-value: 2.99e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRRLWFLNC-LEGPSpTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSS--YQKILDMENLN 255
Cdd:cd19532      1 TEPMSFGQSRFWFLQQyLEDPT-TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGepMQGVLASSPLR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  256 LEMViTNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYkarcqgDR 335
Cdd:cd19532     80 LEHV-QISDEAEVEEEFERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY------NG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  336 VQLETLPVQYADYALWQQQLLGDETTpesliSTQLDFWKEELKGLPDQMEL------PTdyqRPVETSYRGETIHFHIDE 409
Cdd:cd19532    153 QPLLPPPLQYLDFAARQRQDYESGAL-----DEDLAYWKSEFSTLPEPLPLlpfakvKS---RPPLTRYDTHTAERRLDA 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  410 GMHSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGspI--AGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKEL 487
Cdd:cd19532    225 ALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADV 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  488 LNRVKQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAF-QNTPE-ATFnaPDLEASLEIQSVGSAKFDLTFEIS 565
Cdd:cd19532    303 LKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYrQGVAEsRPF--GDCELEGEEFEDARTPYDLSLDII 380

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1698252301  566 ESneVDGTPnglhgLLEFST--DLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19532    381 DN--PDGDC-----LLTLKVqsSLYSEEDAELLLDSYVNLLEAFARDP 421
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
648-1150 3.01e-74

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 258.89  E-value: 3.01e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  648 LFEKQAHINPNSIAVVFED-----KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:COG0365     14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNSS----------------VEIECDESLKILV-----------DDVNVMEEIEKYS 775
Cdd:COG0365     94 VFPGFGAEALADRIEDAEAKVLITADGglrggkvidlkekvdeALEELPSLEHVIVvgrtgadvpmeGDLDWDELLAAAS 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  776 eeniDEMEClKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNV-VRLLGATDHWFQFDADDV--------WTMFHSYAfdfs 846
Cdd:COG0365    174 ----AEFEP-EPTDADDPLFILYTSGTTGKPKGVVHTHGGYlVHAATTAKYVLDLKPGDVfwctadigWATGHSYI---- 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  847 vweIWGPLLYGGRLVV---VPHTvsRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKL---SLRYVVFGGE 920
Cdd:COG0365    245 ---VYGPLLNGATVVLyegRPDF--PDPGRLWELIEKYGVTVFFTAPTAIRALMKAG---DEPLKKYdlsSLRLLGSAGE 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  921 AL--ELSRledWYSRH---PhnapkVINMYGITETTVH-VSYIELDEsivsLRANSlIGCSIPDLKVYVLDNYLQPVPPG 994
Cdd:COG0365    317 PLnpEVWE---WWYEAvgvP-----IVDGWGQTETGGIfISNLPGLP----VKPGS-MGKPVPGYDVAVVDEDGNPVPPG 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  995 VVGEMYVAGA--GLARGYLGRAgltaERFIADPFGK-PGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIE 1071
Cdd:COG0365    384 EEGELVIKGPwpGMFRGYWNDP----ERYRETYFGRfPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1072 AVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETID---TNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRK 1148
Cdd:COG0365    458 SALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537


                   ..
gi 1698252301 1149 AL 1150
Cdd:COG0365    538 LL 539
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 643-1150 5.59e-73

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 253.96  E-value: 5.59e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK06187     6 LTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNSSVE-----------------IECDESLKILVDDVNVMEEI-----EKYSEENID 780
Cdd:PRK06187    86 INIRLKPEEIAYILNDAEDRVVLVDSEFVpllaailpqlptvrtviVEGDGPAAPLAPEVGEYEELlaaasDTFDFPDID 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  781 EMEclkplapshIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWT----MFHSYAfdfsvweiWG---- 852
Cdd:PRK06187   166 END---------AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHA--------WGlpyl 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  853 PLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENeevGQKLS-LRYVVFGGEALELSRLEDWY 931
Cdd:PRK06187   229 ALMAGAKQVIPRRF---DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAY---FVDFSsLRLVIYGGAALPPALLREFK 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  932 SRhpHNApKVINMYGITET--TVHVSYIELDESIVSLRANSlIGCSIPDLKVYVLDNYLQPVPP--GVVGEMYVAGAGLA 1007
Cdd:PRK06187   303 EK--FGI-DLVQGYGMTETspVVSVLPPEDQLPGQWTKRRS-AGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLM 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1008 RGYLGRAGLTAERFIADpfgkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIV 1087
Cdd:PRK06187   379 QGYWNRPEATAETIDGG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIG 450

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1088 REDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06187   451 VPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 645-1150 6.62e-73

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: 251.71  E-value: 6.62e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCvltnssveIECDESLKilvddvNVMEEIEKYSEEnidemeclKPLAPSHIAYVIYTSGSTG 804
Cdd:cd05936     81 PLYTPRELEHILNDSGAKA--------LIVAVSFT------DLLAAGAPLGER--------VALTPEDVAVLQYTSGTTG 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNVVRLLGATDHWFQF--DADDVWT----MFHSYAFDFSVWEiwgPLLYGGRLVVVPhtvSRSPKEFLQLL 878
Cdd:cd05936    139 VPKGAMLTHRNLVANALQIKAWLEDllEGDDVVLaalpLFHVFGLTVALLL---PLALGATIVLIP---RFRPIGVLKEI 212

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSAFYQLMQAdrenEEVGQKL--SLRYVVFGGEALELSRLEDWysrHPHNAPKVINMYGITET--TVHV 954
Cdd:cd05936    213 RKHRVTIFPGVPTMYIALLNA----PEFKKRDfsSLRLCISGGAPLPVEVAERF---EELTGVPIVEGYGLTETspVVAV 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  955 SYIEldesiVSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmy 1034
Cdd:cd05936    286 NPLD-----GPRKPGS-IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------- 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1035 RTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEM 1114
Cdd:cd05936    352 RTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEI 431

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1698252301 1115 RQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05936    432 IAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 669-1150 3.17e-72

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: 249.31  E-value: 3.17e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNs 748
Cdd:cd17654     17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 sveiecdeslkilvddvnvmEEIEKYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ 828
Cdd:cd17654     96 --------------------KELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKE-KVTVLNQTPSAFYQLMQADRENEEVG 907
Cdd:cd17654    156 ITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFRRFGSQSIKSTVLS 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  908 QKLSLRYVVFGGEAL-ELSRLEDWysRHPHNAPKVINMYGITETTVHVSYIEldesIVSLRANSLIGCSIPDLKVYVLDN 986
Cdd:cd17654    236 ATSSLRVLALGGEPFpSLVILSSW--RGKGNRTRIFNIYGITEVSCWALAYK----VPEEDSPVQLGSPLLGTVIEVRDQ 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  987 ylqpvpPGVVGEMYVAGAGLARGYlgragltaerFIADPFGKPGTRMYRTGDLARwRQDGTLDYIGRADHQIKIRGFRIE 1066
Cdd:cd17654    310 ------NGSEGTGQVFLGGLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRIN 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1067 LGEIEAVIMKHDKVEQVAVIVREDQpgdkRLVAYIVASNNETIDTNEMRQH--ASGSLPDYmvpyaFVVVNELPLTPNGK 1144
Cdd:cd17654    373 LDLIQQVIESCLGVESCAVTLSDQQ----RLIAFIVGESSSSRIHKELQLTllSSHAIPDT-----FVQIDKLPLTSHGK 443


                   ....*.
gi 1698252301 1145 LDRKAL 1150
Cdd:cd17654    444 VDKSEL 449
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 182-427 9.92e-69

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 231.47  E-value: 9.92e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  182 LSFAQRRLWFLnclEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEMV-- 259
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVdl 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  260 ---ITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDRV 336
Cdd:COG4908     78 salPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  337 QLETLPVQYADYALWQQQLLGDETtpeslISTQLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSRLV 416
Cdd:COG4908    158 PLPELPIQYADYAAWQRAWLQSEA-----LEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK 232

                          250
                   ....*....|.
gi 1698252301  417 ELGRKNGVSLF 427
Cdd:COG4908    233 ALAKAHGATVN 243
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 179-607 7.41e-65

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: 227.14  E-value: 7.41e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRRLWFLNC-LEGPSpTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLE 257
Cdd:cd20483      1 PRPMSTFQRRLWFLHNfLEDKT-FLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  258 MVITNTCKD---ELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKA-RCQG 333
Cdd:cd20483     80 VIDLSEAADpeaALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlRAGR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 DRVQLETLPVQYADYALWQQQLLGDETTPESListqlDFWKEELKGLPDQME-LPTDYQ-RPVETSYRGETIHFHIDEGM 411
Cdd:cd20483    160 DLATVPPPPVQYIDFTLWHNALLQSPLVQPLL-----DFWKEKLEGIPDASKlLPFAKAeRPPVKDYERSTVEATLDKEL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  412 HSRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRV 491
Cdd:cd20483    235 LARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLEST 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  492 KQVNLAAYENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQ---NTPEATFnapdleASLEIQSVGS----AKFDLTFEI 564
Cdd:cd20483    315 KTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvhgKFPEYDT------GDFKFTDYDHydipTACDIALEA 388

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1698252301  565 SESNEvdgtpNGLHGLLEFSTDLYKRETVQKLIERFILLLDDA 607
Cdd:cd20483    389 EEDPD-----GGLDLRLEFSTTLYDSADMERFLDNFVTFLTSV 426
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 667-1153 5.02e-64

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: 227.79  E-value: 5.02e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  667 KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVlt 746
Cdd:cd17647     19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGL-- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 nssveiecdeslkILVDDVNVMeeiekyseenidemeclkpLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHW 826
Cdd:cd17647     97 -------------IVIRAAGVV-------------------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKR 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  827 FQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPsAFYQLMQADreneEV 906
Cdd:cd17647    145 FNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTP-AMGQLLTAQ----AT 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  907 GQKLSLRYVVFGGEAL---ELSRLEDWysrhpHNAPKVINMYGITETTVHVSYIEL-----DESIV-SLRANSLIGCSIP 977
Cdd:cd17647    220 TPFPKLHHAFFVGDILtkrDCLRLQTL-----AENVRIVNMYGTTETQRAVSYFEVpsrssDPTFLkNLKDVMPAGRGML 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  978 DLKVYVLDNY--LQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPG---------------------TRMY 1034
Cdd:cd17647    295 NVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprDRLY 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1035 RTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNE- 1113
Cdd:cd17647    375 RTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFa 454

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1114 --------------------------MRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAP 1153
Cdd:cd17647    455 qedvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 643-1150 8.29e-64

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 226.71  E-value: 8.29e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK07656     5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCV------LTNSSVEIECDESLKILV-----DDVNVMEEIEKYSE--ENIDEMECLKPLA 789
Cdd:PRK07656    85 LNTRYTADEAAYILARGDAKALfvlglfLGVDYSATTRLPALEHVViceteEDDPHTEKMKTFTDflAAGDPAERAPEVD 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHsyAFDFSVwEIWGPLLYGGRLVVVPH 865
Cdd:PRK07656   165 PDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylaANPFFH--VFGYKA-GVNAPLMRGATILPLPV 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  866 TvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgqKL-SLRYVVFGGEALELSRLEDWYSRHPhnAPKVINM 944
Cdd:PRK07656   242 F---DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE---DLsSLRLAVTGAASMPVALLERFESELG--VDIVLTG 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  945 YGITETTVHVSYIELDESIVSLrANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIAD 1024
Cdd:PRK07656   314 YGLSEASGVTTFNRLDDDRKTV-AGT-IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1025 PFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIvredqpG--DKRL----V 1098
Cdd:PRK07656   392 GW-------LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------GvpDERLgevgK 458

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1099 AYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK07656   459 AYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 644-1152 6.59e-63

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


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 224.28  E-value: 6.59e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPL 723
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 DPDYPSDRISFMLHDAKPSCVLTNSS-------VEIEC-DESLKILVDDVNvmEEIEKYSEENI---DEMECLKPLAPSH 792
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSErldllhpALPGChDLRTLIIVGDPA--HASEGHPGEEPaswPKLLALGDADPPH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 ------IAYVIYTSGSTGRPKGVMIPHQNVVrlLGA--TDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVP 864
Cdd:TIGR03098  159 pvidsdMAAILYTSGSTGRPKGVVLSHRNLV--AGAqsVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  865 HTVsrsPKEFLQLLVKEKVTVLNQTPSAFYQLMQADREnEEVGQklSLRYVVFGGEALELSRLEDWYSRHPHNapKVINM 944
Cdd:TIGR03098  237 YLL---PRDVLKALEKHGITGLAAVPPLWAQLAQLDWP-ESAAP--SLRYLTNSGGAMPRATLSRLRSFLPNA--RLFLM 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  945 YGITEtTVHVSYieLDESIVSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIAD 1024
Cdd:TIGR03098  309 YGLTE-AFRSTY--LPPEEVDRRPDS-IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPL 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1025 P-----FGKPGTRMYrTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDkRLV 1098
Cdd:TIGR03098  385 PpfpgeLHLPELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQ-AIV 462

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1099 AYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:TIGR03098  463 LVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 649-1147 1.95e-61

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


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 217.48  E-value: 1.95e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  649 FEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYP 728
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  729 SDRISFMLHDAKPscvltnssveiecdeslKILVDDvnvmeeiekyseenidemeclkplapshIAYVIYTSGSTGRPKG 808
Cdd:cd17631     81 PPEVAYILADSGA-----------------KVLFDD----------------------------LALLMYTSGTTGRPKG 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  809 VMIPHQNVV-RLLGATDHWFqFDADDVWT----MFHSYAFDFsvweIWGPLLY-GGRLVVVPHTvsrSPKEFLQLLVKEK 882
Cdd:cd17631    116 AMLTHRNLLwNAVNALAALD-LGPDDVLLvvapLFHIGGLGV----FTLPTLLrGGTVVILRKF---DPETVLDLIERHR 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  883 VTVLNQTPSAFYQLMQADRENEevgQKLS-LRYVVFGGEALELSRLEDWYSRHphnaPKVINMYGITETTVHVSYIELDE 961
Cdd:cd17631    188 VTSFFLVPTMIQALLQHPRFAT---TDLSsLRAVIYGGAPMPERLLRALQARG----VKFVQGYGMTETSPGVTFLSPED 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  962 SIVSLRAnslIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAErFIADPFgkpgtrmYRTGDLAR 1041
Cdd:cd17631    261 HRRKLGS---AGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-AFRDGW-------FHTGDLGR 329

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1042 WRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGS 1121
Cdd:cd17631    330 LDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRER 409

                          490       500
                   ....*....|....*....|....*.
gi 1698252301 1122 LPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:cd17631    410 LARYKIPKSVEFVDALPRNATGKILK 435
PRK12316 PRK12316
peptide synthase; Provisional
 1-596 1.82e-59

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 227.15  E-value: 1.82e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRpndkRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:PRK12316  3466 LLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP 3541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   81 DFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIREtLSVELGIGKLFESPTVAELAK 159
Cdd:PRK12316  3542 DAALLQQDYVApVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKDLFQHQTIQGLAR 3620

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  160 --------QLNHAKSARPAIQKASRPNEVPLSFAQRRLWFLNCLEGPSptyniplvirmnGILNRQALQGAFYDVVEKHE 231
Cdd:PRK12316  3621 varvgggvAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPR------------EALDAAALEAALQALVEHHD 3688

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  232 TLRTIFPNVLG---SSYQKILDMENLNLEMVITNTckDELESVLSEAVRySFNLDFEPAVRLQLFTVSENEHVLLILLHH 308
Cdd:PRK12316  3689 ALRLRFVEDAGgwtAEHLPVELGGALLWRAELDDA--EELERLGEEAQR-SLDLADGPLLRALLATLADGSQRLLLVIHH 3765

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  309 IVGDGWSLQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLLGDETtpeslISTQLDFWKEELKGLPDqmELPT 388
Cdd:PRK12316  3766 LVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEA-----LKAELAYWQEQLQGVSS--ELPC 3838

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  389 DYQRPVETSYRGETIHFHIDEGMHSRLV-ELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRND---DV-LSD 463
Cdd:PRK12316  3839 DHPQGALQNRHAASVQTRLDRELTRRLLqQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfaDIdLSR 3918

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  464 IVGLFVNTLVLRTNTSGDpsFKELLNRVKQvNLAAYENQDVPFERLvevlnpvRTRNSHPLFQVmLAFQNTPEATFN--- 540
Cdd:PRK12316  3919 TVGWFTSLFPVRLSPVED--LGASIKAIKE-QLRAIPNKGIGFGLL-------RYLGDEESRRT-LAGLPVPRITFNylg 3987

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301  541 ----APDLEASLEIQSVGSAKFDLTFEISESNEVDGTPNGLHGLLE----FSTDLYKRETVQKL 596
Cdd:PRK12316  3988 qfdgSFDEEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSldwtFSREMFEEATIQRL 4051
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 665-1145 2.95e-59

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: 212.84  E-value: 2.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  665 EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCV 744
Cdd:cd05911      7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  745 LTNSSVEIECDESLKILVDDVNV---------MEEIEKY-SEENIDEMECLKP---LAPSHIAYVIYTSGSTGRPKGVMI 811
Cdd:cd05911     87 FTDPDGLEKVKEAAKELGPKDKIivlddkpdgVLSIEDLlSPTLGEEDEDLPPplkDGKDDTAAILYSSGTTGLPKGVCL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  812 PHQNVV-RLLGATDHWF-QFDADDVW----TMFHSYAFDFSVWEiwgpLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTV 885
Cdd:cd05911    167 SHRNLIaNLSQVQTFLYgNDGSNDVIlgflPLYHIYGLFTTLAS----LLNGATVIIMPKF---DSELFLDLIEKYKITF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  886 LNQTPSAFYQLMQADRENEEvgqKL-SLRYVVFGGEALeLSRLEDWYSRHPHNApKVINMYGITETTVHVSY-IELDESI 963
Cdd:cd05911    240 LYLVPPIAAALAKSPLLDKY---DLsSLRVILSGGAPL-SKELQELLAKRFPNA-TIKQGYGMTETGGILTVnPDGDDKP 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  964 VSlranslIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARW 1042
Cdd:cd05911    315 GS------VGRLLPNVEAKIVDdDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYF 381

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLdYI-GRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGS 1121
Cdd:cd05911    382 DEDGYL-YIvDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKK 460

                          490       500
                   ....*....|....*....|....*...
gi 1698252301 1122 LPDYmvpYAF----VVVNELPLTPNGKL 1145
Cdd:cd05911    461 VASY---KQLrggvVFVDEIPKSASGKI 485
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 181-611 1.49e-56

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: 202.82  E-value: 1.49e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIF-PNVLGSSYQKI-----LDMENL 254
Cdd:cd19543      3 PLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLQVVlkdrkLPWREL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  255 NLEMVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGD 334
Cdd:cd19543     83 DLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQ 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  335 RVQLETlPVQYADYALWQQQLLGDETtpeslistqLDFWKEELKGLPDQMELPTDYQRPVETSYRGETIHFHIDEGMHSR 414
Cdd:cd19543    163 PPSLPP-VRPYRDYIAWLQRQDKEAA---------EAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTAR 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  415 LVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDV--LSDIVGLFVNTLVLRTNTSGDPSFKELLNRVK 492
Cdd:cd19543    233 LQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELpgIETMVGLFINTLPVRVRLDPDQTVLELLKDLQ 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  493 QVNLAAYENQDVPferLVEVLNpvRTRNSHPLFQVMLAFQNTP-EATFNAPDLEASLEIQSVGSAK---FDLTFEISESN 568
Cdd:cd19543    313 AQQLELREHEYVP---LYEIQA--WSEGKQALFDHLLVFENYPvDESLEEEQDEDGLRITDVSAEEqtnYPLTVVAIPGE 387

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1698252301  569 EvdgtpngLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19543    388 E-------LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 181-611 1.20e-54

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: 197.54  E-value: 1.20e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEMV- 259
Cdd:cd20484      3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEd 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  260 ITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDRVQLE 339
Cdd:cd20484     83 ISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  340 TLPVQYADYALWQQQLLGDETTPEslistQLDFWKEELKG-LPDqMELPTDYQRPVETSYRGETIHFHIDEGMHSRLVEL 418
Cdd:cd20484    163 SSPASYYDFVAWEQDMLAGAEGEE-----HRAYWKQQLSGtLPI-LELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSF 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  419 GRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVNLAA 498
Cdd:cd20484    237 ARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  499 YENQDVPFERLVEVLNPVRTRNSHPLFQVMLAFQNTPEAT----FNAPD-----LEASLEIQSVGsaKFDLTFEISESNE 569
Cdd:cd20484    317 LDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQSTslqqFLAEYqdvlsIEFVEGIHQEG--EYELVLEVYEQED 394

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1698252301  570 vDGTPNglhglLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd20484    395 -RFTLN-----IKYNPDLFDASTIERMMEHYVKLAEELIANP 430
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 676-1150 4.05e-54

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: 196.89  E-value: 4.05e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  676 RKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAG----YLPLDPDYPSDRISFMLHDAKPSCVLtnssve 751
Cdd:cd05922      1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVL------ 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  752 ieCDESLKILVDDVNVM--EEIEKYSEENIDEMECLK---PLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHW 826
Cdd:cd05922     75 --ADAGAADRLRDALPAspDPGTVLDADGIRAARASApahEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  827 FQFDADDVW--TMFHSYAFDFSVWEIwgPLLYGGRLVVvpHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENE 904
Cdd:cd05922    153 LGITADDRAltVLPLSYDYGLSVLNT--HLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPA 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  905 EVGqklSLRYVVFGGEALELSRLEDWYSRHPhnAPKVINMYGITETTVHVSYIELDESivsLRANSLIGCSIPDLKVYVL 984
Cdd:cd05922    229 KLP---SLRYLTQAGGRLPQETIARLRELLP--GAQVYVMYGQTEATRRMTYLPPERI---LEKPGSIGLAIPGGEFEIL 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  985 DNYLQPVPPGVVGEMYVAGAGLARGYLGRagltaERFIADPfGKPGTRMYrTGDLARWRQDGTLDYIGRADHQIKIRGFR 1064
Cdd:cd05922    301 DDDGTPTPPGEPGEIVHRGPNVMKGYWND-----PPYRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNR 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1065 IELGEIEAVIMKHDKVEQVAVIVREDQPGDkRLVAYIVASNNetIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGK 1144
Cdd:cd05922    374 ISPTEIEAAARSIGLIIEAAAVGLPDPLGE-KLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGK 450


                   ....*.
gi 1698252301 1145 LDRKAL 1150
Cdd:cd05922    451 VDYAAL 456
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 659-1150 1.45e-52

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: 193.30  E-value: 1.45e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  659 SIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHD 738
Cdd:cd05926      5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  739 AKPSCVLTNSSVEIECDES---LKILVDDVnvmeEIEKYSEENIDEMECLKPLAPSH-------------IAYVIYTSGS 802
Cdd:cd05926     85 LGSKLVLTPKGELGPASRAaskLGLAILEL----ALDVGVLIRAPSAESLSNLLADKknaksegvplpddLALILHTSGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  803 TGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHSYAFdfsVWEIWGPLLYGGRlVVVPHtvSRSPKEFLQLL 878
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDrtlvVMPLFHVHGL---VASLLSTLAAGGS-VVLPP--RFSASTFWPDV 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSaFYQLMQADRENEEVGQKLSLRYVVFGGEALE---LSRLEDWYsrhphNAPkVINMYGITETTVHVS 955
Cdd:cd05926    235 RDYNATWYTAVPT-IHQILLNRPEPNPESPPPKLRFIRSCSASLPpavLEALEATF-----GAP-VLEAYGMTEAAHQMT 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  956 YIELDESIvslRANSLIGcsIPD-LKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmY 1034
Cdd:cd05926    308 SNPLPPGP---RKPGSVG--KPVgVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------F 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1035 RTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEM 1114
Cdd:cd05926    376 RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEEL 455

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1698252301 1115 RQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05926    456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 658-1150 9.08e-52

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: 189.42  E-value: 9.08e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  658 NSIAVVFEDKKLTYEKLNRKANKIARFLIAKG-VGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPScvltnssveiecdeslkILVDDvnvmeeiekyseenidemeclkplapshiAYVIYTSGSTGRPKGVMIPHQNV 816
Cdd:cd05941     81 TDSEPS-----------------LVLDP-----------------------------ALILYTSGTTGRPKGVVLTHANL 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 ---VRLLgaTDHWfQFDADDVWT----MFHSYAFdfsVWEIWGPLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQT 889
Cdd:cd05941    115 aanVRAL--VDAW-RWTEDDVLLhvlpLHHVHGL---VNALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGV 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  890 PSAFYQLMQADRENEEVGQKLS------LRYVVFGGEALELSRLEDWYSRHPHnapKVINMYGITETTVHVSyIELDESi 963
Cdd:cd05941    186 PTIYTRLLQYYEAHFTDPQFARaaaaerLRLMVSGSAALPVPTLEEWEAITGH---TLLERYGMTEIGMALS-NPLDGE- 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  964 vslRANSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARW 1042
Cdd:cd05941    261 ---RRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVV 330

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLDYIGR-ADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNN-ETIDTNEMRQHASG 1120
Cdd:cd05941    331 DEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAKQ 410

                          490       500       510
                   ....*....|....*....|....*....|
gi 1698252301 1121 SLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05941    411 RLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 670-1151 1.40e-51

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: 188.27  E-value: 1.40e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  670 TYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNss 749
Cdd:cd05934      5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  750 veiecdeslkilvddvnvmeeiekyseenidemeclkplapshIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQF 829
Cdd:cd05934     83 -------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  830 DADDVW--TM--FHSYAfdfSVWEIWGPLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLM-QADRENE 904
Cdd:cd05934    120 GEDDVYltVLplFHINA---QAVSVLAALSVGATLVLLPRF---SASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDD 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  905 EVGQklsLRyVVFGGEALElSRLEDWYSRHphnAPKVINMYGITETTVHVSyIELDESivslRANSLIGCSIPDLKVYVL 984
Cdd:cd05934    194 RAHR---LR-AAYGAPNPP-ELHEEFEERF---GVRLLEGYGMTETIVGVI-GPRDEP----RRPGSIGRPAPGYEVRIV 260

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  985 DNYLQPVPPGVVGEMYVAGA---GLARGYLGRAGLTAERFiadPFGkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIR 1061
Cdd:cd05934    261 DDDGQELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM---RNG-----WFHTGDLGYRDADGFFYFVDRKKDMIRRR 332

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1062 GFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTP 1141
Cdd:cd05934    333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTP 412

                          490
                   ....*....|
gi 1698252301 1142 NGKLDRKALP 1151
Cdd:cd05934    413 TEKVAKAQLR 422
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 657-1150 1.22e-49

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: 184.88  E-value: 1.22e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:cd05959     18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNSSV------EIECDESLKILVDDVNVMEEIEKYS--EENIDEMECLKPLAPSH---IAYVIYTSGSTGR 805
Cdd:cd05959     98 EDSRARVVVVSGELapvlaaALTKSEHTLVVLIVSGGAGPEAGALllAELVAAEAEQLKPAATHaddPAFWLYSSGSTGR 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  806 PKGVMIPHQNVV--------RLLGATDhwfqfdaDDVW----TMFHSYAFDFSVWeiwGPLLYGGRLVVVPHTVSrsPKE 873
Cdd:cd05959    178 PKGVVHLHADIYwtaelyarNVLGIRE-------DDVCfsaaKLFFAYGLGNSLT---FPLSVGATTVLMPERPT--PAA 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  874 FLQLLVKEKVTVLNQTPsAFYQLMQADRENEEVGQKlSLRYVVFGGEALELSRLEDWYSRHPHNapkVINMYGITEttvh 953
Cdd:cd05959    246 VFKRIRRYRPTVFFGVP-TLYAAMLAAPNLPSRDLS-SLRLCVSAGEALPAEVGERWKARFGLD---ILDGIGSTE---- 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  954 VSYIELDESIVSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgkpgtrM 1033
Cdd:cd05959    317 MLHIFLSNRPGRVRYGT-TGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE--------W 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1034 YRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV---ASNNETID 1110
Cdd:cd05959    388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEAL 467

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1698252301 1111 TNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05959    468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 669-1145 9.60e-49

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: 180.65  E-value: 9.60e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPscvltns 748
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA------- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 sveiecdeslKILVddvnVMEEiekYSEENIDEMeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGA-TDHWF 827
Cdd:cd05903     75 ----------KVFV----VPER---FRQFDPAAM-------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQyAERLG 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  828 QFDADDVWT---MFHSYAFdfsVWEIWGPLLYGGRLVVVPhtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenE 904
Cdd:cd05903    131 LGPGDVFLVaspMAHQTGF---VYGFTLPLLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLTDLLNAV---E 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  905 EVGQKLS-LRYVVFGGEALELSRLEDWYSRhphNAPKVINMYGITETTVHVSYIELDESIVSLRANsliGCSIPDLKVYV 983
Cdd:cd05903    202 EAGEPLSrLRTFVCGGATVPRSLARRAAEL---LGAKVCSAYGSTECPGAVTSITPAPEDRRLYTD---GRPLPGVEIKV 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  984 LDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAErfiADPFGkpgtrMYRTGDLARWRQDGTLDYIGRADHQIkIR-G 1062
Cdd:cd05903    276 VDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD---AAPEG-----WFRTGDLARLDEDGYLRITGRSKDII-IRgG 346

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1063 FRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGS-LPDYMVPYAFVVVNELPLTP 1141
Cdd:cd05903    347 ENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTP 426


                   ....
gi 1698252301 1142 NGKL 1145
Cdd:cd05903    427 SGKV 430
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 670-1150 1.59e-48

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: 179.95  E-value: 1.59e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  670 TYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSS 749
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  750 VEIEcdeslKILVDDVNvmeEIEKYSEENIdEMECLKPLapSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQF 829
Cdd:TIGR01923   81 LEEK-----DFQADSLD---RIEAAGRYET-SLSASFNM--DQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGF 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  830 DADDVW----TMFHSYAFdfSVweIWGPLLYGGRLVVVphtvsrSPK-EFLQLLVKEKVTVLNQTPSAFYQLMQADRENE 904
Cdd:TIGR01923  150 TEDDNWllslPLYHISGL--SI--LFRWLIEGATLRIV------DKFnQLLEMIANERVTHISLVPTQLNRLLDEGGHNE 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  905 evgqklSLRYVVFGGEALELSRLEDWYSRhphNAPkVINMYGITETTVHVSYIELDESIVSLRANS-LIGCSIpdlKVYV 983
Cdd:TIGR01923  220 ------NLRKILLGGSAIPAPLIEEAQQY---GLP-IYLSYGMTETCSQVTTATPEMLHARPDVGRpLAGREI---KIKV 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  984 lDNYLQpvppgvVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmyRTGDLARWRQDGTLDYIGRADHQIKIRGF 1063
Cdd:TIGR01923  287 -DNKEG------HGEIMVKGANLMKGYLYQGELTPAFEQQGWF--------NTGDIGELDGEGFLYVLGRRDDLIISGGE 351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1064 RIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsnNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNG 1143
Cdd:TIGR01923  352 NIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS--ESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASG 429


                   ....*..
gi 1698252301 1144 KLDRKAL 1150
Cdd:TIGR01923  430 KILRNQL 436
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
643-1150 1.71e-48

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 180.93  E-value: 1.71e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK03640     2 ETMPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNSSVEIECDESLKILVDDVNVMEEIEKYSEENIDEMEclkplapshIAYVIYTSGS 802
Cdd:PRK03640    82 LNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDE---------VATIMYTSGT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  803 TGRPKGVMIPHQNvvrllgatdHWFQ---------FDADDVW----TMFHsyafdfsvweIWG------PLLYGGRLVVV 863
Cdd:PRK03640   153 TGKPKGVIQTYGN---------HWWSavgsalnlgLTEDDCWlaavPIFH----------ISGlsilmrSVIYGMRVVLV 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  864 PHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQadrENEEVGQKLSLRYVVFGGEALELSRLEDwySRHpHNAPkVIN 943
Cdd:PRK03640   214 EKF---DAEKINKLLQTGGVTIISVVSTMLQRLLE---RLGEGTYPSSFRCMLLGGGPAPKPLLEQ--CKE-KGIP-VYQ 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  944 MYGITETTVHVSYIELDESIVSLRA--NSLIGCSIPdlkvyVLDNyLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERF 1021
Cdd:PRK03640   284 SYGMTETASQIVTLSPEDALTKLGSagKPLFPCELK-----IEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1022 IADPFgkpgtrmyRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYI 1101
Cdd:PRK03640   358 QDGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFV 429

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1698252301 1102 VASnnETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK03640   430 VKS--GEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 661-1150 5.67e-48

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: 178.04  E-value: 5.67e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  661 AVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAK 740
Cdd:cd05919      3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  741 PSCVLTNSsveiecdeslkilvDDvnvmeeiekyseenidemeclkplapshIAYVIYTSGSTGRPKGVMIPHQNvvrLL 820
Cdd:cd05919     83 ARLVVTSA--------------DD----------------------------IAYLLYSSGTTGPPKGVMHAHRD---PL 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  821 GATDHW----FQFDADDVW----TMFHSYAFDFSVWeiwGPLLYGGRLVVVPhtVSRSPKEFLQLLVKEKVTVLNQTPSA 892
Cdd:cd05919    118 LFADAMareaLGLTPGDRVfssaKMFFGYGLGNSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTF 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  893 FYQLM-QADRENEEVGqklSLRYVVFGGEALELSRLEDWYSrhpHNAPKVINMYGITEttvhVSYIELDESIVSLRANSL 971
Cdd:cd05919    193 YANLLdSCAGSPDALR---SLRLCVSAGEALPRGLGERWME---HFGGPILDGIGATE----VGHIFLSNRPGAWRLGST 262

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  972 iGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgkpgtrMYRTGDLARWRQDGTLDYI 1051
Cdd:cd05919    263 -GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG--------WYRTGDKFCRDADGWYTHA 333

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1052 GRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMR---QHASGSLPDYMVP 1128
Cdd:cd05919    334 GRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARdihRHLLERLSAHKVP 413

                          490       500
                   ....*....|....*....|..
gi 1698252301 1129 YAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05919    414 RRIAFVDELPRTATGKLQRFKL 435
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 669-1150 4.72e-47

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: 175.22  E-value: 4.72e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 sveiecdeslkilvDDvnvmeeiekyseenidemeclkplapshIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ 828
Cdd:cd05972     81 --------------ED----------------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLG 118

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FDADDV-WTMfHSYAFDFSVW-EIWGPLLYGgrLVVVPHTVSR-SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENee 905
Cdd:cd05972    119 LRPDDIhWNI-ADPGWAKGAWsSFFGPWLLG--ATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYRMLIKQDLSS-- 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  906 vGQKLSLRYVVFGGEALELSRLEDWYSrhpHNAPKVINMYGITETTVHVSyielDESIVSLRANSlIGCSIPDLKVYVLD 985
Cdd:cd05972    194 -YKFSHLRLVVSAGEPLNPEVIEWWRA---ATGLPIRDGYGQTETGLTVG----NFPDMPVKPGS-MGRPTPGYDVAIID 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  986 NYLQPVPPGVVGEMYV--AGAGLARGYLGRAGLTAERFIADpfgkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGF 1063
Cdd:cd05972    265 DDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGY 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1064 RIELGEIEAVIMKHDKVEQVAVIVREDqPGDKRLV-AYIVASNNET---IDTNEMRQHASGSLPDYMVPYAFVVVNELPL 1139
Cdd:cd05972    337 RIGPFEVESALLEHPAVAEAAVVGSPD-PVRGEVVkAFVVLTSGYEpseELAEELQGHVKKVLAPYKYPREIEFVEELPK 415

                          490
                   ....*....|.
gi 1698252301 1140 TPNGKLDRKAL 1150
Cdd:cd05972    416 TISGKIRRVEL 426
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 669-1154 3.27e-45

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: 170.38  E-value: 3.27e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTns 748
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 sveiecdeslkilvddvnvmeeiekySEENIDEMEclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ 828
Cdd:cd05969     79 --------------------------TEELYERTD------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FDADDV--------WTMFHSYAfdfsvweIWGPLLYGGRLVVVPHTVSrsPKEFLQLLVKEKVTVLNQTPSAFYQLMQAD 900
Cdd:cd05969    127 LHPDDIywctadpgWVTGTVYG-------IWAPWLNGVTNVVYEGRFD--AESWYGIIERVKVTVWYTAPTAIRMLMKEG 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  901 RENEEVGQKLSLRYVVFGGEAL--ELSRledwYSRHPHNAPkVINMYGITETTVHV--SYIELDESIVSLransliGCSI 976
Cdd:cd05969    198 DELARKYDLSSLRFIHSVGEPLnpEAIR----WGMEVFGVP-IHDTWWQTETGSIMiaNYPCMPIKPGSM------GKPL 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGA--GLARGYLGRAGLTAERFIadpfgkpgTRMYRTGDLARWRQDGTLDYIGRA 1054
Cdd:cd05969    267 PGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRA 338

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 DHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV-ASNNETIDT--NEMRQHASGSLPDYMVPYAF 1131
Cdd:cd05969    339 DDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlKEGFEPSDElkEEIINFVRQKLGAHVAPREI 418

                          490       500
                   ....*....|....*....|...
gi 1698252301 1132 VVVNELPLTPNGKLDRKALPAPE 1154
Cdd:cd05969    419 EFVDNLPKTRSGKIMRRVLKAKE 441
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 667-1150 3.50e-45

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: 169.92  E-value: 3.50e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  667 KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLT 746
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 nssveiecDESlkilvDDvnvmeeiekyseenidemeclkplapshIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHW 826
Cdd:cd05971     85 --------DGS-----DD----------------------------PALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFP 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  827 FQF---DADDVWTMfHSYAFDFSVWEIWGPLLYGGrLVVVPHTVSR-SPKEFLQLLVKEKVTVLNQTPSAFyQLMQADRE 902
Cdd:cd05971    124 FNLfprDGDLYWTP-ADWAWIGGLLDVLLPSLYFG-VPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTAL-KMMRQQGE 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  903 NEEVGQkLSLRYVVFGGEALElSRLEDWYSRHPHNApkVINMYGITETTVHVSyielDESIVSLRANSLIGCSIPDLKVY 982
Cdd:cd05971    201 QLKHAQ-VKLRAIATGGESLG-EELLGWAREQFGVE--VNEFYGQTECNLVIG----NCSALFPIKPGSMGKPIPGHRVA 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  983 VLDNYLQPVPPGVVGEMYV----AGAGLarGYLGRAGLTAERFIADPFgkpgtrmyRTGDLARWRQDGTLDYIGRADHQI 1058
Cdd:cd05971    273 IVDDNGTPLPPGEVGEIAVelpdPVAFL--GYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVI 342

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1059 KIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETID---TNEMRQHASGSLPDYMVPYAFVVVN 1135
Cdd:cd05971    343 TSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVN 422

                          490
                   ....*....|....*
gi 1698252301 1136 ELPLTPNGKLDRKAL 1150
Cdd:cd05971    423 ELPRTATGKIRRREL 437
PRK12316 PRK12316
peptide synthase; Provisional
 1-389 6.65e-44

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 176.30  E-value: 6.65e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDrpndKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:PRK12316   928 LLEHPWVREAAVLAVDG----KQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP 1003

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   81 DFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETlSVELGIGKLFESPTVAELAk 159
Cdd:PRK12316  1004 EASVAQQGYVApRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLA- 1081

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  160 QLNHAKSArPAIQKASRPNEVPLSFAQRrlWFlncLEGPSPT---YNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTI 236
Cdd:PRK12316  1082 LVAKAGQA-TAADQGPASGEVALAPVQR--WF---FEQAIPQrqhWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLR 1155

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  237 FPNVLGSSYQKILDMENLNLEMVITNTCKDELESVLSEAVRySFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSL 316
Cdd:PRK12316  1156 FREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEAQR-SLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSW 1234

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698252301  317 QPLTRDFTAAYkarcqgdRVQLETLPVQYADYALWQQQLLGDETTpeslISTQLDFWKEELKGLPDqmELPTD 389
Cdd:PRK12316  1235 RILLEDLQRAY-------ADLDADLPARTSSYQAWARRLHEHAGA----RAEELDYWQAQLEDAPH--ELPCE 1294
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 644-1150 1.03e-43

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: 168.02  E-value: 1.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAgyLPL 723
Cdd:COG1021     26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 DPdYPSDR---ISFMLHDAKPSCVLTNSSVE-----------IECDESLK--ILVDDVNVMEEIEKYSEENIDEMEClkP 787
Cdd:COG1021    104 FA-LPAHRraeISHFAEQSEAVAYIIPDRHRgfdyralarelQAEVPSLRhvLVVGDAGEFTSLDALLAAPADLSEP--R 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  788 LAPSHIAYVIYTSGSTGRPKgvMIP--HQ----NV---VRLLGatdhwfqFDADDVW----TMFHSYAFdfSVWEIWGPL 854
Cdd:COG1021    181 PDPDDVAFFQLSGGTTGLPK--LIPrtHDdylySVrasAEICG-------LDADTVYlaalPAAHNFPL--SSPGVLGVL 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  855 LYGGRLVVVPhtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQA-DRENEEVGqklSLRYVVFGGealelSRLEdwysr 933
Cdd:COG1021    250 YAGGTVVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLDAaERSRYDLS---SLRVLQVGG-----AKLS----- 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  934 hPHNAPKVINMYGITETTVH------VSYIELDESiVSLRANSlIGCSI-PDLKVYVLDNYLQPVPPGVVGEMYVAGAGL 1006
Cdd:COG1021    314 -PELARRVRPALGCTLQQVFgmaeglVNYTRLDDP-EEVILTT-QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYT 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1007 ARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIkIRGfrielGE------IEAVIMKHDKV 1080
Cdd:COG1021    391 IRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAV 457

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1081 EQVAVIVREDQPGDKRLVAYIVAsNNETIDTNEMRQH--ASGsLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:COG1021    458 HDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFlrERG-LAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 669-1150 1.17e-43

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: 167.41  E-value: 1.17e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:cd05904     33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SVEiecdESLKILVDDVNVMEEIEKYSEENIDEMECLKPLAP-------SHIAYVIYTSGSTGRPKGVMIPHQNVVRLLg 821
Cdd:cd05904    113 ELA----EKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLIAMV- 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  822 ATDHWF---QFDADDVW----TMFHSYAFdfsVWEIWGPLLYGGRLVVVPHTVSRspkEFLQLLVKEKVTVLNQTPSAFY 894
Cdd:cd05904    188 AQFVAGegsNSDSEDVFlcvlPMFHIYGL---SSFALGLLRLGATVVVMPRFDLE---ELLAAIERYKVTHLPVVPPIVL 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  895 QLmqADRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVHVSYIELDESiVSLRANSlIGC 974
Cdd:cd05904    262 AL--VKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN--VDLGQGYGMTESTGVVAMCFAPEK-DRAKYGS-VGR 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  975 SIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGR 1053
Cdd:cd05904    336 LVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGDLCYIDEDGYLFIVDR 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1054 ADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLpdymVPY---- 1129
Cdd:cd05904    409 LKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV----APYkkvr 484

                          490       500
                   ....*....|....*....|...
gi 1698252301 1130 --AFvvVNELPLTPNGKLDRKAL 1150
Cdd:cd05904    485 kvAF--VDAIPKSPSGKILRKEL 505
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 644-1150 3.31e-43

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: 165.19  E-value: 3.31e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAgyLPL 723
Cdd:cd05920     16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 DPdYPSDRISFMLHDAKPScvltnssveiecdESLKILVDDVNvmeeiekyseENIDEMECLKPLAPSH--IAYVIYTSG 801
Cdd:cd05920     94 LA-LPSHRRSELSAFCAHA-------------EAVAYIVPDRH----------AGFDHRALARELAESIpeVALFLLSGG 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  802 STGRPKgvMIP--HQNVVRLLGATDHWFQFDADDVWTMFHSYAFDF--SVWEIWGPLLYGGRLVVVPhtvSRSPKEFLQL 877
Cdd:cd05920    150 TTGTPK--LIPrtHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFplACPGVLGTLLAGGRVVLAP---DPSPDAAFPL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  878 LVKEKVTVLNQTPSAFYQLMQAdrENEEVGQKLSLRYVVFGGealelSRLEDWYSR--HPHNAPKVINMYGITETTVhvS 955
Cdd:cd05920    225 IEREGVTVTALVPALVSLWLDA--AASRRADLSSLRLLQVGG-----ARLSPALARrvPPVLGCTLQQVFGMAEGLL--N 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  956 YIELDES---IVSLRANSLIgcsiPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtr 1032
Cdd:cd05920    296 YTRLDDPdevIIHTQGRPMS----PDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------ 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1033 mYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsNNETIDTN 1112
Cdd:cd05920    366 -YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL-RDPPPSAA 443

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1698252301 1113 EMRQHASG-SLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05920    444 QLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1-162 1.12e-42

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 171.38  E-value: 1.12e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPND------KRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:PRK10252   879 MQALPDVEQAVTHACVINQAAatggdaRQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR 958

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   75 KKLPAPDFNGMNNERVARNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTV 154
Cdd:PRK10252   959 KALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTV 1038


                   ....*...
gi 1698252301  155 AELAKQLN 162
Cdd:PRK10252  1039 AKLATLLD 1046
PRK12467 PRK12467
peptide synthase; Provisional
 1-355 1.13e-42

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 172.27  E-value: 1.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVReDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:PRK12467  3513 LLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   81 DFNGMNNERVARNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAkq 160
Cdd:PRK12467  3592 DAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-- 3669

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  161 lnhaksarpaiqkasrpnevplsfaqrrlwflncleGPSPTYNIPLvirmNGILNRQALQGAFYDVVEKHETLRTIFpnv 240
Cdd:PRK12467  3670 ------------------------------------GYSPLGDVPV----NLLLDLNRLETGFPALFCRHEGLGTVF--- 3706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  241 lgssyqkildmenlnlemvitntckdelesvlseavrysfnlDFEPAVRLqlftVSENEHVLLILLHHIVGDGWSlqplt 320
Cdd:PRK12467  3707 ------------------------------------------DYEPLAVI----LEGDRHVLGLTCRHLLDDGWQ----- 3735

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1698252301  321 rdftaaykarcqgdRVQLETLPVQYADYALWQQQL 355
Cdd:PRK12467  3736 --------------DTSLQAMAVQYADYILWQQAK 3756
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 181-611 1.36e-42

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: 161.77  E-value: 1.36e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLNLEMVI 260
Cdd:cd19533      3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHID 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  261 TNTCKDELESVLS---EAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGDRVQ 337
Cdd:cd19533     83 LSGDPDPEGAAQQwmqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAP 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  338 LETLPvQYADYALWQQQLLGDEttpesliSTQLD--FWKEELKGLPDQMELPTDYQRPVeTSYRGETIHFhiDEGMHSRL 415
Cdd:cd19533    163 PAPFG-SFLDLVEEEQAYRQSE-------RFERDraFWTEQFEDLPEPVSLARRAPGRS-LAFLRRTAEL--PPELTRTL 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  416 VELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVN 495
Cdd:cd19533    232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSREL 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  496 LAAYENQDVPFERLVEVLNpvRTRNSHPLFQVMLAFQnTPEATFNAPDLEASLEIQSVGSAKfDLTFEISEsnevDGTPN 575
Cdd:cd19533    312 RSLLRHQRYRYEDLRRDLG--LTGELHPLFGPTVNYM-PFDYGLDFGGVVGLTHNLSSGPTN-DLSIFVYD----RDDES 383

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 1698252301  576 GLHGLLEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19533    384 GLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 669-1150 2.54e-42

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


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 161.49  E-value: 2.54e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SVEiecdeslkilvddvnvmeeiekyseenidemeclkplapsHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ 828
Cdd:cd05935     82 ELD----------------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FDADDVWT----MFHSYAFDFSVWeiwGPLLYGGRLVVVphtvSRSPKEFL-QLLVKEKVTVLNQTPSAFYQLMqADREN 903
Cdd:cd05935    122 LTPSDVILaclpLFHVTGFVGSLN---TAVYVGGTYVLM----ARWDRETAlELIEKYKVTFWTNIPTMLVDLL-ATPEF 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  904 EEVGQKlSLRYVVFGGEALELSRLEDWYSRhphNAPKVINMYGITETtvhvsyieLDESIVSLRANSLIGC-SIP----D 978
Cdd:cd05935    194 KTRDLS-SLKVLTGGGAPMPPAVAEKLLKL---TGLRFVEGYGLTET--------MSQTHTNPPLRPKLQClGIP*fgvD 261

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  979 LKVYVLDNyLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPfgkpGTRMYRTGDLARWRQDGTLDYIGRADHQI 1058
Cdd:cd05935    262 ARVIDIET-GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFFVDRVKRMI 336

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1059 KIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV--ASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNE 1136
Cdd:cd05935    337 NVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDE 416

                          490
                   ....*....|....
gi 1698252301 1137 LPLTPNGKLDRKAL 1150
Cdd:cd05935    417 LPRSASGKILWRLL 430
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 656-1150 3.10e-42

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


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 162.68  E-value: 3.10e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  656 NPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFM 735
Cdd:cd05923     16 DACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  736 LHDAK-PSCVLTNSS--VEIECDESLKILVDDVNV-MEEIEKYSEENIDemeclKPLAPSHIAYVIYTSGSTGRPKGVMI 811
Cdd:cd05923     96 IERGEmTAAVIAVDAqvMDAIFQSGVRVLALSDLVgLGEPESAGPLIED-----PPREPEQPAFVFYTSGTTGLPKGAVI 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  812 PHQNVVR--LLGATDHWFQFDADDV----WTMFHSYAFdFSVweIWGPLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTV 885
Cdd:cd05923    171 PQRAAESrvLFMSTQAGLRHGRHNVvlglMPLYHVIGF-FAV--LVAALALDGTYVVVEEF---DPADALKLIEQERVTS 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  886 LNQTPSAFYQLMQADrenEEVGQKL-SLRYVVFGGEALELSRLEdwySRHPHNAPKVINMYGITETtVHVSYIELDESIV 964
Cdd:cd05923    245 LFATPTHLDALAAAA---EFAGLKLsSLRHVTFAGATMPDAVLE---RVNQHLPGEKVNIYGTTEA-MNSLYMRDARTGT 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  965 SLRANSLIGCSIpdlkVYVLDNYLQPVPPGVVGEMYVAGAGLA--RGYLGRAGLTAERFIadpFGKpgtrmYRTGDLARW 1042
Cdd:cd05923    318 EMRPGFFSEVRI----VRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ---DGW-----YRTGDVGYV 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsNNETIDTNEMRQHASGS- 1121
Cdd:cd05923    386 DPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVP-REGTLSADELDQFCRASe 464

                          490       500
                   ....*....|....*....|....*....
gi 1698252301 1122 LPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05923    465 LADFKRPRRYFFLDELPKNAMNKVLRRQL 493
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 641-1148 3.16e-42

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 164.40  E-value: 3.16e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  641 PEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGY 720
Cdd:PRK05605    30 GDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  721 LPLDPDYPSDRISFML--HDAKPSCVLTNSSVEIECdeslkiLVDDVNVmEEIekYSEENIDEMECLKPLA--------- 789
Cdd:PRK05605   110 VEHNPLYTAHELEHPFedHGARVAIVWDKVAPTVER------LRRTTPL-ETI--VSVNMIAAMPLLQRLAlrlpipalr 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 -------------------------------------PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDAD 832
Cdd:PRK05605   181 karaaltgpapgtvpwetlvdaaiggdgsdvshprptPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGD 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  833 D------VWTMFHSY------AFDFSVweiwgpllyGGRLVVVPhtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQAD 900
Cdd:PRK05605   261 GpervlaALPMFHAYgltlclTLAVSI---------GGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  901 RENeevGQKLS-LRYVVFGGEALELSRLEDWYSrhpHNAPKVINMYGITETtvhvSYIELDESIVSLRANSLIGCSIPDL 979
Cdd:PRK05605   329 EER---GVDLSgVRNAFSGAMALPVSTVELWEK---LTGGLLVEGYGLTET----SPIIVGNPMSDDRRPGYVGVPFPDT 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  980 KVYVLD--NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgkpgtrMYRTGDLARWRQDGTLDYIGRADHQ 1057
Cdd:PRK05605   399 EVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKEL 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1058 IKIRGFRIELGEIEAVIMKHDKVEQVAV--IVREDqpGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVN 1135
Cdd:PRK05605   471 IITGGFNVYPAEVEEVLREHPGVEDAAVvgLPRED--GSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVD 548

                          570
                   ....*....|...
gi 1698252301 1136 ELPLTPNGKLDRK 1148
Cdd:PRK05605   549 ELPRDQLGKVRRR 561
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 653-1150 4.05e-42

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 162.36  E-value: 4.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRI 732
Cdd:PRK06145    12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  733 SFMLHDAKPSCVLTNSSVEIECDESLKILVDDVNVMEEIEKYSE--ENIDEMEclkPLAPSHIAYVIYTSGSTGRPKGVM 810
Cdd:PRK06145    92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQggLEIPPQA---AVAPTDLVRLMYTSGTTDRPKGVM 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  811 IPHQNVvrllgatdHWFQFD--------ADD----VWTMFHSYAFDFSVWEIwgpLLYGGRLVVVPHTvsrSPKEFLQLL 878
Cdd:PRK06145   169 HSYGNL--------HWKSIDhvialgltASErllvVGPLYHVGAFDLPGIAV---LWVGGTLRIHREF---DPEAVLAAI 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQTPSAFYQLMQA-DRENEEVGqklSLRYVVFGGEALELSRLEDwYSRHPHNApKVINMYGITETTVHVSYI 957
Cdd:PRK06145   235 ERHRLTCAWMAPVMLSRVLTVpDRDRFDLD---SLAWCIGGGEKTPESRIRD-FTRVFTRA-RYIDAYGLTETCSGDTLM 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  958 ELDESIVSLRANsliGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmyRTG 1037
Cdd:PRK06145   310 EAGREIEKIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSG 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1038 DLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQH 1117
Cdd:PRK06145   379 DVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRH 458

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1698252301 1118 ASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06145   459 CRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PRK05691 PRK05691
peptide synthase; Validated
 1-389 5.03e-41

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 166.88  E-value: 5.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVReDRPNDKRIIAYIVAE-----EKEPINLSE-IRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:PRK05691  2610 LLEHPAVREAVVLAL-DTPSGKQLAGYLVSAvagqdDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDR 2688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   75 KKLPAPDFNGMNNERVA-RNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIREtLSVELGIGKLFESPT 153
Cdd:PRK05691  2689 RALPAPDPELNRQAYQApRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQT 2767

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  154 VAELAKQLNHakSARPAIQKASRPNEVPLSFAQRrlWFLNcLEGPSPT-YNIPLVIRMNGILNRQALQGAFYDVVEKHET 232
Cdd:PRK05691  2768 VQTLAAVATH--SEAAQAEQGPLQGASGLTPIQH--WFFD-SPVPQPQhWNQALLLEPRQALDPALLEQALQALVEHHDA 2842

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  233 LRTIFPNVLG---SSYQKILDMEnlnLEMVITNTCKDELESVLSEAVRySFNLDFEPAVRLQLFTVSENEHVLLILLHHI 309
Cdd:PRK05691  2843 LRLRFSQADGrwqAEYRAVTAQE---LLWQVTVADFAECAALFADAQR-SLDLQQGPLLRALLVDGPQGQQRLLLAIHHL 2918

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  310 VGDGWSLQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLLGDETTPEslistQLDFWKEELKGLPdqMELPTD 389
Cdd:PRK05691  2919 VVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLRE-----ELGWWQAQLGGPR--AELPCD 2991
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 657-1149 7.27e-40

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: 157.02  E-value: 7.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVF------EDKKLTYEKLNRKANKIARFLIAKGvGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS- 729
Cdd:cd05931      7 PDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGr 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 --DRISFMLHDAKPSCVLTNSSV---------EIECDESLKILVDDVnvmeeiekySEENIDEMECLKPLAPSHIAYVIY 798
Cdd:cd05931     86 haERLAAILADAGPRVVLTTAAAlaavrafaaSRPAAGTPRLLVVDL---------LPDTSAADWPPPSPDPDDIAYLQY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWT----MFHSYAFDFSvweIWGPLLYGGRLVVV-PHTVSRSPKE 873
Cdd:cd05931    157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlpLYHDMGLIGG---LLTPLYSGGPSVLMsPAAFLRRPLR 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  874 FLQLLVKEKVTVlnqtpSA---F-YQLMqADRENEEVGQKL---SLRYVVFGGEALELSRLEDWYSRH-PHN-APKVIN- 943
Cdd:cd05931    234 WLRLISRYRATI-----SAapnFaYDLC-VRRVRDEDLEGLdlsSWRVALNGAEPVRPATLRRFAEAFaPFGfRPEAFRp 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  944 MYGITETTVHVSYIELDESIVSLR-------------------ANSLIGC--SIPDLKVYVLD-NYLQPVPPGVVGEMYV 1001
Cdd:cd05931    308 SYGLAEATLFVSGGPPGTGPVVLRvdrdalagravavaaddpaARELVSCgrPLPDQEVRIVDpETGRELPDGEVGEIWV 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1002 AGAGLARGYLGRAGLTAERFIADPfGKPGTRMYRTGDLARwRQDGTLdYI-GRADHQIKIRGFRIELGEIEAVIMKHDKV 1080
Cdd:cd05931    388 RGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLGF-LHDGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEAHPA 464

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1081 EQ---VAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDY--MVPYAFVVV--NELPLTPNGKLDRKA 1149
Cdd:cd05931    465 LRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADVVLVrpGSIPRTSSGKIQRRA 540
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 670-1150 7.57e-40

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: 156.25  E-value: 7.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  670 TYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSS 749
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  750 VE--IE-CDESLK-----ILVDDVNVMEE-----IEKYsEENID--EMECLKPLAPSHIAYVI-YTSGSTGRPKGVMIPH 813
Cdd:cd12119    107 FLplLEaIAPRLPtvehvVVMTDDAAMPEpagvgVLAY-EELLAaeSPEYDWPDFDENTAAAIcYTSGTTGNPKGVVYSH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  814 QNVV--RLLGATDHWFQFDADDVWT----MFHSYAfdfsvweiWG-P---LLYGGRLVVV-PHTvsrSPKEFLQLLVKEK 882
Cdd:cd12119    186 RSLVlhAMAALLTDGLGLSESDVVLpvvpMFHVNA--------WGlPyaaAMVGAKLVLPgPYL---DPASLAELIEREG 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  883 VTVLNQTPSAFYQLMQA-DRENEEVgqkLSLRYVVFGGEALELSRLEDWYSRHPhnapKVINMYGITETT--VHVSYI-- 957
Cdd:cd12119    255 VTFAAGVPTVWQGLLDHlEANGRDL---SSLRRVVIGGSAVPRSLIEAFEERGV----RVIHAWGMTETSplGTVARPps 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  958 ---ELD-ESIVSLRANSliGCSIPDLKVYVLDNYLQPVP--PGVVGEMYVAGAGLARGYLGRAGlTAERFIADPFgkpgt 1031
Cdd:cd12119    328 ehsNLSeDEQLALRAKQ--GRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGW----- 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1032 rmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDT 1111
Cdd:cd12119    400 --LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA 477

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1698252301 1112 NEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd12119    478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
650-1150 8.74e-40

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 155.40  E-value: 8.74e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  650 EKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAK-GVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYP 728
Cdd:PRK06839     9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  729 SDRISFMLHDAKPSCVL-----TNSSVEIECDESLKILVDdVNVMEEIEKYSEENIDEMECLKPLapshiaYVIYTSGST 803
Cdd:PRK06839    89 ENELIFQLKDSGTTVLFvektfQNMALSMQKVSYVQRVIS-ITSLKEIEDRKIDNFVEKNESASF------IICYTSGTT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  804 GRPKGVMIPHQNVvrLLGATDHWFQFD--ADDV----WTMFHS-----YAFdfsvweiwgPLLYGGRLVVVPHTVSrsPK 872
Cdd:PRK06839   162 GKPKGAVLTQENM--FWNALNNTFAIDltMHDRsivlLPLFHIggiglFAF---------PTLFAGGVIIVPRKFE--PT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  873 EFLQLLVKEKVTVLNQTPSAFYQLMQA-DRENEEVGqklSLRYVVFGGEALELSRLEDWYSRhphnAPKVINMYGITETT 951
Cdd:PRK06839   229 KALSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQ---SVRWFYNGGAPCPEELMREFIDR----GFLFGQGFGMTETS 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  952 VHVSYIELDESivsLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERfIADPFgkpgt 1031
Cdd:PRK06839   302 PTVFMLSEEDA---RRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW----- 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1032 rmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDT 1111
Cdd:PRK06839   373 --LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE 450

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1698252301 1112 NEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06839   451 KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 661-1154 8.79e-40

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 155.15  E-value: 8.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  661 AVVFEDKKLTYEKLNRKANKIARfliakGVGPDQLVA-LAMPrSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDA 739
Cdd:PRK07787    18 AVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAvLATP-TLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADS 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  740 KPSCVLTNSSveiecDESLKILVDDVNVMEEI-EKYSEENidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNVVR 818
Cdd:PRK07787    92 GAQAWLGPAP-----DDPAGLPHVPVRLHARSwHRYPEPD-----------PDAPALIVYTSGTTGPPKGVVLSRRAIAA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  819 LLGA-TDHWfQFDADDVWT----MFHSYAFdfsVWEIWGPLLYGGRLVvvpHTVSRSPKEFLQLLvKEKVTVLNQTPSAF 893
Cdd:PRK07787   156 DLDAlAEAW-QWTADDVLVhglpLFHVHGL---VLGVLGPLRIGNRFV---HTGRPTPEAYAQAL-SEGGTLYFGVPTVW 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  894 YQLMqadrENEEVGQKLS-LRYVVFGGEALELSRLEDWYSRHPHnapKVINMYGITETTVhvsyieldesIVSLRANS-- 970
Cdd:PRK07787   228 SRIA----ADPEAARALRgARLLVSGSAALPVPVFDRLAALTGH---RPVERYGMTETLI----------TLSTRADGer 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  971 ---LIGCSIPDLKVYVLDNYLQPVP--PGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQD 1045
Cdd:PRK07787   291 rpgWVGLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPD 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1046 GTLDYIGR-ADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASnnETIDTNEMRQHASGSLPD 1124
Cdd:PRK07787   364 GMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGA--DDVAADELIDFVAQQLSV 441

                          490       500       510
                   ....*....|....*....|....*....|
gi 1698252301 1125 YMVPYAFVVVNELPLTPNGKLDRKALPAPE 1154
Cdd:PRK07787   442 HKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 181-603 2.78e-39

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: 151.57  E-value: 2.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIF---PN----VLGSSYQKILDMEN 253
Cdd:cd19537      3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYvprDGglrrSYSSSPPRVQRVDT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  254 LNLemvitntckdelesvlSEAVRYSFNLDFEPAVRLqlfTVSENEhvLLILLHHIVGDGWSLQPLTRDFTAAYKARcqg 333
Cdd:cd19537     83 LDV----------------WKEINRPFDLEREDPIRV---FISPDT--LLVVMSHIICDLTTLQLLLREVSAAYNGK--- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 drvQLETLPVQYADYALWQQQLlgdetTPEslistQLDFWKEELKGLPdQMELPTdyqRPVETSYRGETIHFHIDEGMHS 413
Cdd:cd19537    139 ---LLPPVRREYLDSTAWSRPA-----SPE-----DLDFWSEYLSGLP-LLNLPR---RTSSKSYRGTSRVFQLPGSLYR 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  414 RLVELGRKNGVSLfmvLQAGLSALFTRLGA---GTDIPIGSPIAGRNDDVLSDIVGLFVNTLVLR--TNTSGDPSFKELL 488
Cdd:cd19537    202 SLLQFSTSSGITL---HQLALAAVALALQDlsdRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFL 278

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  489 NRVKQVNLAAYENQdVPFERLVEVLNPVRTRNSHPLFQVMLAFQN--TPEATFNAPDLEaSLEIQSVGsAKFDLTFEISE 566
Cdd:cd19537    279 RAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMVTFHDdrGVSLALPIPGVE-PLYTWAEG-AKFPLMFEFTA 355

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1698252301  567 SNEvDGTpnGLHglLEFSTDLYKRETVQkLIERFILL 603
Cdd:cd19537    356 LSD-DSL--LLR--LEYDTDCFSEEEID-RIESLILA 386
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 656-1153 4.47e-39

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 153.99  E-value: 4.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  656 NPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFM 735
Cdd:PRK06188    25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  736 LHDAKPSCVLTNSSVEIE--------CDESLKIL----VDD-VNVMEEIEKYSEenidemeclKPL----APSHIAYVIY 798
Cdd:PRK06188   105 LEDAGISTLIVDPAPFVEralallarVPSLKHVLtlgpVPDgVDLLAAAAKFGP---------APLvaaaLPPDIAGLAY 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHSYAFDFSvweiwgP-LLYGGRLVVVPhtvSRSPKE 873
Cdd:PRK06188   176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPrflmCTPLSHAGGAFFL------PtLLRGGTVIVLA---KFDPAE 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  874 FLQLLVKEKVTVLNQTPSAFYQLMQADRENEevgQKLS-LRYVVFGGEALELSRLEDWYSRHphnAPKVINMYGITETTV 952
Cdd:PRK06188   247 VLRAIEEQRITATFLVPTMIYALLDHPDLRT---RDLSsLETVYYGASPMSPVRLAEAIERF---GPIFAQYYGQTEAPM 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  953 HVSYI---ELDESIVSLRANSliGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFiadpfgKP 1029
Cdd:PRK06188   321 VITYLrkrDHDPDDPKRLTSC--GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RD 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1030 GtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDKrLVAYIVASNNET 1108
Cdd:PRK06188   393 G--WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgVPDEKWGEA-VTAVVVLRPGAA 469

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1698252301 1109 IDTNEMRQH---ASGSLpdyMVPYAFVVVNELPLTPNGKLDRKALPAP 1153
Cdd:PRK06188   470 VDAAELQAHvkeRKGSV---HAPKQVDFVDSLPLTALGKPDKKALRAR 514
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
642-1150 8.98e-39

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 153.75  E-value: 8.98e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFE-DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGY 720
Cdd:PRK06087    22 DASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  721 LPLDPDYPSDRISFMLHDAK------PSCVLTNSSVE--IECDESLKILVDDVNVMEEIEKYSE----ENIDEMECLKPL 788
Cdd:PRK06087   102 VPLLPSWREAELVWVLNKCQakmffaPTLFKQTRPVDliLPLQNQLPQLQQIVGVDKLAPATSSlslsQIIADYEPLTTA 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 APSH---IAYVIYTSGSTGRPKGVMIPHQNVV---RLLGATDHwfqFDADDVWTM----FHSYAFDFSVweiWGPLLYGG 858
Cdd:PRK06087   182 ITTHgdeLAAVLFTSGTEGLPKGVMLTHNNILaseRAYCARLN---LTWQDVFMMpaplGHATGFLHGV---TAPFLIGA 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  859 RLVVVPHTvsrSPKEFLQLLVKEKVT-VLNQTPSAFYQLMQADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRHphn 937
Cdd:PRK06087   256 RSVLLDIF---TPDACLALLEQQRCTcMLGATPFIYDLLNLLEKQPADLS---ALRFFLCGGTTIPKKVARECQQRG--- 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  938 aPKVINMYGITETTVHVsYIELDESIVSLRANSliGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLT 1017
Cdd:PRK06087   327 -IKLLSVYGSTESSPHA-VVNLDDPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELT 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1018 AERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRaDHQIKIRGFR-IELGEIEAVIMKHDKVEQVAVIVREDQPGDKR 1096
Cdd:PRK06087   403 ARALDEEGW-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGER 474

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1097 LVAYIVASNNE-TIDTNEMRQH-ASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06087   475 SCAYVVLKAPHhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 656-1145 1.60e-38

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


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 153.50  E-value: 1.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  656 NPNSIAVVFED------KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:cd17634     66 NGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAP 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAKPSCVLTNS-------SVEIE--CDESLK---------ILVD------------DVNVMEEIEKYSEENI 779
Cdd:cd17634    146 EAVAGRIIDSSSRLLITADggvragrSVPLKknVDDALNpnvtsvehvIVLKrtgsdidwqegrDLWWRDLIAKASPEHQ 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  780 DEmeclkPLAPSHIAYVIYTSGSTGRPKGVMipHQNVVRLLGAT---DHWFQFDADDV--------WTMFHSyafdfsvW 848
Cdd:cd17634    226 PE-----AMNAEDPLFILYTSGTTGKPKGVL--HTTGGYLVYAAttmKYVFDYGPGDIywctadvgWVTGHS-------Y 291

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  849 EIWGPLLYGGRLVV---VPhtVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELS 925
Cdd:cd17634    292 LLYGPLACGATTLLyegVP--NWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPE 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  926 RLEdWYSRH--PHNAPkVINMYGITETTVHVSyieldeSIVSLRANSLIGCS---IPDLKVYVLDNYLQPVPPGVVGEMY 1000
Cdd:cd17634    370 AYE-WYWKKigKEKCP-VVDTWWQTETGGFMI------TPLPGAIELKAGSAtrpVFGVQPAVVDNEGHPQPGGTEGNLV 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1001 VAGA--GLARGYLGRAGLTAERFIADPFGkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHD 1078
Cdd:cd17634    442 ITDPwpGQTRTLFGDHERFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1079 KVEQVAVIVREDQPGDKRLVAYIVASNNETID---TNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:cd17634    517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 642-1146 6.00e-38

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 150.81  E-value: 6.00e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PRK07798     2 AWNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFMLHDAKPSCVLTNSS------------------VEIECDESLKILVDDVNVMEEIEKYSEEnideme 783
Cdd:PRK07798    82 NVNYRYVEDELRYLLDDSDAVALVYEREfaprvaevlprlpklrtlVVVEDGSGNDLLPGAVDYEDALAAGSPE------ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  784 clkPLAPSHIA---YVIYTSGSTGRPKGVMIPHQNVVR-LLGATDHWFQFDADDVWT------------------MFHSY 841
Cdd:PRK07798   156 ---RDFGERSPddlYLLYTGGTTGMPKGVMWRQEDIFRvLLGGRDFATGEPIEDEEElakraaagpgmrrfpappLMHGA 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  842 AFdfsvWEIWGPLLYGGRLVVVPHtVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEA 921
Cdd:PRK07798   233 GQ----WAAFAALFSGQTVVLLPD-VRFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGAL 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  922 LELSRLEDWYSRHPHNApkVINMYGITET----TVHVS---------YIELDESIVslransligcsipdlkvyVLDNYL 988
Cdd:PRK07798   308 FSPSVKEALLELLPNVV--LTDSIGSSETgfggSGTVAkgavhtggpRFTIGPRTV------------------VLDEDG 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  989 QPVPPGVVGEMYVAGAG-LARGYLGRAGLTAERF-IADpfgkpGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIE 1066
Cdd:PRK07798   368 NPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETFpTID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVF 442

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1067 LGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLD 1146
Cdd:PRK07798   443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 191-611 2.89e-37

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: 145.91  E-value: 2.89e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  191 FLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIF--PNVLGSSYQKILDmeNLNLEMVITNTCKDEL 268
Cdd:cd19542     11 MLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVVLK--SLDPPIEEVETDEDSL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  269 ESVLSEAVRYSFnLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKArcqgdrvQLETLPVQYADY 348
Cdd:cd19542     89 DALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLPPAPPFSDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  349 ALWQQQLLGDETtpeslistqLDFWKEELKGLPDQMElptdyqrPVETSYRGETIHFHIDEGMHSRLVELGRKNGVSLFM 428
Cdd:cd19542    161 ISYLQSQSQEES---------LQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLAS 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  429 VLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLS--DIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVNLAAYENQDVPF 506
Cdd:cd19542    225 LFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGidDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSL 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  507 ERLVEVLNPVRTRnshPLFQVMLAFQNTPEATFNAPDLEASLEIQSVGSA-KFDLTFEISESnevdgtPNGLHGLLEFST 585
Cdd:cd19542    305 REIQRALGLWPSG---TLFNTLVSYQNFEASPESELSGSSVFELSAAEDPtEYPVAVEVEPS------GDSLKVSLAYST 375

                          410       420
                   ....*....|....*....|....*.
gi 1698252301  586 DLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19542    376 SVLSEEQAEELLEQFDDILEALLANP 401
PRK05691 PRK05691
peptide synthase; Validated
 644-1257 9.42e-37

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 153.01  E-value: 9.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVF------EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALaMPRSLNMVVSLLAVLKAG 717
Cdd:PRK05691    10 TLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARASFGDRAVLL-FPSGPDYVAAFFGCLYAG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  718 AGYLPLDPDYPS-----DRISFMLHDAKPSCVLTNSSVEiecdESLkilvddvnvmEEIEKYSEENIDEMEC---LKP-- 787
Cdd:PRK05691    89 VIAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLR----DSL----------LQMEELAAANAPELLCvdtLDPal 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  788 --------LAPSHIAYVIYTSGSTGRPKGVMIPHQNVVrllgatdhwfqfdADDvWTMFHSYAFDFS---VWEIWGPL-- 854
Cdd:PRK05691   155 aeawqepaLQPDDIAFLQYTSGSTALPKGVQVSHGNLV-------------ANE-QLIRHGFGIDLNpddVIVSWLPLyh 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  855 ---LYGGRLVV----VPhTVSRSPKEFLQLLVK--EKVTVLNQT----PSAFYQLMqADRENEEVGQKLSL---RYVVFG 918
Cdd:PRK05691   221 dmgLIGGLLQPifsgVP-CVLMSPAYFLERPLRwlEAISEYGGTisggPDFAYRLC-SERVSESALERLDLsrwRVAYSG 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  919 GEALELSRLE---DWYSRHPHNAPKVINMYGITETTVHVSYIELDESIVSLRANS---------------LIGCSI--PD 978
Cdd:PRK05691   299 SEPIRQDSLErfaEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAealarnraepgtgsvLMSCGRsqPG 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  979 LKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIAdpfgKPGTRMYRTGDLArWRQDGTLDYIGRADHQ 1057
Cdd:PRK05691   379 HAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLG-FLRDGELFVTGRLKDM 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1058 IKIRGFRIELGEIEAVIMKHDKV---EQVAVIVREDQPGDKRLVAYIVASNNETIDTNE-----MRQHASGSLPDymVPY 1129
Cdd:PRK05691   454 LIVRGHNLYPQDIEKTVEREVEVvrkGRVAAFAVNHQGEEGIGIAAEISRSVQKILPPQaliksIRQAVAEACQE--APS 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1130 AFVVVN--ELPLTPNGKLDRKA---------------LPAPEFIASSSSRGPRTPQEEMLCDLFTEVLSVSQIGIDDGFF 1192
Cdd:PRK05691   532 VVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFF 611

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1193 DLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLA---ERLEIGNGQSALDVllPLRASGDQLP 1257
Cdd:PRK05691   612 LLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSaavARQLAGGGAAQAAI--ARLPRGQALP 677
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 669-1150 1.10e-36

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: 144.97  E-value: 1.10e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SveiecdeSLKILVDDVNVMeeiekyseenidemeclkplapshiayvIYTSGSTGRPKGVMIPhqnvVRLLGATDHWFQ 828
Cdd:cd05973     81 A-------NRHKLDSDPFVM----------------------------MFTSGTTGLPKGVPVP----LRALAAFGAYLR 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  829 FD------------ADDVWTMFHSYAfdfsvweIWGPLLYGgrlvvVPHTVSR---SPKEFLQLLVKEKVTVLNQTPSAF 893
Cdd:cd05973    122 DAvdlrpedsfwnaADPGWAYGLYYA-------ITGPLALG-----HPTILLEggfSVESTWRVIERLGVTNLAGSPTAY 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  894 YQLMQADREnEEVGQKLSLRYVVFGGEALElSRLEDWYSR------HPHnapkvinmYGITETTVHVSYIELDESIVslR 967
Cdd:cd05973    190 RLLMAAGAE-VPARPKGRLRRVSSAGEPLT-PEVIRWFDAalgvpiHDH--------YGQTELGMVLANHHALEHPV--H 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  968 ANSLiGCSIPDLKVYVLDNYLQPVPPGVVGEMY--VAGAGLA--RGYLGRAgltaerfIADPFGkpgtRMYRTGDLARWR 1043
Cdd:cd05973    258 AGSA-GRAMPGWRVAVLDDDGDELGPGEPGRLAidIANSPLMwfRGYQLPD-------TPAIDG----GYYLTGDTVEFD 325

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1044 QDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDT---NEMRQHASG 1120
Cdd:cd05973    326 PDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPalaDELQLHVKK 405

                          490       500       510
                   ....*....|....*....|....*....|
gi 1698252301 1121 SLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05973    406 RLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 668-1150 1.60e-36

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: 144.03  E-value: 1.60e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  668 KLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCvltn 747
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  748 ssveiecdeslkilvDDvnvmeeiekyseenidemeclkplapshIAYVIYTSGSTGRPKGVMIPHQNvvrllgatdHWF 827
Cdd:cd05912     77 ---------------DD----------------------------IATIMYTSGTTGKPKGVQQTFGN---------HWW 104

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  828 Q---------FDADDVW----TMFHSYAFdfSVweIWGPLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFY 894
Cdd:cd05912    105 SaigsalnlgLTEDDNWlcalPLFHISGL--SI--LMRSVIYGMTVYLVDKF---DAEQVLHLINSGKVTIISVVPTMLQ 177

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  895 QLMQADRENEEVgqklSLRYVVFGGEALELSRLEDWYSRhphNAPkVINMYGITETTVHVSYIELDESIVSLranSLIGC 974
Cdd:cd05912    178 RLLEILGEGYPN----NLRCILLGGGPAPKPLLEQCKEK---GIP-VYQSYGMTETCSQIVTLSPEDALNKI---GSAGK 246

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  975 SIPDLKVYVLDNylqPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmyRTGDLARWRQDGTLDYIGRA 1054
Cdd:cd05912    247 PLFPVELKIEDD---GQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRR 315

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 DHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsnNETIDTNEMRQHASGSLPDYMVPYAFVVV 1134
Cdd:cd05912    316 SDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPKKIYFV 393

                          490
                   ....*....|....*.
gi 1698252301 1135 NELPLTPNGKLDRKAL 1150
Cdd:cd05912    394 DELPRTASGKLLRHEL 409
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 653-1152 5.37e-36

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 145.07  E-value: 5.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALaMPR-SLNMVVSLLAVLKAGAGYLPLDPDYPS-- 729
Cdd:PRK07788    59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARnHRGFVLALYAAGKVGARIILLNTGFSGpq 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 -------DRISFMLHDAKPSCVLTNSSVEIEcdeslKILVDDVNVMEEIEKYSE-----ENIDEMECLK-PLAPSHIAYV 796
Cdd:PRK07788   138 laevaarEGVKALVYDDEFTDLLSALPPDLG-----RLRAWGGNPDDDEPSGSTdetldDLIAGSSTAPlPKPPKPGGIV 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  797 IYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFHSyafdfsvweiWGPLLYGGRLVVVPHTVSR--- 869
Cdd:PRK07788   213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTllpaPMFHA----------TGWAHLTLAMALGSTVVLRrrf 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKL---SLRYVVFGGEAL--ELSRledwysR-HPHNAPKVIN 943
Cdd:PRK07788   283 DPEATLEDIAKHKATALVVVPVMLSRILDLG---PEVLAKYdtsSLKIIFVSGSALspELAT------RaLEAFGPVLYN 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  944 MYGITEttVHVSYIELDESIVslRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYlgragltaerfiA 1023
Cdd:PRK07788   354 LYGSTE--VAFATIATPEDLA--EAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------------T 417

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1024 DPFGKPGTR-MYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV 1102
Cdd:PRK07788   418 DGRDKQIIDgLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVV 497

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1103 ASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:PRK07788   498 KAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 666-1150 5.89e-36

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: 143.00  E-value: 5.89e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  666 DKKLTYEKLNRKANKIARFLIAKGVG-PDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCV 744
Cdd:cd05958      8 EREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  745 LtnssveieCDESLKIlVDDVnvmeeiekyseenidemeCLkplapshiayVIYTSGSTGRPKGVMIPHQNV-------- 816
Cdd:cd05958     88 L--------CAHALTA-SDDI------------------CI----------LAFTSGTTGAPKATMHFHRDPlasadrya 130

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VRLLGATDhwfqfdaDDVWTMFHSYAFDFSV-WEIWGPLLYGGRLVVVPhtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQ 895
Cdd:cd05958    131 VNVLRLRE-------DDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAYRA 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  896 LMQADRENEEVGQklSLRYVVFGGEALELSRLEDWYSRhphNAPKVINMYGITETtVHVsYIELDESivSLRANSLiGCS 975
Cdd:cd05958    201 MLAHPDAAGPDLS--SLRKCVSAGEALPAALHRAWKEA---TGIPIIDGIGSTEM-FHI-FISARPG--DARPGAT-GKP 270

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  976 IPDLKVYVLDNYLQPVPPGVVGEMYVAGAglargylgraglTAERFIADPfgkpGTRMY------RTGDLARWRQDGTLD 1049
Cdd:cd05958    271 VPGYEAKVVDDEGNPVPDGTIGRLAVRGP------------TGCRYLADK----RQRTYvqggwnITGDTYSRDPDGYFR 334

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1050 YIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETID---TNEMRQHASGSLPDYM 1126
Cdd:cd05958    335 HQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGpvlARELQDHAKAHIAPYK 414

                          490       500
                   ....*....|....*....|....
gi 1698252301 1127 VPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05958    415 YPRAIEFVTELPRTATGKLQRFAL 438
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 793-1150 2.06e-35

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: 138.23  E-value: 2.06e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 IAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFH--SYAFdfsvweIWGPLLYGGRLVVVPHt 866
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWllslPLYHvgGLAI------LVRSLLAGAELVLLER- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  867 vsRSPkeFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKLSLRYVVFGG-----EALELSRLEDWysrhphnapKV 941
Cdd:cd17630     75 --NQA--LAEDLAPPGVTHVSLVPTQLQRLLDSG---QGPAALKSLRAVLLGGapippELLERAADRGI---------PL 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITETTVHVSYIELDESivslrANSLIGCSIPDLKVYVLDNylqpvppgvvGEMYVAGAGLARGYLgragltaERF 1021
Cdd:cd17630    139 YTTYGMTETASQVATKRPDGF-----GRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL-------RGQ 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1022 IADPFGKPGTrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYI 1101
Cdd:cd17630    197 LVPEFNEDGW--FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI 274

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1698252301 1102 VasNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd17630    275 V--GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
638-1102 5.15e-35

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 142.93  E-value: 5.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  638 QIAPEMTLPQLFEKQAHINPNSIAVVFED----KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAV 713
Cdd:COG1022      6 DVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  714 LKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS--------SVEIECDESLKILV-------DDVNVM--EEIEKYSE 776
Cdd:COG1022     86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDqeqldkllEVRDELPSLRHIVVldprglrDDPRLLslDELLALGR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  777 ENIDE---MECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMF----HSYAFDFSVWe 849
Cdd:COG1022    166 EVADPaelEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplaHVFERTVSYY- 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  850 iwgpLLYGGrlVVVPHTvsRSPKEFLQLL--VK-----------EKV------TVLNQTP----------SAFYQLMQAD 900
Cdd:COG1022    245 ----ALAAG--ATVAFA--ESPDTLAEDLreVKptfmlavprvwEKVyagiqaKAEEAGGlkrklfrwalAVGRRYARAR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  901 RENEEVGQKLSLRY-----VVF----------------GGEALElSRLEDWYsrhpHNA--PkVINMYGITETTVHVSYI 957
Cdd:COG1022    317 LAGKSPSLLLRLKHaladkLVFsklrealggrlrfavsGGAALG-PELARFF----RALgiP-VLEGYGLTETSPVITVN 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  958 ELDEsivsLRANSlIGCSIPDLKVYVLDNylqpvppgvvGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTG 1037
Cdd:COG1022    391 RPGD----NRIGT-VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTG 448

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1038 DLARWRQDGTLDYIGRADHQIKIR-GFRIELGEIEAVIMKHDKVEQVAVIvredqpGDKR--LVAYIV 1102
Cdd:COG1022    449 DIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV------GDGRpfLAALIV 510
PRK12316 PRK12316
peptide synthase; Provisional
 1-167 8.50e-35

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 146.26  E-value: 8.50e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDrPNDKRIIAYIVAEEKEPINLSE--------IRSYVSESLANYMIPSAFVVLEELPLTPNGKV 72
Cdd:PRK12316  4971 LREHPAVREAVVIAQEG-AVGKQLVGYVVPQDPALADADEaqaelrdeLKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   73 DRKKLPAPDFNGMNNERVArnPKEEILCD---LFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLF 149
Cdd:PRK12316  5050 DRKALPQPDASLLQQAYVA--PRSELEQQvaaIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELF 5127

                          170
                   ....*....|....*...
gi 1698252301  150 ESPTVAELAKQLNHAKSA 167
Cdd:PRK12316  5128 QTPTLAAFVELAAAAGSG 5145
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
669-1235 1.23e-34

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 143.25  E-value: 1.23e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:PRK06060    31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SVeieCDEslkilVDDVNVMEEIEKYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGAT-DHWF 827
Cdd:PRK06060   111 AL---RDR-----FQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKAL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  828 QFDADDVW----TMFHSYAFDFSVWeiwGPLLYGGRLVVVPHTVSRSPKEFLQllVKEKVTVLNQTPSAFYQLMQADREN 903
Cdd:PRK06060   183 RLTPEDTGlcsaRMYFAYGLGNSVW---FPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVPNFFARVIDSCSPD 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  904 eevgQKLSLRYVVFGGEALELS---RLEDWYSRHPhnapkVINmyGITETTVHVSYIEldESIVSLRANSLiGCSIPDLK 980
Cdd:PRK06060   258 ----SFRSLRCVVSAGEALELGlaeRLMEFFGGIP-----ILD--GIGSTEVGQTFVS--NRVDEWRLGTL-GRVLPPYE 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  981 VYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAgltaerfiaDPFGKPGTRMyRTGDLARWRQDGTLDYIGRADHQIKI 1060
Cdd:PRK06060   324 IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVI 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1061 RGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMR---QHASGSLPDYMVPYAFVVVNEL 1137
Cdd:PRK06060   394 GGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRL 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1138 PLTPNGKLDRKAL----------------------------PAPEFIASSS-SRGPRTPQE-------------EMLCDL 1175
Cdd:PRK06060   474 PRTPNGKLVRGALrkqsptkpiwelsltepgsgvraqrddlSASNMTIAGGnDGGATLRERlvalrqerqrlvvDAVCAE 553

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1176 FTEVLSVSQIGI---DDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLE 1235
Cdd:PRK06060   554 AAKMLGEPDPWSvdqDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLE 616
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 656-1150 2.55e-34

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: 141.30  E-value: 2.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  656 NPNSIAVVFE------DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:cd05967     64 RGDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAKPSCVLTnSSVEIE----------CDESLK---------ILVDDVNVMEEIEKySEENIDEMECLK---- 786
Cdd:cd05967    144 KELASRIDDAKPKLIVT-ASCGIEpgkvvpykplLDKALElsghkphhvLVLNRPQVPADLTK-PGRDLDWSELLAkaep 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  787 ----PLAPSHIAYVIYTSGSTGRPKGVMIP---HqnVVRL---------LGATDHWFQfdADDV-WTMFHSYAfdfsvwe 849
Cdd:cd05967    222 vdcvPVAATDPLYILYTSGTTGKPKGVVRDnggH--AVALnwsmrniygIKPGDVWWA--ASDVgWVVGHSYI------- 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  850 IWGPLLYG-------GRLVVVPhtvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrENEEVGQKL---SLRYVVFGG 919
Cdd:cd05967    291 VYGPLLHGattvlyeGKPVGTP-----DPGAFWRVIEKYQVNALFTAPTAIRAIRKED-PDGKYIKKYdlsSLRTLFLAG 364

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  920 EALELSRLEdWYSRHPHnAPkVINMYGITETTVHVSYIELDESIVSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEM 999
Cdd:cd05967    365 ERLDPPTLE-WAENTLG-VP-VIDHWWQTETGWPITANPVGLEPLPIKAGS-PGKPVPGYQVQVLDEDGEPVGPNELGNI 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1000 YVAGAgLARGYLGRAGLTAERFIADPFGK-PGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHD 1078
Cdd:cd05967    441 VIKLP-LPPGCLLTLWKNDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHP 517

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1079 KVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYA----FVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05967    518 AVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPVAafrlVIFVKRLPKTRSGKILRRTL 593
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 657-1150 2.65e-34

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 140.19  E-value: 2.65e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVV------FEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSD 730
Cdd:PRK13295    38 PDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRER 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  731 RISFMLHDAKpSCVLTNSSVEIECD-----ESLK--------ILV---DDVNVMEE--IEKYSEENIDEMECLKPLAPS- 791
Cdd:PRK13295   118 ELSFMLKHAE-SKVLVVPKTFRGFDhaamaRRLRpelpalrhVVVvggDGADSFEAllITPAWEQEPDAPAILARLRPGp 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  792 -HIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFHSYAFdfsvweiwgplLYGGRLVVV--P 864
Cdd:PRK13295   197 dDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIlmasPMAHQTGF-----------MYGLMMPVMlgA 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  865 HTVSR---SPKEFLQLLVKEKVT-VLNQTPsaFyqLMQADRENEEVGQKL-SLRYVVFGGEALELSRLEDwySRHPHNAp 939
Cdd:PRK13295   266 TAVLQdiwDPARAAELIRTEGVTfTMASTP--F--LTDLTRAVKESGRPVsSLRTFLCAGAPIPGALVER--ARAALGA- 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  940 KVINMYGITETTVhVSYIELDESivSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAE 1019
Cdd:PRK13295   339 KIVSAWGMTENGA-VTLTKLDDP--DERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT 415

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1020 RfiADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIkIRGFR-IELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLV 1098
Cdd:PRK13295   416 D--ADGW-------FDTGDLARIDADGYIRISGRSKDVI-IRGGEnIPVVEIEALLYRHPAIAQVAIVAYPDERLGERAC 485

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1099 AYIVASNNETIDTNEMRQ--HASGSLPDYMvPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK13295   486 AFVVPRPGQSLDFEEMVEflKAQKVAKQYI-PERLVVRDALPRTPSGKIQKFRL 538
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-434 3.07e-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: 143.84  E-value: 3.07e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:COG1020    892 LLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAP 971

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   81 DFNGMNNERVARNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAKQ 160
Cdd:COG1020    972 AAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAA 1051

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  161 LNHAKSARPAIQKASRPNEV-------PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETL 233
Cdd:COG1020   1052 AAAAAAAAAAPLAAAAAPLPlpplllsLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAV 1131

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  234 RTIFPNVLGSSYQKILDMENLNLEMVITntcKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDG 313
Cdd:COG1020   1132 RQEGPRLRLLVALAAALALAALLALLLA---AAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLL 1208

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  314 WSLQPLTRDFTAAYKARCQGDRVQLETLPVQYADYALWQQQLLGDETTPESLISTQLDFWKEELKGLPDQMELPTDYQRP 393
Cdd:COG1020   1209 LLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARA 1288

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1698252301  394 VETSYRGETIHFHIDEGMHSRLVELGRKNGVSLFMVLQAGL 434
Cdd:COG1020   1289 ARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 644-1150 1.53e-33

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 137.12  E-value: 1.53e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFED-----KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGA 718
Cdd:PRK08008     8 HLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  719 GYLPLDPDYPSDRISFMLHDAKPSCVLTN-------SSVEIECDESLK-ILVDDVNVMEE-----IEKYSEENIDEMECL 785
Cdd:PRK08008    88 IMVPINARLLREESAWILQNSQASLLVTSaqfypmyRQIQQEDATPLRhICLTRVALPADdgvssFTQLKAQQPATLCYA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  786 KPLAPSHIAYVIYTSGSTGRPKGVMIPHQNvVRLLGATDHW-FQFDADDVW-TMFHSYAFDFSVWEIWGPLLYGGRLVVV 863
Cdd:PRK08008   168 PPLSTDDTAEILFTSGTTSRPKGVVITHYN-LRFAGYYSAWqCALRDDDVYlTVMPAFHIDCQCTAAMAAFSAGATFVLL 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  864 PhtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLM-QADRENEevgQKLSLRYVVFggeALELSRLE--DWYSRHphnAPK 940
Cdd:PRK08008   247 E---KYSARAFWGQVCKYRATITECIPMMIRTLMvQPPSAND---RQHCLREVMF---YLNLSDQEkdAFEERF---GVR 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  941 VINMYGITETTVHVsyieLDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMY---VAGAGLARGYLGRAGLT 1017
Cdd:PRK08008   315 LLTSYGMTETIVGI----IGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKTIFKEYYLDPKAT 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1018 AERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRL 1097
Cdd:PRK08008   391 AKVLEADGW-------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAI 463

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1098 VAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK08008   464 KAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
635-1150 6.68e-33

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 135.78  E-value: 6.68e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  635 GGFQIAPEMTLPQLF---EKQAHINPNSIAVVFEDKK--LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVS 709
Cdd:PRK05852     5 GGAAPMASDFGPRIAdlvEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  710 LLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSSVEIECDE-SLKILVDDVNVMEEieKYSEENIDEMECLKPL 788
Cdd:PRK05852    85 LLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEpTTRWWPLTVNVGGD--SGPSGGTLSVHLDAAT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 APSHI-----------AYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHSYAFDFSVWEIwgp 853
Cdd:PRK05852   163 EPTPAtstpeglrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDatvaVMPLYHGHGLIAALLAT--- 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  854 lLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELSR---LEDW 930
Cdd:PRK05852   240 -LASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETaqaLQTE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  931 YSrhphnAPkVINMYGITETTVHVSYIELDESIVS---LRANSLIGCSI-PDLKVYVLDNylQPVPPGVVGEMYVAGAGL 1006
Cdd:PRK05852   319 FA-----AP-VVCAFGMTEATHQVTTTQIEGIGQTenpVVSTGLVGRSTgAQIRIVGSDG--LPLPAGAVGEVWLRGTTV 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1007 ARGYLGRAGLTAERFIADPFgkpgtrmyRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI 1086
Cdd:PRK05852   391 VRGYLGDPTITAANFTDGWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVF 462

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1087 VREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK05852   463 GVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 668-1150 1.11e-32

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: 134.00  E-value: 1.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  668 KLTYEKLNRKANKIARfLIAKGVGPDQLVALAMPRSLNMVVSLLAVlkAGAGYLPLDPDYPS--DRISFMLHDAKPSCVL 745
Cdd:cd05909      7 SLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFAL--ALSGKVPVMLNYTAglRELRACIKLAGIKTVL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  746 TnSSVEIECDESLKILVDDVNV----MEEIE---------------KYSEENIDEMECLKPLAPSHIAYVIYTSGSTGRP 806
Cdd:cd05909     84 T-SKQFIEKLKLHHLFDVEYDArivyLEDLRakiskadkckaflagKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  807 KGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFHSYAFDFSvweIWGPLLYGGRLVVVPHTVsrSPKEFLQLLVKEK 882
Cdd:cd05909    163 KGVVLSHKNLLANVEQITAIFDPNPEDVVfgalPFFHSFGLTGC---LWLPLLSGIKVVFHPNPL--DYKKIPELIYDKK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  883 VTVLNQTPSAFYQLmqADRENEEvgQKLSLRYVVFGGEALELSRLEDWYSRHphnaPKVINM-YGITETT--VHVSYIEL 959
Cdd:cd05909    238 ATILLGTPTFLRGY--ARAAHPE--DFSSLRLVVAGAEKLKDTLRQEFQEKF----GIRILEgYGTTECSpvISVNTPQS 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  960 DesivslRANSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAErfiadpfgKPGTRMYRTGD 1038
Cdd:cd05909    310 P------NKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF--------AFGDGWYDTGD 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1039 LARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKH--DKVEQVAVIVREDQPGDKRLVAYIvasnNETIDTNEMRQ 1116
Cdd:cd05909    376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGEKIVLLTT----TTDTDPSSLND 451

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1698252301 1117 HASGS-LPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05909    452 ILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 644-1150 1.73e-32

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: 134.33  E-value: 1.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPN----SIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAG 719
Cdd:cd05906     11 TLLELLLRAAERGPTkgitYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFV 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  720 YLPLDP----DYPSDR------ISFMLHDAKpscVLTNSSVEIECDESLKILVDDVNVMEEIEKYSEENIDEMecLKPLA 789
Cdd:cd05906     91 PAPLTVpptyDEPNARlrklrhIWQLLGSPV---VLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHD--LPQSR 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 PSHIAYVIYTSGSTGRPKGVMIPHQNVV-RLLGATDHwFQFDADDV---WTMFHSYAfdfSVWEI-WGPLLYGGRLVVVP 864
Cdd:cd05906    166 PDDLALLMLTSGSTGFPKAVPLTHRNILaRSAGKIQH-NGLTPQDVflnWVPLDHVG---GLVELhLRAVYLGCQQVHVP 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  865 -HTVSRSPKEFLQLLVKEKVTVlnqT--PSAFYQLM--QADRENEEVGQKLSLRYVVFGGEALE-------LSRLEdwys 932
Cdd:cd05906    242 tEEILADPLRWLDLIDRYRVTI---TwaPNFAFALLndLLEEIEDGTWDLSSLRYLVNAGEAVVaktirrlLRLLE---- 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  933 rhPHNAP--KVINMYGITETTVHVSYIELDESIVSLRANSL--IGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLAR 1008
Cdd:cd05906    315 --PYGLPpdAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTK 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1009 GYLGRAGLTAERFIADPFgkpgtrmYRTGDLArWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQ---VAV 1085
Cdd:cd05906    393 GYYNNPEANAEAFTEDGW-------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftAAF 464

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1086 IVREDQPGDKRL-VAYIVASNN-----ETIDtnEMRQHAS---GSLPDYMVPyafVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05906    465 AVRDPGAETEELaIFFVPEYDLqdalsETLR--AIRSVVSrevGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 652-1150 1.76e-32

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 133.39  E-value: 1.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  652 QAHINPNSIAVV--FEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:PRK09088     4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAKPSCVLTNSSVEiecdeSLKILVDDVNVMeeiekyseenIDEMECLKP-----LAPSHIAYVIYTSGSTG 804
Cdd:PRK09088    84 SELDALLQDAEPRLLLGDDAVA-----AGRTDVEDLAAF----------IASADALEPadtpsIPPERVSLILFTSGTSG 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNVVR------LLGATDHWFQFDADDvwTMFHSYAFDFSVWEIwgpLLYGGRLVVVPhtvSRSPKEFLQLL 878
Cdd:PRK09088   149 QPKGVMLSERNLQQtahnfgVLGRVDAHSSFLCDA--PMFHIIGLITSVRPV---LAVGGSILVSN---GFEPKRTLGRL 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  879 VKEKVTVLNQ--TPsafyQLMQADRENEEV-GQKL-SLRYVVFGGEALELSRLEDWYSrhphNAPKVINMYGITETTVhV 954
Cdd:PRK09088   221 GDPALGITHYfcVP----QMAQAFRAQPGFdAAALrHLTALFTGGAPHAAEDILGWLD----DGIPMVDGFGMSEAGT-V 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  955 SYIELDESIVSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmY 1034
Cdd:PRK09088   292 FGMSVDCDVIRAKAGA-AGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------F 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1035 RTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEM 1114
Cdd:PRK09088   364 RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERI 443

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1698252301 1115 RQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK09088   444 RSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 637-1150 2.11e-32

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 137.75  E-value: 2.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  637 FQIAPEMTLPQLFEKQAHINPNSIAVVfeD---KKLTYEKLNRKANKIARfLIAKGVGPDQLVALAMPRSLNMVVSLLAV 713
Cdd:PRK08633   609 SRKEALPPLAEAWIDTAKRNWSRLAVA--DstgGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLAL 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  714 LKAGAgyLPLDPDYPSDRISFM--LHDAKPSCVLTnSSVEIEcdeSLKILVDDVNVMEEIE-KYSEENIDEME------- 783
Cdd:PRK08633   686 LLAGK--VPVNLNYTASEAALKsaIEQAQIKTVIT-SRKFLE---KLKNKGFDLELPENVKvIYLEDLKAKISkvdklta 759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  784 ---------------CLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDV----WTMFHSyaFD 844
Cdd:PRK08633   760 llaarllparllkrlYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVilssLPFFHS--FG 837

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  845 FSVwEIWGPLLYGGRLVVVPhtvsrSPKEFL---QLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQklSLRYVVFGGEA 921
Cdd:PRK08633   838 LTV-TLWLPLLEGIKVVYHP-----DPTDALgiaKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFA--SLRLVVAGAEK 909

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  922 LELSRLEDWYSRHPHnapKVINMYGITETT----VHVSYIELDESIVsLRANSL--IGCSIPDLKVYVLD-NYLQPVPPG 994
Cdd:PRK08633   910 LKPEVADAFEEKFGI---RILEGYGATETSpvasVNLPDVLAADFKR-QTGSKEgsVGMPLPGVAVRIVDpETFEELPPG 985

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  995 VVGEMYVAGAGLARGYLGRAGLTAErFIADPFGKpgtRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIE--- 1071
Cdd:PRK08633   986 EDGLILIGGPQVMKGYLGDPEKTAE-VIKDIDGI---GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeel 1061

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1072 AVIMKHDKVEQVAVIVREDQPGDKRLVAYivasNNETIDTNEMRQH-ASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK08633  1062 AKALGGEEVVFAVTAVPDEKKGEKLVVLH----TCGAEDVEELKRAiKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 641-1145 2.23e-32

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 134.32  E-value: 2.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  641 PEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAK-GVGPDQLVALAMPRSLNMVVSLLAVLKAGAG 719
Cdd:PRK08314     8 PETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  720 YLPLDPDYPSDRISFMLHDAKPSCVLT-----------NSSVEIEC-----------DESLKILVDDVNVMEEIEKYSEE 777
Cdd:PRK08314    88 VVPVNPMNREEELAHYVTDSGARVAIVgselapkvapaVGNLRLRHvivaqysdylpAEPEIAVPAWLRAEPPLQALAPG 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  778 NI----DEMEC-LKPLA----PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWT----MFHSYAFD 844
Cdd:PRK08314   168 GVvawkEALAAgLAPPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLavlpLFHVTGMV 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  845 FSVWeiwGPLLYGGRLVVVPhtvsRSPKEF-LQLLVKEKVTVLNQTPSAFYQLMQADRENEevgQKL-SLRYVVFGGEAL 922
Cdd:PRK08314   248 HSMN---APIYAGATVVLMP----RWDREAaARLIERYRVTHWTNIPTMVVDFLASPGLAE---RDLsSLRYIGGGGAAM 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  923 ELS---RLEDWYSRhphnapKVINMYGITETTVHvsyieldeSIVSLRANSLIGC-SIPDLKV--YVLD-NYLQPVPPGV 995
Cdd:PRK08314   318 PEAvaeRLKELTGL------DYVEGYGLTETMAQ--------THSNPPDRPKLQClGIPTFGVdaRVIDpETLEELPPGE 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  996 VGEMYVAGAGLARGYLGRAGLTAERFIA-DpfgkpGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVI 1074
Cdd:PRK08314   384 VGEIVVHGPQVFKGYWNRPEATAEAFIEiD-----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLL 458

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1075 MKHDKVEQVAVI-VREDQPGDkRLVAYIV--ASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:PRK08314   459 YKHPAIQEACVIaTPDPRRGE-TVKAVVVlrPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
PRK05691 PRK05691
peptide synthase; Validated
 1-180 3.21e-32

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 137.99  E-value: 3.21e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREdRPNDKRIIAYIVAEEKEPIN---LSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK05691  4144 LHEQAEVREAAVAVQE-GVNGKHLVGYLVPHQTVLAQgalLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   78 PAPDFNGMNNE--RVARNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVA 155
Cdd:PRK05691  4223 PALDIGQLQSQayLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVE 4302

                          170       180
                   ....*....|....*....|....*
gi 1698252301  156 ELAKQLNHAKSARPAIQKASRPNEV 180
Cdd:PRK05691  4303 ELAEYIEGLAGSAIDEQKVDRLSDL 4327
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 647-1152 7.65e-32

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: 133.38  E-value: 7.65e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  647 QLFEKQAHINPNSIAVVFED-----KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:cd05968     65 QLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFMLHDAKPSCVLTNS---------SVEIECDESL-------KILV-------------DDVNVMEEIE 772
Cdd:cd05968    145 PIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACaqcptveKVVVvrhlgndftpakgRDLSYDEEKE 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  773 KYSEEnIDEMECLKPLApshiayVIYTSGSTGRPKGVMIPHQNVvRLLGATDHWFQFD--ADDVWTMFHSYAFDFSVWEI 850
Cdd:cd05968    225 TAGDG-AERTESEDPLM------IIYTSGTTGKPKGTVHVHAGF-PLKAAQDMYFQFDlkPGDLLTWFTDLGWMMGPWLI 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  851 WGPLLYGGRLVV---VP-HTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRyvVFGGEAlELSR 926
Cdd:cd05968    297 FGGLILGATMVLydgAPdHP---KADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLR--VLGSTG-EPWN 370

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  927 LEDW----YSRHPHNAPkVINMYGITETTvhvSYIELDESIVSLRANSLIGcSIPDLKVYVLDNYLQPVPPgVVGEMYVA 1002
Cdd:cd05968    371 PEPWnwlfETVGKGRNP-IINYSGGTEIS---GGILGNVLIKPIKPSSFNG-PVPGMKADVLDESGKPARP-EVGELVLL 444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1003 GA--GLARGYLGraglTAERFIADPFGK-PGTRMYrtGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDK 1079
Cdd:cd05968    445 APwpGMTRGFWR----DEDRYLETYWSRfDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPA 518

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301 1080 VEQVAVI-VREDQPGDKrLVAYIVASNNET---IDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:cd05968    519 VLESAAIgVPHPVKGEA-IVCFVVLKPGVTpteALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 653-1150 7.98e-32

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: 132.23  E-value: 7.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVF-----EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDY 727
Cdd:cd05970     27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  728 PSDRISFMLHDAKPSCVLTNSSVEI---------EC-DESLKILVDDvNVMEEIEKYSEEnIDEMECL--KPLAPSH--- 792
Cdd:cd05970    107 TAKDIVYRIESADIKMIVAIAEDNIpeeiekaapECpSKPKLVWVGD-PVPEGWIDFRKL-IKNASPDfeRPTANSYpcg 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 --IAYVIYTSGSTGRPKgvMIPHQNVVRL--LGATDHWFQFDADDVWTMFHSYAFDFSVW-EIWGPLLYGGRLVVVPHTv 867
Cdd:cd05970    185 edILLVYFSSGTTGMPK--MVEHDFTYPLghIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYD- 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  868 SRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGqklSLRYVVFGGEALELSRLEDWYSrhpHNAPKVINMYGI 947
Cdd:cd05970    262 KFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS---SLRYCTTAGEALNPEVFNTFKE---KTGIKLMEGFGQ 335

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  948 TETTVHVSYIELDESivslRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGA-----GLARGYLGRAGLTAERFi 1022
Cdd:cd05970    336 TETTLTIATFPWMEP----KPGS-MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW- 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1023 adpfgKPGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV 1102
Cdd:cd05970    410 -----HDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1103 ASNNETID---TNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05970    483 LAKGYEPSeelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 646-1144 8.55e-32

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 131.27  E-value: 8.55e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  646 PQLF-EKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:cd12118      6 PLSFlERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVLTNSSVEIECdeslkiLVDDVNVMEEIEKYSEENidemeclKPLApshiayVIYTSGSTG 804
Cdd:cd12118     86 TRLDAEEIAFILRHSEAKVLFVDREFEYED------LLAEGDPDFEWIPPADEW-------DPIA------LNYTSGTTG 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  805 RPKGVMIPHQNV-VRLLGATDHWfQFDADDV--WT--MFHSYAFDFsvweIWGPLLYGGRLVVVPHTvsrSPKEFLQLLV 879
Cdd:cd12118    147 RPKGVVYHHRGAyLNALANILEW-EMKQHPVylWTlpMFHCNGWCF----PWTVAAVGGTNVCLRKV---DAKAIYDLIE 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  880 KEKVTVLNQTPSAFYQLMQAdreNEEVGQKLSLRYVVFGGEALElsrledwysrHPHNAPKVINM-------YGITET-- 950
Cdd:cd12118    219 KHKVTHFCGAPTVLNMLANA---PPSDARPLPHRVHVMTAGAPP----------PAAVLAKMEELgfdvthvYGLTETyg 285

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  951 --TVHVSYIELDESIVSLRA--NSLIGCSIPDLK-VYVLD-NYLQPVP-PGV-VGEMYVAGAGLARGYLGRAGLTAERFi 1022
Cdd:cd12118    286 paTVCAWKPEWDELPTEERArlKARQGVRYVGLEeVDVLDpETMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEATAEAF- 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1023 adpfgKPGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV 1102
Cdd:cd12118    365 -----RGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1698252301 1103 ASNNETIDTNEMRQHASGSLPDYMVPYAfVVVNELPLTPNGK 1144
Cdd:cd12118    438 LKEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGK 478
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 644-1145 9.23e-32

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 131.98  E-value: 9.23e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPl 723
Cdd:PRK08316    12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 dpdypsdrISFMLHDAKPSCVLTNS-SVEIECDESLKILVDDVNVMEEIEKY-------------SEENIDEM------- 782
Cdd:PRK08316    91 --------VNFMLTGEELAYILDHSgARAFLVDPALAPTAEAALALLPVDTLilslvlggreapgGWLDFADWaeagsva 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  783 ECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDV----WTMFHSYAFD-FsvweiWGPLLY- 856
Cdd:PRK08316   163 EPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIplhaLPLYHCAQLDvF-----LGPYLYv 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  857 GGRLVVVPhtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQ-ADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRHP 935
Cdd:PRK08316   238 GATNVILD---APDPELILRTIEAERITSFFAPPTVWISLLRhPDFDTRDLS---SLRKGYYGASIMPVEVLKELRERLP 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  936 hnAPKVINMYGITETTVHVSYIELDESIvsLRANSligCSIPDLKV--YVLDNYLQPVPPGVVGEMYVAGAGLARGYLGR 1013
Cdd:PRK08316   312 --GLRFYNCYGQTEIAPLATVLGPEEHL--RRPGS---AGRPVLNVetRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDD 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1014 AGLTAERFIADPFgkpgtrmyRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPG 1093
Cdd:PRK08316   385 PEKTAEAFRGGWF--------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKW 456

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1094 DKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:PRK08316   457 IEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 650-1150 1.06e-31

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: 133.07  E-value: 1.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  650 EKQAHINPNSIAVVFE------DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGA----- 718
Cdd:cd05966     60 DRHLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvv 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  719 --GYlplDPDYPSDRIsfmlHDAKPSCVLTnssveieCDES--------LKILVD--------------------DVNVM 768
Cdd:cd05966    140 faGF---SAESLADRI----NDAQCKLVIT-------ADGGyrggkvipLKEIVDealekcpsvekvlvvkrtggEVPMT 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  769 EEIEKYSEENID--EMEC-LKPLAPSHIAYVIYTSGSTGRPKGVMipHQNVVRLLGA--TDHW-FQFDADDV-------- 834
Cdd:cd05966    206 EGRDLWWHDLMAkqSPECePEWMDSEDPLFILYTSGSTGKPKGVV--HTTGGYLLYAatTFKYvFDYHPDDIywctadig 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  835 WTMFHSYAfdfsvweIWGPLLYGGRLVV---VPH--TVSRspkeFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQK 909
Cdd:cd05966    284 WITGHSYI-------VYGPLANGATTVMfegTPTypDPGR----YWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDL 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  910 LSLRyvVFG--GE-----ALElsrledWYSRHPHN--APkVINMYGITETTVHVsyIELDESIVSLRANSligCSIP--D 978
Cdd:cd05966    353 SSLR--VLGsvGEpinpeAWM------WYYEVIGKerCP-IVDTWWQTETGGIM--ITPLPGATPLKPGS---ATRPffG 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  979 LKVYVLDNYLQPVPPGVVGEMYVAGA--GLARGYLGraglTAERFIADPFGK-PGtrMYRTGDLARWRQDGTLDYIGRAD 1055
Cdd:cd05966    419 IEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYG----DHERYEDTYFSKfPG--YYFTGDGARRDEDGYYWITGRVD 492

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1056 HQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETID---TNEMRQHASGSLPDYMVPYAFV 1132
Cdd:cd05966    493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQ 572

                          570
                   ....*....|....*...
gi 1698252301 1133 VVNELPLTPNGKLDRKAL 1150
Cdd:cd05966    573 FVPGLPKTRSGKIMRRIL 590
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 795-1146 1.08e-31

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


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 128.27  E-value: 1.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  795 YVIYTSGSTGRPKGVMIPHQNVVR-LLGATDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYG-----------GRLVV 862
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQEDIFRmLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGtgswtafggllGGQTV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  863 VPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQ-LMQADRENEEVGQKlSLRYVVFGGEALELSrLEDWYSRHPHNApKV 941
Cdd:cd05924     87 VLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDALRDAGPYDLS-SLFAISSGGALLSPE-VKQGLLELVPNI-TL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITET----TVHVsyielDESIVSLRANSLIGcsiPDlkVYVLDNYLQPVPPGVVGEMYVAGAGL-ARGYLGRAGL 1016
Cdd:cd05924    164 VDAFGSSETgftgSGHS-----AGSGPETGPFTRAN---PD--TVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAK 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1017 TAERFiadpFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKR 1096
Cdd:cd05924    234 TAETF----PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1097 LVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLD 1146
Cdd:cd05924    310 VVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 643-1150 1.10e-31

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 131.05  E-value: 1.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQlVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK07638     1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNS--SVEIECDESLKILVDDVNVMEEIEKYSEENIDEMEclkpLAPshiAYVIYTS 800
Cdd:PRK07638    80 LDIKWKQDELKERLAISNADMIVTERykLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENVQ----NAP---FYMGFTS 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  801 GSTGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHSYAFDFSVweiwGPLLYGGRLVVVPhtvSRSPKEFLQ 876
Cdd:PRK07638   153 GSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDsvliAGTLVHSLFLYGAI----STLYVGQTVHLMR---KFIPNQVLD 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  877 LLVKEKVTVLNQTPS---AFYqlmqadRENEEVGQKLSlryVVFGGEALELSRLEDWYSRHPHnaPKVINMYGITETTVh 953
Cdd:PRK07638   226 KLETENISVMYTVPTmleSLY------KENRVIENKMK---IISSGAKWEAEAKEKIKNIFPY--AKLYEFYGASELSF- 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  954 VSYIELDESivSLRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAErfiadpfgkPGTRM 1033
Cdd:PRK07638   294 VTALVDEES--ERRPNS-VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE---------LNADG 361

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1034 YRT-GDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNEtidtN 1112
Cdd:PRK07638   362 WMTvRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK----Q 437

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1698252301 1113 EMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK07638   438 QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
 650-1150 1.51e-31

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


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 132.76  E-value: 1.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  650 EKQAHINPNSIAVVFE------DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGA----- 718
Cdd:TIGR02188   64 DRHLEARPDKVAIIWEgdepgeVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAihsvv 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  719 --GYlplDPDYPSDRISfmlhDAKPSCVLT-----------------NSSVEIECDESLKILV-----DDVNVM------ 768
Cdd:TIGR02188  144 fgGF---SAEALADRIN----DAGAKLVITadeglrggkviplkaivDEALEKCPVSVEHVLVvrrtgNPVVPWvegrdv 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  769 ---EEIEKYSeeniDEMEClKPLAPSHIAYVIYTSGSTGRPKGVMipHQNVVRLLGA-TDHWFQFD--ADDV-------- 834
Cdd:TIGR02188  217 wwhDLMAKAS----AYCEP-EPMDSEDPLFILYTSGSTGKPKGVL--HTTGGYLLYAaMTMKYVFDikDGDIfwctadvg 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  835 WTMFHSYAfdfsvweIWGPLLYGGRLVV---VPHTVSRSpkEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLS 911
Cdd:TIGR02188  290 WITGHSYI-------VYGPLANGATTVMfegVPTYPDPG--RFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSS 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  912 LRyvVFG--GEALELSRLEdWY------SRHPhnapkVINMYGITETTVHVsyIELDESIVSLRANSligCS--IPDLKV 981
Cdd:TIGR02188  361 LR--LLGsvGEPINPEAWM-WYykvvgkERCP-----IVDTWWQTETGGIM--ITPLPGATPTKPGS---ATlpFFGIEP 427

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  982 YVLDNYLQPVP-PGVVGEMYVAGA--GLARGYLGraglTAERFIADPFGK-PGtrMYRTGDLARWRQDGTLDYIGRADHQ 1057
Cdd:TIGR02188  428 AVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYG----DHERFVDTYFSPfPG--YYFTGDGARRDKDGYIWITGRVDDV 501

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1058 IKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTN---EMRQHASGSLPDYMVPYAFVVV 1134
Cdd:TIGR02188  502 INVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDElrkELRKHVRKEIGPIAKPDKIRFV 581

                          570
                   ....*....|....*.
gi 1698252301 1135 NELPLTPNGKLDRKAL 1150
Cdd:TIGR02188  582 PGLPKTRSGKIMRRLL 597
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 798-1147 2.18e-31

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 127.01  E-value: 2.18e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  798 YTSGSTGRPKGVMIPHQNVV---RLLGatdHWFQFDADDVWT----MFHSYAfdfSVWEIWGPLLYGGRLVVVphTVSRS 870
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVnngYFIG---ERLGLTEQDRLCipvpLFHCFG---SVLGVLACLTHGATMVFP--SPSFD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  871 PKEFLQLLVKEKVTVLNQTPSAFY-QLMQADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRhpHNAPKVINMYGITE 949
Cdd:cd05917     81 PLAVLEAIEKEKCTALHGVPTMFIaELEHPDFDKFDLS---SLRTGIMAGAPCPPELMKRVIEV--MNMKDVTIAYGMTE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  950 TTvHVSYIELDESIVSLRANSlIGCSIPDLKVYVLDNYLQPVPP-GVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgk 1028
Cdd:cd05917    156 TS-PVSTQTRTDDSIEKRVNT-VGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD---- 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1029 pgtRMYRTGDLARWRQDGTLDYIGRADHQIkIRGFR-IELGEIEAVIMKHDKVEQVAVI-VREDQPGDKrLVAYIVASNN 1106
Cdd:cd05917    230 ---GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVgVPDERYGEE-VCAWIRLKEG 304

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1698252301 1107 ETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:cd05917    305 AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 667-1150 2.33e-31

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: 129.25  E-value: 2.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  667 KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLdpdYPSDRISFMLHdakpscVLT 746
Cdd:cd05907      4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI---YPTSSAEQIAY------ILN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 NSSVEIecdeslkILVDDvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHW 826
Cdd:cd05907     75 DSEAKA-------LFVED-------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAER 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  827 FQFDADDVWTMF----HSYAfdfSVWEIWGPLLYGGRLVVVPhtvsrSPKEFLQLLVKEKVTVLNQTPSaFYQLMQADRE 902
Cdd:cd05907    123 LPATEGDRHLSFlplaHVFE---RRAGLYVPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPR-VWEKVYAAIK 193

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  903 NEEVG---QKL-------SLRYVVFGGEALELsRLEDWYsrHPHNAPkVINMYGITETTVHVSYIELDEsivsLRANSlI 972
Cdd:cd05907    194 VKAVPglkRKLfdlavggRLRFAASGGAPLPA-ELLHFF--RALGIP-VYEGYGLTETSAVVTLNPPGD----NRIGT-V 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  973 GCSIPDLKVYVLDNylqpvppgvvGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIG 1052
Cdd:cd05907    265 GKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITG 327

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1053 RADHQIKIRGFR-IELGEIEAVIMKHDKVEQVAVIvredqpGDKR--LVAYIV---------ASNNETIDTN-------- 1112
Cdd:cd05907    328 RKKDLIITSGGKnISPEPIENALKASPLISQAVVI------GDGRpfLVALIVpdpealeawAEEHGIAYTDvaelaanp 401

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1113 -------EMRQHASGSLPDY-------MVPYAFVVVNELpLTPNGKLDRKAL 1150
Cdd:cd05907    402 avraeieAAVEAANARLSRYeqikkflLLPEPFTIENGE-LTPTLKLKRPVI 452
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1-167 3.83e-31

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: 133.65  E-value: 3.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIV-----------------AEEKEPIN---------LSEIRSYVSESLANYMI 54
Cdd:TIGR03443  720 LSQHPLVRENVTLVRRDKDEEPTLVSYIVpqdksdeleefksevddEESSDPVVkglikyrklIKDIREYLKKKLPSYAI 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   55 PSAFVVLEELPLTPNGKVDRKKLPAPDFNGMNneRVARN-----------PKEEILCDLFAEVL--GVSRINIDDNFFEM 121
Cdd:TIGR03443  800 PTVIVPLKKLPLNPNGKVDKPALPFPDTAQLA--AVAKNrsasaadeeftETEREIRDLWLELLpnRPATISPDDSFFDL 877

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1698252301  122 GGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAKQLNHAKSA 167
Cdd:TIGR03443  878 GGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKG 923
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 1257-1411 5.50e-31

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 122.11  E-value: 5.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1257 PLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEELPKSLEEMAADYLKHVREIQPHGPYRLLGWSLGGNVVHA 1336
Cdd:pfam00975    2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFE 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1337 MAAQLQNEGEEVELLVMLDSYPGHFLPNT-EAPTEEEALIALLALGGYDPDNMDGKPLTMESAVEILRKDGSALAS 1411
Cdd:pfam00975   82 VARRLERQGEAVRSLFLSDASAPHTVRYEaSRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALES 157
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 650-1166 1.10e-30

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 129.13  E-value: 1.10e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  650 EKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:PRK07786    24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAKPSCVLTNSS---VEIECDESLKILVDDVNVMEEIEKYS---EENIDEMEclKPLAPSHI-----AYVIY 798
Cdd:PRK07786   104 PEIAFLVSDCGAHVVVTEAAlapVATAVRDIVPLLSTVVVAGGSSDDSVlgyEDLLAEAG--PAHAPVDIpndspALIMY 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVMIPHQNVV-RLLGATDHWFQFDADDVW----TMFHSYAFDfSVweiwGPLLYGGRLVVVPHTVSRSPKE 873
Cdd:PRK07786   182 TSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGfvgvPLFHIAGIG-SM----LPGLLLGAPTVIYPLGAFDPGQ 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  874 FLQLLVKEKVTVLNQTPsAFYQLMQADRENEevGQKLSLRYVVFGGEALELSRLEDWYSRHPHNApkVINMYGITETTVH 953
Cdd:PRK07786   257 LLDVLEAEKVTGIFLVP-AQWQAVCAEQQAR--PRDLALRVLSWGAAPASDTLLRQMAATFPEAQ--ILAAFGQTEMSPV 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  954 VSYIELDESIvslRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrm 1033
Cdd:PRK07786   332 TCMLLGEDAI---RKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF------- 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1034 yRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYI-VASNNETIDTN 1112
Cdd:PRK07786   402 -HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLE 480

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1113 EMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLD----RKALPAPEFIASSSSRGPRT 1166
Cdd:PRK07786   481 DLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGFT 538
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 642-1150 2.83e-30

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 127.57  E-value: 2.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PRK06155    20 ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFMLHDAKPSCVLtnssVEIECDESLKILVDDVNVMEEIEKYSEEN---------------IDEMECLK 786
Cdd:PRK06155   100 PINTALRGPQLEHILRNSGARLLV----VEAALLAALEAADPGDLPLPAVWLLDAPAsvsvpagwstaplppLDAPAPAA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  787 PLAPSHIAYVIYTSGSTGRPKGVMIPH-------QNVVRLLGATdhwfqfdADDVW----TMFHSYAFD--FSVweiwgp 853
Cdd:PRK06155   176 AVQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLEIG-------ADDVLyttlPLFHTNALNafFQA------ 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  854 LLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTV-----------LNQTPSAfyqlmqADRENeevgqklSLRYVVFGGEAL 922
Cdd:PRK06155   243 LLAGATYVLEPRF---SASGFWPAVRRHGATVtyllgamvsilLSQPARE------SDRAH-------RVRVALGPGVPA 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  923 ELsrLEDWYSRHphnAPKVINMYGITETTVhVSYIELDESivslRANSLiGCSIPDLKVYVLDNYLQPVPPGVVGEMYVA 1002
Cdd:PRK06155   307 AL--HAAFRERF---GVDLLDGYGSTETNF-VIAVTHGSQ----RPGSM-GRLAPGFEARVVDEHDQELPDGEPGELLLR 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1003 GA---GLARGYLGRAGLTAERFiadpfgkpGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDK 1079
Cdd:PRK06155   376 ADepfAFATGYFGMPEKTVEAW--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPA 447

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1080 VEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06155   448 VAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 644-1147 7.71e-30

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 126.43  E-value: 7.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVF--EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PRK12583    19 TIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISF-----------------------MLHDAKPSCVLTNSSvEIECDE--SLKILVD-DVN--------- 766
Cdd:PRK12583    99 NINPAYRASELEYalgqsgvrwvicadafktsdyhaMLQELLPGLAEGQPG-ALACERlpELRGVVSlAPApppgflawh 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  767 -VMEEIEKYSEENIDEMEC-LKPLAPSHIAYviyTSGSTGRPKGVMIPHQNVV-------RLLGATDHwfqfdadDVWT- 836
Cdd:PRK12583   178 eLQARGETVSREALAERQAsLDRDDPINIQY---TSGTTGFPKGATLSHHNILnngyfvaESLGLTEH-------DRLCv 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  837 ---MFHSYAFDFSVWEIwgplLYGGRLVVVPhTVSRSPKEFLQLLVKEKVTVLNQTPSAFY-QLMQADRENEEVGqklSL 912
Cdd:PRK12583   248 pvpLYHCFGMVLANLGC----MTVGACLVYP-NEAFDPLATLQAVEEERCTALYGVPTMFIaELDHPQRGNFDLS---SL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  913 RYVVFGGEA--LELSR--LEDWysrhphNAPKVINMYGITETTvHVSYIELDESIVSLRANSlIGCSIPDLKVYVLDNYL 988
Cdd:PRK12583   320 RTGIMAGAPcpIEVMRrvMDEM------HMAEVQIAYGMTETS-PVSLQTTAADDLERRVET-VGRTQPHLEVKVVDPDG 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  989 QPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrMYrTGDLARWRQDGTLDYIGRADHQIkIRGFR-IEL 1067
Cdd:PRK12583   392 ATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW------MH-TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYP 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1068 GEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:PRK12583   464 REIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 662-1147 9.58e-30

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


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 124.86  E-value: 9.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  662 VVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKP 741
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  742 SCVLTNssveiecDEslkilvDDVnvmeeiekyseenidemeclkplapshiAYVIYTSGSTGRPKGVMIPHQN------ 815
Cdd:cd05914     81 KAIFVS-------DE------DDV----------------------------ALINYTSGTTGNSKGVMLTYRNivsnvd 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  816 ---VVRLLGATDHWFQFdaddvWTMFHSY--AFDFSVweiwgPLLYGGRLVV---VPHTVSRSPKEF-----------LQ 876
Cdd:cd05914    120 gvkEVVLLGKGDKILSI-----LPLHHIYplTFTLLL-----PLLNGAHVVFldkIPSAKIIALAFAqvtptlgvpvpLV 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  877 LLVKEKVTVLNQTPSA-FYQLMQA----DRENEEVGQKLS------LRYVVFGGEALELSRLEDWYSRhphNAPKVINmY 945
Cdd:cd05914    190 IEKIFKMDIIPKLTLKkFKFKLAKkinnRKIRKLAFKKVHeafggnIKEFVIGGAKINPDVEEFLRTI---GFPYTIG-Y 265

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  946 GITETTVHVSY-----IELDESivslransliGCSIPDLKVYVLDnylqPVPPGVVGEMYVAGAGLARGYLGRAGLTAER 1020
Cdd:cd05914    266 GMTETAPIISYsppnrIRLGSA----------GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEA 331

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1021 FIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKI-RGFRIELGEIEAVIMKHDKVEQVAVIVREdqpgdKRLVA 1099
Cdd:cd05914    332 FDKDGW-------FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQE-----KKLVA 399

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1100 YIVA----------SNNETIDT--NEMRQHASGSLPDYMVPYAFVVVNE-LPLTPNGKLDR 1147
Cdd:cd05914    400 LAYIdpdfldvkalKQRNIIDAikWEVRDKVNQKVPNYKKISKVKIVKEeFEKTPKGKIKR 460
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 669-1150 9.75e-30

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 125.37  E-value: 9.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:PRK07514    29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 SVEiecdESLKILVDDVNV--------------MEEIEKYSEENIDEmeclkPLAPSHIAYVIYTSGSTGRPKGVMIPHQ 814
Cdd:PRK07514   109 ANF----AWLSKIAAAAGAphvetldadgtgslLEAAAAAPDDFETV-----PRGADDLAAILYTSGTTGRSKGAMLSHG 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  815 NVV-RLLGATDHWfQFDADDVWT----MFHSYAFdFSVweIWGPLLYGGRLVVVPhtvSRSPKEFLQLLvkEKVTVLNQT 889
Cdd:PRK07514   180 NLLsNALTLVDYW-RFTPDDVLIhalpIFHTHGL-FVA--TNVALLAGASMIFLP---KFDPDAVLALM--PRATVMMGV 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  890 PSaFY-QLMQADRENEEVGQKlsLRYVVFGGEALELSRLEDWYSRHPHnapKVINMYGITETTVHVSYIELDEsivslRA 968
Cdd:PRK07514   251 PT-FYtRLLQEPRLTREAAAH--MRLFISGSAPLLAETHREFQERTGH---AILERYGMTETNMNTSNPYDGE-----RR 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  969 NSLIGCSIPDLKVYVLDNYL-QPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGT 1047
Cdd:PRK07514   320 AGTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDERGY 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1048 LDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDKrLVAYIVASNNETIDTNEMRQHASGSLPDYM 1126
Cdd:PRK07514   393 VHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgVPHPDFGEG-VTAVVVPKPGAALDEAAILAALKGRLARFK 471

                          490       500
                   ....*....|....*....|....
gi 1698252301 1127 VPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK07514   472 QPKRVFFVDELPRNTMGKVQKNLL 495
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 645-1154 1.33e-29

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 125.92  E-value: 1.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:PRK06710    26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVL-----------TNSSVEIEC------------------------DESLKILVDD---VN 766
Cdd:PRK06710   106 PLYTERELEYQLHDSGAKVILcldlvfprvtnVQSATKIEHvivtriadflpfpknllypfvqkkQSNLVVKVSEsetIH 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  767 VMEEIEKYSEENIDemeclKPLAPSH-IAYVIYTSGSTGRPKGVMIPHQNVVR--LLGAtdHWFQFDADD------VWTM 837
Cdd:PRK06710   186 LWNSVEKEVNTGVE-----VPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSntLMGV--QWLYNCKEGeevvlgVLPF 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  838 FHSYAFDfSVWEIwgPLLYGGRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgQKLSLRYVVF 917
Cdd:PRK06710   259 FHVYGMT-AVMNL--SIMQGYKMVLIPKF---DMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEY--DISSIRACIS 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  918 GGEALELSRLEDWYSRhphNAPKVINMYGITETT--VHVSYIEldesivSLRANSLIGCSIPDLKVYVLD-NYLQPVPPG 994
Cdd:PRK06710   331 GSAPLPVEVQEKFETV---TGGKLVEGYGLTESSpvTHSNFLW------EKRVPGSIGVPWPDTEAMIMSlETGEALPPG 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  995 VVGEMYVAGAGLARGYLGRAGLTAErFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVI 1074
Cdd:PRK06710   402 EIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1075 MKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPE 1154
Cdd:PRK06710   474 YEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 790-1150 2.14e-29

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 121.43  E-value: 2.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDV----WTMFHSYAfdfSVWEIWGPLLYGGRLVVVPH 865
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVllcgLPLFHVNG---SVVTLLTPLASGAHVVLAGP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  866 TVSRSP---KEFLQLLVKEKVTVLNQTPSAFYQLMQADrENEEVGqklSLRYVVFGGEAL--EL-SRLEDwysrhpHNAP 939
Cdd:cd05944     78 AGYRNPglfDNFWKLVERYRITSLSTVPTVYAALLQVP-VNADIS---SLRFAMSGAAPLpvELrARFED------ATGL 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  940 KVINMYGITETT--VHVSYIELDESIVSlranslIGCSIP--DLKVYVLD---NYLQPVPPGVVGEMYVAGAGLARGYLG 1012
Cdd:cd05944    148 PVVEGYGLTEATclVAVNPPDGPKRPGS------VGLRLPyaRVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLY 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1013 RAGlTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIkIR-GFRIELGEIEAVIMKHDKVEQVAVIVREDQ 1091
Cdd:cd05944    222 TEG-NKNAFVADGW-------LNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDA 292

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1092 PGDKRLVAYIVASNNETIDTNEMRQHASGSLPDY-MVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05944    293 HAGELPVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 653-1150 7.87e-29

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 123.61  E-value: 7.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRI 732
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  733 SFMLHDAKPSCVLTNSS----VEIECDE-SLK-ILVDDVNVM-------------EEIEKYSEENIDEMECLK------- 786
Cdd:PRK06178   123 SYELNDAGAEVLLALDQlapvVEQVRAEtSLRhVIVTSLADVlpaeptlplpdslRAPRLAAAGAIDLLPALRactapvp 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  787 --PLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVrLLGATDHWF--QFDADDVwtmFHSYAFDFsvWeIWG-------PLL 855
Cdd:PRK06178   203 lpPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVavVGGEDSV---FLSFLPEF--W-IAGenfgllfPLF 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  856 YGGRLVVVphtvSR-SPKEFLQLLVKEKVTVLNQTPSAFYQLMqadrENEEVGQK--LSLRYVvfgGEALELSRLEDWYS 932
Cdd:PRK06178   276 SGATLVLL----ARwDAVAFMAAVERYRVTRTVMLVDNAVELM----DHPRFAEYdlSSLRQV---RVVSFVKKLNPDYR 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  933 RHPHNAPKVINM---YGITET----TVHVSYIELDESIVSlrANSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGA 1004
Cdd:PRK06178   345 QRWRALTGSVLAeaaWGMTEThtcdTFTAGFQDDDFDLLS--QPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTP 422

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1005 GLARGYLGRAGLTAERFiadpfgKPGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVA 1084
Cdd:PRK06178   423 SLLKGYWNKPEATAEAL------RDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1085 VIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPyAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06178   495 VVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 641-1140 1.21e-27

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 120.36  E-value: 1.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  641 PEMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAgy 720
Cdd:PRK08279    35 SKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA-- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  721 lpldpdypsdrISFML----------H-----DAK---------------PSCVLTNSSVEIECDESLKILVDDVNVMEE 770
Cdd:PRK08279   113 -----------VVALLntqqrgavlaHslnlvDAKhlivgeelveafeeaRADLARPPRLWVAGGDTLDDPEGYEDLAAA 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  771 IEKYSEENIDEMEclkPLAPSHIAYVIYTSGSTGRPKGVMIPHqnvVRLLGATdHWFQ----FDADDVW----TMFHSYA 842
Cdd:PRK08279   182 AAGAPTTNPASRS---GVTAKDTAFYIYTSGTTGLPKAAVMSH---MRWLKAM-GGFGgllrLTPDDVLycclPLYHNTG 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  843 FDFSvweiWGPLLYGGRLVVVPHTVSRSpkEFLQLLVKEKVTV-----------LNQTPSAfyqlmqADRENeevgqklS 911
Cdd:PRK08279   255 GTVA----WSSVLAAGATLALRRKFSAS--RFWDDVRRYRATAfqyigelcrylLNQPPKP------TDRDH-------R 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  912 LRYVVfgGEALELSRLEDWYSRhpHNAPKVINMYGITETTvhVSYIELDEsivslRANSlIGCSIPDLKV------YVLD 985
Cdd:PRK08279   316 LRLMI--GNGLRPDIWDEFQQR--FGIPRILEFYAASEGN--VGFINVFN-----FDGT-VGRVPLWLAHpyaivkYDVD 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  986 N---------YLQPVPPGVVGEMY--VAGAGLARGYLGRAGlTAERFIADPFgKPGTRMYRTGDLArwRQDGtLDYIGRA 1054
Cdd:PRK08279   384 TgepvrdadgRCIKVKPGEVGLLIgrITDRGPFDGYTDPEA-SEKKILRDVF-KKGDAWFNTGDLM--RDDG-FGHAQFV 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 DhqikiR-G--FR-----IELGEIEAVIMKHDKVEQ-----VAVivredqPG-DKRL-VAYIVASNNETIDTNEMRQHAS 1119
Cdd:PRK08279   459 D-----RlGdtFRwkgenVATTEVENALSGFPGVEEavvygVEV------PGtDGRAgMAAIVLADGAEFDLAALAAHLY 527

                          570       580
                   ....*....|....*....|..
gi 1698252301 1120 GSLPDYMVPyAFV-VVNELPLT 1140
Cdd:PRK08279   528 ERLPAYAVP-LFVrLVPELETT 548
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 665-1150 2.04e-27

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 118.72  E-value: 2.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  665 EDKKLTYEKLNRKANKIARFLI-AKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSC 743
Cdd:cd05928     38 DEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  744 VLTNSSVEIECD------ESL--KILVDD------VNVMEEIEKYSEENIdemeCLKplAPSHIAYVIY-TSGSTGRPKg 808
Cdd:cd05928    118 IVTSDELAPEVDsvasecPSLktKLLVSEksrdgwLNFKELLNEASTEHH----CVE--TGSQEPMAIYfTSGTTGSPK- 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  809 vMIPHQNVVRLLGAT---DHWFQFDADDV-WTMFHSYAFDFSVWEIWGPLLYGGrLVVVPHTVSRSPKEFLQLLVKEKVT 884
Cdd:cd05928    191 -MAEHSHSSLGLGLKvngRYWLDLTASDImWNTSDTGWIKSAWSSLFEPWIQGA-CVFVHHLPRFDPLVILKTLSSYPIT 268

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  885 VLNQTPSAFYQLMQADRENEevgQKLSLRYVVFGGEALELSRLEDWYSRhphNAPKVINMYGITETTVhvsyIELDESIV 964
Cdd:cd05928    269 TFCGAPTVYRMLVQQDLSSY---KFPSLQHCVTGGEPLNPEVLEKWKAQ---TGLDIYEGYGQTETGL----ICANFKGM 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  965 SLRANSLiGCSIPDLKVYVLDNYLQPVPPGVVGEMYV-----AGAGLARGYLGRAGLTAERFIADpfgkpgtrMYRTGDL 1039
Cdd:cd05928    339 KIKPGSM-GKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD--------FYLTGDR 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1040 ARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIV-----ASNNETIDTNEM 1114
Cdd:cd05928    410 GIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqfLSHDPEQLTKEL 489

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1698252301 1115 RQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05928    490 QQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 793-1145 2.28e-27

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: 114.91  E-value: 2.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 IAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHSYAFDFSvweIWGPLLYGGrlVVVPHTVS 868
Cdd:cd17638      2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDryliINPFFHTFGYKAG---IVACLLTGA--TVVPVAVF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  869 RSPKeFLQLLVKEKVTVLNQTPSAFYQLM-QADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRHPHNApkVINMYGI 947
Cdd:cd17638     77 DVDA-ILEAIERERITVLPGPPTLFQSLLdHPGRKKFDLS---SLRAAVTGAATVPVELVRRMRSELGFET--VLTAYGL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  948 TETTVhVSYIELDESIVSLRANSliGCSIPDLKVYVLDNylqpvppgvvGEMYVAGAGLARGYLGRAGLTAERFIADPFg 1027
Cdd:cd17638    151 TEAGV-ATMCRPGDDAETVATTC--GRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW- 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1028 kpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNE 1107
Cdd:cd17638    217 ------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV 290

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1698252301 1108 TIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:cd17638    291 TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1-77 3.23e-27

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: 116.86  E-value: 3.23e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05930    368 LLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 658-1154 3.53e-27

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 118.46  E-value: 3.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  658 NSIAVVFEDK----KLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRIS 733
Cdd:PRK04319    59 DKVALRYLDAsrkeKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  734 FMLHDAKPSCVLTNSSV--EIECDE--SLK--ILVDDVNvmEEIEKY------SEENIDEMEClKPLAPSHIAYVIYTSG 801
Cdd:PRK04319   139 DRLEDSEAKVLITTPALleRKPADDlpSLKhvLLVGEDV--EEGPGTldfnalMEQASDEFDI-EWTDREDGAILHYTSG 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  802 STGRPKGVMIPHQNVVRLLgATDHWFQ-FDADDV--------WTMFHSYAfdfsvweIWGPLLYGGRLVVVphtVSR-SP 871
Cdd:PRK04319   216 STGKPKGVLHVHNAMLQHY-QTGKYVLdLHEDDVywctadpgWVTGTSYG-------IFAPWLNGATNVID---GGRfSP 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 KEFLQLLVKEKVTVLNQTPSAFYQLMQAdreNEEVGQKL---SLRYVVFGGEAL--ELSRledWysrhphnAPKVINM-- 944
Cdd:PRK04319   285 ERWYRILEDYKVTVWYTAPTAIRMLMGA---GDDLVKKYdlsSLRHILSVGEPLnpEVVR---W-------GMKVFGLpi 351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  945 ---YGITETTVH--VSYIELDesivsLRANSLiGCSIPDLKVYVLDNYLQPVPPGVVGEmyvagagLA---------RGY 1010
Cdd:PRK04319   352 hdnWWMTETGGImiANYPAMD-----IKPGSM-GKPLPGIEAAIVDDQGNELPPNRMGN-------LAikkgwpsmmRGI 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1011 LGRAGLTAERFIADpfgkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVRED 1090
Cdd:PRK04319   419 WNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD 490

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301 1091 QPGDKRLVAYIVASNNETIDTN---EMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPE 1154
Cdd:PRK04319   491 PVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWE 557
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 791-1147 5.27e-27

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: 113.89  E-value: 5.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  791 SHIAYVIYTSGSTGRPKGVMIPHQNvvrLLGATDHW----FQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHT 866
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKT---FFAVPDILqkegLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  867 VSRspKEFLQLLVKEKVTVLNQTPSAFYQLMQADRE-NEEVGQklsLRYVVFGGEAL--ELSRLEDWYSRhphnaPKVIN 943
Cdd:cd17635     78 TTY--KSLFKILTTNAVTTTCLVPTLLSKLVSELKSaNATVPS---LRLIGYGGSRAiaADVRFIEATGL-----TNTAQ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  944 MYGITETTVhVSYIELDESIVSLRAnslIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIA 1023
Cdd:cd17635    148 VYGLSETGT-ALCLPTDDDSIEINA---VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1024 DPFgkpgtrmyRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVA 1103
Cdd:cd17635    224 GWV--------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA 295

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1698252301 1104 SnnETIDTNEMR---QHASGSLPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:cd17635    296 S--AELDENAIRalkHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1-78 1.38e-26

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: 115.22  E-value: 1.38e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17644    388 LSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 962-1235 1.42e-26

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 111.77  E-value: 1.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  962 SIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLAR 1041
Cdd:COG3433     10 PPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1042 WRQDGTLdyiGRADHQIKIRGFRIELGEIEAVIMK----HDKVEQVAVIVREDQPGDKRLVAYIVASnnETIDTNEMRQH 1117
Cdd:COG3433     90 RRGLGPG---GGLERLVQQVVIRAERGEEEELLLVlraaAVVRVAVLAALRGAGVGLLLIVGAVAAL--DGLAAAAALAA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1118 ASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPEFI-----ASSSSRGPRTPQEEMLCDLFTEVL--SVSQIGIDDG 1190
Cdd:COG3433    165 LDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEallaaASPAPALETALTEEELRADVAELLgvDPEEIDPDDN 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1698252301 1191 FFDLGGHSLLAVQLMSRMKEAlGVELNIGTLFAAPTVAGLAERLE 1235
Cdd:COG3433    245 LFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLA 288
PRK13382 PRK13382
bile acid CoA ligase;
642-1153 1.45e-26

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 116.40  E-value: 1.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PRK13382    42 GMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFMLHDAKPSCVLTNSsveiECDESLKILVDDVNVMEEIEKYSEEN--------IDEMECLKPL-APSH 792
Cdd:PRK13382   122 LLNTSFAGPALAEVVTREGVDTVIYDE----EFSATVDRALADCPQATRIVAWTDEDhdltvevlIAAHAGQRPEpTGRK 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 IAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADD----VWTMFHSYAFdfsvweiwGPLLYGGRLVVVPHTVS 868
Cdd:PRK13382   198 GRVILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEptviVAPMFHAWGF--------SQLVLAASLACTIVTRR 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  869 R-SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHphnAPKVINMYGI 947
Cdd:PRK13382   270 RfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF---GDVIYNNYNA 346

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  948 TEttvhVSYIELdESIVSLRANSLIGCSIPD-LKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYL-GRAGLTAERFIAdp 1025
Cdd:PRK13382   347 TE----AGMIAT-ATPADLRAAPDTAGRPAEgTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTsGSTKDFHDGFMA-- 419

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1026 fgkpgtrmyrTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASN 1105
Cdd:PRK13382   420 ----------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 1698252301 1106 NETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAP 1153
Cdd:PRK13382   490 GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 645-1162 2.13e-26

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 116.09  E-value: 2.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  645 LPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAK-GVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPL 723
Cdd:PLN02574    43 VSFIFSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTM 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 DPDYPSDRISFMLHDAKPSCVLTnSSVEIECDESLKILVDDV-------NVMEEIEKYSEENIDEMECL-KPLAPSH-IA 794
Cdd:PLN02574   123 NPSSSLGEIKKRVVDCSVGLAFT-SPENVEKLSPLGVPVIGVpenydfdSKRIEFPKFYELIKEDFDFVpKPVIKQDdVA 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  795 YVIYTSGSTGRPKGVMIPHQNvvrLLGATDHWFQFDA--------DDVW----TMFHSYAFDFSVWEiwgpLLYGGRLVV 862
Cdd:PLN02574   202 AIMYSSGTTGASKGVVLTHRN---LIAMVELFVRFEAsqyeypgsDNVYlaalPMFHIYGLSLFVVG----LLSLGSTIV 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  863 VPHTVSRSpkEFLQLLVKEKVTVLNQTPSAFYQLMQADREneEVGQKL-SLRYVVFGGEALELSRLEDWYSRHPHnaPKV 941
Cdd:PLN02574   275 VMRRFDAS--DMVKVIDRFKVTHFPVVPPILMALTKKAKG--VCGEVLkSLKQVSCGAAPLSGKFIQDFVQTLPH--VDF 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITETTVhVSYIELDESivSLRANSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAER 1020
Cdd:PLN02574   349 IQGYGMTESTA-VGTRGFNTE--KLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQST 425

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1021 FIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAY 1100
Cdd:PLN02574   426 IDKDGW-------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAF 498

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1101 IVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPApEFIASSSSR 1162
Cdd:PLN02574   499 VVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR-SLTNSVSSR 559
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 789-1150 9.33e-26

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 114.09  E-value: 9.33e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 APSHIAYVIYTSGSTGRPKGVMIPHQNVV-------RLLGATDHwfqfDADDV----WTMFHSYAFDFSVWEIwgpLLYG 857
Cdd:PRK05677   205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVanmlqcrALMGSNLN----EGCEIliapLPLYHIYAFTFHCMAM---MLIG 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  858 GRLVVVPHtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMqadreNEEVGQKL---SLRYVVFGGEALELSRLEDWYSRh 934
Cdd:PRK05677   278 NHNILISN--PRDLPAMVKELGKWKFSGFVGLNTLFVALC-----NNEAFRKLdfsALKLTLSGGMALQLATAERWKEV- 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  935 phNAPKVINMYGITETTVHVS-----YIELdesivslranSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARG 1009
Cdd:PRK05677   350 --TGCAICEGYGMTETSPVVSvnpsqAIQV----------GTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1010 YLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVRE 1089
Cdd:PRK05677   418 YWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP 490

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1090 DQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK05677   491 DEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 666-1153 9.84e-26

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 113.25  E-value: 9.84e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  666 DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVL 745
Cdd:PRK12406     9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  746 TNS----SVEIECDESLKILVddVNVMEEI-EKYSeenIDEMECLKPlaPSHIAY--------------------VIYTS 800
Cdd:PRK12406    89 AHAdllhGLASALPAGVTVLS--VPTPPEIaAAYR---ISPALLTPP--AGAIDWegwlaqqepydgppvpqpqsMIYTS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  801 GSTGRPKGVM----IPHQNVVR-LLGATDHWFQFDADDVWT--MFHS--YAFDFSVWEIwgpllyGGRLVVVPHTvsrSP 871
Cdd:PRK12406   162 GTTGHPKGVRraapTPEQAAAAeQMRALIYGLKPGIRALLTgpLYHSapNAYGLRAGRL------GGVLVLQPRF---DP 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 KEFLQLLVKEKVTVLNQTPSAFYQLMqadRENEEVGQKL---SLRYVVFGGE--ALELSR-LEDWYsrhphnAPKVINMY 945
Cdd:PRK12406   233 EELLQLIERHRITHMHMVPTMFIRLL---KLPEEVRAKYdvsSLRHVIHAAApcPADVKRaMIEWW------GPVIYEYY 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  946 GITETTVhvsyIELDESIVSLRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLAR-GYLG----RAGLTAER 1020
Cdd:PRK12406   304 GSTESGA----VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNkpekRAEIDRGG 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1021 FIAdpfgkpgtrmyrTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAY 1100
Cdd:PRK12406   380 FIT------------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAV 447

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1101 IVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAP 1153
Cdd:PRK12406   448 VEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 670-1150 1.56e-25

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


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 113.01  E-value: 1.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  670 TYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNss 749
Cdd:cd17642     46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS-- 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  750 vEIECDESLKI-----LVDDVNVMEEIEKYSEENIDEMECLKPLAPS---------------HIAYVIYTSGSTGRPKGV 809
Cdd:cd17642    124 -KKGLQKVLNVqkklkIIKTIIILDSKEDYKGYQCLYTFITQNLPPGfneydfkppsfdrdeQVALIMNSSGSTGLPKGV 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  810 MIPHQN-VVRLLGATDHWF--QFDAD----DVWTMFHSyafdFSVWEIWGPLLYGGRLVVVPhtvSRSPKEFLQLLVKEK 882
Cdd:cd17642    203 QLTHKNiVARFSHARDPIFgnQIIPDtailTVIPFHHG----FGMFTTLGYLICGFRVVLMY---KFEEELFLRSLQDYK 275

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  883 VTVLNQTPSAFYQLMQADRENEevgQKLSLRYVVFGGEAlELSR-LEDWYSRHpHNAPKVINMYGITETTVHVsYIELDE 961
Cdd:cd17642    276 VQSALLVPTLFAFFAKSTLVDK---YDLSNLHEIASGGA-PLSKeVGEAVAKR-FKLPGIRQGYGLTETTSAI-LITPEG 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  962 SIvslRANSlIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLA 1040
Cdd:cd17642    350 DD---KPGA-VGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW-------LHSGDIA 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1041 RWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASG 1120
Cdd:cd17642    419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVAS 498

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1698252301 1121 SL-PDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd17642    499 QVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 642-1140 1.72e-25

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 112.91  E-value: 1.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PRK06164     9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFM-----------------------LHDAKPSCVLTNSSVEIECDESLKI---------LVDDVNVME 769
Cdd:PRK06164    89 AVNTRYRSHEVAHIlgrgrarwlvvwpgfkgidfaaiLAAVPPDALPPLRAIAVVDDAADATpapapgarvQLFALPDPA 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  770 EIEKYSEENIDemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTMFHSY--AFDFSV 847
Cdd:PRK06164   169 PPAAAGERAAD---------PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFcgVFGFST 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  848 weIWGPLLYGGRLVVVPhtVSRSPKEfLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGqklSLRYVVFGGEALELSRL 927
Cdd:PRK06164   240 --LLGALAGGAPLVCEP--VFDAART-ARALRRHRVTHTFGNDEMLRRILDTAGERADFP---SARLFGFASFAPALGEL 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  928 EDWYSRhpHNAPkVINMYGITETTVHVSYIELDESiVSLRANSLIGCSIPDLKVYVLDNYLQPV-PPGVVGEMYVAGAGL 1006
Cdd:PRK06164   312 AALARA--RGVP-LTGLYGSSEVQALVALQPATDP-VSVRIEGGGRPASPEARVRARDPQDGALlPDGESGEIEIRAPSL 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1007 ARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVE--QVA 1084
Cdd:PRK06164   388 MRGYLDNPDATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAaaQVV 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1085 VIVREDQPgdkRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLT 1140
Cdd:PRK06164   461 GATRDGKT---VPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 653-1150 2.17e-25

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 111.50  E-value: 2.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDri 732
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP-- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  733 sfMLHDAKPScvLTNSSVEIECDESLKILVDDVNVMEEIEKYSEenidemeclkPLAPSHIAYVIYTSGSTGRPKGVMIP 812
Cdd:PRK09029    91 --LLEELLPS--LTLDFALVLEGENTFSALTSLHLQLVEGAHAV----------AWQPQRLATMTLTSGSTGLPKAAVHT 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  813 HQN-------VVRLlgatdhwFQFDADDVW----TMFHsyafdFS----VWEiWgpLLYGGRLVVvphtvsRSPKEFLQL 877
Cdd:PRK09029   157 AQAhlasaegVLSL-------MPFTAQDSWllslPLFH-----VSgqgiVWR-W--LYAGATLVV------RDKQPLEQA 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  878 LvkEKVTVLNQTPSAFYQLMQADReneevgQKLSLRYVVFGGEA--LELSR------LEDWYSrhphnapkvinmYGITE 949
Cdd:PRK09029   216 L--AGCTHASLVPTQLWRLLDNRS------EPLSLKAVLLGGAAipVELTEqaeqqgIRCWCG------------YGLTE 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  950 --TTVHVSyieldesivslRANSLIGCSIP----DLKVyvldnylqpvppgVVGEMYVAGAGLARGYLGRAGLTAerfIA 1023
Cdd:PRK09029   276 maSTVCAK-----------RADGLAGVGSPlpgrEVKL-------------VDGEIWLRGASLALGYWRQGQLVP---LV 328

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1024 DPFGKPGTRmyrtgDLARWrQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVA 1103
Cdd:PRK09029   329 NDEGWFATR-----DRGEW-QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVES 402

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1104 SNNETIDtnEMRQHASGSLPDYMVPYAFVVvneLPLT-PNG--KLDRKAL 1150
Cdd:PRK09029   403 DSEAAVV--NLAEWLQDKLARFQQPVAYYL---LPPElKNGgiKISRQAL 447
PRK07529 PRK07529
AMP-binding domain protein; Validated
 647-1150 3.04e-25

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 113.13  E-value: 3.04e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  647 QLFEKQAHINPNSIAVVF--------EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGA 718
Cdd:PRK07529    29 ELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  719 GYlPLDPDYPSDRISFMLHDAKPSCV------------------------------------LTNSSVEIECDESLKILV 762
Cdd:PRK07529   109 AN-PINPLLEPEQIAELLRAAGAKVLvtlgpfpgtdiwqkvaevlaalpelrtvvevdlaryLPGPKRLAVPLIRRKAHA 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  763 DDVNVMEEIEKYSEeniDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVrllgaTDHW-----FQFDADDV--- 834
Cdd:PRK07529   188 RILDFDAELARQPG---DRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEV-----ANAWlgallLGLGPGDTvfc 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  835 -WTMFHSYAfdfSVWEIWGPLLYGGRLVVVPHTVSRSP---KEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGqkl 910
Cdd:PRK07529   260 gLPLFHVNA---LLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDIS--- 333

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  911 SLRYVVFGGEAL--EL-SRLEDwysrhpHNAPKVINMYGITETT--VHVSYIELDESIVSlranslIGCSIP--DLKVYV 983
Cdd:PRK07529   334 SLRYALCGAAPLpvEVfRRFEA------ATGVRIVEGYGLTEATcvSSVNPPDGERRIGS------VGLRLPyqRVRVVI 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  984 LD---NYLQPVPPGVVGEMYVAGAGLARGYLGRA---GLTAERfiadpfgkpgtRMYRTGDLARWRQDGTLDYIGRADHQ 1057
Cdd:PRK07529   402 LDdagRYLRDCAVDEVGVLCIAGPNVFSGYLEAAhnkGLWLED-----------GWLNTGDLGRIDADGYFWLTGRAKDL 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1058 IkIR-GFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPD-YMVPYAFVVVN 1135
Cdd:PRK07529   471 I-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILD 549

                          570
                   ....*....|....*
gi 1698252301 1136 ELPLTPNGKLDRKAL 1150
Cdd:PRK07529   550 ALPKTAVGKIFKPAL 564
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 657-1152 6.81e-25

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 110.86  E-value: 6.81e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFML 736
Cdd:PRK13383    49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  737 HDAKPSCVLTNSsveiECDESLKILVDDVNVMEEIEKYSEENIDEMeclKPLAPSHIayVIYTSGSTGRPKGVmiPHQNV 816
Cdd:PRK13383   129 RAHHISTVVADN----EFAERIAGADDAVAVIDPATAGAEESGGRP---AVAAPGRI--VLLTSGTTGKPKGV--PRAPQ 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  817 VR--------LLGATDHWFQFDADDVWTMFHSYAFDFSVWEIwgplLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQ 888
Cdd:PRK13383   198 LRsavgvwvtILDRTRLRTGSRISVAMPMFHGLGLGMLMLTI----ALGGTVLTHRHFDAEAALAQASLHRADAFTAVPV 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  889 TPSAFYQLMQADRENEEVGQklsLRYVVFGGEALELS---RLEDWYsrhphnAPKVINMYGITETTVHVSYIELDesivs 965
Cdd:PRK13383   274 VLARILELPPRVRARNPLPQ---LRVVMSSGDRLDPTlgqRFMDTY------GDILYNGYGSTEVGIGALATPAD----- 339

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  966 LR-ANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGltaeRFIADPfgkpgtrMYRTGDLARWRQ 1044
Cdd:PRK13383   340 LRdAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGG----KAVVDG-------MTSTGDMGYLDN 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1045 DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPD 1124
Cdd:PRK13383   409 AGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSR 488

                          490       500
                   ....*....|....*....|....*...
gi 1698252301 1125 YMVPYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:PRK13383   489 FEQPRDINIVSSIPRNPTGKVLRKELPG 516
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 646-1150 1.47e-24

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 110.49  E-value: 1.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  646 PQLFEKQA-HINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLD 724
Cdd:PLN03102    16 PITFLKRAsECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPIN 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISFMLHDAKPSCVLTNSSVEIECDESLKILVDD----------VNVMEEIEKYSEENIDeMECL----KPlAP 790
Cdd:PLN03102    96 TRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEdsnlnlpvifIHEIDFPKRPSSEELD-YECLiqrgEP-TP 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  791 SHIAYVI------------YTSGSTGRPKGVMIPHQNV-VRLLGATDHWfQFDADDV--WT--MFHSYAFDFSvweiWGP 853
Cdd:PLN03102   174 SLVARMFriqdehdpislnYTSGTTADPKGVVISHRGAyLSTLSAIIGW-EMGTCPVylWTlpMFHCNGWTFT----WGT 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  854 LLYGGRLVVVPHTVSrspKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgQKLSLRYVVFGGE---ALELSRLEDW 930
Cdd:PLN03102   249 AARGGTSVCMRHVTA---PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS--PRSGPVHVLTGGSpppAALVKKVQRL 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  931 ysrhphnAPKVINMYGITETTVHVSYIELDESIVSLRANSLI------GCSIPDLKVYVLDN--YLQPVPPG--VVGEMY 1000
Cdd:PLN03102   324 -------GFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMelkarqGVSILGLADVDVKNkeTQESVPRDgkTMGEIV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1001 VAGAGLARGYLGRAGLTAERFiadpfgKPGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKV 1080
Cdd:PLN03102   397 IKGSSIMKGYLKNPKATSEAF------KHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1081 EQVAVIVREDQPGDKRLVAYIVASNNET--------IDTNE--MRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PLN03102   469 LETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdkLVTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 666-1144 1.77e-24

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: 108.60  E-value: 1.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  666 DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAgylpldpdypsdrisfmlhdaKPSCVL 745
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA---------------------VAALIN 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  746 TNssveiecdESLKILVddvnvmeeiekyseenidemECLKPLAPSHI----AYVIYTSGSTGRPKGVMIPHQNVVRLLG 821
Cdd:cd05940     60 YN--------LRGESLA--------------------HCLNVSSAKHLvvdaALYIYTSGTTGLPKAAIISHRRAWRGGA 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  822 ATDHWFQFDADDVW--TM--FHSYAFDFSvweiWGPLLYGGRLVVVPHTVSRSpkEFLQLLVKEKVTVLNQTPSAFYQLM 897
Cdd:cd05940    112 FFAGSGGALPSDVLytCLplYHSTALIVG----WSACLASGATLVIRKKFSAS--NFWDDIRKYQATIFQYIGELCRYLL 185

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  898 QADRENEEVGQKLSlryVVFgGEALELSRLEDWYSRhpHNAPKVINMYGITETTvhVSYIELDESIVSL-RANSLIGCSI 976
Cdd:cd05940    186 NQPPKPTERKHKVR---MIF-GNGLRPDIWEEFKER--FGVPRIAEFYAATEGN--SGFINFFGKPGAIgRNPSLLRKVA 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKV-YVLDN---------YLQPVPPGVVGEMYVAGAGLAR--GYLGrAGLTAERFIADPFgKPGTRMYRTGDLARWRQ 1044
Cdd:cd05940    258 PLALVkYDLESgepirdaegRCIKVPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDG 335

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1045 DGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRL-VAYIVASNNETIDTNEMRQHASGSLP 1123
Cdd:cd05940    336 EGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNEEFDLSALAAHLEKNLP 415

                          490       500
                   ....*....|....*....|.
gi 1698252301 1124 DYMVPYAFVVVNELPLTPNGK 1144
Cdd:cd05940    416 GYARPLFLRLQPEMEITGTFK 436
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1-81 2.28e-24

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: 108.95  E-value: 2.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkePINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:cd17655    412 LLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489


                   .
gi 1698252301   81 D 81
Cdd:cd17655    490 D 490
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 668-1150 2.47e-24

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 110.22  E-value: 2.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  668 KLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS----DRISFM-------- 735
Cdd:PTZ00237    92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVksliDRIETItpkliitt 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  736 ---------------LHDA------KPSCVLTNSSVEIECDESLKILVD------DVNVMEEIEKYSEENIDEMECLKPL 788
Cdd:PTZ00237   172 nygilndeiitftpnLKEAielstfKPSNVITLFRNDITSESDLKKIETiptipnTLSWYDEIKKIKENNQSPFYEYVPV 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 APSHIAYVIYTSGSTGRPKGVMipHQNVVRLLGATDHWFQFDADDVWTMFHSYAfdfSV-WEIWGPLLYG----GRLVVV 863
Cdd:PTZ00237   252 ESSHPLYILYTSGTTGNSKAVV--RSNGPHLVGLKYYWRSIIEKDIPTVVFSHS---SIgWVSFHGFLYGslslGNTFVM 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  864 PHTVSRSPK----EFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKL---SLRYVVFGGEALELSRLEdwYSRHPH 936
Cdd:PTZ00237   327 FEGGIIKNKhiedDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKYdlsNLKEIWCGGEVIEESIPE--YIENKL 404

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  937 NApKVINMYGITETTVhvSYIeLDESIVSLRANSLiGCSIPDLKVYVLDN--------------YLQPVPPGVVGEMYVa 1002
Cdd:PTZ00237   405 KI-KSSRGYGQTEIGI--TYL-YCYGHINIPYNAT-GVPSIFIKPSILSEdgkelnvneigevaFKLPMPPSFATTFYK- 478

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1003 gaglargylgraglTAERFiADPFGK-PGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVE 1081
Cdd:PTZ00237   479 --------------NDEKF-KQLFSKfPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVL 541

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1082 QVAVIVREDQPGDKRLVAYIV---ASNNETIDTNEMRQHASGSLPDYMVPYAF----VVVNELPLTPNGKLDRKAL 1150
Cdd:PTZ00237   542 ECCSIGIYDPDCYNVPIGLLVlkqDQSNQSIDLNKLKNEINNIITQDIESLAVlrkiIIVNQLPKTKTGKIPRQII 617
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1-78 2.54e-24

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: 108.11  E-value: 2.54e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17652    359 LTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 644-1150 2.62e-24

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 109.34  E-value: 2.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPL 723
Cdd:PRK07059    24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  724 DPDYPSDRISFMLHD--AKPSCVLTN--SSVE-IECDESLKILVddVNVMEE-------IEKYSEENIDEM--------- 782
Cdd:PRK07059   104 NPLYTPRELEHQLKDsgAEAIVVLENfaTTVQqVLAKTAVKHVV--VASMGDllgfkghIVNFVVRRVKKMvpawslpgh 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  783 ------------ECLKP--LAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQF------DADDVWTM----- 837
Cdd:PRK07059   182 vrfndalaegarQTFKPvkLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPafekkpRPDQLNFVcalpl 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  838 FHSYAFdfSVWEIWGpLLYGGRLVVVPHtvSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMqadreNEEVGQKL---SLRY 914
Cdd:PRK07059   262 YHIFAL--TVCGLLG-MRTGGRNILIPN--PRDIPGFIKELKKYQVHIFPAVNTLYNALL-----NNPDFDKLdfsKLIV 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  915 VVFGGEALELSRLEDWYSRHphNAPkVINMYGITETTVHVSYIELDESIVSlranSLIGCSIPDLKVYVLDNYLQPVPPG 994
Cdd:PRK07059   332 ANGGGMAVQRPVAERWLEMT--GCP-ITEGYGLSETSPVATCNPVDATEFS----GTIGLPLPSTEVSIRDDDGNDLPLG 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  995 VVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVI 1074
Cdd:PRK07059   405 EPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1075 MKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDtNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK07059   478 ASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTE-EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1-77 2.66e-24

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: 108.44  E-value: 2.66e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkePINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd12117    409 LRAHPGVREAVVVVREDAGGDKRLVAYVVAEG--ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 667-1102 8.33e-24

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: 106.67  E-value: 8.33e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  667 KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAkpscvlt 746
Cdd:cd17640      4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHS------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 nssveiecdESLKILVDDvnvmeeiekyseenidemeclkplAPSHIAYVIYTSGSTGRPKGVMIPHQNVVrllgatdhw 826
Cdd:cd17640     77 ---------ESVALVVEN------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLL--------- 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  827 fqFDADDVWTMFHSYAFD--FSVWEIWgpllyggrlvvvpHTVSR----------------SPKEFLQLLVKEKVTVLNQ 888
Cdd:cd17640    115 --HQIRSLSDIVPPQPGDrfLSILPIW-------------HSYERsaeyfifacgcsqaytSIRTLKDDLKRVKPHYIVS 179

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  889 TP---SAFYQLMQADRENEEVGQKLSLRYVVFGGE---------ALELSrLEDWYsrhphNAP--KVINMYGITETTVHV 954
Cdd:cd17640    180 VPrlwESLYSGIQKQVSKSSPIKQFLFLFFLSGGIfkfgisgggALPPH-VDTFF-----EAIgiEVLNGYGLTETSPVV 253

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  955 SYIELDESIvslraNSLIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrm 1033
Cdd:cd17640    254 SARRLKCNV-----RGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------- 321

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1034 YRTGDLARWRQDGTLDYIGRADHQIKIR-GFRIELGEIEAVIMKHDKVEQVaVIVREDQpgdKRLVAYIV 1102
Cdd:cd17640    322 FNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQI-MVVGQDQ---KRLGALIV 387
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
667-1150 9.84e-24

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 107.66  E-value: 9.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  667 KKLTYEKLNRKANKIARFLIakgvGPDQL-----VALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKP 741
Cdd:PRK08751    49 KTITYREADQLVEQFAAYLL----GELQLkkgdrVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  742 SC--VLTNSSVEIE---CDESLKILVDD-------------VN-VMEEIEKYSEE-----NIDEMECLK----------P 787
Cdd:PRK08751   125 SVlvVIDNFGTTVQqviADTPVKQVITTglgdmlgfpkaalVNfVVKYVKKLVPEyringAIRFREALAlgrkhsmptlQ 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  788 LAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDA------DDVWT---MFHSYAfdfsvweiwgplLYGG 858
Cdd:PRK08751   205 IEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGkleegcEVVITalpLYHIFA------------LTAN 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  859 RLVVVP-----HTVS--RSPKEFLQLLVKEKVTVLNQTPSAFYQLMqadreNEEVGQKL---SLRYVVFGGEALELSRLE 928
Cdd:PRK08751   273 GLVFMKiggcnHLISnpRDMPGFVKELKKTRFTAFTGVNTLFNGLL-----NTPGFDQIdfsSLKMTLGGGMAVQRSVAE 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  929 DWYSRhphNAPKVINMYGITETT--VHVSYIELDESivslraNSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGL 1006
Cdd:PRK08751   348 RWKQV---TGLTLVEAYGLTETSpaACINPLTLKEY------NGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1007 ARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI 1086
Cdd:PRK08751   419 MKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301 1087 -VREDQPGDkrLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK08751   492 gVPDEKSGE--IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 643-1150 1.47e-23

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 106.66  E-value: 1.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK07470     7 MNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTNSSV--------EIECDESLKILVDDVNVMEEIEKYSEENIDEMecLKPLAPSH-- 792
Cdd:PRK07470    87 TNFRQTPDEVAYLAEASGARAMICHADFpehaaavrAASPDLTHVVAIGGARAGLDYEALVARHLGAR--VANAAVDHdd 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 IAYVIYTSGSTGRPKGVMIPHQNVVRLLgaTDHWfqfdADDVWTMFHSyafDFSVweIWGPLLYG-----------GRLV 861
Cdd:PRK07470   165 PCWFFFTSGTTGRPKAAVLTHGQMAFVI--TNHL----ADLMPGTTEQ---DASL--VVAPLSHGagihqlcqvarGAAT 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMqadrENEEVGQ--KLSLRYVVFGG-------EALELSRLedwys 932
Cdd:PRK07470   234 VLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLV----EHPAVDRydHSSLRYVIYAGapmyradQKRALAKL----- 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  933 rhphnAPKVINMYGITETTVHVSYI-----ELDESivslrANSLIG-CSIP--DLKVYVLDNYLQPVPPGVVGEMYVAGA 1004
Cdd:PRK07470   305 -----GKVLVQYFGLGEVTGNITVLppalhDAEDG-----PDARIGtCGFErtGMEVQIQDDEGRELPPGETGEICVIGP 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1005 GLARGYLGRAGLTAERFIADPFgkpgtrmyRTGDLARWRQDGTLdYI-GRADHQIKIRGFRIELGEIEAVIMKHDKVEQV 1083
Cdd:PRK07470   375 AVFAGYYNNPEANAKAFRDGWF--------RTGDLGHLDARGFL-YItGRASDMYISGGSNVYPREIEEKLLTHPAVSEV 445

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301 1084 AVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK07470   446 AVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 669-1154 1.53e-23

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


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 105.34  E-value: 1.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP----LDPDYPSDRIsfmlhdakpscv 744
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRV------------ 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  745 ltnssveiECDESLKILVDDVNVMEEiekyseenidemeclkPLapshiaYVIYTSGSTGRPKgvMIPHQNVVRLLG--A 822
Cdd:cd05974     69 --------DRGGAVYAAVDENTHADD----------------PM------LLYFTSGTTSKPK--LVEHTHRSYPVGhlS 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  823 TDHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVVVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRE 902
Cdd:cd05974    117 TMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA 196

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  903 NEEVGqklsLRYVVFGGEALElsrledwysrhphnaPKVINM------------YGITETTVHVSyielDESIVSLRANS 970
Cdd:cd05974    197 SFDVK----LREVVGAGEPLN---------------PEVIEQvrrawgltirdgYGQTETTALVG----NSPGQPVKAGS 253

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  971 LiGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAG--AGLARGYLGRAGLTAERFiadpfgkpGTRMYRTGDLARWRQDGTL 1048
Cdd:cd05974    254 M-GRPLPGYRVALLDPDGAPATEGEVALDLGDTrpVGLMKGYAGDPDKTAHAM--------RGGYYRTGDIAMRDEDGYL 324

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1049 DYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIvreDQPGDKRLV---AYIV--ASNNETIDTN-EMRQHasgsL 1122
Cdd:cd05974    325 TYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVV---PSPDPVRLSvpkAFIVlrAGYEPSPETAlEIFRF----S 397

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1698252301 1123 PDYMVPYAFV---VVNELPLTPNGKLDRKALPAPE 1154
Cdd:cd05974    398 RERLAPYKRIrrlEFAELPKTISGKIRRVELRRRE 432
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 796-1147 1.56e-23

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: 103.50  E-value: 1.56e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  796 VIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFHSYAFDFSVweiwGPLLYGGRLVVVPHTvsrSP 871
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYlnmlPLFHIAGLNLAL----ATFHAGGANVVMEKF---DP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 KEFLQLLVKEKVTVLNQTPSAFYQLMQAdreNEEVGQKL-SLRYVvFGGEALE-LSRLEDwysrhpHNAPKVINMYGITE 949
Cdd:cd17637     78 AEALELIEEEKVTLMGSFPPILSNLLDA---AEKSGVDLsSLRHV-LGLDAPEtIQRFEE------TTGATFWSLYGQTE 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  950 TTVHVSYIELDEsivslRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFiadpfgKP 1029
Cdd:cd17637    148 TSGLVTLSPYRE-----RPGS-AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF------RN 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1030 GtrMYRTGDLARWRQDGTLDYIGRADHQ--IKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNE 1107
Cdd:cd17637    216 G--WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA 293

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1698252301 1108 TIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:cd17637    294 TLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
644-1150 2.09e-23

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 106.68  E-value: 2.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  644 TLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFL-----IAKGvgpDQlVALAMPRSLNMVVSLLAVLKAGA 718
Cdd:PRK08974    24 SLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLqnglgLKKG---DR-VALMMPNLLQYPIALFGILRAGM 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  719 GYLPLDPDYPSDRISFMLHD--AKPSCVLTNSSVEIEcdeslKIlVDDVNVMEEI-------------------EKYSEE 777
Cdd:PRK08974   100 IVVNVNPLYTPRELEHQLNDsgAKAIVIVSNFAHTLE-----KV-VFKTPVKHVIltrmgdqlstakgtlvnfvVKYIKR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  778 NIDE------------------MECLKP-LAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLgatdhwFQFDAddvwtmf 838
Cdd:PRK08974   174 LVPKyhlpdaisfrsalhkgrrMQYVKPeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL------EQAKA------- 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  839 hsyafdfsvweIWGPLLYGG-RLVVVP----H----TVS-----------------RSPKEFLQLLVKEKVTVLNQTPSA 892
Cdd:PRK08974   241 -----------AYGPLLHPGkELVVTAlplyHifalTVNcllfielggqnllitnpRDIPGFVKELKKYPFTAITGVNTL 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  893 FYQLMQadreNEEVgQKL---SLRYVVFGGEALELSRLEDWysrHPHNAPKVINMYGITETT--VHVSYIELDESivslr 967
Cdd:PRK08974   310 FNALLN----NEEF-QELdfsSLKLSVGGGMAVQQAVAERW---VKLTGQYLLEGYGLTECSplVSVNPYDLDYY----- 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  968 aNSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAErFIADPFgkpgtrmYRTGDLARWRQDGT 1047
Cdd:PRK08974   377 -SGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW-------LATGDIAVMDEEGF 447

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1048 LDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDkrLVAYIVASNNETIDTNEMRQHASGSLPDYM 1126
Cdd:PRK08974   448 LRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVgVPSEVSGE--AVKIFVVKKDPSLTEEELITHCRRHLTGYK 525

                          570       580
                   ....*....|....*....|....
gi 1698252301 1127 VPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK08974   526 VPKLVEFRDELPKSNVGKILRREL 549
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 181-611 2.55e-23

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: 104.70  E-value: 2.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFP-NVLGSSYQKILD-----MENL 254
Cdd:cd19547      3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDdlappWALL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  255 NLEMVITNTCKDELESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQGD 334
Cdd:cd19547     83 DWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  335 RVQLEtlPVQ-YADYALWQQQLLGDETTPESlistqldFWKEELKGLPdqmelPTDY-QRPVETSYRGETIHFHIDEGMH 412
Cdd:cd19547    163 EPQLS--PCRpYRDYVRWIRARTAQSEESER-------FWREYLRDLT-----PSPFsTAPADREGEFDTVVHEFPEQLT 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  413 SRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDVLSD--IVGLFVNTLVLRTNTSGDPSFKELLNR 490
Cdd:cd19547    229 RLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSehMVGIFINTIPLRIRLDPDQTVTGLLET 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  491 VKQvNLAAYENQ-DVPFERLVEVLNPVRTRNSHpLFQVMLAFQNTPEAtfNAPDLEASLEIqsvgsakFDLtfeisESNE 569
Cdd:cd19547    309 IHR-DLATTAAHgHVPLAQIKSWASGERLSGGR-VFDNLVAFENYPED--NLPGDDLSIQI-------IDL-----HAQE 372

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 1698252301  570 VDGTPNGLHGL--------LEFSTDLYKRETVQKLIERFILLLDDAATNP 611
Cdd:cd19547    373 KTEYPIGLIVLplqklafhFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 796-1146 2.83e-23

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: 102.77  E-value: 2.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  796 VIYTSGSTGRPKGVMIPHQN------VVRLLGATDHWFQFDadDVWTMFHSYAFDFSVweiwGPLLYGGRLVVVPHTvsr 869
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQAllaqalVLAVLQAIDEGTVFL--NSGPLFHIGTLMFTL----ATFHAGGTNVFVRRV--- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 SPKEFLQLLVKEKVTVLNQTPSAFYQLMQAdreNEEVGQKLSLRYVVFGgealelsrLEDWYS-RHPHNAPKVINM--YG 946
Cdd:cd17636     76 DAEEVLELIEAERCTHAFLLPPTIDQIVEL---NADGLYDLSSLRSSPA--------APEWNDmATVDTSPWGRKPggYG 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  947 ITETTVHVSYIELDESivslrANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIAdpf 1026
Cdd:cd17636    145 QTEVMGLATFAALGGG-----AIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--- 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1027 gkpgtRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNN 1106
Cdd:cd17636    217 -----GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1698252301 1107 ETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLD 1146
Cdd:cd17636    292 ASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 662-1145 2.91e-23

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 105.76  E-value: 2.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  662 VVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKp 741
Cdd:PRK08276     5 MAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  742 SCVLTNSSveiECDESLKILVDDVN--------VMEEIEKYSeeniDEMECLKPLAPSHIAYVI------YTSGSTGRPK 807
Cdd:PRK08276    84 AKVLIVSA---ALADTAAELAAELPagvplllvVAGPVPGFR----SYEEALAAQPDTPIADETagadmlYSSGTTGRPK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  808 GVMI------PHQNVVRLLGATDHWFQFDADDVWTM----FHSYAFDFSVWEiwgpLLYGGRLVVVPHTvsrSPKEFLQL 877
Cdd:PRK08276   157 GIKRplpgldPDEAPGMMLALLGFGMYGGPDSVYLSpaplYHTAPLRFGMSA----LALGGTVVVMEKF---DAEEALAL 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  878 LVKEKVTVLNQTPSAFYQLMQADrenEEVGQKL---SLRYVVFGGE--ALELSR-LEDWYsrhphnAPKVINMYGITE-- 949
Cdd:PRK08276   230 IERYRVTHSQLVPTMFVRMLKLP---EEVRARYdvsSLRVAIHAAApcPVEVKRaMIDWW------GPIIHEYYASSEgg 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  950 -TTVHVSYIELDESIVSLRAnsLIGcsipdlKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIadpfgk 1028
Cdd:PRK08276   301 gVTVITSEDWLAHPGSVGKA--VLG------EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------ 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1029 pGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDkRLVAYIVASNNE 1107
Cdd:PRK08276   367 -PHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFgVPDEEMGE-RVKAVVQPADGA 444

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1698252301 1108 TID---TNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:PRK08276   445 DAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 181-536 3.26e-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: 3.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  181 PLSFAQRRLWFLNCLEGPSPTYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNV-LGSSYQKILdmENLNLEMV 259
Cdd:cd19536      3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDgLGQPVQVVH--RQAQVPVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  260 ITNTCKDE-----LESVLSEAVRYSFNLDFEPAVRLQLFTVSENEHVLL-ILLHHIVGDGWSLQPLTRDFTAAYKARCQG 333
Cdd:cd19536     81 ELDLTPLEeqldpLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 DRVQLetLPVQ-YADYALWQQQLLGDETTpeslistqLDFWKEELKGLPDQmelPTDYQRPVETSYRGETIHFHIDEGMH 412
Cdd:cd19536    161 KPLSL--PPAQpYRDFVAHERASIQQAAS--------ERYWREYLAGATLA---TLPALSEAVGGGPEQDSELLVSVPLP 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  413 SRLVELGRKNGVSLFMVLQAGLSALFTRLGAGTDIPIGSPIAGRNDDV--LSDIVGLFVNTLVLRTNTSgDPSFKELLNR 490
Cdd:cd19536    228 VRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETtgAERLLGLFLNTLPLRVTLS-EETVEDLLKR 306

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1698252301  491 VKQVNLAAYENQDVPferlveVLNPVRTRNSHPLFQVMLAFQNTPE 536
Cdd:cd19536    307 AQEQELESLSHEQVP------LADIQRCSEGEPLFDSIVNFRHFDL 346
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 643-1053 4.47e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 105.79  E-value: 4.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFED---------KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAmPRSLNMVVSLLAV 713
Cdd:PRK05850     1 SSVPSLLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  714 LKAGAGYLPLDPDYPS---DRISFMLHDAKPSCVLTNSSVeiecdeslkilVDDVnvMEEIEKYSEEN------IDEME- 783
Cdd:PRK05850    80 LQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAV-----------VDDV--TEYVAPQPGQSappvieVDLLDl 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  784 ------CLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVV--------RLLGATDHWFQFDADDV-WTMF-HSYAFdfsV 847
Cdd:PRK05850   147 dsprgsDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIanfeqlmsDYFGDTGGVPPPDTTVVsWLPFyHDMGL---V 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  848 WEIWGPLLyGGRLVVVPHTVS--RSPKEFLQLLVKEkvtvlnqtPSAF-------YQLmQADRENEEVGQKLSLRYV--- 915
Cdd:PRK05850   224 LGVCAPIL-GGCPAVLTSPVAflQRPARWMQLLASN--------PHAFsaapnfaFEL-AVRKTSDDDMAGLDLGGVlgi 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  916 VFGGEALE---LSRLEDWYSRHpHNAPKVIN-MYGITETTVHVSYIELDESIVSLR------------------ANSLIG 973
Cdd:PRK05850   294 ISGSERVHpatLKRFADRFAPF-NLRETAIRpSYGLAEATVYVATREPGQPPESVRfdyeklsaghakrcetggGTPLVS 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  974 CSIPDLK-VYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERF---IADPF-GKPGTRMYRTGDLArWRQDGT 1047
Cdd:PRK05850   373 YGSPRSPtVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSpGTPEGPWLRTGDLG-FISEGE 451


                   ....*.
gi 1698252301 1048 LDYIGR 1053
Cdd:PRK05850   452 LFIVGR 457
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
654-1150 7.65e-23

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 104.69  E-value: 7.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  654 HINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAgyLPLDPDYpSDRIS 733
Cdd:PRK10946    34 HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALF-SHQRS 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  734 FMLHDAK---PSCVLTN------------SSVEIECDESLKILVDDVNVMEEIEKYSEENIDEMECLkPLAPSHIAYVIY 798
Cdd:PRK10946   111 ELNAYASqiePALLIADrqhalfsdddflNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFTAT-PSPADEVAFFQL 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKgvMIP--HQNVVRLLGATDHWFQFDADdvwTMF-------HSYAFdfSVWEIWGPLLYGGRLVVVPhtvSR 869
Cdd:PRK10946   190 SGGSTGTPK--LIPrtHNDYYYSVRRSVEICGFTPQ---TRYlcalpaaHNYPM--SSPGALGVFLAGGTVVLAP---DP 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGealelSRLEDWYSRHphnAPKVIN-----M 944
Cdd:PRK10946   260 SATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGG-----ARLSETLARR---IPAELGcqlqqV 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  945 YGITETTVhvSYIELDESivSLRANSLIGCSI-PDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIA 1023
Cdd:PRK10946   332 FGMAEGLV--NYTRLDDS--DERIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDA 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1024 DPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVRED-QPGDKRlVAYIV 1102
Cdd:PRK10946   408 NGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDeLMGEKS-CAFLV 479

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1698252301 1103 AsnNETIDTNEMRQHASG-SLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK10946   480 V--KEPLKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1-78 8.78e-23

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: 103.96  E-value: 8.78e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17651    414 LARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1-77 1.37e-22

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: 102.77  E-value: 1.37e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd17643    374 LATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 206-611 1.84e-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: 101.61  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  206 LVIRMNGILNRQALQGAFYDVVEKHETLRT-IFPNVLGSSYQKILDmenlnlEMVITNTCKDELESVLSEAVRYSFNLDf 284
Cdd:cd19545     26 RVFELPPDIDLARLQAAWEQVVQANPILRTrIVQSDSGGLLQVVVK------ESPISWTESTSLDEYLEEDRAAPMGLG- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  285 EPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCqgdrvqlETLPVQYADYalwqQQLLGDETTPES 364
Cdd:cd19545     99 GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEP-------VPQPPPFSRF----VKYLRQLDDEAA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  365 listqLDFWKEELKGLPDQM--ELPTDYQRPVETSYRgeTIHFHIDEGMHSrlvelgrknGVSLFMVLQAGLSALFTRLG 442
Cdd:cd19545    168 -----AEFWRSYLAGLDPAVfpPLPSSRYQPRPDATL--EHSISLPSSASS---------GVTLATVLRAAWALVLSRYT 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  443 AGTDIPIGSPIAGRN---DDVLsDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVNLAAyenqdVPFE----RLVEVLNP 515
Cdd:cd19545    232 GSDDVVFGVTLSGRNapvPGIE-QIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM-----IPFEhtglQNIRRLGP 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  516 vRTRnSHPLFQVMLAFQNTPEATfNAPDLEASLEIQSVGSAKFD---LTFEIsesnEVDGTPNGLHGLleFSTDLYKRET 592
Cdd:cd19545    306 -DAR-AACNFQTLLVVQPALPSS-TSESLELGIEEESEDLEDFSsygLTLEC----QLSGSGLRVRAR--YDSSVISEEQ 376

                          410
                   ....*....|....*....
gi 1698252301  593 VQKLIERFILLLDDAATNP 611
Cdd:cd19545    377 VERLLDQFEHVLQQLASAP 395
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 669-1150 2.00e-22

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 103.75  E-value: 2.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAK-GVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSC---- 743
Cdd:PRK12492    50 LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAlvyl 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  744 ---------VLTNSSVE--IECD-----------------ESLKILVDDVNVMEEIEKYSEENIDEMECLKPLAPSH--I 793
Cdd:PRK12492   130 nmfgklvqeVLPDTGIEylIEAKmgdllpaakgwlvntvvDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLddI 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  794 AYVIYTSGSTGRPKGVMIPHQNVV----------RLLGATDHWFQFDADDVWT----MFHSYAFDFSVWEIwgpLLYGGR 859
Cdd:PRK12492   210 AVLQYTGGTTGLAKGAMLTHGNLVanmlqvraclSQLGPDGQPLMKEGQEVMIaplpLYHIYAFTANCMCM---MVSGNH 286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  860 LVVVphTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMqadreNEEVGQKL---SLRYVVFGGEALELSRLEDWYSRhph 936
Cdd:PRK12492   287 NVLI--TNPRDIPGFIKELGKWRFSALLGLNTLFVALM-----DHPGFKDLdfsALKLTNSGGTALVKATAERWEQL--- 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  937 NAPKVINMYGITETTVHVS---YIELDesivslRANSlIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGR 1013
Cdd:PRK12492   357 TGCTIVEGYGLTETSPVAStnpYGELA------RLGT-VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQ 429

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1014 AGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQP 1092
Cdd:PRK12492   430 PEATAEALDAEGW-------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIgVPDERS 502

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1093 GDKrlVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK12492   503 GEA--VKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 795-1150 1.24e-21

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: 100.14  E-value: 1.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  795 YVIYTSGSTGRPKGVMIPH-----QNVVRLLGATDHWFQFDadDVW----TMFHSYAFDFSVweiwGPLLYGGRLVVVPH 865
Cdd:cd05929    129 KMLYSGGTTGRPKGIKRGLpggppDNDTLMAAALGFGPGAD--SVYlspaPLYHAAPFRWSM----TALFMGGTLVLMEK 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  866 TvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLM---QADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRHPhnaPKVI 942
Cdd:cd05929    203 F---DPEEFLRLIERYRVTFAQFVPTMFVRLLklpEAVRNAYDLS---SLKRVIHAAAPCPPWVKEQWIDWGG---PIIW 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  943 NMYGITETtVHVSYIELDESivsLRANSLIGCSIPDlKVYVLDNYLQPVPPGVVGEMYVAGAGlARGYLGRAGLTAERFI 1022
Cdd:cd05929    274 EYYGGTEG-QGLTIINGEEW---LTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARN 347

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1023 ADPFgkpgtrmyRT-GDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYI 1101
Cdd:cd05929    348 EGGW--------STlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV 419

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1102 ---VASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05929    420 qpaPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 179-600 1.34e-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: 99.63  E-value: 1.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  179 EVPLSFAQRrlWFLN-CLEGPSPtYNIPLVIRMNGILNRQALQGAFYDVVEKHETLRTIFPNVLGSSYQKILDMENLN-- 255
Cdd:cd19534      1 EVPLTPIQR--WFFEqNLAGRHH-FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELfr 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  256 LEM--VITNTCKDELESVLSEAVRySFNLDFEPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYKARCQG 333
Cdd:cd19534     78 LEVvdLSSLAQAAAIEALAAEAQS-SLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  334 DRVQLETLPvQYADYALWQQQLLGDETTpesliSTQLDFWKEELKglPDQMELPTDYQRPVETSyrgETIHFHIDEGMHS 413
Cdd:cd19534    157 EPIPLPSKT-SFQTWAELLAEYAQSPAL-----LEELAYWRELPA--ADYWGLPKDPEQTYGDA---RTVSFTLDEEETE 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  414 RLveLGRKNGvslfmVLQAG-----LSALFTRLGAGTDipiGSPIA------GRNDDV----LSDIVGLFvnT----LVL 474
Cdd:cd19534    226 AL--LQEANA-----AYRTEindllLAALALAFQDWTG---RAPPAifleghGREEIDpgldLSRTVGWF--TsmypVVL 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  475 RTNTSGDPSfkELLNRVKQvNLAAYENQDVPFERLvevlnpvrtRNSHPLFQVMLAFQNTPEATFN------APDLEASL 548
Cdd:cd19534    294 DLEASEDLG--DTLKRVKE-QLRRIPNKGIGYGIL---------RYLTPEGTKRLAFHPQPEISFNylgqfdQGERDDAL 361

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  549 EIQSVGSAKFDLT--------FEISESNEvDGTpngLHGLLEFSTDLYKRETVQKLIERF 600
Cdd:cd19534    362 FVSAVGGGGSDIGpdtprfalLDINAVVE-GGQ---LVITVSYSRNMYHEETIQQLADSY 417
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 635-1149 1.78e-21

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 100.97  E-value: 1.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  635 GGFQIAPEMTLPQLFEKQAHINPNSIAVVFED---------KKLTYEKLNRKANKI-ARflIAKGVGPDQLVALAMPRSL 704
Cdd:PRK12476    26 GNIALPPGTTLISLIERNIANVGDTVAYRYLDhshsaagcaVELTWTQLGVRLRAVgAR--LQQVAGPGDRVAILAPQGI 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  705 NMVVSLLAVLKAGAGYLPL-DPDYP--SDRISFMLHDAKPSCVLTNSSVEIECDESLK----------ILVDDVnvmeei 771
Cdd:PRK12476   104 DYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFLRnlprlrrprvIAIDAI------ 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  772 ekysEENIDEMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQ----NVVRLLGATDhWFQFDADDV-W-TMFHsyafDF 845
Cdd:PRK12476   178 ----PDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRavgtNLVQMILSID-LLDRNTHGVsWlPLYH----DM 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  846 SVWEIWGPLLYGGRLVVV-PHTVSRSPKEFLQLLVKEKVT--VLNQTPSAFYQLmQADRENEEVGQKLSLRYVVF--GGE 920
Cdd:PRK12476   249 GLSMIGFPAVYGGHSTLMsPTAFVRRPQRWIKALSEGSRTgrVVTAAPNFAYEW-AAQRGLPAEGDDIDLSNVVLiiGSE 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  921 ALELSRLEDWYSRH-PHNAPK--VINMYGITETTVHVSYIELDE--SIVSL------------------RANSLIGCSIP 977
Cdd:PRK12476   328 PVSIDAVTTFNKAFaPYGLPRtaFKPSYGIAEATLFVATIAPDAepSVVYLdreqlgagravrvaadapNAVAHVSCGQV 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  978 ---DLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIAD-----PFGK------PGTRMYRTGDLARWR 1043
Cdd:PRK12476   408 arsQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKlqsrlAEGShadgaaDDGTWLRTGDLGVYL 487

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1044 qDGTLDYIGRADHQIKIRGFRIELGEIEAVimkhdkVEQVAVIVREDQ------PGDKRLVAYIVASNN----------- 1106
Cdd:PRK12476   488 -DGELYITGRIADLIVIDGRNHYPQDIEAT------VAEASPMVRRGYvtaftvPAEDNERLVIVAERAagtsradpapa 560

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1698252301 1107 -ETIDTNEMRQHAsgslpdymVPYA---FVVVNELPLTPNGKLDRKA 1149
Cdd:PRK12476   561 iDAIRAAVSRRHG--------LAVAdvrLVPAGAIPRTTSGKLARRA 599
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 639-1150 3.03e-21

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 99.67  E-value: 3.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  639 IAPEMTLPQLFEKQAHINPNSIAVV--FEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKA 716
Cdd:PLN02330    24 VPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  717 GAGYLPLDPDYPSDRISFMLHDAKPSCVLTNSS-----------VEIECDESLKILVDDVNVMEEIEKYSEENIDEmECL 785
Cdd:PLN02330   104 GGVFSGANPTALESEIKKQAEAAGAKLIVTNDTnygkvkglglpVIVLGEEKIEGAVNWKELLEAADRAGDTSDNE-EIL 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  786 KplapSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGAT------DHWFQFDADDVWTMFHSYAFdfsVWEIWGPLLYGGR 859
Cdd:PLN02330   183 Q----TDLCALPFSSGTTGISKGVMLTHRNLVANLCSSlfsvgpEMIGQVVTLGLIPFFHIYGI---TGICCATLRNKGK 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  860 LVVVPHTVSRSpkeFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPhnAP 939
Cdd:PLN02330   256 VVVMSRFELRT---FLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFP--GV 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  940 KVINMYGITE-TTVHVSYIELDESIVSLRANSlIGCSIPDLKVYVLD-NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLT 1017
Cdd:PLN02330   331 QVQEAYGLTEhSCITLTHGDPEKGHGIAKKNS-VGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET 409

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1018 AERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRL 1097
Cdd:PLN02330   410 DRTIDEDGW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIP 482

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1098 VAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PLN02330   483 AACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1-77 4.55e-21

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: 98.52  E-value: 4.55e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRpNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd12116    395 LAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 792-1147 2.60e-20

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: 93.62  E-value: 2.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  792 HIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVW----TMFHSYAfdfsvweIWGPL--LYGGRLVVVPH 865
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAIlapgPLSHSLF-------LYGAIsaLYLGGTFIGQR 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  866 TVSrsPKEFLQLLVKEKVTVLNQTPSAFYQLMqadRENEEVgqkLSLRYVVFGGEALELSRLEDWYSRHPHnaPKVINMY 945
Cdd:cd17633     74 KFN--PKSWIRKINQYNATVIYLVPTMLQALA---RTLEPE---SKIKSIFSSGQKLFESTKKKLKNIFPK--ANLIEFY 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  946 GITETTvHVSYIELDESivsLRANSlIGCSIPDLKVYVLDNylqpvPPGVVGEMYVAGAGLARGYLGRAGLTAerfiadp 1025
Cdd:cd17633    144 GTSELS-FITYNFNQES---RPPNS-VGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNP------- 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1026 fgkpgTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsn 1105
Cdd:cd17633    207 -----DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG-- 279

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1698252301 1106 nETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:cd17633    280 -DKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 650-1150 3.38e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 96.30  E-value: 3.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  650 EKQAHINPNSIAVVF--EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDY 727
Cdd:PRK13391     4 GIHAQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  728 PSDRISFMLHDAKPSCVLTNSSVEIECDESLK--------ILVDDVNVMEEIEKYSEenidemeCLKPLAPSHIA----- 794
Cdd:PRK13391    84 TPAEAAYIVDDSGARALITSAAKLDVARALLKqcpgvrhrLVLDGDGELEGFVGYAE-------AVAGLPATPIAdeslg 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  795 -YVIYTSGSTGRPKGVM--IPHQNVVRLLGATD---HWFQFDADDVW----TMFHSyafdfsvweiwGPLLY-------G 857
Cdd:PRK13391   157 tDMLYSSGTTGRPKGIKrpLPEQPPDTPLPLTAflqRLWGFRSDMVYlspaPLYHS-----------APQRAvmlvirlG 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  858 GRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMqadRENEEVGQKL---SLRYVVFGGE---ALELSRLEDWY 931
Cdd:PRK13391   226 GTVIVMEHF---DAEQYLALIEEYGVTHTQLVPTMFSRML---KLPEEVRDKYdlsSLEVAIHAAApcpPQVKEQMIDWW 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  932 srhphnAPKVINMYGITE---TTVHVSYIELDESIVSLRAnsLIGcsipdlKVYVLDNYLQPVPPGVVGEMYVAGaGLAR 1008
Cdd:PRK13391   300 ------GPIIHEYYAATEglgFTACDSEEWLAHPGTVGRA--MFG------DLHILDDDGAELPPGEPGTIWFEG-GRPF 364

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1009 GYLGRAGLTAERFIADPfgkpgtRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-V 1087
Cdd:PRK13391   365 EYLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFgV 438

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1088 REDQPGDkrlVAYIVASNNETIDTN-----EMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK13391   439 PNEDLGE---EVKAVVQPVDGVDPGpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1-77 5.56e-20

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: 94.69  E-value: 5.56e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd12115    371 LRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 777-1152 5.83e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 95.48  E-value: 5.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  777 ENIDEMECLKPLA---PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDV----WTMFHSYAfdfsVWE 849
Cdd:PRK13388   133 ELVAAAGALTPHRevdAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVcyvsMPLFHSNA----VMA 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  850 IWGPLLYGGRLVVVPHTVSRSpkEFLQLLVKEKVTVLNQTPSAFYQLMQA-----DRENeevgqklSLRyVVFGGEALEL 924
Cdd:PRK13388   209 GWAPAVASGAAVALPAKFSAS--GFLDDVRRYGATYFNYVGKPLAYILATperpdDADN-------PLR-VAFGNEASPR 278

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  925 SRLEdwYSRHphNAPKVINMYGITETTVhvsyieldesIVSLRAN---SLIGCSIPDLKVYVLDNyLQPVPPGV------ 995
Cdd:PRK13388   279 DIAE--FSRR--FGCQVEDGYGSSEGAV----------IVVREPGtppGSIGRGAPGVAIYNPET-LTECAVARfdahga 343

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  996 -------VGEMY-VAGAGLARGYLGRAGLTAERFiadpfgKPGtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIEL 1067
Cdd:PRK13388   344 llnadeaIGELVnTAGAGFFEGYYNNPEATAERM------RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSA 415

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1068 GEIEAVIMKHDKVEQVAVI-VREDQPGDKrLVAYIVASNNETIDTNEMRQ--HASGSLPDYMVPYAFVVVNELPLTPNGK 1144
Cdd:PRK13388   416 APIERILLRHPAINRVAVYaVPDERVGDQ-VMAALVLRDGATFDPDAFAAflAAQPDLGTKAWPRYVRIAADLPSTATNK 494


                   ....*...
gi 1698252301 1145 LDRKALPA 1152
Cdd:PRK13388   495 VLKRELIA 502
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1-78 6.60e-20

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: 94.85  E-value: 6.60e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKepINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17656    404 LLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQE--LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1-77 9.84e-20

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: 94.07  E-value: 9.84e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKepINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd17650    373 LARHPAIDEAVVAVREDKGGEARLCAYVVAAAT--LNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 787-1149 3.51e-19

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 93.14  E-value: 3.51e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  787 PLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDAD-DV---W-TMFHSYAFdfsVWEIWGPLLYGGRLV 861
Cdd:PRK07768   148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVmvsWlPLFHDMGM---VGFLTVPMYFGAELV 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VV-PHTVSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQ-KLS-LRYVVFGGEALELSRLEDWY---SRHP 935
Cdd:PRK07768   225 KVtPMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKPGAfDLSsLRFALNGAEPIDPADVEDLLdagARFG 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  936 HNAPKVINMYGITETTVHVSYIELDESIV---------------------SLRANSLIGCSIPDLKVYVLDNYLQPVPPG 994
Cdd:PRK07768   305 LRPEAILPAYGMAEATLAVSFSPCGAGLVvdevdadllaalrravpatkgNTRRLATLGPPLPGLEVRVVDEDGQVLPPR 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  995 VVGEMYVAGAGLARGYlgragLTAERFIA--DPFGkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEA 1072
Cdd:PRK07768   385 GVGVIELRGESVTPGY-----LTMDGFIPaqDADG-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIER 454

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1073 VIMkhdKVEQV----AVIVREDQPGDKRLVAYIVASNN--ETIDTNEMRQ---HASGSLPDyMVPYAFVVV--NELPLTP 1141
Cdd:PRK07768   455 AAA---RVEGVrpgnAVAVRLDAGHSREGFAVAVESNAfeDPAEVRRIRHqvaHEVVAEVG-VRPRNVVVLgpGSIPKTP 530


                   ....*...
gi 1698252301 1142 NGKLDRKA 1149
Cdd:PRK07768   531 SGKLRRAN 538
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1-77 7.99e-19

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: 91.57  E-value: 7.99e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIV-AEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd17646    411 LAAHPAVTHAVVVARAAPAGAARLVGYVVpAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1-77 4.06e-18

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: 89.23  E-value: 4.06e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEE-KEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05945    372 LRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 668-1150 4.56e-18

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


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 89.06  E-value: 4.56e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  668 KLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPscvltn 747
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP------ 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  748 ssveiecDESLKIlvddvnvmeeiekyseenidemeclkPLApSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWF 827
Cdd:cd05910     76 -------DAFIGI--------------------------PKA-DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  828 QFDADDVwtmfhsyafD---FSVWEIWGPLLygGRLVVVP---HT--VSRSPKEFLQLLVKEKVTVLNQTPSAFYQLMqa 899
Cdd:cd05910    122 GIRPGEV---------DlatFPLFALFGPAL--GLTSVIPdmdPTrpARADPQKLVGAIRQYGVSIVFGSPALLERVA-- 188

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  900 dRENEEVGQKL-SLRYVVFGGEALELSRLEDwYSRHPHNAPKVINMYGITEtTVHVSYIELDESIVSLR------ANSLI 972
Cdd:cd05910    189 -RYCAQHGITLpSLRRVLSAGAPVPIALAAR-LRKMLSDEAEILTPYGATE-ALPVSSIGSRELLATTTaatsggAGTCV 265

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  973 GCSIPDLKVYVL----------DNYLQpVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPfgkPGTRMYRTGDLARW 1042
Cdd:cd05910    266 GRPIPGVRVRIIeiddepiaewDDTLE-LPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYL 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1043 RQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAvIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSL 1122
Cdd:cd05910    342 DDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA-LVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALA 420

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1698252301 1123 PDYMVPY---AFVVVNELPLTP--NGKLDRKAL 1150
Cdd:cd05910    421 KDYPHTQrigRFLIHPSFPVDIrhNAKIFREKL 453
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 789-1152 1.02e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 88.58  E-value: 1.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 APSHIAYVIYTSGSTGRPKGVMIPHQNVV---RLLgaTDHwFQFDADDV----WTMFHSYAfdfsVWEIWGPLLYGGRLV 861
Cdd:PRK07867   150 DPDDLFMLIFTSGTSGDPKAVRCTHRKVAsagVML--AQR-FGLGPDDVcyvsMPLFHSNA----VMAGWAVALAAGASI 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VVPHTVSRSpkEFLQLLVKEKVTVLNQTPSAFYQLMQA-----DRENeevgqklSLRyVVFGGEAL--ELSRLEDWYSRH 934
Cdd:PRK07867   223 ALRRKFSAS--GFLPDVRRYGATYANYVGKPLSYVLATperpdDADN-------PLR-IVYGNEGApgDIARFARRFGCV 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  935 phnapkVINMYGITETTVHVSYIEldesivSLRANSLiGCSIPDLKVYVLDNyLQPVPPGV------------VGEMY-V 1001
Cdd:PRK07867   293 ------VVDGFGSTEGGVAITRTP------DTPPGAL-GPLPPGVAIVDPDT-GTECPPAEdadgrllnadeaIGELVnT 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1002 AGAGLARGYLGRAGLTAERfIADPfgkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVE 1081
Cdd:PRK07867   359 AGPGGFEGYYNDPEADAER-MRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301 1082 QVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQ--HASGSLPDYMVPyAFV-VVNELPLTPNGKLDRKALPA 1152
Cdd:PRK07867   431 EVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEflAAQPDLGPKQWP-SYVrVCAELPRTATFKVLKRQLSA 503
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 790-1077 1.03e-17

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


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 88.72  E-value: 1.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVWTM----FHSYAFD----FsvweiwgPLLYGgrLV 861
Cdd:PRK06334   182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSflppFHAYGFNsctlF-------PLLSG--VP 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  862 VVPHTVSRSPKEFLQLLVKEKVTVLNQTPSAF-YQLMQADRENEEVGqklSLRYVVFGGEALELSRLEDWYSRHPHNAPK 940
Cdd:PRK06334   253 VVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFdYILKTAKKQESCLP---SLRFVVIGGDAFKDSLYQEALKTFPHIQLR 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  941 viNMYGITETTVHVSYIELDesivSLRANSLIGCSIPDLKVYVLDNYLQ-PVPPGVVGEMYVAGAGLARGYLGragltae 1019
Cdd:PRK06334   330 --QGYGTTECSPVITINTVN----SPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLG------- 396

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1020 rfiADP----FGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKH 1077
Cdd:PRK06334   397 ---EDFgqgfVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
PRK08315 PRK08315
AMP-binding domain protein; Validated
 642-1144 1.22e-17

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 88.33  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  642 EMTLPQLFEKQAHINPNSIAVVFEDK--KLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAG 719
Cdd:PRK08315    15 EQTIGQLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  720 YLPLDPDYPSDRISFMLHDAKPSCVLTNSS------VEI------ECDES------------LK--ILVDDVN------- 766
Cdd:PRK08315    95 LVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyVAMlyelapELATCepgqlqsarlpeLRrvIFLGDEKhpgmlnf 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  767 --VMEEIEKYSEENIDE-MECLKPLAPSHIAYviyTSGSTGRPKGVMIPHQNVV---RLLGATdhwFQFDADD-----Vw 835
Cdd:PRK08315   175 deLLALGRAVDDAELAArQATLDPDDPINIQY---TSGTTGFPKGATLTHRNILnngYFIGEA---MKLTEEDrlcipV- 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  836 TMFHSYafdfsvweiwGPLLygGRLVVVPH---TV----SRSPKEFLQLLVKEKVTVLNQTPSAFY-QLMQADRENEEVG 907
Cdd:PRK08315   248 PLYHCF----------GMVL--GNLACVTHgatMVypgeGFDPLATLAAVEEERCTALYGVPTMFIaELDHPDFARFDLS 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  908 qklSLRYVVFGGEA--LELSRledwysrhphnapKVI---NM------YGITETTvHVSYI-ELDESIvSLRANSlIGCS 975
Cdd:PRK08315   316 ---SLRTGIMAGSPcpIEVMK-------------RVIdkmHMsevtiaYGMTETS-PVSTQtRTDDPL-EKRVTT-VGRA 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  976 IPDLKVYVLDNYL-QPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrMyRTGDLARWRQDGTLDYIGRa 1054
Cdd:PRK08315   377 LPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW------M-HTGDLAVMDEEGYVNIVGR- 448

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 dhqIK---IRGfrielGE------IEAVIMKHDKVEQVAVIvredqpG--DKR----LVAYIVASNNETIDTNEMRQHAS 1119
Cdd:PRK08315   449 ---IKdmiIRG-----GEniypreIEEFLYTHPKIQDVQVV------GvpDEKygeeVCAWIILRPGATLTEEDVRDFCR 514

                          570       580
                   ....*....|....*....|....*
gi 1698252301 1120 GSLPDYMVPYAFVVVNELPLTPNGK 1144
Cdd:PRK08315   515 GKIAHYKIPRYIRFVDEFPMTVTGK 539
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 652-1147 1.23e-17

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 88.32  E-value: 1.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  652 QAHI----------NPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYL 721
Cdd:PLN02860     6 QAHIcqcltrlatlRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  722 PLDPDYPSDRISFMLHDAKPSCVLTNSSVEIECDE-------SLK--ILVDDVNVMEEIEKYSEENIDEM--ECLKPL-- 788
Cdd:PLN02860    86 PLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEElqndrlpSLMwqVFLESPSSSVFIFLNSFLTTEMLkqRALGTTel 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  789 ----APSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVwtmfhsYAFDFSVWEIWG------PLLYGG 858
Cdd:PLN02860   166 dyawAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDV------YLHTAPLCHIGGlssalaMLMVGA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  859 RLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELSRLEDWYSRHPhNA 938
Cdd:PLN02860   240 CHVLLPKF---DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFP-NA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  939 pKVINMYGITETTVHVSYIELDESIVSLRANSLIGCSIPdlkvyvldnYLQPVPPGV----------------------V 996
Cdd:PLN02860   316 -KLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQT---------KSSSVHQPQgvcvgkpaphvelkigldessrV 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  997 GEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMK 1076
Cdd:PLN02860   386 GRILTRGPHVMLGYWGQNSETASVLSNDGW-------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQ 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1077 HDKVEQVAVIvredqpG--DKRLVAYIVA----------SNNE--------TIDTNEMRQHAS-GSLPDYMVPYAFVVVN 1135
Cdd:PLN02860   459 HPGVASVVVV------GvpDSRLTEMVVAcvrlrdgwiwSDNEkenakknlTLSSETLRHHCReKNLSRFKIPKLFVQWR 532

                          570
                   ....*....|...
gi 1698252301 1136 E-LPLTPNGKLDR 1147
Cdd:PLN02860   533 KpFPLTTTGKIRR 545
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
793-1150 1.77e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 85.87  E-value: 1.77e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  793 IAYVIYTSGSTGRPKGVMIPHQNVVRLLGATdhwfqfdaddvwtmfHSYafdfsvweIWGPllyGGRLVVVP-HTVSRsp 871
Cdd:PRK07824    37 VALVVATSGTTGTPKGAMLTAAALTASADAT---------------HDR--------LGGP---GQWLLALPaHHIAG-- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  872 kefLQLLVKEKV-----TVLNQT----PSAF------------Y------QLMQADRENEEVGQKLSLRYVVFGGEALEL 924
Cdd:PRK07824    89 ---LQVLVRSVIagsepVELDVSagfdPTALpravaelgggrrYtslvpmQLAKALDDPAATAALAELDAVLVGGGPAPA 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  925 SRLEdwysRHPHNAPKVINMYGITETTVHVSYielDesivslransliGCSIPDLKVYVLDnylqpvppgvvGEMYVAGA 1004
Cdd:PRK07824   166 PVLD----AAAAAGINVVRTYGMSETSGGCVY---D------------GVPLDGVRVRVED-----------GRIALGGP 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1005 GLARGYlgRAGLTAerfiaDPFGKPGtrMYRTGDLARWrQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVA 1084
Cdd:PRK07824   216 TLAKGY--RNPVDP-----DPFAEPG--WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCA 285

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1085 VIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK07824   286 VFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 1028-1154 1.97e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 86.63  E-value: 1.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1028 KPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASnnE 1107
Cdd:PRK08308   287 KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--E 364

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1698252301 1108 TIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPAPE 1154
Cdd:PRK08308   365 EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
PLN02479 PLN02479
acetate-CoA ligase
 648-1152 3.66e-17

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 86.82  E-value: 3.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  648 LFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDY 727
Cdd:PLN02479    25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  728 PSDRISFMLHDAKPSCVLTNSSVEIECDESLKILVDDVN---------VME------------------EIEKYSEENID 780
Cdd:PLN02479   105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKssfkpplliVIGdptcdpkslqyalgkgaiEYEKFLETGDP 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  781 EMECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQN--VVRLLGATDHWFQFDADDVWT--MFHSYAFDFSvweiWGPLLY 856
Cdd:PLN02479   185 EFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGayLMALSNALIWGMNEGAVYLWTlpMFHCNGWCFT----WTLAAL 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  857 GGRLVVVPHTvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADREnEEVGQKLSLRYVVFGGEALELSRLedwySRHPH 936
Cdd:PLN02479   261 CGTNICLRQV---TAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKS-ETILPLPRVVHVMTAGAAPPPSVL----FAMSE 332

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  937 NAPKVINMYGITET----TVHVSYIELDESIVSLRAN----------SLIGCSIPDLKVyvldnyLQPVPP--GVVGEMY 1000
Cdd:PLN02479   333 KGFRVTHTYGLSETygpsTVCAWKPEWDSLPPEEQARlnarqgvryiGLEGLDVVDTKT------MKPVPAdgKTMGEIV 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1001 VAGAGLARGYLGRAGLTAERFiadpfgkpGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKV 1080
Cdd:PLN02479   407 MRGNMVMKGYLKNPKANEEAF--------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301 1081 EQVAVIVREDQPGDKRLVAYI-----VASNNETIDTNEMRQHASGSLPDYMVPYAfVVVNELPLTPNGKLDRKALPA 1152
Cdd:PLN02479   479 LEASVVARPDERWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVLRA 554
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 669-1150 3.78e-17

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: 86.50  E-value: 3.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGagyLPLDPDYPS---DRISFMLHDAKPSCVL 745
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYATlgeDALIHSLNETECSAIF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  746 TNSSveiecdeslkilvddvnvmeeiekyseenidemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQNVVR-LLGATD 824
Cdd:cd17639     83 TDGK----------------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGD 122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  825 HWFQF-DADDVWTMF----HSYAFDF-SVWEIWGPLL-YGGRLVVVPHTVSRSPKEFLQL---------LVKEKV--TVL 886
Cdd:cd17639    123 RVPELlGPDDRYLAYlplaHIFELAAeNVCLYRGGTIgYGSPRTLTDKSKRGCKGDLTEFkptlmvgvpAIWDTIrkGVL 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  887 NQTPSA-------FYQLMQADRE-----------NEEVGQKL------SLRYVVFGGEALelsrledwySRHPHN----- 937
Cdd:cd17639    203 AKLNPMgglkrtlFWTAYQSKLKalkegpgtpllDELVFKKVraalggRLRYMLSGGAPL---------SADTQEflniv 273

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  938 -APkVINMYGITETTVHVSYIELDESIVSlRANSLIGC------SIPDLKvYVLDNylqPVPPGvvgEMYVAGAGLARGY 1010
Cdd:cd17639    274 lCP-VIQGYGLTETCAGGTVQDPGDLETG-RVGPPLPCceiklvDWEEGG-YSTDK---PPPRG---EILIRGPNVFKGY 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1011 LGRAGLTAERFIADpfgkpgtRMYRTGDLARWRQDGTLDYIGRADHQIKIR-GFRIELGEIEAVIMKHDKVEQVAVIVRE 1089
Cdd:cd17639    345 YKNPEKTKEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADP 417

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1090 DQ--------PGDKRLVAYIVASNNETID--------------TNEMRQHA-SGSLPDYMVPYAFVVVNElPLTP-NG-- 1143
Cdd:cd17639    418 DKsypvaivvPNEKHLTKLAEKHGVINSEweelcedkklqkavLKSLAETArAAGLEKFEIPQGVVLLDE-EWTPeNGlv 496

                          570
                   ....*....|.
gi 1698252301 1144 ----KLDRKAL 1150
Cdd:cd17639    497 taaqKLKRKEI 507
PRK09274 PRK09274
peptide synthase; Provisional
 653-1095 3.97e-17

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 86.88  E-value: 3.97e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDKK----------LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLP 722
Cdd:PRK09274    16 AQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  723 LDPDYPSDRISFMLHDAKPSCVLTN--------------SSVEiecdesLKILVDD-----VNVMEEIEKYSEENIDEME 783
Cdd:PRK09274    96 VDPGMGIKNLKQCLAEAQPDAFIGIpkahlarrlfgwgkPSVR------RLVTVGGrllwgGTTLATLLRDGAAAPFPMA 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  784 CLKPLAPshiAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDVwtmfhsyafD---FSVWEIWGPLLyGGRL 860
Cdd:PRK09274   170 DLAPDDM---AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI---------DlptFPLFALFGPAL-GMTS 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  861 VVVPHTVSR----SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENeevGQKL-SLRYVVFGGEALELSRLEDWYSRHP 935
Cdd:PRK09274   237 VIPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEAN---GIKLpSLRRVISAGAPVPIAVIERFRAMLP 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  936 HNAPkVINMYGITEtTVHVSYIELDESIVSLRANS------LIGCSIPDLKVYVL---DNYL------QPVPPGVVGEMY 1000
Cdd:PRK09274   314 PDAE-ILTPYGATE-ALPISSIESREILFATRAATdngagiCVGRPVDGVEVRIIaisDAPIpewddaLRLATGEIGEIV 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1001 VAGAGLARGYLGRAGLTAERFIADPFGkpGTRmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKV 1080
Cdd:PRK09274   392 VAGPMVTRSYYNRPEATRLAKIPDGQG--DVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468

                          490       500
                   ....*....|....*....|....*..
gi 1698252301 1081 ------------EQVAVIVREDQPGDK 1095
Cdd:PRK09274   469 krsalvgvgvpgAQRPVLCVELEPGVA 495
prpE PRK10524
propionyl-CoA synthetase; Provisional
 657-1152 5.52e-17

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 86.54  E-value: 5.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  657 PNSIAVVF------EDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSD 730
Cdd:PRK10524    67 PEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASH 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  731 RISFMLHDAKPSCVLTNSS-------VEIEC--DESLK---------ILVD------------DVNVMEEIEKYSEENId 780
Cdd:PRK10524   147 SLAARIDDAKPVLIVSADAgsrggkvVPYKPllDEAIAlaqhkprhvLLVDrglapmarvagrDVDYATLRAQHLGARV- 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  781 emeclkP---LAPSHIAYVIYTSGSTGRPKGVmiphQN-----VVRLLGATDHWFQ-------FDADDV-WTMFHSYAfd 844
Cdd:PRK10524   226 ------PvewLESNEPSYILYTSGTTGKPKGV----QRdtggyAVALATSMDTIFGgkagetfFCASDIgWVVGHSYI-- 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  845 fsvweIWGPLLYGGRLVVVPHTVSR-SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALE 923
Cdd:PRK10524   294 -----VYAPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLD 368

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  924 LSRLEdWYSRHPhNAPkVINMYGITET----TVHVSYIELDESivslRANSligcsiPDLKVYVLDNYL------QPVPP 993
Cdd:PRK10524   369 EPTAS-WISEAL-GVP-VIDNYWQTETgwpiLAIARGVEDRPT----RLGS------PGVPMYGYNVKLlnevtgEPCGP 435

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  994 GVVGeMYVAGAGLARGYLGRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAV 1073
Cdd:PRK10524   436 NEKG-VLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEES 514

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1074 IMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMV--------PYAFVVVNELPLTPNGKL 1145
Cdd:PRK10524   515 ISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKEIMALVDsqlgavarPARVWFVSALPKTRSGKL 594


                   ....*..
gi 1698252301 1146 DRKALPA 1152
Cdd:PRK10524   595 LRRAIQA 601
PLN02246 PLN02246
4-coumarate--CoA ligase
 667-1152 6.08e-17

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 86.19  E-value: 6.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  667 KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLT 746
Cdd:PLN02246    49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 NSSV-----EIECDESLKILVDDVNVmEEIEKYSE-ENIDEMECLKP-LAPSHIAYVIYTSGSTGRPKGVMIPHQNVV-- 817
Cdd:PLN02246   129 QSCYvdklkGLAEDDGVTVVTIDDPP-EGCLHFSElTQADENELPEVeISPDDVVALPYSSGTTGLPKGVMLTHKGLVts 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  818 ---RLLGATDHwFQFDADD----VWTMFHSYAFDfSVweiwgpLLYGGRlvvVPHTVSRSPK----EFLQLLVKEKVTVL 886
Cdd:PLN02246   208 vaqQVDGENPN-LYFHSDDvilcVLPMFHIYSLN-SV------LLCGLR---VGAAILIMPKfeigALLELIQRHKVTIA 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  887 NQTPSafyqLMQADRENEEVGQK--LSLRYVVFGGEALElSRLEDWYSRHPHNApKVINMYGITET-------------- 950
Cdd:PLN02246   277 PFVPP----IVLAIAKSPVVEKYdlSSIRMVLSGAAPLG-KELEDAFRAKLPNA-VLGQGYGMTEAgpvlamclafakep 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  951 ---------TVhVSYIELdeSIVSLRAnsliGCSIPdlkvyvldnYLQPvppgvvGEMYVAGAGLARGYLGRAGLTAERF 1021
Cdd:PLN02246   351 fpvksgscgTV-VRNAEL--KIVDPET----GASLP---------RNQP------GEICIRGPQIMKGYLNDPEATANTI 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1022 IADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYI 1101
Cdd:PLN02246   409 DKDGW-------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1102 VASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:PLN02246   482 VRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1-78 9.36e-17

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: 84.91  E-value: 9.36e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPInlSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17645    365 LMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH--EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1069-1144 1.55e-16

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: 75.66  E-value: 1.55e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1069 EIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGK 1144
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 799-1090 1.88e-16

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


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 83.66  E-value: 1.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  799 TSGSTGRPKGVM-------IPHQNVVRLLgatdHWFQFDADDVwtMFHSYAFDFSVweiWGPLLYGG--RL--VVVPHTV 867
Cdd:COG1541     91 SSGTTGKPTVVGytrkdldRWAELFARSL----RAAGVRPGDR--VQNAFGYGLFT---GGLGLHYGaeRLgaTVIPAGG 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  868 SRSPKEfLQLLVKEKVTVLNQTPS-AFYQLMQADRENEEVgQKLSLRYVVFGGEAL--EL-SRLEDWYsrhphNApKVIN 943
Cdd:COG1541    162 GNTERQ-LRLMQDFGPTVLVGTPSyLLYLAEVAEEEGIDP-RDLSLKKGIFGGEPWseEMrKEIEERW-----GI-KAYD 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  944 MYGITETTVHVSYieldESivslRANSliGCSIPDLKVYV--LD-NYLQPVPPGVVGEMYVAGaglargyLGRAGLtaer 1020
Cdd:COG1541    234 IYGLTEVGPGVAY----EC----EAQD--GLHIWEDHFLVeiIDpETGEPVPEGEEGELVVTT-------LTKEAM---- 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1021 fiadpfgkPGTRmYRTGDLARWRQD----GT----LDYI-GRADHQIKIRGFRIELGEIEAVIMKHDKVEQ--VAVIVRE 1089
Cdd:COG1541    293 --------PLIR-YRTGDLTRLLPEpcpcGRthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPeyQIVVDRE 363


                   .
gi 1698252301 1090 D 1090
Cdd:COG1541    364 G 364
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 669-1150 2.14e-16

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: 84.19  E-value: 2.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGV--GPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLt 746
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  747 nssveieCDESLKILVddvnvMEEIEKYSEENIDEmecLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDH- 825
Cdd:cd05927     85 -------CDAGVKVYS-----LEEFEKLGKKNKVP---PPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKi 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  826 ---WFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGR----------------------LVVVPH-----------TVSR 869
Cdd:cd05927    150 leiLNKINPTDVYISYLPLAHIFERVVEALFLYHGAKigfysgdirlllddikalkptvFPGVPRvlnriydkifnKVQA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 SP--KEFL-QLLVKEKVTVLNQ---TPSAFYQLMQADRENEEVGQKlsLRYVVFGGEALELSRLEdwYSRHPHNAPkVIN 943
Cdd:cd05927    230 KGplKRKLfNFALNYKLAELRSgvvRASPFWDKLVFNKIKQALGGN--VRLMLTGSAPLSPEVLE--FLRVALGCP-VLE 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  944 MYGITETTVHVSYIELDESIVslranSLIGCSIPDLKVYVLD----NYLQPVPPGvVGEMYVAGAGLARGYLGRAGLTAE 1019
Cdd:cd05927    305 GYGQTECTAGATLTLPGDTSV-----GHVGGPLPCAEVKLVDvpemNYDAKDPNP-RGEVCIRGPNVFSGYYKDPEKTAE 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1020 RFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKI-RGFRIELGEIEAVIMKHDKVEQ------------VAVI 1086
Cdd:cd05927    379 ALDEDGW-------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQifvygdslksflVAIV 451

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1087 V---------REDQPG----------DKRLVAYIVASNNETIDTN-----EMRQHAsgslpdYMVPYAFVVVNELpLTPN 1142
Cdd:cd05927    452 VpdpdvlkewAASKGGgtgsfeelckNPEVKKAILEDLVRLGKENglkgfEQVKAI------HLEPEPFSVENGL-LTPT 524


                   ....*...
gi 1698252301 1143 GKLDRKAL 1150
Cdd:cd05927    525 FKLKRPQL 532
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 658-1150 2.34e-16

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 84.42  E-value: 2.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  658 NSIAVVFE------DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGA-------GYlplD 724
Cdd:PRK00174    82 DKVAIIWEgddpgdSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAvhsvvfgGF---S 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  725 PDYPSDRISfmlhDAKPSCVLTnssveieCDES--------LKILVDDV--------NVM-------------------- 768
Cdd:PRK00174   159 AEALADRII----DAGAKLVIT-------ADEGvrggkpipLKANVDEAlancpsveKVIvvrrtggdvdwvegrdlwwh 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  769 EEIEKYSEENIDE-MECLKPLapshiaYVIYTSGSTGRPKGVMipHQNVVRLLGA--TDHW-FQFDADDV--------WT 836
Cdd:PRK00174   228 ELVAGASDECEPEpMDAEDPL------FILYTSGSTGKPKGVL--HTTGGYLVYAamTMKYvFDYKDGDVywctadvgWV 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  837 MFHSYAfdfsvweIWGPLLYGGRLVV---VPH--TVSRspkeFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLS 911
Cdd:PRK00174   300 TGHSYI-------VYGPLANGATTLMfegVPNypDPGR----FWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSS 368

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  912 LRyvVFG--GE-----ALElsrledWY------SRHPhnapkVINMYGITETTVHVsyIELDESIVSLRANSligCS--I 976
Cdd:PRK00174   369 LR--LLGsvGEpinpeAWE------WYykvvggERCP-----IVDTWWQTETGGIM--ITPLPGATPLKPGS---ATrpL 430

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDLKVYVLDNYLQPVPPGVVGEMYVAGA--GLARGYLGraglTAERFIADPFGK-PGtrMYRTGDLARWRQDGtldYI-- 1051
Cdd:PRK00174   431 PGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYG----DHERFVKTYFSTfKG--MYFTGDGARRDEDG---YYwi 501

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1052 -GRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETID---TNEMRQHAS---GSL-- 1122
Cdd:PRK00174   502 tGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVRkeiGPIak 581

                          570       580
                   ....*....|....*....|....*...
gi 1698252301 1123 PDYMvpyafVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK00174   582 PDVI-----QFAPGLPKTRSGKIMRRIL 604
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 640-1041 5.10e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 83.56  E-value: 5.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  640 APEMTLPQLFEKQAHINPNSIAVVFED------KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAV 713
Cdd:PRK12582    46 PYPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  714 LKAGAGYLPLDPDYpsdriSFMLHD----------AKPSCVLTNSSVEIEcdESLKIL----VDDVNVMEEIEKYSEENI 779
Cdd:PRK12582   126 MQAGVPAAPVSPAY-----SLMSHDhaklkhlfdlVKPRVVFAQSGAPFA--RALAALdlldVTVVHVTGPGEGIASIAF 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  780 DEMECLKP----------LAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQFDADDV------W-----TMF 838
Cdd:PRK12582   199 ADLAATPPtaavaaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvsldWmpwnhTMG 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  839 HSYAFDFSVWEiwGPLLY--GGRLVvvphtvsrsPKEF---LQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKL--S 911
Cdd:PRK12582   279 GNANFNGLLWG--GGTLYidDGKPL---------PGMFeetIRNLREISPTVYGNVPAGYAMLAEAMEKDDALRRSFfkN 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  912 LRYVVFGGEALElsrlEDWYSRHPHNAPK-------VINMYGITET---TVHVSYIEldesivslRANSLIGCSIPDLKv 981
Cdd:PRK12582   348 LRLMAYGGATLS----DDLYERMQALAVRttghripFYTGYGATETaptTTGTHWDT--------ERVGLIGLPLPGVE- 414

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  982 yvldnyLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLAR 1041
Cdd:PRK12582   415 ------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAAR 461
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1-78 5.16e-16

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: 82.42  E-value: 5.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVmVREDRPNDKRIIAYIVAE--EKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17649    372 LLEHPGVREAAV-VALDGAGGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1164-1235 1.36e-15

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: 72.96  E-value: 1.36e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301 1164 PRTPQEEMLCDLFTEVLSV--SQIGIDDGFF-DLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERLE 1235
Cdd:COG0236      2 PREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLE 76
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 798-1150 1.46e-15

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 81.72  E-value: 1.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  798 YTSGSTGRPKGVMIPHQ-NVVRLLGAT--DHWFQFDAD---DVWTMFH--SYAFDFSvweiwGPLLyGGRLVVvphtvsr 869
Cdd:PRK06018   184 YTSGTTGDPKGVLYSHRsNVLHALMANngDALGTSAADtmlPVVPLFHanSWGIAFS-----APSM-GTKLVM------- 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 sPKEFL------QLLVKEKVTVLNQTPSAFYQLMQADRENeevGQKL-SLRYVVFGGEALELSRL---EDWYSrhphnap 939
Cdd:PRK06018   251 -PGAKLdgasvyELLDTEKVTFTAGVPTVWLMLLQYMEKE---GLKLpHLKMVVCGGSAMPRSMIkafEDMGV------- 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  940 KVINMYGITET----TVHVSYIELDESIVSLRANSLIGCSIP----DLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYL 1011
Cdd:PRK06018   320 EVRHAWGMTEMsplgTLAALKPPFSKLPGDARLDVLQKQGYPpfgvEMKITDDAGKELPWDGKTFGRLKVRGPAVAAAYY 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1012 gRAGltAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQ 1091
Cdd:PRK06018   400 -RVD--GEILDDDGF-------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP 469

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301 1092 PGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK06018   470 KWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PLN02654 PLN02654
acetate-CoA ligase
 656-1086 2.52e-15

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 81.48  E-value: 2.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  656 NPNSIAVVFE------DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:PLN02654   102 NGDKIAIYWEgnepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAKPSCVLTNSSVEIECDE-SLKILVDDVNVMEEIEKYS------EENIDEM---------------ECLKP 787
Cdd:PLN02654   182 ESLAQRIVDCKPKVVITCNAVKRGPKTiNLKDIVDAALDESAKNGVSvgicltYENQLAMkredtkwqegrdvwwQDVVP 261

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  788 LAPSHIA----------YVIYTSGSTGRPKGVMipHQNVVRLL-GATDHWFQFD----------ADDVWTMFHSYAfdfs 846
Cdd:PLN02654   262 NYPTKCEvewvdaedplFLLYTSGSTGKPKGVL--HTTGGYMVyTATTFKYAFDykptdvywctADCGWITGHSYV---- 335

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  847 vweIWGPLLYGGRLVVVPHTVSR-SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELS 925
Cdd:PLN02654   336 ---TYGPMLNGATVLVFEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPS 412

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  926 RLEdWY------SRHPhnapkVINMYGITETTvhvsyieldesivSLRANSLIGC--------SIPDLKVyvldnylQPV 991
Cdd:PLN02654   413 AWR-WFfnvvgdSRCP-----ISDTWWQTETG-------------GFMITPLPGAwpqkpgsaTFPFFGV-------QPV 466

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  992 ppgVVGEMYVAGAGLARGYLGRAGL----------TAERFIADPFgKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIR 1061
Cdd:PLN02654   467 ---IVDEKGKEIEGECSGYLCVKKSwpgafrtlygDHERYETTYF-KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVS 542

                          490       500
                   ....*....|....*....|....*
gi 1698252301 1062 GFRIELGEIEAVIMKHDKVEQVAVI 1086
Cdd:PLN02654   543 GHRIGTAEVESALVSHPQCAEAAVV 567
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1-77 3.01e-15

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: 80.39  E-value: 3.01e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVReDRPNDKRIIAYIVAEEK-EPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd12114    401 LQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDgTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 652-1145 3.17e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 80.44  E-value: 3.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  652 QAHINPNSIAVVFED--KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:PRK13390     6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAK-----PSCVLTNSSVEIECDESLKIL----VDDVNVMEEIEKYSEENIDEMECLkplapshiAYVIYTS 800
Cdd:PRK13390    86 PEADYIVGDSGarvlvASAALDGLAAKVGADLPLRLSfggeIDGFGSFEAALAGAGPRLTEQPCG--------AVMLYSS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  801 GSTGRPKGVM---------IPHQNVVRLLGAtdhWFQFDADDVWtmfhsyafdFSVWEIW--GPLLYGGRLVVVPHTVSR 869
Cdd:PRK13390   158 GTTGFPKGIQpdlpgrdvdAPGDPIVAIARA---FYDISESDIY---------YSSAPIYhaAPLRWCSMVHALGGTVVL 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 SpKEF-----LQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGGEALELS---RLEDWYsrhphnAPKV 941
Cdd:PRK13390   226 A-KRFdaqatLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDvkhAMIDWL------GPIV 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  942 INMYGITEttVH-VSYIELDEsivSLRANSLIGCSIPDlKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAE- 1019
Cdd:PRK13390   299 YEYYSSTE--AHgMTFIDSPD---WLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAa 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1020 RFIADPFgkpgtrMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDK--- 1095
Cdd:PRK13390   373 QHPAHPF------WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgVPDPEMGEQvka 446

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301 1096 --RLVAYIVASNN---ETIDTNEMRqhasgsLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:PRK13390   447 viQLVEGIRGSDElarELIDYTRSR------IAHYKAPRSVEFVDELPRTPTGKL 495
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
664-1146 6.53e-15

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 80.39  E-value: 6.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  664 FEDKKLTYEKLNRKANKIARfLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGagylpldpdypsdRISFMLH------ 737
Cdd:PRK06814   654 PVNGPLTYRKLLTGAFVLGR-KLKKNTPPGENVGVMLPNANGAAVTFFALQSAG-------------RVPAMINfsagia 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  738 DAKPSC-------VLTnSSVEIEcdeslKILVDDVnvMEEIEK-----YSEE---NIDEMECLKPLA------------- 789
Cdd:PRK06814   720 NILSACkaaqvktVLT-SRAFIE-----KARLGPL--IEALEFgiriiYLEDvraQIGLADKIKGLLagrfplvyfcnrd 791

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 PSHIAYVIYTSGSTGRPKGVMIPHQNVV--------RL-LGATDHWFqfdadDVWTMFHSyaFDFSVWEIWgPLLYGGRL 860
Cdd:PRK06814   792 PDDPAVILFTSGSEGTPKGVVLSHRNLLanraqvaaRIdFSPEDKVF-----NALPVFHS--FGLTGGLVL-PLLSGVKV 863

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  861 VVVPhtvsrSPKEFLqlLVKEKVTVLNQT-----------------PSAFYqlmqadreneevgqklSLRYVVFGGEALE 923
Cdd:PRK06814   864 FLYP-----SPLHYR--IIPELIYDTNATilfgtdtflngyaryahPYDFR----------------SLRYVFAGAEKVK 920

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  924 LSRLEDWYSRHPHnapKVINMYGITETTvhvsyieldeSIVSL------RANSlIGCSIPDLkvyvlDNYLQPVPpGVV- 996
Cdd:PRK06814   921 EETRQTWMEKFGI---RILEGYGVTETA----------PVIALntpmhnKAGT-VGRLLPGI-----EYRLEPVP-GIDe 980

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  997 -GEMYVAGAGLARGYLgraglTAErfiadpfgKPGT------RMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGE 1069
Cdd:PRK06814   981 gGRLFVRGPNVMLGYL-----RAE--------NPGVleppadGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAA 1047

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1070 IEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVAsnnETIDTNEMRQHASG-SLPDYMVPYAFVVVNELPLTPNGKLD 1146
Cdd:PRK06814  1048 VEELAAELWPDALHAAVSIPDARKGERIILLTTA---SDATRAAFLAHAKAaGASELMVPAEIITIDEIPLLGTGKID 1122
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1-79 7.09e-15

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: 79.08  E-value: 7.09e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPA 79
Cdd:COG0318    365 LAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 634-1053 1.01e-14

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 79.39  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  634 NGGFQIAPEMTLPQLFEKQAHINPNSIAVVFED---------KKLTYEKLNRKANKIARFL--IAKgvgPDQLVALAMPR 702
Cdd:PRK07769    12 NGKIRFPPNTNLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLqqVTK---PGDRVAILAPQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  703 SLNMVVSLLAVLKAGAGYLPL-DPDYP--SDRISFMLHDAKPSCVLTNSsveiECDESLKILVDDVNVMEEIEKYSEENI 779
Cdd:PRK07769    89 NLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTT----DSAEGVRKFFRARPAKERPRVIAVDAV 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  780 -DEM-ECLKPLAPSH--IAYVIYTSGSTGRPKGVMIPHQ----NVVRLLGAtdhwFQFDADD---VW-TMFHsyafDFSV 847
Cdd:PRK07769   165 pDEVgATWVPPEANEdtIAYLQYTSGSTRIPAGVQITHLnlptNVLQVIDA----LEGQEGDrgvSWlPFFH----DMGL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  848 WEIWGPLLYGGRLVVV-PHTVSRSPKEFLQLLVKEK---VTVLNQTPSAFYQLMQA---DRENEEvgqKLSLRYV---VF 917
Cdd:PRK07769   237 ITVLLPALLGHYITFMsPAAFVRRPGRWIRELARKPggtGGTFSAAPNFAFEHAAArglPKDGEP---PLDLSNVkglLN 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  918 GGEALELSRLEDWYSRH-PHNAPK--VINMYGITETTVHVSYIELDE--SIVSLRANSL------------------IGC 974
Cdd:PRK07769   314 GSEPVSPASMRKFNEAFaPYGLPPtaIKPSYGMAEATLFVSTTPMDEepTVIYVDRDELnagrfvevpadapnavaqVSA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  975 ---SIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERF-------IADPFG---KPGTRMYRTGDLAR 1041
Cdd:PRK07769   394 gkvGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAegaPDDALWVRTGDYGV 473

                          490
                   ....*....|...
gi 1698252301 1042 WrQDGTLdYI-GR 1053
Cdd:PRK07769   474 Y-FDGEL-YItGR 484
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 666-1150 2.13e-14

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: 77.47  E-value: 2.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  666 DKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAgylpldpdyPSDRISFMLH-DAKPSCV 744
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGV---------ETALINSNLRlESLLHCI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  745 LTNSSveiecdeslKILVddVNVMEEIEKYSEENIDEMECLKplAPSHIAYvIYTSGSTGRPKGVMIPHQNVVRLLGATD 824
Cdd:cd05939     72 TVSKA---------KALI--FNLLDPLLTQSSTEPPSQDDVN--FRDKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAY 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  825 HWFQFDADDVW----TMFHSYAFDFSVweiwGPLLYGGRLVVVPHTVSRSpkEFLQLLVKEKVTVLNQTPS-AFYQLMQA 899
Cdd:cd05939    138 YAFGMRPEDVVydclPLYHSAGGIMGV----GQALLHGSTVVIRKKFSAS--NFWDDCVKYNCTIVQYIGEiCRYLLAQP 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  900 DRENEevgQKLSLRYVVfgGEALELSRLEDWYSRhpHNAPKVINMYGITETTvhVSYIELDESIVSLRANSLIGCSIPDL 979
Cdd:cd05939    212 PSEEE---QKHNVRLAV--GNGLRPQIWEQFVRR--FGIPQIGEFYGATEGN--SSLVNIDNHVGACGFNSRILPSVYPI 282

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  980 KVYVLDNYL-----------QPVPPGVVGEMY---VAGAGLAR--GYLGRaGLTAERFIADPFgKPGTRMYRTGDLARWR 1043
Cdd:cd05939    283 RLIKVDEDTgelirdsdglcIPCQPGEPGLLVgkiIQNDPLRRfdGYVNE-GATNKKIARDVF-KKGDSAFLSGDVLVMD 360

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1044 QDGTLDYIGRADHQIKIRGFRIELGEIEAVI-----MKHDKVEQVAVIVREDQPGdkrlVAYIVASNNETiDTNEMRQHA 1118
Cdd:cd05939    361 ELGYLYFKDRTGDTFRWKGENVSTTEVEGILsnvlgLEDVVVYGVEVPGVEGRAG----MAAIVDPERKV-DLDRFSAVL 435

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1698252301 1119 SGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05939    436 AKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 97-156 4.84e-14

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: 67.97  E-value: 4.84e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301   97 EILCDLFAEVLGVS--RINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAE 156
Cdd:pfam00550    1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1250-1405 1.83e-13

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 71.81  E-value: 1.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1250 RASGDQLPLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQ--ARGIAENEELPKSLEEMAADYlkhVREIQPH--GPYRLL 1325
Cdd:COG3208      1 PRPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQlpGRGDRLGEPPLTSLEELADDL---AEELAPLldRPFALF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1326 GWSLGGNVVHAMAAQLQNEGEEVELLVMLDSYPGHFLPNTEAPT---EEEALIALL-ALGGYDPDNMDGKPLtMESAVEI 1401
Cdd:COG3208     78 GHSMGALLAFELARRLERRGRPLPAHLFVSGRRAPHLPRRRRPLhdlSDAELLAELrRLGGTPEEVLADPEL-LELFLPI 156


                   ....
gi 1698252301 1402 LRKD 1405
Cdd:COG3208    157 LRAD 160
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
 653-1144 2.24e-13

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 75.00  E-value: 2.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVVFEDK-----KLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDY 727
Cdd:cd05943     78 RHADADDPAAIYAAEdgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  728 PS----DRISfmlhDAKPSCVLTNSSV-----EIECDESLKILVDDVNVMEEI----EKYSEENIDEMECLK-------- 786
Cdd:cd05943    158 GVpgvlDRFG----QIEPKVLFAVDAYtyngkRHDVREKVAELVKGLPSLLAVvvvpYTVAAGQPDLSKIAKaltledfl 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  787 -----------PLAPSHIAYVIYTSGSTGRPK-------GVMIPHQNVVRL---LGATDHWFQFDADDvWTMFHsyafdf 845
Cdd:cd05943    234 atgaagelefePLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILhcdLRPGDRLFYYTTCG-WMMWN------ 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  846 svWEIWGpLLYGGRLVV------VPhtvsrSPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQKLSLRYVVFGG 919
Cdd:cd05943    307 --WLVSG-LAVGATIVLydgspfYP-----DTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTG 378

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  920 EALeLSRLEDWYSRHPHNAPKVINMYGITEttvhvsyieldesivslransLIGCsipdlkvYVLDNYLQPVPPGvvgEM 999
Cdd:cd05943    379 SPL-KPESFDYVYDHIKPDVLLASISGGTD---------------------IISC-------FVGGNPLLPVYRG---EI 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1000 YVAGAGLAR---GYLGRA--GLTAERFIADPF--------GKPGTRMYRT------------GDLARWRQDGTLDYIGRA 1054
Cdd:cd05943    427 QCRGLGMAVeafDEEGKPvwGEKGELVCTKPFpsmpvgfwNDPDGSRYRAayfakypgvwahGDWIEITPRGGVVILGRS 506

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1055 DHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDtNEMRQH-----ASGSLPDYmVPY 1129
Cdd:cd05943    507 DGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELD-DELRKRirstiRSALSPRH-VPA 584

                          570
                   ....*....|....*
gi 1698252301 1130 AFVVVNELPLTPNGK 1144
Cdd:cd05943    585 KIIAVPDIPRTLSGK 599
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
643-1150 3.16e-13

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 74.43  E-value: 3.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  643 MTLPQLFEKQAHINPNSIAVVFED---KKLTYEKLNRKANKIARFLIAK-GVGPDQLVALAMPRSLNMVVSLLAVLKAGA 718
Cdd:PRK05620    10 LSLTRILEYGSTVHGDTTVTTWGGaeqEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  719 GYLPLDPDYPSDRISFMLHDAKP-----SCVLTNSSVEI--ECDESLKILV---DDVN-----VMEEIEKYSEEN-IDEM 782
Cdd:PRK05620    90 VFNPLNKQLMNDQIVHIINHAEDevivaDPRLAEQLGEIlkECPCVRAVVFigpSDADsaaahMPEGIKVYSYEAlLDGR 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  783 ECLK--PLAPSHIAYVI-YTSGSTGRPKGVMIPHQNVVRllgatdHWFQFDADDVWTMFHSYAFDFSV--WEI--WG-PL 854
Cdd:PRK05620   170 STVYdwPELDETTAAAIcYSTGTTGAPKGVVYSHRSLYL------QSLSLRTTDSLAVTHGESFLCCVpiYHVlsWGvPL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  855 ---LYGGRLVVVPHTVSrsPKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEvgQKLSLRYVVFGGEALELSRLEDWY 931
Cdd:PRK05620   244 aafMSGTPLVFPGPDLS--APTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPP--ERMSLQEIYVGGSAVPPILIKAWE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  932 SRHphnAPKVINMYGITETTVhVSYIELDESIVS--LRANSLI--GCSIPDLKVYVLDN------------YLQPVPPGV 995
Cdd:PRK05620   320 ERY---GVDVVHVWGMTETSP-VGTVARPPSGVSgeARWAYRVsqGRFPASLEYRIVNDgqvmestdrnegEIQVRGNWV 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  996 VGEMYVA----GAGLARGYLGRAGLTA-ERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEI 1070
Cdd:PRK05620   396 TASYYHSpteeGGGAASTFRGEDVEDAnDRFTADGW-------LRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQL 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1071 EAVIMKHDKVEQVAVI-VREDQPGDKRLVAYIVASNNE-TIDTNE-MRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDR 1147
Cdd:PRK05620   469 ENYIMAAPEVVECAVIgYPDDKWGERPLAVTVLAPGIEpTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDK 548


                   ...
gi 1698252301 1148 KAL 1150
Cdd:PRK05620   549 KDL 551
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 96-166 3.32e-13

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 66.42  E-value: 3.32e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301   96 EEILCDLFAEVLGV--SRINIDDNFF-EMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAKQLNHAKS 166
Cdd:COG0236      7 EERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 650-1150 5.28e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 73.44  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  650 EKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPS 729
Cdd:PRK08162    25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  730 DRISFMLHDAKPSCVLTN---SSV---EIECDESLKILVDDVnVMEEiekYSE-ENIDEMECLKPLAPSHIAYVI----- 797
Cdd:PRK08162   105 ASIAFMLRHGEAKVLIVDtefAEVareALALLPGPKPLVIDV-DDPE---YPGgRFIGALDYEAFLASGDPDFAWtlpad 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  798 --------YTSGSTGRPKGVMIPHQNV-VRLLGATDHWfQFDADDV--WT--MFHSYAFDFSvweiWGPLLYGGRLVVVp 864
Cdd:PRK08162   181 ewdaialnYTSGTTGNPKGVVYHHRGAyLNALSNILAW-GMPKHPVylWTlpMFHCNGWCFP----WTVAARAGTNVCL- 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  865 htvsR--SPKEFLQLLVKEKVTVLNQTPSAFYQLMQADrenEEVGQKLSLRYVVFGGEAlelsrledwysrhphnAP--- 939
Cdd:PRK08162   255 ----RkvDPKLIFDLIREHGVTHYCGAPIVLSALINAP---AEWRAGIDHPVHAMVAGA----------------APpaa 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  940 ----------KVINMYGITET----TVHVSYIELDESIVSLRA--NSLIGCSIPDLK-VYVLD-NYLQPVPPG--VVGEM 999
Cdd:PRK08162   312 viakmeeigfDLTHVYGLTETygpaTVCAWQPEWDALPLDERAqlKARQGVRYPLQEgVTVLDpDTMQPVPADgeTIGEI 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1000 YVAGAGLARGYLGRAGLTAERFiADPFgkpgtrmYRTGDLARWRQDGtldYIgradhQIKIR--------GFRIELGEIE 1071
Cdd:PRK08162   392 MFRGNIVMKGYLKNPKATEEAF-AGGW-------FHTGDLAVLHPDG---YI-----KIKDRskdiiisgGENISSIEVE 455

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301 1072 AVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAfVVVNELPLTPNGKLDRKAL 1150
Cdd:PRK08162   456 DVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFVL 533
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 1-77 7.07e-13

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: 72.87  E-value: 7.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDrPNDK--RIIAYIVAE----EKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:TIGR01734  415 LRQSSYIESAVVVPKYN-KDHKveYLIAAIVPEtedfEKEFQLTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDR 493


                   ...
gi 1698252301   75 KKL 77
Cdd:TIGR01734  494 KAL 496
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 669-1086 8.10e-13

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: 72.89  E-value: 8.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFmlhdakpscVLTNS 748
Cdd:cd05932      7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRY---------VLEHS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 sveiECDESLKILVDDVNVM-----EEIEKYSEENIDEMECLK----------PL------APSHIAYVIYTSGSTGRPK 807
Cdd:cd05932     78 ----ESKALFVGKLDDWKAMapgvpEGLISISLPPPSAANCQYqwddliaqhpPLeerptrFPEQLATLIYTSGTTGQPK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  808 GVMIPH-------QNVVRLLGATDhwfqfdaDDvwTMFhSYAFDFSVWE---IWGPLLYGGRLVVVPHT-------VSRS 870
Cdd:cd05932    154 GVMLTFgsfawaaQAGIEHIGTEE-------ND--RML-SYLPLAHVTErvfVEGGSLYGGVLVAFAESldtfvedVQRA 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  871 -PKEFL---QLLVKEKVTVLNQTPSAFYQ-LMQADRENEEVGQKL-------SLRYVVFGGEALELSRLeDWYSRHPHNa 938
Cdd:cd05932    224 rPTLFFsvpRLWTKFQQGVQDKIPQQKLNlLLKIPVVNSLVKRKVlkglgldQCRLAGCGSAPVPPALL-EWYRSLGLN- 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  939 pkVINMYGITETTV--HVSYIELDESivslranSLIGCSIPDLKVYVLDNylqpvppgvvGEMYVAGAGLARGYLGRAGL 1016
Cdd:cd05932    302 --ILEAYGMTENFAysHLNYPGRDKI-------GTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEA 362

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301 1017 TAERFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKI-RGFRIELGEIEAVIMKHDKVEQVAVI 1086
Cdd:cd05932    363 TAEAFTADGF-------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1-169 8.51e-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: 70.93  E-value: 8.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVsesLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:COG3433    123 RAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDK---VPPDVVAASAVVALDALLLLALKVVARAAPAL 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301   81 DFNGMNNE------RVARNPKEEILCDLFAEVLGVS--RINIDDNFFEMGGHSLLASRLMARIRETlSVELGIGKLFESP 152
Cdd:COG3433    200 AAAEALLAaaspapALETALTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHP 278

                          170
                   ....*....|....*..
gi 1698252301  153 TVAELAKQLNHAKSARP 169
Cdd:COG3433    279 TLAAWWALLAAAQAAAA 295
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 214-504 1.07e-12

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


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 71.75  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  214 LNRQALQGAFYDVVEKHETLRTIFpnvLGSSYQKIL------DMENLNLEMVITNTCKDELESV---LSEAVrysFNLDF 284
Cdd:cd19535     37 LDPDRLERAWNKLIARHPMLRAVF---LDDGTQQILpevpwyGITVHDLRGLSEEEAEAALEELrerLSHRV---LDVER 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  285 EPAVRLQLFTVSENEHVLLILLHHIVGDGWSLQPLTRDFTAAYkarcQGDRVQLETLPVQYADYALWQQQLlgdettPES 364
Cdd:cd19535    111 GPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFRDYLLAEQAL------RET 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  365 LISTQLDFWKEELKGLPDQMELPTdYQRPvetsyrgETI--------HFHIDEGMHSRLVELGRKNGVSLFMVLqagLSA 436
Cdd:cd19535    181 AYERARAYWQERLPTLPPAPQLPL-AKDP-------EEIkeprftrrEHRLSAEQWQRLKERARQHGVTPSMVL---LTA 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  437 -------------------LFTRLGAGTDIPigspiagrnddvlsDIVGLFVNTLVLRTNTSGDPSFKELLNRVKQVNLA 497
Cdd:cd19535    250 yaevlarwsgqprfllnltLFNRLPLHPDVN--------------DVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWE 315


                   ....*..
gi 1698252301  498 AYENQDV 504
Cdd:cd19535    316 DLDHSSY 322
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1-77 2.17e-12

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 71.46  E-value: 2.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREdrPNDK--RIIAYIVAE----EKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:PRK04813   417 LRQSSYVESAVVVPYN--KDHKvqYLIAYVVPKeedfEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494


                   ...
gi 1698252301   75 KKL 77
Cdd:PRK04813   495 KAL 497
PRK09192 PRK09192
fatty acyl-AMP ligase;
669-1147 2.86e-12

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 71.19  E-value: 2.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYP-------SDRISFMLHDAKP 741
Cdd:PRK09192    50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQP 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  742 SCVLTNssveiecDESLKILVDDVNVMEEIEKYSEENIDEMEC----LKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVV 817
Cdd:PRK09192   130 AAIITP-------DELLPWVNEATHGNPLLHVLSHAWFKALPEadvaLPRPTPDDIAYLQYSSGSTRFPRGVIITHRALM 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  818 -RLLGATDHWFQFDADDVWtmfhsyafdFSvweiWGPL-----LYGGRLVVVPHTVS----------RSPKEFLQLLVKE 881
Cdd:PRK09192   203 aNLRAISHDGLKVRPGDRC---------VS----WLPFyhdmgLVGFLLTPVATQLSvdylptrdfaRRPLQWLDLISRN 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  882 KVTVlNQTPSAFYQLMqADRENEEVGQKLSL---RYVVFGGEALELSRLEDW---YSRHPHNAPKVINMYGITETTVHVS 955
Cdd:PRK09192   270 RGTI-SYSPPFGYELC-ARRVNSKDLAELDLscwRVAGIGADMIRPDVLHQFaeaFAPAGFDDKAFMPSYGLAEATLAVS 347

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  956 YIELDESIVSL---------------------RANSLIGC--SIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLG 1012
Cdd:PRK09192   348 FSPLGSGIVVEevdrdrleyqgkavapgaetrRVRTFVNCgkALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFR 427

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1013 RAgLTAERFIADPFgkpgtrmYRTGDLArWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQ--VAVIVRED 1090
Cdd:PRK09192   428 DE-ESQDVLAADGW-------LDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAAFSIAQ 498

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1698252301 1091 QPGDKrLVAYIVASNNETIDTNEMRQHASGSLpdYMVPYAFVVV-----NELPLTPNGKLDR 1147
Cdd:PRK09192   499 ENGEK-IVLLVQCRISDEERRGQLIHALAALV--RSEFGVEAAVelvppHSLPRTSSGKLSR 557
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 779-1102 2.88e-12

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


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 70.98  E-value: 2.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  779 IDEMECLKPLaPSHIAYVIYTSGSTGRPKGVMIPHQNVVR----LLGATDhWFQFDADDVW-TMFHSY---AFDFSvwei 850
Cdd:cd05908     95 ITEEEVLCEL-ADELAFIQFSSGSTGDPKGVMLTHENLVHnmfaILNSTE-WKTKDRILSWmPLTHDMgliAFHLA---- 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  851 wgPLLYGGRLVVVPHTV-SRSPKEFLQLLVKEKVTVLNqTPSAFYQLMqADRENEEVGQKL---SLRYVVFGGE--ALEL 924
Cdd:cd05908    169 --PLIAGMNQYLMPTRLfIRRPILWLKKASEHKATIVS-SPNFGYKYF-LKTLKPEKANDWdlsSIRMILNGAEpiDYEL 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  925 -SRLEDWYSRHPHNAPKVINMYGITETTVHVSYIELDESIVSL---RANSLIGCSIPDL--------------------K 980
Cdd:cd05908    245 cHEFLDHMSKYGLKRNAILPVYGLAEASVGASLPKAQSPFKTItlgRRHVTHGEPEPEVdkkdsecltfvevgkpidetD 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  981 VYVLDNYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGDLARWRqDGTLDYIGRADHQIKI 1060
Cdd:cd05908    325 IRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLGFIR-NGRLVITGREKDIIFV 396

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1698252301 1061 RGFRIELGEIEAVIMKHDKVE--QVAVI-VREDQPGDKRLVAYIV 1102
Cdd:cd05908    397 NGQNVYPHDIERIAEELEGVElgRVVACgVNNSNTRNEEIFCFIE 441
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1-80 6.93e-12

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: 69.85  E-value: 6.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSE---------------------------IRSYVSESLANYM 53
Cdd:cd17647    414 ISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFaqedvpkevstdpivkgligyrklikdIREFLKKRLASYA 493

                           90       100
                   ....*....|....*....|....*..
gi 1698252301   54 IPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:cd17647    494 IPSLIVVLDKLPLNPNGKVDKPKLQFP 520
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1172-1228 9.34e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 61.43  E-value: 9.34e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301 1172 LCDLFTEVL--SVSQIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVA 1228
Cdd:pfam00550    3 LRELLAEVLgvPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
PRK05857 PRK05857
fatty acid--CoA ligase;
651-1152 1.94e-11

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 68.50  E-value: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  651 KQAHINPNSIAVVFED--KKLTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYP 728
Cdd:PRK05857    22 EQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  729 SDRISFMLHDAKPSCVLTNSSVEIECDESLKILVDDVNVMEEIEKYSEENIDEMECLKPLA-PSHIA----YVIYTSGST 803
Cdd:PRK05857   102 IAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGnADQGSedplAMIFTSGTT 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  804 GRPKGVMIPHQ------NVVRLLGAtdHWFQFDADDVWTMFHSYAFDFSVWEIWGPLLYGGRLVvvphTVSRSPKEFLQL 877
Cdd:PRK05857   182 GEPKAVLLANRtffavpDILQKEGL--NWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCV----TGGENTTSLLEI 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  878 LVKEKVTVLNQTPSAFYQLMQADRENEEVGQklSLRYVVFGGE---ALELSRLEdwysrhpHNAPKVINMYGITETTVHV 954
Cdd:PRK05857   256 LTTNAVATTCLVPTLLSKLVSELKSANATVP--SLRLVGYGGSraiAADVRFIE-------ATGVRTAQVYGLSETGCTA 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  955 SYIELD-ESIVSLRANSlIGCSIPDLKVYVLD------NYLQPVPPGVVGEMYVAGAGLARGYLGRAGLTAErFIADPFg 1027
Cdd:PRK05857   327 LCLPTDdGSIVKIEAGA-VGRPYPGVDVYLAAtdgigpTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAE-VLIDGW- 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1028 kpgtrmYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVI-VREDQPGDKRLVAYIVASNN 1106
Cdd:PRK05857   404 ------VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYeIPDEEFGALVGLAVVASAEL 477

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1107 ETIDTNEMRQHASGSL---PDYMV-PYAFVVVNELPLTPNGKLDRKALPA 1152
Cdd:PRK05857   478 DESAARALKHTIAARFrreSEPMArPSTIVIVTDIPRTQSGKVMRASLAA 527
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1-77 3.71e-11

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: 67.57  E-value: 3.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRH-ENIQQAVVMV--REDRPNDKRIIAYIVAEEKEP-----------------INLSEIRSYVSESLANYMIPSAFVV 60
Cdd:cd05918    377 LRQSlPGAKEVVVEVvkPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLP 456

                           90
                   ....*....|....*..
gi 1698252301   61 LEELPLTPNGKVDRKKL 77
Cdd:cd05918    457 LSHLPLTASGKIDRRAL 473
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 945-1151 5.68e-11

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 66.56  E-value: 5.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  945 YGITETTVHVSYIELDESivsLRANSLIGCSIPDLKVYVLDNylqpvppgVVGEMYVAGAGLARGYLgragltaerfiad 1024
Cdd:PRK07445   261 YGMTETASQIATLKPDDF---LAGNNSSGQVLPHAQITIPAN--------QTGNITIQAQSLALGYY------------- 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1025 PFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAyIVAS 1104
Cdd:PRK07445   317 PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTA-IYVP 395

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1698252301 1105 NNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKALP 1151
Cdd:PRK07445   396 KDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1-73 6.66e-11

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: 65.77  E-value: 6.66e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVD 73
Cdd:cd04433    264 LLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 798-1145 9.66e-11

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


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 66.27  E-value: 9.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  798 YTSGSTGRPKGVMIPHQNVV--RLLGATDHWFQFDADD----VWTMFHSYAfdfsvweiWG-PL---LYGGRLVVV-PHT 866
Cdd:PRK07008   183 YTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDavlpVVPMFHVNA--------WGlPYsapLTGAKLVLPgPDL 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  867 VSRSPKEflqLLVKEKVTVLNQTPSAFYQLMQADRENeevGQKLS-LRYVVFGGEALE---LSRLEDWYSrhphnaPKVI 942
Cdd:PRK07008   255 DGKSLYE---LIEAERVTFSAGVPTVWLGLLNHMREA---GLRFStLRRTVIGGSACPpamIRTFEDEYG------VEVI 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  943 NMYGITE----------TTVHVSYIELDESIVSLRANSLIgCSIpDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGYLG 1012
Cdd:PRK07008   323 HAWGMTEmsplgtlcklKWKHSQLPLDEQRKLLEKQGRVI-YGV-DMKIVGDDGRELPWDGKAFGDLQVRGPWVIDRYFR 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1013 RAGltaerfiaDPFGKpgtRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQP 1092
Cdd:PRK07008   401 GDA--------SPLVD---GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPK 469

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1698252301 1093 GDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKL 1145
Cdd:PRK07008   470 WDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1164-1234 3.18e-10

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: 58.03  E-value: 3.18e-10
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301  1164 PRTPQEEMLCDLF-TEVLSV------SQIGIDDGFFDLGGHSLLAVQLMSRMKEALGVELNIGTLFAAPTVAGLAERL 1234
Cdd:smart00823    5 PPAERRRLLLDLVrEQVAAVlghaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1-71 3.45e-10

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: 57.55  E-value: 3.45e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGK 71
Cdd:pfam13193    6 LVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 769-1106 3.56e-10

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


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 64.75  E-value: 3.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  769 EEIEKYSEENidEMECLKPLaPSHIAYVIYTSGSTGRPKGVMIPHQNVVRL----------LGATD---------HWFQF 829
Cdd:PLN02387   231 SEVEKLGKEN--PVDPDLPS-PNDIAVIMYTSGSTGLPKGVMMTHGNIVATvagvmtvvpkLGKNDvylaylplaHILEL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  830 DADDVwtmfhsyafdfsVWEIWGPLLYGGrlvvvPHTVSRSPKEfLQLLVKEKVTVLNQTpsafyqLMQA-----DRENE 904
Cdd:PLN02387   308 AAESV------------MAAVGAAIGYGS-----PLTLTDTSNK-IKKGTKGDASALKPT------LMTAvpailDRVRD 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  905 EVGQKLSLRyvvfGGEALELSRLEdwYSRH---------------------------------------PHNAP------ 939
Cdd:PLN02387   364 GVRKKVDAK----GGLAKKLFDIA--YKRRlaaiegswfgawglekllwdalvfkkiravlggrirfmlSGGAPlsgdtq 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  940 KVINM---------YGITETTVHVSYIELDESIVSlRANSLIGCSIPDLKVYVLDNYLQPVPPGVVGEMYVAGAGLARGY 1010
Cdd:PLN02387   438 RFINIclgapigqgYGLTETCAGATFSEWDDTSVG-RVGPPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGY 516

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1011 LGRAGLTAERFIADpfgKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIR-GFRIELGEIEAVIMKHDKVEQvaVIVRE 1089
Cdd:PLN02387   517 FKNQEKTDEVYKVD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDN--IMVHA 591

                          410
                   ....*....|....*..
gi 1698252301 1090 DqPGDKRLVAYIVASNN 1106
Cdd:PLN02387   592 D-PFHSYCVALVVPSQQ 607
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1-77 3.57e-10

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: 63.87  E-value: 3.57e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRpndkrIIAYIVAEEkepINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd17653    363 LQSQPEVTQAAAIVVNGR-----LVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 664-1150 4.36e-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: 63.99  E-value: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  664 FEDKKLTYEKLNRKANKIARFLI-AKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRisfMLHdakps 742
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDP---LIH----- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  743 CV-LTNSSVEIECDESLKILvddvnvmeeiekyseenidemeclkplapshiayvIYTSGSTGRPKGVMIPHQNVVRLLG 821
Cdd:cd05937     73 CLkLSGSRFVIVDPDDPAIL-----------------------------------IYTSGTTGLPKAAAISWRRTLVTSN 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  822 ATDHWFQFDADDVW----TMFHSYAFDFSVWEIwgplLYGGRLVVVPHTVSRSpkEFLQLLVKEKVTVLNQTPSAFYQLM 897
Cdd:cd05937    118 LLSHDLNLKNGDRTytcmPLYHGTAAFLGACNC----LMSGGTLALSRKFSAS--QFWKDVRDSGATIIQYVGELCRYLL 191

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  898 QADRENEEVGQKLSLRYvvfgGEALelsRLEDWYS-RHPHNAPKVINMYGITE----TTVHVS----------------- 955
Cdd:cd05937    192 STPPSPYDRDHKVRVAW----GNGL---RPDIWERfRERFNVPEIGEFYAATEgvfaLTNHNVgdfgagaighhglirrw 264

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  956 YIELDESIVSLRANSliGCSIPDLKvyvlDNYLQPVPPGVVGEMYVA----GAGLARGYLGRAGLTAERFIADPFGKpGT 1031
Cdd:cd05937    265 KFENQVVLVKMDPET--DDPIRDPK----TGFCVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRK-GD 337

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1032 RMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVAVIVREDQPGDKRLVAYIVASNNE---- 1107
Cdd:cd05937    338 IYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESsavp 417

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1698252301 1108 -TIDTNEMRQHASGSLPDYMVPYAFVVVNELPLTPNGKLDRKAL 1150
Cdd:cd05937    418 tEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
787-1146 1.18e-09

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 63.19  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  787 PLAPSHIAYVIYTSGSTGRPKGVMIPHQ----NVVRLLGATDhwfqFDADDVWT----MFHsyAFDFSVwEIWGPLLYGG 858
Cdd:PRK08043   361 KQQPEDAALILFTSGSEGHPKGVVHSHKsllaNVEQIKTIAD----FTPNDRFMsalpLFH--SFGLTV-GLFTPLLTGA 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  859 RLVVVPhtvsrSPKEFL---QLLVKEKVTVLNQT------------PSAFYQlmqadreneevgqklsLRYVVFGGEALE 923
Cdd:PRK08043   434 EVFLYP-----SPLHYRivpELVYDRNCTVLFGTstflgnyarfanPYDFAR----------------LRYVVAGAEKLQ 492

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  924 LSRLEDWYSRHphnAPKVINMYGITETTVHVSyIELDesiVSLRANSlIGCSIPDlkvyvLDNYLQPVpPGVV--GEMYV 1001
Cdd:PRK08043   493 ESTKQLWQDKF---GLRILEGYGVTECAPVVS-INVP---MAAKPGT-VGRILPG-----MDARLLSV-PGIEqgGRLQL 558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1002 AGAGLARGYL--GRAGLTAERFIADPFGKPGTRMYRTGDLARWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMKHDK 1079
Cdd:PRK08043   559 KGPNIMNGYLrvEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSP 638

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301 1080 VEQVAVIVREDQPGDKRLVAYivaSNNETIDTNEMRQHASGS-LPDYMVPYAFVVVNELPLTPNGKLD 1146
Cdd:PRK08043   639 DKQHATAIKSDASKGEALVLF---TTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 1271-1384 1.46e-09

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 59.55  E-value: 1.46e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  1271 YAGLMKSLGTDYPIYGVQARGIAENEELPKSLEeMAADYLKH-VREIQPHGPYRLLGWSLGGNVVHAMAAQLQNEGEEVE 1349
Cdd:smart00824   15 YARLAAALRGRRDVSALPLPGFGPGEPLPASAD-ALVEAQAEaVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGIPPA 93

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1698252301  1350 LLVMLDSY-PGHFLPNTEAPTEEEALIA------------LLALGGYD 1384
Cdd:smart00824   94 AVVLLDTYpPGDPAPEGWLPELLRGVFEredsfvpmddarLTAMGAYL 141
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1-77 2.71e-09

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: 61.70  E-value: 2.71e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkEPINLSEIRSYVSES-LANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:COG1021    451 LLAHPAVHDAAVVAMPDEYLGERSCAFVVPRG-EPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 7-78 4.37e-09

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: 60.49  E-value: 4.37e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    7 IQQAVVMVRED-----RPNDKRIIAYIVAEEkEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd17648    378 VRECAVVAKEDasqaqSRIQKYLVGYYLPEP-GHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 10-77 4.67e-09

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 60.59  E-value: 4.67e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301   10 AVVMVredrPNDK---RIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK06187   447 AVIGV----PDEKwgeRPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 875-1098 5.31e-09

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 60.33  E-value: 5.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  875 LQLLVKEKVTVLNQTPS-AFYQLMQADRENEEvGQKLSLRYVVFGGEAL------ELSRLEDWysrhphnapKVINMYGI 947
Cdd:cd05913    163 LQLIKDFGPTVLCCTPSyALYLAEEAEEEGID-PRELSLKVGIFGAEPWteemrkRIERRLGI---------KAYDIYGL 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  948 TETtvhvsyIELDESIVSLRANSLIG---CSIPDLkvyVLDNYLQPVPPGVVGEMYVAGaglargyLGRAGLtaerfiad 1024
Cdd:cd05913    233 TEI------IGPGVAFECEEKDGLHIwedHFIPEI---IDPETGEPVPPGEVGELVFTT-------LTKEAM-------- 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1025 pfgkPGTRmYRTGDLARW------------RQDGTldyIGRADHQIKIRGFRIELGEIEAVIMKHDKVEQVA-VIVREDQ 1091
Cdd:cd05913    289 ----PLIR-YRTRDITRLlpgpcpcgrthrRIDRI---TGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYqLILTRQE 360


                   ....*..
gi 1698252301 1092 PGDKRLV 1098
Cdd:cd05913    361 HLDELTI 367
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1-77 6.49e-09

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: 60.05  E-value: 6.49e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkePINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05912    335 LLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
785-1147 6.86e-09

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 60.16  E-value: 6.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  785 LKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVV-RLLGATDHWFQFDADDV---W-TMFHSYAFDFSVWEIWGpllyGGR 859
Cdd:PRK05851   146 LTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLsNLRGLNARVGLDAATDVgcsWlPLYHDMGLAFLLTAALA----GAP 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  860 LVVVPHTV-SRSPKEFLQLLVKEKVTvLNQTPSAFYQLM--QADRENE-EVGqklSLRYVVFGGEALE---LSRLEDWYS 932
Cdd:PRK05851   222 LWLAPTTAfSASPFRWLSWLSDSRAT-LTAAPNFAYNLIgkYARRVSDvDLG---ALRVALNGGEPVDcdgFERFATAMA 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  933 RHPHNAPKVINMYGITETTVHVSY------IELDESI----VSLRANSLIGCSIPDLKVYVldnylQPV--PPGV----V 996
Cdd:PRK05851   298 PFGFDAGAAAPSYGLAESTCAVTVpvpgigLRVDEVTtddgSGARRHAVLGNPIPGMEVRI-----SPGdgAAGVagreI 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  997 GEMYVAGAGLARGYLGRAGLTAERFiadpfgkpgtrmYRTGDLArWRQDGTLDYIGRADHQIKIRGFRIELGEIEAVIMK 1076
Cdd:PRK05851   373 GEIEIRGASMMSGYLGQAPIDPDDW------------FPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQ 439

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301 1077 HDKVEQVAVIV-----REDQPGdkRLVAYIVASNNETIDTNEMRQH-AS--GSLPDYMVpyaFVVVNELPLTPNGKLDR 1147
Cdd:PRK05851   440 VRGVREGAVVAvgtgeGSARPG--LVIAAEFRGPDEAGARSEVVQRvASecGVVPSDVV---FVAPGSLPRTSSGKLRR 513
PRK13382 PRK13382
bile acid CoA ligase;
1-80 1.50e-08

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 59.00  E-value: 1.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:PRK13382   458 LATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 1-77 1.90e-08

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: 58.86  E-value: 1.90e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05926    415 LLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 1-77 3.74e-08

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: 57.57  E-value: 3.74e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05936    391 LYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 1-79 4.59e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 57.35  E-value: 4.59e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkePINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPA 79
Cdd:PRK08308   333 MLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 8-158 4.66e-08

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


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 57.79  E-value: 4.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    8 QQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAPDFNGMNN 87
Cdd:COG3319    427 VAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAA 506

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1698252301   88 ERVARNPKEEILCDLFAEVLGVSRINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELA 158
Cdd:COG3319    507 APAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALA 577
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 1-81 8.88e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 56.86  E-value: 8.88e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAP 80
Cdd:PRK07788   469 LAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548


                   .
gi 1698252301   81 D 81
Cdd:PRK07788   549 D 549
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 1-77 9.28e-08

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: 56.57  E-value: 9.28e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkEPINLSEIRSYVSE-SLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05920    406 LLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 96-161 9.43e-08

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: 51.10  E-value: 9.43e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301    96 EEILCDLFAEVLGVS---RINIDDNFFEMGGHSLLASRLMARIRETLSVELGIGKLFESPTVAELAKQL 161
Cdd:smart00823   14 LDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1-77 1.62e-07

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 55.74  E-value: 1.62e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkePINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK03640   402 LLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSG--EVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1-77 9.93e-07

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: 53.23  E-value: 9.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLS---EIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05919    356 IIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 669-1145 1.11e-06

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 53.23  E-value: 1.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIA-RFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKP------ 741
Cdd:cd17632     68 ITYAELWERVGAVAaAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPrllavs 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  742 --------SCVLTNSSV--------------EIECDESLKILVDDVNVMEEIEkysEENIDEMECLKPLAPSHI------ 793
Cdd:cd17632    148 aehldlavEAVLEGGTPprlvvfdhrpevdaHRAALESARERLAAVGIPVTTL---TLIAVRGRDLPPAPLFRPepdddp 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  794 -AYVIYTSGSTGRPKGVMIPHQNVVRLlgatdhWFQFDADDVWTMFHSYAFDF--------SVWeIWGPLLYGGrlvvVP 864
Cdd:cd17632    225 lALLIYTSGSTGTPKGAMYTERLVATF------WLKVSSIQDIRPPASITLNFmpmshiagRIS-LYGTLARGG----TA 293

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  865 HTVSRS-------------PKEFL------QLLVKEKVTVLNQTPSAfyqlmQADRENEEVGQKLSLRYVVFGGEALels 925
Cdd:cd17632    294 YFAAASdmstlfddlalvrPTELFlvprvcDMLFQRYQAELDRRSVA-----GADAETLAERVKAELRERVLGGRLL--- 365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  926 rledwySRHPHNAPKVINMYGITETTVHVSYIE---LDESIVSLRANSLigcsipdLKVYVLDNYLQPVP---------P 993
Cdd:cd17632    366 ------AAVCGSAPLSAEMKAFMESLLDLDLHDgygSTEAGAVILDGVI-------VRPPVLDYKLVDVPelgyfrtdrP 432

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  994 GVVGEMYVAGAGLARGYLGRAGLTAERFIADPFgkpgtrmYRTGD-LARWRQDgTLDYIGRADHQIKI-RGFRIELGEIE 1071
Cdd:cd17632    433 HPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLE 504

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1072 AVIMKHDKVEQV------------AVIVredqPGDKRLVAYIVASNNETIDTNEMRQHASGSLPDYMVPYAFVVVNElPL 1139
Cdd:cd17632    505 AVFAASPLVRQIfvygnserayllAVVV----PTQDALAGEDTARLRAALAESLQRIAREAGLQSYEIPRDFLIETE-PF 579


                   ....*..
gi 1698252301 1140 TP-NGKL 1145
Cdd:cd17632    580 TIaNGLL 586
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 653-1143 1.22e-06

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: 53.12  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  653 AHINPNSIAVvfEDKKLTYEKLNRKANKIARFLIAK-GVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDR 731
Cdd:cd05905      1 AYTLLDSKGK--EATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  732 ISFML-----HDAKPSCVLT--------NSSVEIECDESLKI--LVDDVNVMEEIEKYSEENIDEmeclKPLAPSHIAYV 796
Cdd:cd05905     79 LGFLLgtckvRVALTVEACLkglpkkllKSKTAAEIAKKKGWpkILDFVKIPKSKRSKLKKWGPH----PPTRDGDTAYI 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  797 IYTSGSTGRPKGVMIPHQ---NVVRLLGATDHWFQfdADDVWTMFHSY-AFDFSVWEIWGplLYGGRLVVV--PHTVSRS 870
Cdd:cd05905    155 EYSFSSDGSLSGVAVSHSsllAHCRALKEACELYE--SRPLVTVLDFKsGLGLWHGCLLS--VYSGHHTILipPELMKTN 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  871 PKEFLQLLVKEKVTVLNQTPSAFYQLMQADRENEEVGQK----LS-LRY-VVFGGEALELSRLEDW-------------- 930
Cdd:cd05905    231 PLLWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNrdvnLSsLRMcMVPCENRPRISSCDSFlklfqtlglsprav 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  931 ---YSRHPHNAPKVINMYGITETTVHVSYIELDESIVSLR----ANSLI----GCSIPDLKVYVLD-NYLQPVPPGVVGE 998
Cdd:cd05905    311 steFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDerdkPNSLPlqdsGKVLPGAQVAIVNpETKGLCKDGEIGE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  999 MYVAGAGLARGYLGRAG---LTAERFIADPFGKP--GTRMYRTGDLARWRQDGTLDY----------IGRADHQIKIRGF 1063
Cdd:cd05905    391 IWVNSPANASGYFLLDGetnDTFKVFPSTRLSTGitNNSYARTGLLGFLRPTKCTDLnveehdllfvVGSIDETLEVRGL 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1064 RIELGEIEAVIMK-HDKVEQVA--------VIVREDQPGDKRLVAYIVASNNETIDTnemrQHASGSlpdYMVpyAFVVV 1134
Cdd:cd05905    471 RHHPSDIEATVMRvHPYRGRCAvfsitglvVVVAEQPPGSEEEALDLVPLVLNAILE----EHQVIV---DCV--ALVPP 541


                   ....*....
gi 1698252301 1135 NELPLTPNG 1143
Cdd:cd05905    542 GSLPKNPLG 550
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1257-1379 1.45e-06

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 50.77  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1257 PLFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENE--ELPKSLEEMAADyLKHVREIQPHGPYRLLGWSLGGNVV 1334
Cdd:COG0596     25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDkpAGGYTLDDLADD-LAALLDALGLERVVLVGHSMGGMVA 103

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1698252301 1335 HAMAAQlqnEGEEVELLVMLDSYPGHFLPNTEAPTE-EEALIALLA 1379
Cdd:COG0596    104 LELAAR---HPERVAGLVLVDEVLAALAEPLRRPGLaPEALAALLR 146
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
1-77 2.08e-06

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 52.30  E-value: 2.08e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAeeKEPINLSEIRSYVSE-SLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK10946   451 LLRHPAVIHAALVSMEDELMGEKSCAFLVV--KEPLKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 1-75 2.15e-06

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: 51.56  E-value: 2.15e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkePINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:cd17630    247 LAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG--PADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 4-77 3.29e-06

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: 51.48  E-value: 3.29e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301    4 HENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd12119    443 HPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 1-77 3.71e-06

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 51.44  E-value: 3.71e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK07656   434 LYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1-77 4.47e-06

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


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 50.74  E-value: 4.47e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQA-VVMVREDRPNDKrIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05917    272 LHTHPKVSDVqVVGVPDERYGEE-VCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 1-78 4.68e-06

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


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 50.75  E-value: 4.68e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:cd05934    345 ILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 11-77 8.40e-06

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


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 50.13  E-value: 8.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301   11 VVMVREDRPNDKRIIAYIVAEEKepINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05922    392 AAAVGLPDPLGEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 1-77 1.20e-05

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 49.68  E-value: 1.20e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK08008   440 IATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 1-74 1.82e-05

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: 49.15  E-value: 1.82e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQ-AVVMVredrPNDK---RIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:cd17631    362 LYEHPAVAEvAVIGV----PDEKwgeAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
1-77 2.37e-05

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 48.50  E-value: 2.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK07824   275 LATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK07868 PRK07868
acyl-CoA synthetase; Validated
 638-727 2.97e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 48.95  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  638 QIAP--EMTLPQLFEKQAHINPNSIAVVFEDKKLTYEKLNRKANKIARFLIAKGVGPDQLVALAM---PRSLnMVVSLLA 712
Cdd:PRK07868   440 QINDhtRISLGRIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMetrPSAL-VAIAALS 518

                           90
                   ....*....|....*
gi 1698252301  713 VLKAGAGYLPLDPDY 727
Cdd:PRK07868   519 RLGAVAVLMPPDTDL 533
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 754-1108 3.02e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 48.66  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  754 CDESLKILVDDVNVMEEiEKYSEENI-------DEMECL--------KPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVR 818
Cdd:PLN02430   169 SAKRLKAIVSFTSVTEE-ESDKASQIgvktyswIDFLHMgkenpsetNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVAT 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  819 LLGATDHWF-QFD----ADDVWTMFHSYA---------FDF----SVWEIWGPL---------LYGGRLVVVPHTVSR-- 869
Cdd:PLN02430   248 FVRGVDLFMeQFEdkmtHDDVYLSFLPLAhildrmieeYFFrkgaSVGYYHGDLnalrddlmeLKPTLLAGVPRVFERih 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  870 ----------SP--KEFLQLLVKEKVTVLN-----QTPSAFYQLMQADRENEEVGQKlsLRYVVFGGEALELSRLEdwYS 932
Cdd:PLN02430   328 egiqkalqelNPrrRLIFNALYKYKLAWMNrgyshKKASPMADFLAFRKVKAKLGGR--LRLLISGGAPLSTEIEE--FL 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  933 RHPHNApKVINMYGITETTVHVSYIELDE----SIVSLRA--NSLIGCSIPDLKVYVLDNylqpvPPgvVGEMYVAGAGL 1006
Cdd:PLN02430   404 RVTSCA-FVVQGYGLTETLGPTTLGFPDEmcmlGTVGAPAvyNELRLEEVPEMGYDPLGE-----PP--RGEICVRGKCL 475

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1007 ARGYLGRAGLTAErFIADPFgkpgtrmYRTGDLARWRQDGTLDYIGRADHQIKI-RGFRIELGEIEAVIMKHDKVEQVAV 1085
Cdd:PLN02430   476 FSGYYKNPELTEE-VMKDGW-------FHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWV 547

                          410       420
                   ....*....|....*....|....*
gi 1698252301 1086 IvredqpGD--KRLVAYIVASNNET 1108
Cdd:PLN02430   548 Y------GDsfKSMLVAVVVPNEEN 566
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1-77 3.32e-05

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 48.57  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAeeKEPINLS-----EIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:COG0365    460 LVSHPAVAEAAVVGVPDEIRGQVVKAFVVL--KPGVEPSdelakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537


                   ..
gi 1698252301   76 KL 77
Cdd:COG0365    538 LL 539
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 752-858 3.71e-05

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: 48.12  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  752 IECDESLKILVDDVNVMEEIEKYSEENIDE--MECLKPLAPSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQF 829
Cdd:cd05933    109 IQYKEPLKEKEPNLYSWDEFMELGRSIPDEqlDAIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDL 188

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1698252301  830 D-ADDVWTMFHSYaFDFS-----VWEIWGPLLYGG 858
Cdd:cd05933    189 RpATVGQESVVSY-LPLShiaaqILDIWLPIKVGG 222
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1-75 3.92e-05

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 47.96  E-value: 3.92e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:PRK05852   450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 790-1085 5.51e-05

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 47.71  E-value: 5.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  790 PSHIAYVIYTSGSTGRPKGVMIPHQNVVRLLGATDHWFQ-----FDADDVWTMFHSYA--FDFSVWEIWgpLLYGGRLVV 862
Cdd:PLN02614   222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGF 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  863 VPHTVsrspKEFLQLLVKEKVTVLNQTPSAFyqlmqaDRENEEVGQKLS----LRYVVF-------------GGEALELS 925
Cdd:PLN02614   300 WRGDV----KLLIEDLGELKPTIFCAVPRVL------DRVYSGLQKKLSdggfLKKFVFdsafsykfgnmkkGQSHVEAS 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  926 RLED--WYSRHPHN------------AP---------------KVINMYGITETTVHvSYIELDESIVSLranSLIGCSI 976
Cdd:PLN02614   370 PLCDklVFNKVKQGlggnvriilsgaAPlashvesflrvvaccHVLQGYGLTESCAG-TFVSLPDELDML---GTVGPPV 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  977 PDlkvyvLDNYLQPVP--------PGVVGEMYVAGAGLARGYLGRAGLTAERFIADpfgkpgtrMYRTGDLARWRQDGTL 1048
Cdd:PLN02614   446 PN-----VDIRLESVPemeydalaSTPRGEICIRGKTLFSGYYKREDLTKEVLIDG--------WLHTGDVGEWQPNGSM 512

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1698252301 1049 DYIGRADHQIKI-RGFRIELGEIEAVIMKHDKVEQVAV 1085
Cdd:PLN02614   513 KIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWV 550
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 1-77 5.77e-05

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 47.74  E-value: 5.77e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYV-SESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK13295   461 LYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 1-76 7.58e-05

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 47.30  E-value: 7.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVV--MVREDrpNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKK 76
Cdd:PRK05605   487 LREHPGVEDAAVvgLPRED--GSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 1-77 9.37e-05

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: 46.98  E-value: 9.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIV--AEEKEPINL-SEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05959    428 LVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrPGYEDSEALeEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 4-77 9.39e-05

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: 46.90  E-value: 9.39e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1698252301    4 HENIQQAVVMVREDRPNDKRIIAYIVAEE-KEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05941    366 HPGVSECAVIGVPDPDWGERVVAVVVLRAgAAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 1-77 1.28e-04

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 46.56  E-value: 1.28e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK06710   473 LYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 1-74 1.29e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 46.31  E-value: 1.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEkepiNLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:PRK07638   403 LHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA----TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 1-77 1.33e-04

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: 46.31  E-value: 1.33e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVRedrpNDKRIIAYIVAEEKEpinlSEIRSYV-SESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd17654    380 IESCLGVESCAVTLS----DQQRLIAFIVGESSS----SRIHKELqLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
1-77 1.41e-04

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 46.39  E-value: 1.41e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK06839   413 INKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 669-845 1.52e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 46.37  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  669 LTYEKLNRKANKIARFLIAKGVGPDQLVALAMPRSLNMVVSLLAVLKAGAGYLPLDPDYPSDRISFMLHDAKPSCVLTNS 748
Cdd:PLN02861    78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301  749 S-------VEIECDESLKILVDDVNVMEEIEKYSEE------------NIDEMEC-LKPLAPSHIAYVIYTSGSTGRPKG 808
Cdd:PLN02861   158 SkissilsCLPKCSSNLKTIVSFGDVSSEQKEEAEElgvscfsweefsLMGSLDCeLPPKQKTDICTIMYTSGTTGEPKG 237

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1698252301  809 VMIPHQNVVRLLGATDHWFqFDADDVWTMFHSYaFDF 845
Cdd:PLN02861   238 VILTNRAIIAEVLSTDHLL-KVTDRVATEEDSY-FSY 272
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 787-817 2.75e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 45.48  E-value: 2.75e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1698252301  787 PLAPSHIAYVIYTSGSTGRPKGVMIPHQNVV 817
Cdd:PLN02736   217 PPKPEDVATICYTSGTTGTPKGVVLTHGNLI 247
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 26-77 3.08e-04

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 45.18  E-value: 3.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1698252301   26 AYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK09088   428 LAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
PRK08315 PRK08315
AMP-binding domain protein; Validated
 1-77 4.68e-04

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 44.80  E-value: 4.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQA-VVMVredrPNDK---RIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKK 76
Cdd:PRK08315   469 LYTHPKIQDVqVVGV----PDEKygeEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFK 544


                   .
gi 1698252301   77 L 77
Cdd:PRK08315   545 M 545
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 1-77 4.84e-04

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 44.65  E-value: 4.84e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVlEELPLTPNGKVDRKKL 77
Cdd:PRK06178   484 LGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRIV-DALPMTATGKVRKQDL 559
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 1258-1393 6.29e-04

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.85  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1258 LFCVHpagGLSWCYAGLMKSLGTDYPIYGVQARGIAENEELPKSLEEmAADYLKHVREIQPHGPYRLLGWSLGGNVVHAM 1337
Cdd:pfam12697    1 VVLVH---GAGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLAD-LADLAALLDELGAARPVVLVGHSLGGAVALAA 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301 1338 AAQLQNEGeevellVMLDSYPGHFLPNTEAPTEEEALIALLALGGYDPDNMDGKPL 1393
Cdd:pfam12697   77 AAAALVVG------VLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGF 126
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 1-77 6.56e-04

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: 43.91  E-value: 6.56e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVS-ESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05903    358 LLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 10-77 1.09e-03

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 43.34  E-value: 1.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301   10 AVVMVREDRPNDkRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK06145   425 AVIGVHDDRWGE-RITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 760-815 1.30e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 43.55  E-value: 1.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301  760 ILVDDVnVMEEIEKYSEENIDemeclkplaPSHIAYVIYTSGSTGRPKGVMIPHQN 815
Cdd:PTZ00342   283 ILFDDM-TKNKTTNYKIQNED---------PDFITSIVYTSGTSGKPKGVMLSNKN 328
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1-77 1.96e-03

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 42.81  E-value: 1.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIV-AEEKEPINLSEIRSYVSES-LANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK06087   452 LLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 1-77 1.99e-03

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: 42.50  E-value: 1.99e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKePINLSEIRSYVSES-LANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05923    417 LSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 1-77 2.33e-03

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: 42.08  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVA---EEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05958    359 LLQHPAVAECAVVGHPDESRGVVVKAFVVLrpgVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 1-77 2.60e-03

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: 42.03  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIV---AEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05971    358 LLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 1258-1358 2.61e-03

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 41.34  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1258 LFCVHPAGGLSWCYAGLMKSLGTDYPIYGVQARGIAENEEL-PKSLEEMAADYLKHVREiqphgPYRLLGWSLGGNVVHA 1336
Cdd:TIGR01738    7 LVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFgPLSLADMAEAIAAQAPD-----PAIWLGWSLGGLVALH 81

                           90       100
                   ....*....|....*....|..
gi 1698252301 1337 MAAQLQnegEEVELLVMLDSYP 1358
Cdd:TIGR01738   82 IAATHP---DRVRALVTVASSP 100
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1-79 2.68e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 42.29  E-value: 2.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPA 79
Cdd:PRK13383   438 LAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 1-74 3.10e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 42.07  E-value: 3.10e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDR 74
Cdd:PRK12583   470 LFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 1-72 3.52e-03

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: 41.33  E-value: 3.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1698252301    1 LQRHENIQQ-AVVMVREDRPNDKRIiAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKV 72
Cdd:cd17638    257 LAEHPGVAQvAVIGVPDERMGEVGK-AFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 1-77 3.57e-03

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 41.90  E-value: 3.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAfVVLEELPLTPNGKVDRKKL 77
Cdd:cd12118    409 LYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKT-VVFGELPKTSTGKIQKFVL 484
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 10-77 3.69e-03

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 41.73  E-value: 3.69e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1698252301   10 AVVMVREDRPNDKrIIAYIVAEEKEpINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:PRK12492   493 AAIGVPDERSGEA-VKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 8-86 4.71e-03

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 41.51  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301    8 QQAVVMVredrPNDK---RIIAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLPAPDFNG 84
Cdd:PRK06188   443 QVAVIGV----PDEKwgeAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWEG 518


                   ..
gi 1698252301   85 MN 86
Cdd:PRK06188   519 RG 520
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 23-78 4.80e-03

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 41.13  E-value: 4.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1698252301   23 RIIAyIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKLP 78
Cdd:PRK07445   388 VVTA-IYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 25-75 5.26e-03

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 41.18  E-value: 5.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1698252301   25 IAYIVAEEKEPINLSEIRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRK 75
Cdd:PRK07470   460 VAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 1257-1480 7.90e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 39.80  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1257 PLFCVH--PAGGLSWCyaGLMKSLG-TDYPIYGVQARGIAENEElPKSLEEMA----ADYLKHVREIQPHGPYRLLGWSL 1329
Cdd:pfam00561    2 PVLLLHglPGSSDLWR--KLAPALArDGFRVIALDLRGFGKSSR-PKAQDDYRtddlAEDLEYILEALGLEKVNLVGHSM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1330 GGNVVHAMAAQLQN----------------EGEEVELLVM-----LDSYPGHFLPNTEAPTEEealiALLALGGYDPDNM 1388
Cdd:pfam00561   79 GGLIALAYAAKYPDrvkalvllgaldppheLDEADRFILAlfpgfFDGFVADFAPNPLGRLVA----KLLALLLLRLRLL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698252301 1389 DGKPLTMESAVEilrkDGSALASLEEETILNLKETYvnSVGLLGKYVPKvYNGDILFFRSTvipdwFDPISPNTWLNYLD 1468
Cdd:pfam00561  155 KALPLLNKRFPS----GDYALAKSLVTGALLFIETW--STELRAKFLGR-LDEPTLIIWGD-----QDPLVPPQALEKLA 222

                          250
                   ....*....|....*.
gi 1698252301 1469 GDI----VQHDIDCRH 1480
Cdd:pfam00561  223 QLFpnarLVVIPDAGH 238
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 1-77 9.51e-03

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: 40.15  E-value: 9.51e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698252301    1 LQRHENIQQAVVMVREDRPNDKRIIAYIVAEEKEPINLSE--IRSYVSESLANYMIPSAFVVLEELPLTPNGKVDRKKL 77
Cdd:cd05935    352 LYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEedIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
 
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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