|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1048-1622 |
0e+00 |
|
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: 786.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1048 LYTLLNCRGTIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIA 1126
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1127 TTLPTVKMivEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA-----QIYKPSNPDTLAYLDFSV 1201
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1202 STTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAV 1281
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1282 SQYKVRDTFCSYSVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGCRV 1361
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1362 NLAICLqphrlwtlaeQGTSGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHL 1441
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1442 GEIWVHSAHNASGYFTIYGDESLQSDHFNS-RLSFGDTQTIWARTGYLGFLRRTELTDANGERHDALYVVGALDEAMELR 1520
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1521 GMRYHPIDIETSVIRAHKSVTECAVFTWTNLLVVVVELD-GSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINS 1599
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 1958706127 1600 RGEKQRMHLRDGFLADQLDPIYV 1622
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
392-968 |
0e+00 |
|
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: 737.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 392 CLTTMDTNGKPLYILTYGKLWTRSMKVAYNILHKLGTKqepmvrPGDRVALVFPnnDPAAFMVAFYGCLLAEVVPVPIEV 471
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLK------PGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 472 PLtrkdaGSQQIGFLLGSCGVTVALTSDACHKGLPKS-----PTGEIPQFKGWPKLLWFVTESKHLSKPPRDWFPHIKDA 546
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 547 NNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYALM 626
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 627 KVNPLSWIQKVCQYKAKVACVKSRDMHWAL------VAHRDQRDVNLSSLRMLIVADGaNPWSISSCDAFLNVFQSKGLR 700
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 701 QEvicpcASSPEALTVAIRRPTD--DSNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQDVGLVMPGAIMCSVKPDGVP 778
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWqgTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 779 qLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEVFPMTSSGAPISEYPFIRTGLLGFVGPG----------GLVFVVGK 848
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 849 MDGLMVVSGRRHNADDIVATALAVEPmkfvYRGRIAVFSVTvlhdERIVIVAEQRPDStEEDSFQWMSRVLQAIDSIHQV 928
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPPGS-EEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1958706127 929 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHPCNV 968
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1038-1580 |
2.09e-69 |
|
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: 244.46 E-value: 2.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1038 WRAQTTPDHLLYTLLNCRGTIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITV 1117
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1118 RPPHPqniATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSnPDTLAYL 1197
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1198 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALW 1277
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1278 LLAVSQYkvRDTFcsySVM-----ELCTKglgsQTESLKARGLDLSRVRTCVVVAEeRPRIALTQSFSKLFKDLGLHPRA 1352
Cdd:cd05931 235 LRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFRPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1353 VSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVRII 1426
Cdd:cd05931 305 FRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1427 IANPETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRLSFGDtqTIWARTGYLGFLRRteltdanGErhda 1506
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDE--GGWLRTGDLGFLHD-------GE---- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1507 LYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTW----TNLLVVVVELDGSeQEALDLVPLVTNV---VL 1577
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVA 510
|
...
gi 1958706127 1578 EEH 1580
Cdd:cd05931 511 REH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
406-959 |
8.36e-60 |
|
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: 216.34 E-value: 8.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAYNILHKLgtkqepmvRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPLTRKDAgsQQIGF 485
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVG--------KPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPPPTPGRHA--ERLAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 486 LLGSCGVTVALTSDACHKGLPKSptgeIPQFKGWPKLLWFVTESKHLSkPPRDWFPHIKDANnDTAYIEYKTCKDGSVLG 565
Cdd:cd05931 93 ILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPPPSPDPD-DIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 566 VTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISI-PYALMKvNPLSWIQKVCQYKAKV 644
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 645 ACVKsrDMHWALVAHR----DQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIR 719
Cdd:cd05931 246 SAAP--NFAYDLCVRRvrdeDLEGLDLSSWRVALN--GAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 720 RPtddsNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQdVGLVMPG---AIMCsvkPDGVpQLCRTDEIGELCVC--AV 794
Cdd:cd05931 322 PP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDqevRIVD---PETG-RELPDGEVGEIWVRgpSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 795 ATGtsYYGLSGMTKNTFEVFpmtssgAPISEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEP 874
Cdd:cd05931 393 ASG--YWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 875 MkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSET 954
Cdd:cd05931 464 A--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRAC 541
|
....*
gi 1958706127 955 KQLFL 959
Cdd:cd05931 542 RAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1036-1520 |
5.82e-57 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 204.08 E-value: 5.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1036 LQWRAQTTPDHLLYTllNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPI 1115
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGR---RLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1116 TVRPphpqniATTLPTVKMIVEVSRSACLMTTQlICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSN----- 1190
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDD-ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1191 ------PDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCE----LYPSREVAICLDPYCGLGFVLWCLCSVYSGH 1260
Cdd:pfam00501 148 pppppdPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1261 QSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSVMELCtkglgsqTESLKARGLDLSRVRTCVVVAeERPRIALTQSFS 1340
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1341 KLFkdlglhPRAVSTSFGcrvnlaiclqphrlwtLAEqgTSGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 1420
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDEDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1421 PGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDAN 1500
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 1958706127 1501 GErhdaLYVVGALDEAMELR 1520
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1193-1567 |
3.20e-38 |
|
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: 147.05 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1193 TLAYLDFSVSTTGMLAGVKMSH---AATSAFCRSIKlqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSe 1269
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnlLAAAAALAASG----GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1270 letNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPrIALTQSFSKLfkdlglh 1349
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1350 pravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVRIIIAN 1429
Cdd:cd04433 138 -------PGIKL--------VNGYGLTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1430 PETkGPLGDSHLGEIWVHSAHNASGYFTiygdeslqsdhfNSRLSFGDTQTIWARTGYLGFLrrteltDANGErhdaLYV 1509
Cdd:cd04433 184 PDG-GELPPGEIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------DEDGY----LYI 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958706127 1510 VGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 1567
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1032-1562 |
5.15e-35 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 147.24 E-value: 5.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1032 LSEVLQWRAQTTPDHLLYTLLNCRGTIANSLTCVQLHKRAEKIAVMLMERGHLqdGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1112 CV------PITVRPPHPQNIATtlptvkmIVEVSRSACLMTTQLICKLLRSREAAAAVDVrtwPLILDTDDLPKKRPAQI 1185
Cdd:PRK05691 89 VIavpaypPESARRHHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1186 YKPS-NPDTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsiklqCELYPSREVAICLDP----------YCGLGFVLWCLC 1254
Cdd:PRK05691 159 QEPAlQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1255 SVYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGsqtESLKARgLDLSRVRtcVVVAEERP-RI 1333
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVS---ESALER-LDLSRWR--VAYSGSEPiRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1334 ALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHDRVRLVErGS 1407
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-GS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1408 phslPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgDTQTiWARTGY 1487
Cdd:PRK05691 368 ----VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGY---WRNPEASAKTFVEH----DGRT-WLRTGD 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958706127 1488 LGFLRRTEltdangerhdaLYVVGALDEAMELRGMRYHPIDIETSVIRahksvtECAVFTWTNLLVVVVELDGSE 1562
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1035-1576 |
1.59e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 135.07 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1035 VLQWRAQTTPDHLLYTLLNCR---GTIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1112 CVPITVRPPHPQN--------IATTLPTVkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA 1183
Cdd:PRK05850 84 LIAVPLSVPQGGAhdervsavLRDTSPSV-----------VLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1184 QIYKPSNPDTlAYLDFSVSTTGMLAGVKMSHAATSAFCRsiKLQCELYPSREVAICLD-------P-YCGLGFVLWCLCS 1255
Cdd:PRK05850 153 DARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1256 VYSGHQSILIPPSELETNPALW--LLAVSQYkvrdtfcSYSV-----MELCTKglgsQTESLKARGLDLSRVRTcVVVAE 1328
Cdd:PRK05850 230 ILGGCPAVLTSPVAFLQRPARWmqLLASNPH-------AFSAapnfaFELAVR----KTSDDDMAGLDLGGVLG-IISGS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1329 ERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAE------QGTSGPDPTTVYVDMRALRHDRVR- 1401
Cdd:PRK05850 298 ERVHPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEKLSAGHAKr 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1402 --------LVERGSPHSlplmesgkilPGVRIIiaNPETKGPLGDSHLGEIWVHSAHNASGYFTiyGDESLQSDhFNSRL 1473
Cdd:PRK05850 362 cetgggtpLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAAGYWQ--KPEETERT-FGATL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1474 ---SFGDTQTIWARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVirahKSVT--ECAVFT- 1547
Cdd:PRK05850 427 vdpSPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATI----QEITggRVAAISv 491
|
570 580 590
....*....|....*....|....*....|....*
gi 1958706127 1548 ---WTNLLVVVVEL---DGSEQEALDLVPLVTNVV 1576
Cdd:PRK05850 492 pddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1032-1569 |
2.73e-31 |
|
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: 129.16 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1032 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:COG0318 1 LADLLRRAAARHPDR---PALVFGGR---RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1112 CVPITVrpphpqNIATTLPTVKMIVEVSRSACLMTtqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnp 1191
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1192 dtlAYLDFSvS-TTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPpsel 1270
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1271 ETNPALWLLAVSQYKVrdTFCSYS---VMELCtkglgsqtESLKARGLDLSRVRTCVVVAEerpriALTQSFSKLFKDLg 1347
Cdd:COG0318 175 RFDPERVLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1348 lhpravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVRIII 1427
Cdd:COG0318 239 ---------FGVRI--------VEGYGLTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRI 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1428 ANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLqsdhfnSRLSFGDTqtiWARTGYLGFLrrteltDANGErhdaL 1507
Cdd:COG0318 283 VDEDGR-ELPPGEVGEIVVRGPNVMKGY---WNDPEA------TAEAFRDG---WLRTGDLGRL------DEDGY----L 339
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958706127 1508 YVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLVVVVEL-DGSEQEALDLV 1569
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
373-961 |
6.88e-31 |
|
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: 129.71 E-value: 6.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 373 PPSLEAALQRWGTISPKAPClTTMDTNGKPlYILTYGKLWTRsmkvAYNILHKLGTKQepmVRPGDRVALVFPNNDpaAF 452
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSE-EFQSYQDLLED----ARRLAAGLRQLG---LRPGDSVILQFDDNE--DF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 453 MVAFYGCLLAEVVPVPIEVPLTRKDAGSQ-----QIGFLLGSCgvtVALTSDACHKGLpksptgeIPQFKGWPKLLWFVT 527
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSP---VVLTDAELVAEF-------AGLETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 528 ESKHLSKPPRDWFPHIKDAnNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHG 607
Cdd:cd05906 148 SIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 608 ILTSVMNMMHVISIPYALMKVNPLSWIQKVCQYKAKV------ACVKSRDmhwaLVAHRDQRDVNLSSLRMLIVADGANp 681
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 682 wSISSCDAFLNVFQSKGLRQEVICPCASSPEalTVAirrptddsnqppgrgvlsmhGLTYGviRVDSEEKLS-VLTVQDV 760
Cdd:cd05906 302 -VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS--------------------GVIYS--RSFPTYDHSqALEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 761 GLVMPGAIMCSVKPDGvpQLCRTDEIGELCVCavatGTS----YYGLSGMTKNTFevfpmTSSGapiseypFIRTGLLGF 836
Cdd:cd05906 357 GRPIPGVSMRIVDDEG--QLLPEGEVGRLQVR----GPVvtkgYYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 837 VGPGGLVFvVGKMDGLMVVSGRRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHD--ERIVIVAeqrpdSTEEDSFQW 914
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFF-----VPEYDLQDA 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1958706127 915 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHLSETKQLFLEG 961
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
376-963 |
2.61e-29 |
|
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: 123.38 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 376 LEAALQRWGTISPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVA 455
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS--PEFVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 456 FYGCLLAEVVPVPIEVPLTRKdagsqQIGFLLGSCGVTVALTSDACH----KGLPKsptgeipqfkgwpkllwfvteskh 531
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 532 lskpprdwfphikdanndtayieyktckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTS 611
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 612 VMNMMHVISIPyalmKVNPLSWIQKVCQYKA-KVACVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAF 690
Cdd:COG0318 164 LLAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 691 LNVFQSkglrqeVICPC-ASSpEALTVAIRRPTDDSNQPPGRgvlsmhgltygvirvdseeklsvltvqdVGLVMPGAIM 769
Cdd:COG0318 236 EERFGV------RIVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 770 CSVKPDGVPqlCRTDEIGELCVC--AVATGtsYYGLSGMTKNTFEVfpmtssgapiseyPFIRTGLLGFVGPGGLVFVVG 847
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVVRgpNVMKG--YWNDPEATAEAFRD-------------GWLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 848 KMDGLMVVSGRRHNADDIVATALAVEPMKfvyrgRIAVFSVTV-LHDERIV--IVAEQRPDSTEEDSFQWMSRVL---QA 921
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1958706127 922 IDSIHQVGvyclalvpanTLPKTPLGGIHLSETKQLFLEGSL 963
Cdd:COG0318 419 PRRVEFVD----------ELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
406-965 |
1.25e-28 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 123.19 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAYNILhKLGtkqepmVRPGDRVALVfPNNDPAaFMVAFYGCLLAEVVPVPIEVP--LTRKDAGSQQI 483
Cdd:PRK09192 50 LPYQTLRARAEAGARRLL-ALG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 484 GFLLGSCGVTVALTSDACHKGLPKSPTGEIPQFKGWPKLLwfvteskHLSKPPRDWFPHIKDanNDTAYIEYKTckdGSV 563
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWF-------KALPEADVALPRPTP--DDIAYLQYSS---GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 564 ---LGVTVTRIALLTHCQALTQ-ACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYALMKVNPLSWIQKVCQ 639
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 640 YKAKVAcvKSRDMHWALVAHR----DQRDVNLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlT 715
Cdd:PRK09192 269 NRGTIS--YSPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 716 VAIrrptddSNQPPGRGV----LSMHGLTYGVIRVDSEEK-LSVLTVQDVGLVMPGAIMCSVKPDG--VPQLcrtdEIGE 788
Cdd:PRK09192 344 LAV------SFSPLGSGIvveeVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGmpLPER----VVGH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 789 LCVcavatgtsyYGLSGMTkntfEVFPMTSSGAPISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVAT 868
Cdd:PRK09192 414 ICV---------RGPSLMS----GYFRDEESQDVLAADGWLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 869 AlavEPMKFVYRGRIAVFSVTVLHDERIVIVAEQRPdSTEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLG 947
Cdd:PRK09192 480 A---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSG 553
|
570
....*....|....*...
gi 1958706127 948 GIHLSETKQLFLEGSLHP 965
Cdd:PRK09192 554 KLSRAKAKKRYLSGAFAS 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
435-963 |
1.18e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 117.52 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 435 RPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPltrKDAG-SQQIGFLLGSCGVTVALTSDACHKGLPKSptgei 513
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP---AEPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKF----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 514 pqFKGWPKllwfvteskhlSKPPR-------------DWFPhiKDANNDT-AYIEYKTckdGSV---LGVTVTRIALLTH 576
Cdd:PRK07769 147 --FRARPA-----------KERPRviavdavpdevgaTWVP--PEANEDTiAYLQYTS---GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 577 CQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNmmHVISI--PYALMKvNPLSWIQKVCQYKAKVACVKSRDMHW 654
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 655 A--LVAHR-----DQRDVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEALTVAIRRPTDDSNQ 727
Cdd:PRK07769 286 AfeHAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 728 ppgrgvlsmhgltygVIRVDSEEkLSVLTVQDVGLVMPGAI-------------MCSVKPDGVPQLcRTDEIGELCVCAV 794
Cdd:PRK07769 364 ---------------VIYVDRDE-LNAGRFVEVPADAPNAVaqvsagkvgvsewAVIVDPETASEL-PDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 795 ATGTSYYGLSGMTKNTFE------VFPMTSSGAPiSEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVAT 868
Cdd:PRK07769 427 NIGTGYWGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 869 ALavEPMKFVYRGRIAVFSV-------TVLHD-------------ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQV 928
Cdd:PRK07769 505 AQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGV 582
|
570 580 590
....*....|....*....|....*....|....*
gi 1958706127 929 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSL 963
Cdd:PRK07769 583 TVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1059-1540 |
1.40e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 114.07 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1059 ANSLTCVQLHKRAEKIAVMLMErgHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNIATTLPTVkmiVEV 1138
Cdd:PRK12476 66 AVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTA---LRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1139 SRSACLMTTQLICKLLRSREAAAAVDVRtwPLILDTDDLPKkRPAQIYKPSNPDT--LAYLDFSVSTTGMLAGVKMSHAA 1216
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPD-SAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1217 TSA----FCRSIKLqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHqSILIPPSELETNPALWLLAVSQ-YKVRDTFC 1291
Cdd:PRK12476 218 VGTnlvqMILSIDL---LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1292 SYS--VMELCT-KGLGSQTEslkarGLDLSRVrtCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclq 1368
Cdd:PRK12476 294 AAPnfAYEWAAqRGLPAEGD-----DIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG---------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1369 phrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLG 1442
Cdd:PRK12476 357 ------IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1443 EIWVHSAHNASGYFTiYGDESLQSDH--FNSRLSFG------DTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGALD 1514
Cdd:PRK12476 431 EIWLHGDNIGRGYWG-RPEETERTFGakLQSRLAEGshadgaADDGTWLRTGDLGVYL-------DGE----LYITGRIA 498
|
490 500
....*....|....*....|....*.
gi 1958706127 1515 EAMELRGMRYHPIDIETSVIRAHKSV 1540
Cdd:PRK12476 499 DLIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1036-1540 |
1.20e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 111.36 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1036 LQWRAQTTPDHLLYTLLNC---RGTIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAGC 1112
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDFsteRDGVARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1113 VPITVRPPHPQNIATTLPTVkmIVEVSRSACLMTT---QLICKLLRSREAAAAvdvrtwPLILDTDDLPKKRPAQIYKPS 1189
Cdd:PRK07769 105 IAVPLFDPAEPGHVGRLHAV--LDDCTPSAILTTTdsaEGVRKFFRARPAKER------PRVIAVDAVPDEVGATWVPPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1190 -NPDTLAYLDFSVSTTGMLAGVKMSH--AATSAF--CRSIKLQcelYPSREVAiCLDPYCGLGFVLWCLCSVYSGHQSIL 1264
Cdd:PRK07769 177 aNEDTIAYLQYTSGSTRIPAGVQITHlnLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1265 IPPSELEtNPALWLLAVSQyKVRDTFCSYSV-----MELCT-KGLGSQTESlkarGLDLSRVRtCVVVAEERPRIALTQS 1338
Cdd:PRK07769 253 SPAAFVR-RPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNGSEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1339 FSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLP 1412
Cdd:PRK07769 326 FNEAFAPYGLPPTAIKPSYG----------------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1413 LMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYG--DESLQSDH--FNSRLSFGDTQ-----TIWA 1483
Cdd:PRK07769 390 QVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGY---WGkpEETAATFQniLKSRLSESHAEgapddALWV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958706127 1484 RTGYLGflrrtelTDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSV 1540
Cdd:PRK07769 467 RTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1018-1565 |
1.78e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 110.09 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1018 DNDQARKvRTEFLFLSEVLQWRAQTTPDHLLYTLlncRGTIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPG 1097
Cdd:PRK09192 10 TSSLPRR-YADFPTLVEALDYAALGEAGMNFYDR---RGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1098 IDLIAAFYGCLYAGCVPITVrpPHPQNI---ATTLPTVKMIVEVSRSACLMTTQLICKLLrsREAAAAVDVRtWPLILDT 1174
Cdd:PRK09192 85 GDFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLL-HVLSHAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1175 DDLPKKRPAQIYKPSnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQ-CELYPSREVAICLDPYCGLGFVlWCL 1253
Cdd:PRK09192 160 FKALPEADVALPRPT-PDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGLV-GFL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1254 CSVYSGHQSI-LIPPSELETNPALWLLAVSqyKVRDTFcSYSV---MELCTKGLGSQTESlkarGLDLSRVRTCVVVAEE 1329
Cdd:PRK09192 238 LTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGADM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1330 -RPRIalTQSFSKLFKDLGLHPRAVSTSFG-CRVNLAICLQPHrlwtlaEQGtsgpdpttvyvdMRALRHDRVRLVERGs 1407
Cdd:PRK09192 311 iRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPL------GSG------------IVVEEVDRDRLEYQG- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1408 pHSLPLMES----------GKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESlqsdhfnsrlsfgD 1477
Cdd:PRK09192 370 -KAVAPGAEtrrvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYF---RDEE-------------S 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1478 TQTI----WARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSV-----IRAHksvtECAVFTW 1548
Cdd:PRK09192 432 QDVLaadgWLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqepeLRSG----DAAAFSI 496
|
570 580
....*....|....*....|.
gi 1958706127 1549 TN----LLVVVVELDGSEQEA 1565
Cdd:PRK09192 497 AQengeKIVLLVQCRISDEER 517
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1032-1555 |
2.13e-24 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 109.68 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1032 LSEVLQWRAQTTPDHLLYTllncrgtIANSLTCV-----QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYG 1106
Cdd:cd05906 12 LLELLLRAAERGPTKGITY-------IDADGSEEfqsyqDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1107 CLYAGCVPITVRPPHP-QNIATTLPTVKMIVEVSRSA-CLMTTQLICKLLRSREAA--AAVDVRTWPLILDTDDLPKKRP 1182
Cdd:cd05906 84 CVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPvVLTDAELVAEFAGLETLSglPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1183 AQiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSiKLQCELYPSREVA---ICLDPYCGLGFVlwCLCSVYSG 1259
Cdd:cd05906 164 SR------PDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1260 HQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSvmeLCTKgLGSQTESLKARGLDLSRVRtCVVVAEERPRIALTQSF 1339
Cdd:cd05906 235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1340 SKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQGtSGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKI 1419
Cdd:cd05906 310 LRLLEPYGLPPDAIRPAFG----------------MTETC-SG---VIYSRSFPTYDH----------SQALEFVSLGRP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1420 LPGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltda 1499
Cdd:cd05906 360 IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFLD------- 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958706127 1500 NGErhdaLYVVGALDEAMELRGMRYHPIDIETSV----IRAHKSVTECAVF---TWTNLLVVV 1555
Cdd:cd05906 421 NGN----LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRdpgAETEELAIF 479
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
399-961 |
2.16e-24 |
|
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: 109.11 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 399 NGKPLYIlTYGKLWTrsmkvayNILHKLGTKQEPMVRPGDRValVFPNNDPAAFMVAFYGCLLAEVVPVPievpltrkda 478
Cdd:cd05908 10 DKKEKFV-SYRHLRE-------EALGYLGALQELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVP---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 479 gsqqigfllgscgvtVALTSDACHKglpksptgeIPQFKGWPKLL--WFVTESKHLSKPPrdwfphikdanNDTAYIEYK 556
Cdd:cd05908 70 ---------------VSIGSNEEHK---------LKLNKVWNTLKnpYLITEEEVLCELA-----------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 557 TCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYALMKVNPLSWIQK 636
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 637 VCQYKAKVACVKSRDMHWALVAHRDQR--DVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAl 714
Cdd:cd05908 195 ASEHKATIVSSPNFGYKYFLKTLKPEKanDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 715 TVAIRRPTDDSNQPPgrgvLSMH--GLTYG--VIRVDSEEKlSVLTVQDVGLVMPgaiMCSVK-PDGVPQLCRTDEIGEL 789
Cdd:cd05908 272 SVGASLPKAQSPFKT----ITLGrrHVTHGepEPEVDKKDS-ECLTFVEVGKPID---ETDIRiCDEDNKILPDGYIGHI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 790 CVCAVATGTSYYGLSGMTKNTfevfpMTSSGapiseypFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATA 869
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKV-----FTDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIA 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 870 LAVEPmkfVYRGRIAVFSV--TVLHDERIVIVAEQRpdsTEEDSFQWMSRVLQAID------SIHQVgvyclalVPANTL 941
Cdd:cd05908 411 EELEG---VELGRVVACGVnnSNTRNEEIFCFIEHR---KSEDDFYPLGKKIKKHLnkrggwQINEV-------LPIRRI 477
|
570 580
....*....|....*....|
gi 1958706127 942 PKTPLGGIHLSETKQLFLEG 961
Cdd:cd05908 478 PKTTSGKVKRYELAQRYQSG 497
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
380-856 |
1.56e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 105.47 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 380 LQRWGTISPKAPCLTTMDTngkplYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGC 459
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG-----RRLTYRELDERANRLA-AGLRALG------VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 460 LLAEVVPVPIEVpltrkDAGSQQIGFLLGSCGVTVALTSD--------ACHKGLPKSPTGEIPQFKGWPKLLWFVTESKH 531
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 532 LSKPPRdwfPHIKDANNDTAYIEY--------KtckdgsvlGVTVTRIALLTHCQALTQAC----GYTEAETIVNVLDFK 599
Cdd:pfam00501 142 ADVPPP---PPPPPDPDDLAYIIYtsgttgkpK--------GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 600 KDVGLWHGILTSVMNMMHVISIPYALMKvNPLSWIQKVCQYKAKVACVKSRDMHwALVAHRDQRDVNLSSLRMLIVadGA 679
Cdd:pfam00501 211 HDFGLSLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERYKVTVLYGVPTLLN-MLLEAGAPKRALLSSLRLVLS--GG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 680 NPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptddsnqppGRGVLSMHGLT--YGVIRVDSEEKLSVLTV 757
Cdd:pfam00501 287 APLPPELARRFRELF-----------------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 758 QDVGLVMPGAIMCSVKPDGVpQLCRTDEIGELCV--CAVATGtsYYGLSGMTKNTFEvfpmtssgapisEYPFIRTGLLG 835
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCVrgPGVMKG--YLNDPELTAEAFD------------EDGWYRTGDLG 396
|
490 500
....*....|....*....|.
gi 1958706127 836 FVGPGGLVFVVGKMDGLMVVS 856
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
375-949 |
3.41e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.18 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 375 SLEAALQRWGTISPKAPCLTTMDTNGKPLYI---LTYGKLWTRSMKVAYNiLHKLGtkqepmvRPGDRVALVFPNNdpAA 451
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIDYEQDPAGVaetLTWSQLYRRTLNVAEE-LRRHG-------STGDRAVILAPQG--LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 452 FMVAFYGCLLAEVVPVPIEVPLTRkdAGSQQIGFLLGSCGVTVALTS----DACHKGLPKSPTGEIPqfkgwpkllWFVT 527
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQSAP---------PVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 528 ------ESKHLSKPPRDWFPhikdannDTAYIEYKTCKDGSVLGVTVTRIALLTHC-QALTQACGYTEAE-----TIVNV 595
Cdd:PRK05850 141 vdlldlDSPRGSDARPRDLP-------STAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 596 LDFKKDVGLWHGILTSVMNMMH-VISIPYALMKvNPLSWIQKVCQYKAKVACVKSrdmhWAL-VAHRDQRDVNLSSL--- 670
Cdd:PRK05850 214 LPFYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQLLASNPHAFSAAPN----FAFeLAVRKTSDDDMAGLdlg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 671 RMLIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIRRPtddsNQPPGrgvlsmhgltygVIRVDSE 749
Cdd:PRK05850 289 GVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP----GQPPE------------SVRFDYE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 750 eKLSVLTVQ----DVG--LVMPGAIMCS----VKPDGVPQlCRTDEIGELCVCA--VATGtsYYGLSGMTKNTFE---VF 814
Cdd:PRK05850 353 -KLSAGHAKrcetGGGtpLVSYGSPRSPtvriVDPDTCIE-CPAGTVGEIWVHGdnVAAG--YWQKPEETERTFGatlVD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 815 PmtSSGAPISeyPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalavepMKFVYRGRIAVFSVTVLHDE 894
Cdd:PRK05850 429 P--SPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTE 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 895 RIVIVAE-QRPDSTEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 949
Cdd:PRK05850 498 KLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1066-1545 |
4.38e-23 |
|
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: 103.88 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1066 QLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITvrPPHPQN-IATtlptvkmIVEVSRSA 1142
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAayVPLD--PAYPAErLAF-------ILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1143 CLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAqiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCR 1222
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1223 SIklqCELYPSREVAICLDpYCGLGF------VLWCLcsvYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVM 1296
Cdd:TIGR01733 151 WL---ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1297 ELCtkglgsqtesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLglhpravstsfgcrvnlaiclqphRLWTla 1376
Cdd:TIGR01733 224 ALL----------AAALPPALASLRL-VILGGEALTPALVDRWRARGPGA------------------------RLIN-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1377 eqgTSGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYF 1456
Cdd:TIGR01733 267 ---LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGYL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1457 tiyGDESLQSDHFNSRLSFGDTQTIWARTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRA 1536
Cdd:TIGR01733 335 ---NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLR 400
|
....*....
gi 1958706127 1537 HKSVTECAV 1545
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-174 |
6.09e-23 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 94.79 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 8 GMALPLEVRARLAELELELSEGDITQKGYEKKRSKLIGAYLPQPptangaavvrcrlqpgegvprrpfrsahigvcdire 87
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHP------------------------------------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 88 aaareraasaagnrplfyfrfgvdqalpqerRAPVTPSSASRYHR-RRSSGSRDERYRSDVHTEAVQAALAKHKERKMAV 166
Cdd:pfam06464 46 -------------------------------ETPTKLSAEAQNQLaSLETKLRDEELSEEVYLEKVKALLAKELERENGL 94
|
....*...
gi 1958706127 167 PMPSKRRS 174
Cdd:pfam06464 95 NAPTKEQS 102
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
397-965 |
1.00e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 104.82 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 397 DTNGKPLYiLTYGKLWTRsmkvayniLHKLGTKQEPMVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPI---EVPl 473
Cdd:PRK12476 61 SAAGCAVE-LTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfapELP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 474 trkdAGSQQIGFLLGSCGVTVALTSDAChkglpkspTGEIPQFkgwpkllwfvteskhLSKPPRDWFPH------IKDA- 546
Cdd:PRK12476 129 ----GHAERLDTALRDAEPTVVLTTTAA--------AEAVEGF---------------LRNLPRLRRPRviaidaIPDSa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 547 ----------NNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETI-VNVLDFKKDVGLWHGILTSVMNM 615
Cdd:PRK12476 182 gesfvpveldTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 616 MHVISIPYALMKvNPLSWIQKV---CQYKAKVACVKSRDMHWAlvAHR----DQRDVNLSSLRMLIvadGANPWSISSCD 688
Cdd:PRK12476 262 HSTLMSPTAFVR-RPQRWIKALsegSRTGRVVTAAPNFAYEWA--AQRglpaEGDDIDLSNVVLII---GSEPVSIDAVT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 689 AFLNVFQSKGLRQEVICPCASSPEA-LTVAirrpTDDSNQPPGRGVLSMHGLTYG-VIRVDSEEKLSVLTVQdVGLVMPG 766
Cdd:PRK12476 336 TFNKAFAPYGLPRTAFKPSYGIAEAtLFVA----TIAPDAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 767 AIMCSVKPDGVPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFEV-----FPMTS--SGAPISEyPFIRTGLLGFVGP 839
Cdd:PRK12476 411 QWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDG-TWLRTGDLGVYLD 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 840 GGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVL 919
Cdd:PRK12476 489 GEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1958706127 920 QAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 965
Cdd:PRK12476 566 AAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1056-1546 |
2.38e-22 |
|
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: 102.68 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1056 GTIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCvpitvrPPHPQNIATTLPTVKMI 1135
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1136 VEVSRSACLMTTQliCKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSN--------------PDTLAYLDFSV 1201
Cdd:cd05911 78 LKISKPKVIFTDP--DGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLgeededlppplkdgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1202 STTGMLAGVKMSHaatSAFCRSIKLQC----ELYPSREVAICLDPY---CGLgfvLWCLCSVYSGHQSILIPpselETNP 1274
Cdd:cd05911 156 GTTGLPKGVCLSH---RNLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMP----KFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1275 ALWLLAVSQYKVRDTFCSYSVMELctkgLGSQTESLKArglDLSRVRTCVVVAEerpriALTQSFSKLFKdlglhpravs 1354
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGGA-----PLSKELQELLA---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1355 tsfgCRVNLAICLQphrLWTLAEqgTSGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVRIIIANPETKG 1434
Cdd:cd05911 284 ----KRFPNATIKQ---GYGMTE--TGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1435 PLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALD 1514
Cdd:cd05911 336 SLGPNEPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYF------DEDGY----LYIVDRKK 394
|
490 500 510
....*....|....*....|....*....|..
gi 1958706127 1515 EAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1546
Cdd:cd05911 395 ELIKYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1059-1548 |
7.86e-19 |
|
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: 92.05 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1059 ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPItvrpphPQNIATTLPTVKMIVEV 1138
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1139 SRSACLMTTQLICKLLRSREAAAAVDVRT----------WPLILDTDDLPKKRPAQIYKPSNPDTLAYLDFSVSTTGMLA 1208
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1209 GVKMSHAatsafcrSIKLQCELYPSREVAICLDPYC----------GLGFVLWCLCSVysGHQSILIPpsELETnPALWL 1278
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP--ERPT-PAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1279 LAVSQYKvRDTFcsYSVMELCTKGLGSqtESLKARglDLSRVRTCVVVAEerpriALTQSFSKLFKDLglhpravstsFG 1358
Cdd:cd05959 248 KRIRRYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGE-----ALPAEVGERWKAR----------FG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1359 CRVnlaiclqphrlwtlaEQGTSGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVRIIIANpETKGPLGD 1438
Cdd:cd05959 306 LDI---------------LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1439 SHLGEIWVHSAHNASGYFTIYGDeslqsdhfnSRLSFgdtQTIWARTGYlGFLRrteltDANGerhdALYVVGALDEAME 1518
Cdd:cd05959 356 GEPGELYVRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLK 413
|
490 500 510
....*....|....*....|....*....|
gi 1958706127 1519 LRGMRYHPIDIEtSVIRAHKSVTECAVFTW 1548
Cdd:cd05959 414 VSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1061-1568 |
3.29e-17 |
|
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: 86.43 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1061 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSR 1140
Cdd:cd05930 12 SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE------RLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1141 SACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1220
Cdd:cd05930 85 AKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1221 CRSIKlqcELYP--SREVAICLDPYcglGF------VLWCLCsvySGHQsILIPPSELETNPALWLLAVSQYKVRDTFCS 1292
Cdd:cd05930 122 LLWMQ---EAYPltPGDRVLQFTSF---SFdvsvweIFGALL---AGAT-LVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1293 YSVMELCTKGLGSQteslkarglDLSRVRTcVVVAEERPRIALTQSFSKLFKDlglhpravstsfgcrvnlaiclqpHRL 1372
Cdd:cd05930 192 PSLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPG------------------------ARL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1373 WTLaeqgtSGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNA 1452
Cdd:cd05930 238 VNL-----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1453 SGYftiYGDESLQSDHFNsRLSFGDTQTIWaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIETs 1532
Cdd:cd05930 303 RGY---LNRPELTAERFV-PNPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA- 366
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1958706127 1533 VIRAHKSVTECAVFTWTN------LLVVVVELDGSEQEALDL 1568
Cdd:cd05930 367 ALLAHPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
373-993 |
2.22e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.99 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 373 PPSLEAALQRWGTISPKAPCLTTMDTNGKPLYILTYGKLWTRSMKVAYNIlhklgtkqEPMVRPGDRVALVFPNNdpAAF 452
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 453 MVAFYGCLLAEVVPVPIEVPLTRKDAGSQQIGFLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkGWPKLLwfvTESKHL 532
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPELL---CVDTLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 533 SKPPRDWF-PHIKDanNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACG--YTEAETIVNVLDFKKDVGLWHGIL 609
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 610 TSVMNmmhviSIPYALMKVN-----PLSWIQKVCQYKAKVAcvKSRDMHWALVAHRdQRDVNLSSL---RMLIVADGANP 681
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 682 WSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAirrptddsNQPPGRGVlsmhgltyGVIRVDSE-------EKLS 753
Cdd:PRK05691 302 IRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS--------GGRRGQGI--------PALELDAEalarnraEPGT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 754 VLTVQDVGLVMPGAIMCSVKPDGVPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFevfpMTSSGApiseyPFIRTGL 833
Cdd:PRK05691 366 GSVLMSCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 834 LGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalAVEPMKFVYRGRIAVFSVTVLHDERIVIVAE-----QRPDSTE 908
Cdd:PRK05691 436 LGFLRDGEL-FVTGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 909 EdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLhpcnvlmcphTCVTNLPKPRQKQPE 988
Cdd:PRK05691 513 A----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAA 578
|
....*
gi 1958706127 989 IGPAS 993
Cdd:PRK05691 579 QTAAS 583
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1066-1545 |
1.00e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.96 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1066 QLHKRAEKIAVMLMERGhlqDGDHVALVYPPGIDLIAAFYGCLYAG----CVPITVRPPHPQNIA-TTLptvkmivevSR 1140
Cdd:PRK05851 36 EVHGRAENVAARLLDRD---RPGAVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWAdATL---------TR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1141 SACLMTTQLIC-----KLLRSREAAAAV-DVRTWPlildtddlpKKRPAQIYKPSNPDTLAYLDFSVSTTGMLAGVKMSH 1214
Cdd:PRK05851 104 FAGIGVRTVLShgshlERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1215 AATSAFCRSIKLQCELYPSREVAICLDPY---CGLGFVLwclCSVYSGHQSILIPPSELETNPALWLLAVSQykVRDTFC 1291
Cdd:PRK05851 175 GAVLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSD--SRATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1292 SYSVMELCTKGLGSQteslKARGLDLSRVRTCVVVAEerP-RIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqph 1370
Cdd:PRK05851 250 AAPNFAYNLIGKYAR----RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG------------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1371 rlwtLAEQ--GTSGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVRIIIANPETKGPLGDSHLGEIWVHS 1448
Cdd:PRK05851 312 ----LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1449 AHNASGYFtiyGDESLQSDHfnsrlsfgdtqtiWARTGYLGFlrrteLTDangerhDALYVVGALDEAMELRGMRYHPID 1528
Cdd:PRK05851 380 ASMMSGYL---GQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTE 432
|
490
....*....|....*..
gi 1958706127 1529 IETSVIRAhKSVTECAV 1545
Cdd:PRK05851 433 IERVAAQV-RGVREGAV 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1190-1530 |
1.15e-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: 72.52 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1190 NPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSE 1269
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1270 LETNPALWLLAVSQYKVRDTFCSysvmELCTKGLGSQTESLKARGLDLSRVRTCVVVAEErprIA--LTQSFSKLFKDLG 1347
Cdd:cd05908 184 FIRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1348 LHPRAVSTSFGcrvnlaiclqphrlwtLAEQ--GTSGPDP----TTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKIL 1420
Cdd:cd05908 257 LKRNAILPVYG----------------LAEAsvGASLPKAqspfKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1421 PGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaN 1500
Cdd:cd05908 321 DETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGY---YNNPEATAKVF--------TDDGWLKTGDLGFIR-------N 381
|
330 340 350
....*....|....*....|....*....|
gi 1958706127 1501 GErhdaLYVVGALDEAMELRGMRYHPIDIE 1530
Cdd:cd05908 382 GR----LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
435-947 |
3.28e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 70.93 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 435 RPGDRVALVFPNNDPA---AFMVAFYGCLLAEVVpvpieVPLTrKDAGSQQIGFLLGSCGVTVALTS----DACHKGLPK 507
Cdd:cd05922 16 VRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADagaaDRLRDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 508 SPTGEipqfkgwpklLWFVTESKHLSKPPRDWFPHIKDannDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYT 587
Cdd:cd05922 90 SPDPG----------TVLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 588 EAETIVNVLDFKKDVGLwhgiltSVMNMmH-------VISIPYALmkvnPLSWIQKVCQYKAK-VACVKSrdmHWALVAH 659
Cdd:cd05922 157 ADDRALTVLPLSYDYGL------SVLNT-HllrgatlVLTNDGVL----DDAFWEDLREHGATgLAGVPS---TYAMLTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 660 RDQRDVNLSSLRMLIVADGANPwsisscDAFLNVFQSKGlrqevicpcasspealtvairrptddsnqpPGRGVLSMHGL 739
Cdd:cd05922 223 LGFDPAKLPSLRYLTQAGGRLP------QETIARLRELL------------------------------PGAQVYVMYGQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 740 TYGVIR---VDSEEKLSVLTvqDVGLVMPGAIMCSVKPDGvpQLCRTDEIGELcvcaVATGTSYYgLSGMTKNTFEVFPM 816
Cdd:cd05922 267 TEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDG--TPTPPGEPGEI----VHRGPNVM-KGYWNDPPYRRKEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 817 TSSGApiseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDERI 896
Cdd:cd05922 338 RGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKL 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958706127 897 VIVAEqRPDSTEEDSfqwMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 947
Cdd:cd05922 406 ALFVT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1032-1266 |
6.23e-12 |
|
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: 69.90 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1032 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:cd05936 1 LADLLEEAARRFPDK---TALIFMGR---KLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1112 CVPITVRPphpqniattlptvkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWplildTDDLPKKRPAQIYKPSNP 1191
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1192 DTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsIKLQC-----ELYPSREVAICLDP-YCGLGFVLWCLCSVYSGHQSILI 1265
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 1958706127 1266 P 1266
Cdd:cd05936 201 P 201
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1061-1545 |
1.59e-11 |
|
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: 68.80 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1061 SLTCVQLHKRAEKIAVMLMERGHLQdGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqniATTLPTVKMIVEVSR 1140
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1141 SACLMTT-QLICKLlrsreAAAAVDVrtwpLILDTDD---LPKKRPAQIYKPSNP-------DTLAYLDFSVSTTGMLAG 1209
Cdd:cd05904 105 AKLAFTTaELAEKL-----ASLALPV----VLLDSAEfdsLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1210 VKMSH----AATSAFCRSIKLQCElypSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPSELETnpalWLLAVSQY 1284
Cdd:cd05904 176 VMLTHrnliAMVAQFVAGEGSNSD---SEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1285 KVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPRiALTQSFSKLFKDlglhpravstsfgcrVNLa 1364
Cdd:cd05904 249 KVTHLPVVPPIVLALVK-------SPIVDKYDLSSLRQIMSGAAPLGK-ELIEAFRAKFPN---------------VDL- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1365 icLQPHRLWTLAEQGTSGPDPTtvyvdmralrHDRVRlveRGSphslplmeSGKILPGVRIIIANPETKGPLGDSHLGEI 1444
Cdd:cd05904 305 --GQGYGMTESTGVVAMCFAPE----------KDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1445 WVHSAHNASGYFtiyGDESlqsdhfnsrlsfgDTQ-TI----WARTGYLGFLrrteltDANGErhdaLYVVGALDEAMEL 1519
Cdd:cd05904 362 WIRGPSIMKGYL---NNPE-------------ATAaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKY 415
|
490 500
....*....|....*....|....*.
gi 1958706127 1520 RGMRYHPIDIEtSVIRAHKSVTECAV 1545
Cdd:cd05904 416 KGFQVAPAELE-ALLLSHPEILDAAV 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1040-1571 |
1.01e-10 |
|
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: 66.12 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1040 AQTTPDHLLYTllnCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITV 1117
Cdd:cd05945 1 AAANPDRPAVV---EGGR---TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1118 RPPHPQniattlptVKMIVEVSRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYL 1197
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIAD-------------------------------------------GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1198 DFSVSTTGMLAGVKMSHAATSAFCRSIkLQCELYPSREVAICLDPYcglGF---VLWCLCSVYSGhQSILIPPSELETNP 1274
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPF---SFdlsVMDLYPALASG-ATLVPVPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1275 ALWLLAVSQYKVRDTFCSYSVMELCTkGLGSQTESLkargldLSRVRTCVVVAEERPrIALTQSFSKLFkdlglhPravs 1354
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPES------LPSLRHFLFCGEVLP-HKTARALQQRF------P---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1355 tsfGCRV-NlaiclqphrlwtlaeqgTSGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVRIIIANPETK 1433
Cdd:cd05945 240 ---DARIyN-----------------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILDEDGR 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1434 gPLGDSHLGEIWVHSAHNASGYFtiyGDEslqsDHFNSRLSFGDTQTiWARTGYLGFLrrteltDANGErhdaLYVVGAL 1513
Cdd:cd05945 292 -PVPPGEKGELVISGPSVSKGYL---NNP----EKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRL 352
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958706127 1514 DEAMELRGMRYHPIDIETSViRAHKSVTECAVFTWTNL-----LVVVVELDGSEqEALDLVPL 1571
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1040-1545 |
2.60e-10 |
|
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: 64.67 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1040 AQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG--CVPITV 1117
Cdd:cd17651 5 AARTPDA---PALVAEGR---RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1118 RPPhPQNIAttlptvkMIVEVSRSACLMTTQlickllrsREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSNPDTLAYL 1197
Cdd:cd17651 78 AYP-AERLA-------FMLADAGPVLVLTHP--------ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1198 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF--VLWCLCSVYSGHQSILIPPSELETNPA 1275
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTL----QFAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1276 LWLLAVSQYKVRDTFCSYSVME-LCtkglgsqtESLKARGLDLSRVRtCVVVAEERprialtqsfsklfkdLGLHPRavs 1354
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGEQ---------------LVLTED--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1355 tsfgcrvnlaiclqpHRLWTLAEQG-----TSGPDPTTVyVDMRALRHDRVRlveRGSPHSLplmesGKILPGVRIIIAN 1429
Cdd:cd17651 271 ---------------LREFCAGLPGlrlhnHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1430 PETKgPLGDSHLGEIWVHSAHNASGYFTIYG--DESLQSDHF--NSRLSfgdtqtiwaRTGYLGflRRteltDANGErhd 1505
Cdd:cd17651 327 AALR-PVPPGVPGELYIGGAGLARGYLNRPEltAERFVPDPFvpGARMY---------RTGDLA--RW----LPDGE--- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958706127 1506 aLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1545
Cdd:cd17651 388 -LEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVV 425
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
566-958 |
4.76e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.25 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 566 VTVTRIALLTHCQALTQACGYT-EAETIVNVLDFKKDVGLWhGILTSVMNM-MHVISIPYALMKVNPLSWIQKVCQYKAK 643
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMV-GFLTVPMYFgAELVKVTPMDFLRDPLLWAELISKYRGT 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 644 VACvkSRDMHWALVAHR-----DQRDVNLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVAI 718
Cdd:PRK07768 249 MTA--APNFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEA-TLAV 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 719 rrptddSNQPPGRGvlsmhgLTYGVIRVD--SEEKLSVLTVQD-------VGLVMPGAIMCSVKPDGvpQLCRTDEIGEL 789
Cdd:PRK07768 324 ------SFSPCGAG------LVVDEVDADllAALRRAVPATKGntrrlatLGPPLPGLEVRVVDEDG--QVLPPRGVGVI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 790 CVCAVATgTSYYglsgmtkntfevfpMTSSG--APISEYPFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVA 867
Cdd:PRK07768 390 ELRGESV-TPGY--------------LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIER 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 868 TALAVEPmkfVYRGRIAVFSVTVLHD-ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPKT 944
Cdd:PRK07768 455 AAARVEG---VRPGNAVAVRLDAGHSrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPKT 529
|
410
....*....|....
gi 1958706127 945 PLGGIHLSETKQLF 958
Cdd:PRK07768 530 PSGKLRRANAAELV 543
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
565-949 |
5.10e-10 |
|
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: 63.07 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 565 GVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPyalmKVNPLSWIQKVCQYKAKV 644
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 645 ACVkSRDMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptdd 724
Cdd:cd04433 92 LLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP------------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 725 snqppGRGVLSMHGLT-----YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGVPqlCRTDEIGELCVcavatgTS 799
Cdd:cd04433 139 -----GIKLVNGYGLTetggtVATGPPDDDARKPG----SVGRPVPGVEVRIVDPDGGE--LPPGEIGELVV------RG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 800 YYGLSGMTKNTFEVFPMTSSGapiseypFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvy 879
Cdd:cd04433 202 PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA--- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958706127 880 rgRIAVFSVTvlhDER------IVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 949
Cdd:cd04433 272 --EAAVVGVP---DPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1038-1545 |
7.70e-10 |
|
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: 63.45 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1038 WRAQT--TPDH--LLYTllncrgtiANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1113
Cdd:cd17646 4 VAEQAarTPDApaVVDE--------GRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1114 PITVRPPHPQniattlPTVKMIVEVSRSACLMTTQlickllRSREAAAAVDVRTWPLILDTDDLPKKRPAQiykPSNPDT 1193
Cdd:cd17646 75 YLPLDPGYPA------DRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLV---PPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1194 LAYLDFSVSTTGMLAGVKMSHAatsAFCRSIKLQCELYP--SREVAICLDPycgLGF------VLWCLCsvySGhQSILI 1265
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPlgPGDRVLQKTP---LSFdvsvweLFWPLV---AG-ARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1266 PPSELETNPALWLLAVSQYKVrdTFCSY--SVMELCtkglgsqteslkargLDLSRVRTC-----VVVAEErpriALTQS 1338
Cdd:cd17646 210 ARPGGHRDPAYLAALIREHGV--TTCHFvpSMLRVF---------------LAEPAAGSCaslrrVFCSGE----ALPPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1339 FSKLFKDLglhpravstsFGCRVnlaiclqpHRLWtlaeqgtsGPDPTTVYVDmralrHDRVRlvERGSPHSLPLmesGK 1418
Cdd:cd17646 269 LAARFLAL----------PGAEL--------HNLY--------GPTEAAIDVT-----HWPVR--GPAETPSVPI---GR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1419 ILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHF-------NSRLSfgdtqtiwaRTGYLGfl 1491
Cdd:cd17646 313 PVPNTRLYVLDDALR-PVPVGVPGELYLGGVQLARGY---LGRPALTAERFvpdpfgpGSRMY---------RTGDLA-- 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958706127 1492 RRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAV 1545
Cdd:cd17646 378 RWR----PDGA----LEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVV 422
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1061-1286 |
9.82e-10 |
|
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: 63.06 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1061 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPhPQNIATtlptvkmIVEV 1138
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARREA-------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1139 SRSACLMTTQLICKLLRSREAAAAVDvrtwpliLDTDDLPKKRPAQiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1218
Cdd:cd12114 83 AGARLVLTDGPDAQLDVAVFDVLILD-------LDALAAPAPPPPV---DVAPDDLAYVIFTSGSTGTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958706127 1219 AFCRSIKLQCELYPSREVaICLDPycgLGFVLwclcSVY------SGHQSILIPPSELETNPALWLLAVSQYKV 1286
Cdd:cd12114 153 NTILDINRRFAVGPDDRV-LALSS---LSFDL----SVYdifgalSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1061-1562 |
1.45e-09 |
|
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: 62.31 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1061 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSR 1140
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1141 SACLMTTQlickllrSREAAAAVDVRTWPLILDTDDLPkkrPAQIYKPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1220
Cdd:cd12116 85 PALVLTDD-------ALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1221 CRSIklqcelypsREvaicldpycglgfvlwclcsvysghqsilippsELETNPALWLLAVSQYkvrdTFcSYSVMEL-- 1298
Cdd:cd12116 155 LHSM---------RE---------------------------------RLGLGPGDRLLAVTTY----AF-DISLLELll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1299 ----------CTKGLGSQTESLKARgldLSRVRTCVVVAeerprialTQSFSKLFKDLGLHPRAvstsfGCRV------- 1361
Cdd:cd12116 188 pllagarvviAPRETQRDPEALARL---IEAHSITVMQA--------TPATWRMLLDAGWQGRA-----GLTAlcggeal 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1362 --NLA--ICLQPHRLWTLaeqgtSGPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVRIIIANPETKgPLG 1437
Cdd:cd12116 252 ppDLAarLLSRVGSLWNL-----YGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVLDAALR-PVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1438 DSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWARTGYLgfLRRteltDANGErhdaLYVVGALDEAM 1517
Cdd:cd12116 314 PGVPGELYIGGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR----RADGR----LEYLGRADGQV 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958706127 1518 ELRGMRYHPIDIETsVIRAHKSVTECAVFTWTN----LLVVVVELDGSE 1562
Cdd:cd12116 380 KIRGHRIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1039-1568 |
1.60e-09 |
|
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: 62.95 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1039 RAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPIT 1116
Cdd:COG1020 485 QAARTPDA---VAVVFGDQ---SLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVPLD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1117 vrPPHPQN-IAttlptvkMIVEVSRSACLMTTQlickLLRSREAAAAVDVrtwpLILDTDDLPKKRPAQIYKPSNPDTLA 1195
Cdd:COG1020 558 --PAYPAErLA-------YMLEDAGARLVLTQS----ALAARLPELGVPV----LALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1196 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF------VLWCLCsvySGHQSILIPPsE 1269
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSFdasvweIFGALL---SGATLVLAPP-E 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1270 LETNPALWLLAVSQYKVrdtfcsySVMELcTKGLGSQTesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLH 1349
Cdd:COG1020 693 ARRDPAALAELLARHRV-------TVLNL-TPSLLRAL--LDAAPEALPSLRL-VLVGGEALPPELVRRWRARLPGARLV 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1350 pravstsfgcrvNLaiclqphrlwtlaeqgtSGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVRIIIAn 1429
Cdd:COG1020 762 ------------NL-----------------YGPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL- 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1430 petkgplgDSHL--------GEIWVHSAHNASGYFtiyGDESLQSDHF--NsrlSFGDTQTIWARTGYLGflRRTeltdA 1499
Cdd:COG1020 803 --------DAHLqpvpvgvpGELYIGGAGLARGYL---NRPELTAERFvaD---PFGFPGARLYRTGDLA--RWL----P 862
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958706127 1500 NGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVFTWTN-----LLVVVVELDGSEQEALDL 1568
Cdd:COG1020 863 DGN----LEFLGRADDQVKIRGFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAAL 931
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
407-857 |
1.36e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 59.43 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 407 TYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGCLLAEVVPVPIEVPLTrkdagSQQIGFL 486
Cdd:PRK06187 33 TYAELDERVNRLA-NALRALG------VKKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 487 LGSCGVTVALTSDAcHKGLPKSPTGEIPQFKGW--------PKLLWFVTESKHL--SKPPRDWFPHIKDanNDTAYIEYK 556
Cdd:PRK06187 99 LNDAEDRVVLVDSE-FVPLLAAILPQLPTVRTVivegdgpaAPLAPEVGEYEELlaAASDTFDFPDIDE--NDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 557 TCKDGSVLGVTVTRIALLTHCQALTQACGYTEaetivnvldfkKDVGLwhgiltSVMNMMHV--ISIPY-ALM------- 626
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR-----------DDVYL------VIVPMFHVhaWGLPYlALMagakqvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 627 --KVNPlswiQKVCQY--KAKV---ACVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFqskgl 699
Cdd:PRK06187 239 prRFDP----ENLLDLieTERVtffFAVPT--IWQMLLKAPRAYFVDFSSLRLVIY--GGAALPPALLREFKEKF----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 700 rqevicpcasspealtvairrptddsnqppGRGVLSMHGL--TYGVIRVD--SEEKLSVLTVQ-DVGLVMPG---AImcs 771
Cdd:PRK06187 306 ------------------------------GIDLVQGYGMteTSPVVSVLppEDQLPGQWTKRrSAGRPLPGveaRI--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 772 VKPDGVPQLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEvfpmtsSGapiseypFIRTGLLGFVGPGGLVFVVGKMDG 851
Cdd:PRK06187 353 VDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------GG-------WLHTGDVGYIDEDGYLYITDRIKD 419
|
....*.
gi 1958706127 852 lMVVSG 857
Cdd:PRK06187 420 -VIISG 424
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
369-679 |
5.53e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 57.61 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 369 VTNWPPSLEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNd 448
Cdd:PRK07656 4 WMTLPELLARAARRF----GDKEAYVFGDQR------LTYAELNARVRRAA-AALAALG------IGKGDRVAIWAPNS- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 449 pAAFMVAFYGCLLAEVVPVPIEvplTRKDAGsqQIGFLLGSCGVTVALTSD-------ACHKGLPK----------SPTG 511
Cdd:PRK07656 66 -PHWVIAALGALKAGAVVVPLN---TRYTAD--EAAYILARGDAKALFVLGlflgvdySATTRLPAlehvviceteEDDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 512 EIPQFKGWPKLLwfvteskhLSKPPRDWFPHIKDanNDTAYIEYKTCKDGSVLGVtvtriaLLTHCQALTQA------CG 585
Cdd:PRK07656 140 HTEKMKTFTDFL--------AAGDPAERAPEVDP--DDVADILFTSGTTGRPKGA------MLTHRQLLSNAadwaeyLG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 586 YTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPyalmKVNPLSWIQKVCQYKAKV-ACVKSrdMHWALVAHRDQRD 664
Cdd:PRK07656 204 LTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERITVlPGPPT--MYNSLLQHPDRSA 277
|
330
....*....|....*
gi 1958706127 665 VNLSSLRmLIVADGA 679
Cdd:PRK07656 278 EDLSSLR-LAVTGAA 291
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1036-1566 |
6.74e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.22 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1036 LQWRAQTTPDHLLYTLLNCRGTIAN----SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADGKlaydELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1112 CVPITVRP-------------PHPQ--------NIATTL-----PTVKMIVEVSRSACLMTTQLickllrsreaaaavdv 1165
Cdd:PRK09274 91 AVPVLVDPgmgiknlkqclaeAQPDafigipkaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTL---------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1166 rtwplildtDDLPKKRPAQIYKP--SNPDTLAYLDFSVSTTGMLAGVKMSHaatSAFCRSIKLQCELYPSR--EVAIC-- 1239
Cdd:PRK09274 155 ---------ATLLRDGAAAPFPMadLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQIEALREDYGIEpgEIDLPtf 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1240 -----LDPYCGlgfvlwcLCSVysghqsilIPPSEL----ETNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSL 1310
Cdd:PRK09274 223 plfalFGPALG-------MTSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1311 KARGLDLSRVRTcVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLqphrlwtlaeqgtsgpdpttvy 1389
Cdd:PRK09274 281 EANGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS---------------------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1390 VDMRALRHDRVRLVERGSPHSLplmesGKILPGVRI-IIA---NP-----ETKgPLGDSHLGEIWVHSAHNASGYFtiyg 1460
Cdd:PRK09274 333 IESREILFATRAATDNGAGICV-----GRPVDGVEVrIIAisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYY---- 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1461 deslQSDHFN--SRLSFGDTQtIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHK 1538
Cdd:PRK09274 403 ----NRPEATrlAKIPDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHP 466
|
570 580
....*....|....*....|....*...
gi 1958706127 1539 SVTECAvftwtnllVVVVELDGSEQEAL 1566
Cdd:PRK09274 467 GVKRSA--------LVGVGVPGAQRPVL 486
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
376-497 |
1.19e-07 |
|
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: 56.42 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 376 LEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVA 455
Cdd:cd05936 5 LEEAARRF----PDKTALIFMGRK------LTYRELDALAEAFA-AGLQNLG------VQPGDRVALMLPNC--PQFPIA 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958706127 456 FYGCLLAEVVPVPIEVPLTrkdagSQQIGFLLGSCGVTVALT 497
Cdd:cd05936 66 YFGALKAGAVVVPLNPLYT-----PRELEHILNDSGAKALIV 102
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1062-1570 |
1.66e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1062 LTCVQLHKRAEKIAVMLMERGHLQDGdHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRS 1141
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEV-LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1142 ACLMTTQLICKLLRSREAAAAVDV---RTWplildtDDLPKKRPAqiyKPSNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1218
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDGLASLALdrdEDW------EGFPAHDPA---VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV 4720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1219 AFCRSIKLQCELYPSREVaICLDPYCGLGFVL---WCLCSvysgHQSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSV 1295
Cdd:PRK12316 4721 NHLHATGERYELTPDDRV-LQFMSFSFDGSHEglyHPLIN----GASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1296 MELCTKGlgsqteslKARGLDLSRVRTCVVVAEERPRIALTQSFSKlfkdlglhpravstsfgcrvnlaicLQPHRLWTl 1375
Cdd:PRK12316 4795 LQQLAEH--------AERDGEPPSLRVYCFGGEAVAQASYDLAWRA-------------------------LKPVYLFN- 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1376 aeqgTSGPDPTTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVRIII----ANPETKGPLGDSHLGEIWVhsahn 1451
Cdd:PRK12316 4841 ----GYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVldgqLNPLPVGVAGELYLGGEGV----- 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1452 ASGYFTiygDESLQSDHFNSRlSFGDTQTIWARTGYLGFLRRTELTDangerhdalyVVGALDEAMELRGMRYHPIDIET 1531
Cdd:PRK12316 4904 ARGYLE---RPALTAERFVPD-PFGAPGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEA 4969
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958706127 1532 SvIRAHKSVTECavftwtnlLVVVVELDGSEQEALDLVP 1570
Cdd:PRK12316 4970 R-LREHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1066-1233 |
2.23e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1066 QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLM 1145
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1146 T-TQLICKLLRSREAAAavdvrtwpLILDTD----DLPKKRPAQiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1220
Cdd:PRK12316 2106 TqRHLLERLPLPAGVAR--------LPLDRDaewaDYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170
....*....|...
gi 1958706127 1221 CRSIKLQCELYPS 1233
Cdd:PRK12316 2175 CQAAGERYELSPA 2187
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
400-502 |
2.25e-07 |
|
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: 55.45 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 400 GKPLYI-----LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFpnNDPAAFMVAFYGCLLAEVVPVPIEVPLT 474
Cdd:cd05959 19 DKTAFIddagsLTYAELEAEARRVA-GALRALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 1958706127 475 rkdagSQQIGFLLGSCGVTVALTSDACH 502
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGELA 112
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1036-1569 |
4.74e-07 |
|
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: 54.15 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1036 LQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPi 1115
Cdd:cd17631 1 LRRRARRHPDR---TALVFGGR---SLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVF- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1116 tvrppHPQNIATTLPTVKMIVEVSRSACLMttqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnpDTLA 1195
Cdd:cd17631 73 -----VPLNFRLTPPEVAYILADSGAKVLF----------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1196 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELyPSREVAICLDPYC---GLGfvLWCLCSVYSGHQSILIPpselET 1272
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILR----KF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1273 NPALWLLAVSQYKVRDTFCSYSVME-LCTKGlgsqteslKARGLDLSRVRtCVVVAEERPRIALTQSFSKlfkdlglhpr 1351
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRALQA---------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1352 avstsFGCRvnlaiclqphrLWTLAEQGTSGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVRIIIANPE 1431
Cdd:cd17631 236 -----RGVK-----------FVQGYGMTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPD 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1432 TKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDhfnsrlSFGDTqtiWARTGYLGFLrrteltDANGerhdALYVVG 1511
Cdd:cd17631 284 GR-EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVD 340
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958706127 1512 ALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLV-VVVELDGSEQEALDLV 1569
Cdd:cd17631 341 RKKDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
337-873 |
4.95e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.96 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 337 FEELLEVQQPDPNQPKPEGAqmLATRGEQLGVVTNWPPSLEAALQRWGT---------ISPKAPCLTTMDTNgkplyiLT 407
Cdd:PRK12316 1959 LLHLLEQMAEDAQAALGELA--LLDAGERQRILADWDRTPEAYPRGPGVhqriaeqaaRAPEAIAVVFGDQH------LS 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 408 YGKLWTRSMKVAYNILhKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLA--EVVPVPIEVPLTRkdagsqqIGF 485
Cdd:PRK12316 2031 YAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERS--FELVVALLAVLKAggAYVPLDPNYPAER-------LAY 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 486 LLGSCGVTVALTSDACHKGLPksPTGEIPQFKGWPKLLWFVTESKHlskpprdwfPHIKDANNDTAYIEYKTCKDGSVLG 565
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWADYPDTA---------PAVQLAGENLAYVIYTSGSTGLPKG 2163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 566 VTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPYALMkvNPLSWIQKVCQYKAKVA 645
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELW--DPEQLYDEMERHGVTIL 2240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 646 CVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLN------VFQSKGLRQEVICP-----CASSPE-A 713
Cdd:PRK12316 2241 DFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPllwkcRPQDPCgA 2316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 714 LTVAIRRPTDDsnqppgrgvlsmhgltygvirvdseEKLSVLtvqDVGLvmpgaimcsvkpdgvpQLCRTDEIGELCVCA 793
Cdd:PRK12316 2317 AYVPIGRALGN-------------------------RRAYIL---DADL----------------NLLAPGMAGELYLGG 2352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 794 VATGTSYYGLSGMTKNTFEVFPMTSSGAPIseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVE 873
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1061-1545 |
5.65e-07 |
|
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: 53.85 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1061 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPHPQNIAttlptvkmIVEV 1138
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERIAF--------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1139 SRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATS 1218
Cdd:cd17643 83 SGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1219 AFCRSIKLQCELYPSREVAICldPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAVSQYKVrdtfcsySVMel 1298
Cdd:cd17643 120 ALFAATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV-------TVL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1299 ctkglgSQT--------ESLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDlgLHPRAvstsfgcrVNLaiclqph 1370
Cdd:cd17643 189 ------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1371 rlwtlaeqgtSGPDPTTVYVDMRALRHDRVRLVErGSPhslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHSAH 1450
Cdd:cd17643 245 ----------YGITETTVHVTFRPLDAADLPAAA-ASP-------IGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1451 NASGYFtiyGDESLQSDHFNSrLSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIE 1530
Cdd:cd17643 306 VARGYL---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE 371
|
490
....*....|....*
gi 1958706127 1531 tSVIRAHKSVTECAV 1545
Cdd:cd17643 372 -AALATHPSVRDAAV 385
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1034-1579 |
8.23e-07 |
|
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: 53.74 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1034 EVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1113
Cdd:cd12117 1 ELFEEQAARTPDA---VAVVYGDR---SLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1114 PITVRPPHPQNiattlpTVKMIVEVSRSACLMTtqlickllrSREAAAAVDVRTWPLILDtDDLPKKRPAQIYKPSNPDT 1193
Cdd:cd12117 74 YVPLDPELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGLEVAVVID-EALDAGPAGNPAVPVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1194 LAYLDFSVSTTGMLAGVKMSHAATSAFCRS---IKLQcelypSREVAICLDPYC--GLGFVLWclCSVYSGHQSILIPPS 1268
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtnyVTLG-----PDDRVLQTSPLAfdASTFEIW--GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1269 ELETNPALwLLAVSQYKVrdtfcsySVMELcTKGLGSQteslkargldlsrvrtcvvVAEERPrialtQSFSKLfkdlgl 1348
Cdd:cd12117 211 TLLDPDAL-GALIAEEGV-------TVLWL-TAALFNQ-------------------LADEDP-----ECFAGL------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1349 hpRAVSTSfGCRVNLAIClqphRLWTLAEQGTS-----GPDPTTVYvdmrALRHdrvrLVERG--SPHSLPLmesGKILP 1421
Cdd:cd12117 252 --RELLTG-GEVVSPPHV----RRVLAACPGLRlvngyGPTENTTF----TTSH----VVTELdeVAGSIPI---GRPIA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1422 GVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWaRTGYLGFLRrteltdANG 1501
Cdd:cd12117 314 NTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNRPALTAERF-VADPFGPGERLY-RTGDLARWL------PDG 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958706127 1502 ErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAvftwtnllVVVVELDGSEQEaldlvpLVTNVVLEE 1579
Cdd:cd12117 382 R----LEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAV--------VVVREDAGGDKR------LVAYVVAEG 440
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
406-500 |
9.51e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 53.40 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 485
Cdd:PRK08316 37 WTYAELDAAVNRVA-AALLDLG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAY 102
|
90
....*....|....*
gi 1958706127 486 LLGSCGVTVALTSDA 500
Cdd:PRK08316 103 ILDHSGARAFLVDPA 117
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1034-1214 |
1.95e-06 |
|
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: 52.33 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1034 EVLQWRAQTTPDHllyTLLNCRGtiaNSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC- 1112
Cdd:cd17655 1 ELFEEQAEKTPDH---TAVVFED---QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1113 -VPITvrPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAaavdvrtwpLILDTDDLPKKRPAQIYKPSNP 1191
Cdd:cd17655 74 yLPID--PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKS 136
|
170 180
....*....|....*....|...
gi 1958706127 1192 DTLAYLDFSVSTTGMLAGVKMSH 1214
Cdd:cd17655 137 DDLAYVIYTSGSTGKPKGVMIEH 159
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1188-1545 |
4.76e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 51.15 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1188 PSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYC-GLGFVLWCLCSVYSGHQSILIP 1266
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1267 PSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGSQTESlkaRGLDLSRVRtCVVVAEERPRIALTQSFSKLFKDL 1346
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1347 GLHPRAVSTSFG-CRVNLAICLQPhrlwtlaeqgtSGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPG--V 1423
Cdd:PRK07768 304 GLRPEAILPAYGmAEATLAVSFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGleV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1424 RIIIANPEtkgPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDHfnsrlsfGdtqtiWARTGYLGFLrrTEltdaNGEr 1503
Cdd:PRK07768 372 RVVDEDGQ---VLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE----EGE- 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958706127 1504 hdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTECAV 1545
Cdd:PRK07768 430 ---VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
377-500 |
5.57e-06 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 50.88 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 377 EAALQRWGTISPKAPCLTTMDTNGKPlYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdPAAfMVAF 456
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-PEA-VIAM 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958706127 457 YGCLLAEVVPVPIeVPLTRKDAgsqqIGFLLGSCGVTVALTSDA 500
Cdd:COG0365 82 LACARIGAVHSPV-FPGFGAEA----LADRIEDAEAKVLITADG 120
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
406-497 |
6.65e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAYNILHKLGtkqepmVRPGDRVALvFPNNDPAaFMVAFYGCLLAEVVPVPIEvPLTRkdagSQQIGF 485
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSPQ-FVIAYYAILRANAVVVPVN-PMNR----EEELAH 102
|
90
....*....|..
gi 1958706127 486 LLGSCGVTVALT 497
Cdd:PRK08314 103 YVTDSGARVAIV 114
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
596-961 |
8.36e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.53 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 596 LDFKKDVG-----LWHG-----ILTSVMNMMHVISIPYALMKVNPLSWIQKVCQYKAKVacVKSRDMHWALVAH--RDQR 663
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATL--TAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 664 DVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVAIRRPTddsnqpPGRGVLsmhgltygV 743
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV------PGIGLR--------V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 744 IRVDSEEKLSVLTVQDVGLVMPGA---IMCSVKPDGVPQlcrtDEIGELCVCAVATGTSYYGlsgmtkntfevfpmtssG 820
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMevrISPGDGAAGVAG----REIGEIEIRGASMMSGYLG-----------------Q 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 821 APISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfVYRGRIavfsVTVLHDE-----R 895
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRG---VREGAV----VAVGTGEgsarpG 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958706127 896 IVIVAEQRpdSTEEDSFQwmSRVLQAIDSihQVGVyclalVPAN-------TLPKTPLGGIHLSETKQLFLEG 961
Cdd:PRK05851 462 LVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDvvfvapgSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
380-496 |
1.20e-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: 49.53 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 380 LQRWGTISPKAPCLTTMDTngkplyILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGC 459
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLA-HALRALG------VAKGDRVAVLSKNSP--EFLELLFAA 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958706127 460 LLAEVVPVPIEVPLTRKDagsqqIGFLLGSCGVTVAL 496
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSGAKVLF 97
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
372-500 |
1.72e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 49.27 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 372 WPP-------------SLEAALQRWGTISPKAPCLttmDTNGkplYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGD 438
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958706127 439 RVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKdagsQQIGFLLGSCGVTVALTSDA 500
Cdd:PRK06178 85 RVAVFLPNC--PQFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1032-1216 |
2.60e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 49.27 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1032 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:PRK10252 460 LSALVAQQAAKTPDA---PALADARY---QFSYREMREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAG 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1112 CVPITVRPPHPQNiattlpTVKMIVEVSRSACLMTTQlickLLRSREAAAAVDVRTWPLILDTDdlPKKRPAQIYKPSNP 1191
Cdd:PRK10252 533 AAWLPLDTGYPDD------RLKMMLEDARPSLLITTA----DQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHT 600
|
170 180
....*....|....*....|....*
gi 1958706127 1192 dtlAYLDFSVSTTGMLAGVKMSHAA 1216
Cdd:PRK10252 601 ---AYIIFTSGSTGRPKGVMVGQTA 622
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1034-1221 |
3.20e-05 |
|
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: 48.32 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1034 EVLQWRAQTTPDHLLYTLlncRGtiaNSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCV 1113
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD---RG---QSLTYKQLNEKANQLARHLRGKGVKPD-DQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1114 PITVRPPHPQniattlptvkmivevsrsaclmttQLICKLLRSREAAaavdvrtwpLILdtddlpkkrpaqiykpSNPDT 1193
Cdd:cd17645 75 YVPIDPDYPG------------------------ERIAYMLADSSAK---------ILL----------------TNPDD 105
|
170 180
....*....|....*....|....*...
gi 1958706127 1194 LAYLDFSVSTTGMLAGVKMSHAATSAFC 1221
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1061-1220 |
4.49e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.98 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1061 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIATTLPT--VKMI-- 1135
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALfv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1136 ------VEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDlPKKRPAQIykpsNPDTLAYLDFSVSTTGMLAG 1209
Cdd:PRK07656 109 lglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD-PAERAPEV----DPDDVADILFTSGTTGRPKG 183
|
170
....*....|..
gi 1958706127 1210 VKMSHAAT-SAF 1220
Cdd:PRK07656 184 AMLTHRQLlSNA 195
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1032-1121 |
6.45e-05 |
|
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: 47.45 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1032 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1111
Cdd:COG1021 27 LGDLLRRRAERHPDR---IAVVDGER---RLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 1958706127 1112 CVPITVRPPH 1121
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
406-467 |
9.39e-05 |
|
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: 47.06 E-value: 9.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958706127 406 LTYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPV 467
Cdd:COG1021 51 LSYAELDRRADRLAAG-LLALG------LRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
407-555 |
1.82e-04 |
|
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: 45.72 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 407 TYGKLWTRSMKVAYNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEV--PLTRkdagsqqIG 484
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958706127 485 FLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkgwPKLLWFVTESKHLSKPPRDWFPHikdaNNDTAYIEY 555
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSG----PDDLAYVIY 127
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
388-598 |
2.07e-04 |
|
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: 45.72 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 388 PKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDPAafMVAFYGCLLAEVVPV 467
Cdd:cd12114 1 PDATAVICGDGT------LTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQ--VVAVLGILAAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 468 PIEV--PLTRKDAgsqqigfLLGSCGVTVALTSDACHKGLPKSPTgeipqfkgwpkllwFVTESKHLSKPPRDwFPHIKD 545
Cdd:cd12114 66 PVDIdqPAARREA-------ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDV 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958706127 546 ANNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNV--LDF 598
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALssLSF 178
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
406-605 |
2.66e-04 |
|
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: 46.00 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPI--EVPLTRkdagsqqI 483
Cdd:COG1020 502 LTYAELNARANRLA-HHLRALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER-------L 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 484 GFLLGSCGVTVALTSDACHKGLPKSptgeipqfkgwpKLLWFVTESKHLSKPPRDWfPHIKDANNDTAYIEY-------- 555
Cdd:COG1020 566 AYMLEDAGARLVLTQSALAARLPEL------------GVPVLALDALALAAEPATN-PPVPVTPDDLAYVIYtsgstgrp 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958706127 556 KtckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNV--LDFkkDVGLW 605
Cdd:COG1020 633 K--------GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1043-1214 |
3.40e-04 |
|
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: 45.16 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1043 TPDHLLYTLLNCrgtianSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAG--CVPITvrpP 1120
Cdd:cd17656 1 TPDAVAVVFENQ------KLTYRELNERSNQLARFLREKGVKKD-SIVAIMMERSAEMIVGILGILKAGgaFVPID---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1121 HpqniattLPTVKMIVEVSRSAC-LMTTQLICKLLRSREAAaaVDVRTWPLILDTDDlpkkrpAQIYKPSNPDTLAYLDF 1199
Cdd:cd17656 71 E-------YPEERRIYIMLDSGVrVVLTQRHLKSKLSFNKS--TILLEDPSISQEDT------SNIDYINNSDDLLYIIY 135
|
170
....*....|....*
gi 1958706127 1200 SVSTTGMLAGVKMSH 1214
Cdd:cd17656 136 TSGTTGKPKGVQLEH 150
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
406-500 |
3.68e-04 |
|
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: 44.89 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALvFPNNDPaAFMVAFYGCLLAEVVPVPIevpltRKDAGSQQIGF 485
Cdd:cd05907 6 ITWAEFAEEVRALA-KGLIALG------VEPGDRVAI-LSRNRP-EWTIADLAILAIGAVPVPI-----YPTSSAEQIAY 71
|
90
....*....|....*
gi 1958706127 486 LLGSCGVTVALTSDA 500
Cdd:cd05907 72 ILNDSEAKALFVEDP 86
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1040-1545 |
3.95e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.54 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1040 AQTTPDHLLYTLLNCRgtiansLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP 1119
Cdd:PRK12467 522 ARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPD-VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1120 PHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTDDLPKKRPAQIYKPSNPDTLAYLDF 1199
Cdd:PRK12467 595 EYPQD------RLAYMLDDSGVRLLLTQSHLLAQL-----PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1200 SVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAIcLDPYCGLGFVLWCLCSVYSGHQSILIPPSEletnpalwll 1279
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM-VSTFAFDLGVTELFGALASGATLHLLPPDC---------- 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1280 avsqykVRDTFCSYSVMelCTKGLG--SQTES-----LKARGLDLSRVRTCVVVAEErpriALTQSFSKLFKDLGLhpra 1352
Cdd:PRK12467 733 ------ARDAEAFAALM--ADQGVTvlKIVPShlqalLQASRVALPRPQRALVCGGE----ALQVDLLARVRALGP---- 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1353 vstsfGCrvnlaiclqphRLWTLaeqgtSGPDPTTVYVDMRALRHDRVrlVERGSPHSLPLMESgkilpGVRIIIA--NP 1430
Cdd:PRK12467 797 -----GA-----------RLINH-----YGPTETTVGVSTYELSDEER--DFGNVPIGQPLANL-----GLYILDHylNP 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1431 ETKGPLGDSHLGeiwvhSAHNASGYftiYGDESLQSDHFNSRLSFGDTQTIWaRTGYLGflRRTeltdANGErhdaLYVV 1510
Cdd:PRK12467 849 VPVGVVGELYIG-----GAGLARGY---HRRPALTAERFVPDPFGADGGRLY-RTGDLA--RYR----ADGV----IEYL 909
|
490 500 510
....*....|....*....|....*....|....*
gi 1958706127 1511 GALDEAMELRGMRYHPIDIETSvIRAHKSVTECAV 1545
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEAR-LLAQPGVREAVV 943
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1040-1215 |
4.88e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 44.50 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1040 AQTTPDHLLYtllNCRGTianSLTCVQLHKRAEKIAVMLMERgHLQDGDHVaLVY----PpgiDLIAAFYGCLYAGC--V 1113
Cdd:PRK04813 12 AQTQPDFPAY---DYLGE---KLTYGQLKEDSDALAAFIDSL-KLPDKSPI-IVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1114 PITVRPPhpqniattLPTVKMIVEVSRSACLMTTqlickllrSREAAAAVDVRTwpLILD--TDDLPKKRPAQIYKPSNP 1191
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIPV--ITLDelKDIFATGNPYDFDHAVKG 142
|
170 180
....*....|....*....|....
gi 1958706127 1192 DTLAYLDFSVSTTGMLAGVKMSHA 1215
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
406-499 |
7.54e-04 |
|
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: 43.84 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 485
Cdd:cd05926 15 LTYADLAELVDDLA-RQLAALG------IKKGDRVAIALPNG--LEFVVAFLAAARAGAVVAPLN-PAYKKA----EFEF 80
|
90
....*....|....
gi 1958706127 486 LLGSCGVTVALTSD 499
Cdd:cd05926 81 YLADLGSKLVLTPK 94
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
406-500 |
9.68e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 43.94 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALvFPNNDPaAFMVAFYGCLLAEVVPVPIEVpltrkDAGSQQIGF 485
Cdd:COG1022 41 LTWAEFAERVRALAAG-LLALG------VKPGDRVAI-LSDNRP-EWVIADLAILAAGAVTVPIYP-----TSSAEEVAY 106
|
90
....*....|....*
gi 1958706127 486 LLGSCGVTVALTSDA 500
Cdd:COG1022 107 ILNDSGAKVLFVEDQ 121
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
406-477 |
1.01e-03 |
|
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: 43.60 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPnnDPAAFMVAFYGCLLAEVVPVPIEVPLTRKD 477
Cdd:cd05919 11 VTYGQLHDGANRLG-SALRNLG------VSSGDRVLLLML--DSPELVQLFLGCLARGAIAVVINPLLHPDD 73
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
406-945 |
1.17e-03 |
|
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: 43.29 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEV--PLTRkdagsqqI 483
Cdd:cd05930 13 LTYAELDARANRLA-RYLRERG------VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDPsyPAER-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 484 GFLLGSCGVTVALTSDachkglpksptgeipqfkgwpkllwfvteskhlskpprdwfphikdanNDTAYIEY-------- 555
Cdd:cd05930 77 AYILEDSGAKLVLTDP------------------------------------------------DDLAYVIYtsgstgkp 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 556 KtckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMN--MMHVISipyALMKVNPLSW 633
Cdd:cd05930 109 K--------GVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAgaTLVVLP---EEVRKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 634 IQKVCQYKAKVA-CVKSrdmHW-ALVAHRDQRDvnLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcassp 711
Cdd:cd05930 177 ADLLAEEGITVLhLTPS---LLrLLLQELELAA--LPSLRLVLVG-G--------------------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 712 EALTVAIRRPTDDSNqpPGRGVLSMHGLT-------YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGvpQLCRTD 784
Cdd:cd05930 218 EALPPDLVRRWRELL--PGARLVNLYGPTeatvdatYYRVPPDDEEDGRV----PIGRPIPNTRVYVLDENL--RPVPPG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 785 EIGELCVC--AVATGtsYYGLSGMTKntfEVFPMTSSGAPISEYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNA 862
Cdd:cd05930 290 VPGELYIGgaGLARG--YLNRPELTA---ERFVPNPFGPGERMY---RTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 863 DDIVATALAVEPMkfvyrgRIAVfsVTVLHD----ERIV--IVAEQRPDSTEEDSFQWMSRVLQAidsihqvgvYCL--A 934
Cdd:cd05930 362 GEIEAALLAHPGV------REAA--VVAREDgdgeKRLVayVVPDEGGELDEEELRAHLAERLPD---------YMVpsA 424
|
570
....*....|.
gi 1958706127 935 LVPANTLPKTP 945
Cdd:cd05930 425 FVVLDALPLTP 435
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
406-595 |
1.47e-03 |
|
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: 43.05 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvpltrKDAGSQQIGF 485
Cdd:cd12116 13 LSYAELDERANRLA-ARLRARG------VGPGDRVAVYLPRS--ARLVAAMLAVLKAGAAYVPLD-----PDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 486 LLGSCGVTVALTSDACHKGLPKSPTgeipqfkGWPKLLWFVTESKHLSKPPrdwfphikDANNDTAYIEYKTCKDGSVLG 565
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLP-------VLLLALAAAAAAPAAPRTP--------VSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190
....*....|....*....|....*....|
gi 1958706127 566 VTVTRIALLTHCQALTQACGYTEAETIVNV 595
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDRLLAV 173
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
406-497 |
1.51e-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: 42.85 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 485
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 1958706127 486 LLGSCGVTVALT 497
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1417-1559 |
2.90e-03 |
|
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: 42.04 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1417 GKILPGVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFTIYGDEsLQSDHFNSRLsfgdtqtiwaRTGYLGFLrrtel 1496
Cdd:cd05922 289 GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL----------HTGDLARR----- 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958706127 1497 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSvIRAHKSVTECAVF----TWTNLLVVVVELD 1559
Cdd:cd05922 352 -DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
407-467 |
3.10e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 42.29 E-value: 3.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958706127 407 TYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALVFPNNdPaAFMVAFYGCLLAEVVPV 467
Cdd:PRK05605 59 TYAELGKQVRRAAAG-LRALG------VRPGDRVAIVLPNC-P-QHIVAFYAVLRLGAVVV 110
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1417-1545 |
3.74e-03 |
|
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: 41.48 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1417 GKILPGVRIIIANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLRrtel 1496
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958706127 1497 tdangeRHDALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1545
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1422-1546 |
5.66e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.41 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1422 GVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLrrteltDANG 1501
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---GDPTITAANFTDG---------WLRTGDLGSL------SAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958706127 1502 ErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1546
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
407-501 |
6.49e-03 |
|
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: 40.74 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 407 TYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVplTRKDAGSQQIgfl 486
Cdd:cd05934 5 TYAELLRESARIA-AALAALG------IRPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPINT--ALRGDELAYI--- 70
|
90
....*....|....*
gi 1958706127 487 LGSCGVTVALTSDAC 501
Cdd:cd05934 71 IDHSGAQLVVVDPAS 85
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1066-1210 |
6.75e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.31 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 1066 QLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSRSACLM 1145
Cdd:PRK05691 3750 ELNRAANRLGHALRAAGVGVD-QPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP------AQRLQRIIELSRTPVLV 3822
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958706127 1146 TTQlICkLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQ----IYkpSNPDTLAYLDFSVSTTGMLAGV 1210
Cdd:PRK05691 3823 CSA-AC-REQARALLDELGCANRPRLLVWEEVQAGEVAShnpgIY--SGPDNLAYVIYTSGSTGLPKGV 3887
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
406-555 |
7.54e-03 |
|
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: 40.65 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAYNILHKlGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLA--EVVPVPIEVPLTRkdagsqqI 483
Cdd:cd12117 23 LTYAELNERANRLARRLRAA-G------VGPGDVVGVLAERS--PELVVALLAVLKAgaAYVPLDPELPAER-------L 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958706127 484 GFLLGSCGVTVALTsdacHKGLPKSPTGEIPqfkgwpkLLWFVTESKHLSKPPrdwfPHIKDANNDTAYIEY 555
Cdd:cd12117 87 AFMLADAGAKVLLT----DRSLAGRAGGLEV-------AVVIDEALDAGPAGN----PAVPVSPDDLAYVMY 143
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
406-523 |
7.88e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 40.66 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958706127 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 485
Cdd:PRK08276 12 VTYGELEARSNRLA-HGLRALG------LREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLTAAE-----IAY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958706127 486 LLGSCGVTVALTS----DACHKGLPKSP---------TGEIPQFKGWPKLL 523
Cdd:PRK08276 78 IVDDSGAKVLIVSaalaDTAAELAAELPagvplllvvAGPVPGFRSYEEAL 128
|
|
| |
