|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1044-1608 |
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: 794.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1044 LYTLLNCRGTIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIA 1122
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1123 TTLPTVKMivEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA-----QIYKPSNPDTLAYLDFSV 1197
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1198 STTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAV 1277
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1278 SQYKVRDTFCSYSVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGCRV 1357
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1358 NLAICLQGTSGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHN 1437
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1438 ASGYFTIYGDESLQSDHFNS-RLSFGDTQTIWARTGYLGFLRRTELTDANGERHDALYVVGALDEAMELRGMRYHPIDIE 1516
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1517 TSVIRAHKSVTECAVFTWTNLLVVVVELD-GSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINSRGEKQRMHLR 1595
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 568981374 1596 DGFLADQLDPIYV 1608
Cdd:cd05905 559 QAFLAGKLHPIYV 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: 736.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 392 CLTTMDTNGKPLYILTYGKLWTRSMKVAYNILHKLGTKqepmvrPGDRVALVFPnnDPAAFMVAFYGCLLAEVVPVPIEV 471
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLK------PGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 472 PLtrkdaGSQQIGFLLGSCGVTVALTSDACHKGLPKS-----PTGEIPQFKGWPKLLWFVTESKHLSKPPRDWFPHIKDA 546
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 547 NNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLM 626
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 627 KVNPLSWIQKVCQYKAKVACVKSRDMHWAL------VAHRDQRDVNLSSLRMLIVADGaNPWSISSCDAFLNVFQSKGLR 700
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 701 QEvicpcASSPEALTVAIRRPTD--DSNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQDVGLVMPGAIMCSVKPDGIP 778
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWqgTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 779 qLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEVFPMTSSGAPISEYPFIRTGLLGFVGPG----------GLVFVVGK 848
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 849 MDGLMVVSGRRHNADDIVATALAVEPmkfvYRGRIAVFSVTvlhdERIVIVAEQRPDStEEDSFQWMSRVLQAIDSIHQV 928
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPPGS-EEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 568981374 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 ... |
1034-1566 |
2.02e-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: 2.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1034 WRAQTTPDHLLYTLLNCRGTIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITV 1113
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1114 RPPHPqniATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSnPDTLAYL 1193
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1194 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALW 1273
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1274 LLAVSQYkvRDTFcsySVM-----ELCTKglgsQTESLKARGLDLSRVRTCVVVAEeRPRIALTQSFSKLFKDLGLHPRA 1348
Cdd:cd05931 235 LRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFRPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1349 VSTSFGcrvnLA-ICL---QGTSGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGD 1424
Cdd:cd05931 305 FRPSYG----LAeATLfvsGGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRELPD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1425 SHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRLSFGDtqTIWARTGYLGFLRRteltdanGErhdaLYVVGALDEAME 1504
Cdd:cd05931 380 GEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDE--GGWLRTGDLGFLHD-------GE----LYITGRLKDLII 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981374 1505 LRGMRYHPIDIETSVIRAHKSVTE--CAVFTW----TNLLVVVVELDGSeQEALDLVPLVTNV---VLEEH 1566
Cdd:cd05931 444 VRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
406-959 |
9.69e-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: 215.95 E-value: 9.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAYNILHKLgtkqepmvRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPLTRKDAgsQQIGF 485
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVG--------KPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPPPTPGRHA--ERLAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 486 LLGSCGVTVALTSDACHKGLPKSptgeIPQFKGWPKLLWFVTESKHLSkPPRDWFPHIKDANnDTAYIEYKTCKDGSVLG 565
Cdd:cd05931 93 ILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPPPSPDPD-DIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 566 VTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISI-PYSLMKvNPLSWIQKVCQYKAKV 644
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 645 ACVKsrDMHWALVAHR----DQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIR 719
Cdd:cd05931 246 SAAP--NFAYDLCVRRvrdeDLEGLDLSSWRVALN--GAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 720 RPtddsNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQdVGLVMPG---AIMCsvkPDGiPQLCRTDEIGELCVC--AV 794
Cdd:cd05931 322 PP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDqevRIVD---PET-GRELPDGEVGEIWVRgpSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 795 ATGtsYYGLSGMTKNTFEVFpmtssgAPISEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEP 874
Cdd:cd05931 393 ASG--YWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 875 MkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSET 954
Cdd:cd05931 464 A--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRAC 541
|
....*
gi 568981374 955 KQLFL 959
Cdd:cd05931 542 RAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1032-1506 |
1.33e-58 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 208.71 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1032 LQWRAQTTPDHLLYTllNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPI 1111
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGR---RLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1112 TVRPphpqniATTLPTVKMIVEVSRSACLMTTQlICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSN----- 1186
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDD-ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1187 ------PDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCE----LYPSREVAICLDPYCGLGFVLWCLCSVYSGH 1256
Cdd:pfam00501 148 pppppdPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1257 QSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSVMELCTkglgsqtESLKARGLDLSRVRTCVVVAEeRPRIALTQSFS 1336
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLL-------EAGAPKRALLSSLRLVLSGGA-PLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1337 KLFkdlglhPRAVSTSFGCRVNLAICLQGTSGPDPTTVYvdmralrhdrvrlverGSPhslplmesGKILPGVRIIIANP 1416
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLRSL----------------GSV--------GRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1417 ETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVV 1496
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DEDGY----LEIV 407
|
490
....*....|
gi 568981374 1497 GALDEAMELR 1506
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1189-1553 |
6.59e-39 |
|
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: 148.97 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1189 TLAYLDFSVSTTGMLAGVKMSH---AATSAFCRSIKlqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSe 1265
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnlLAAAAALAASG----GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1266 letNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPrIALTQSFSKLFKD---- 1341
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGIklvn 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1342 -LGLHPRAVSTSFGCRVNLAIclqgtsgpDPTTVyvdmralrhdrvrlvergsphslplmesGKILPGVRIIIANPETkG 1420
Cdd:cd04433 145 gYGLTETGGTVATGPPDDDAR--------KPGSV----------------------------GRPVPGVEVRIVDPDG-G 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1421 PLGDSHLGEIWVHSAHNASGYFTiygdeslqsdhfNSRLSFGDTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALD 1500
Cdd:cd04433 188 ELPPGEIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------DEDGY----LYIVGRLK 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568981374 1501 EAMELRGMRYHPIDIETsVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 1553
Cdd:cd04433 246 DMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1028-1548 |
5.49e-36 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 150.32 E-value: 5.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1028 LSEVLQWRAQTTPDHLLYTLLNCRGTIANSLTCVQLHKRAEKIAVMLMERGHLqdGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1108 CV------PITVRPPHPQNIATtlptvkmIVEVSRSACLMTTQLICKLLRSREAAAAVDVrtwPLILDTDDLPKKRPAQI 1181
Cdd:PRK05691 89 VIavpaypPESARRHHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1182 YKPS-NPDTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsiklqCELYPSREVAICLDP----------YCGLGFVLWCLC 1250
Cdd:PRK05691 159 QEPAlQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1251 SVYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGsqtESLKARgLDLSRVRtcVVVAEERP-RI 1329
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVS---ESALER-LDLSRWR--VAYSGSEPiRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1330 ALTQSFSKLFKDLGLHPRAVSTSFGCRVNLAICLQGTSGPDPTTVYVDMRALRHDRVRLVErGSphslPLMESGKILPGV 1409
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGT-GS----VLMSCGRSQPGH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1410 RIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgDTQTiWARTGYLGFLRRTEltdanger 1489
Cdd:PRK05691 380 AVLIVDPQSLEVLGDNRVGEIWASGPSIAHGY---WRNPEASAKTFVEH----DGRT-WLRTGDLGFLRDGE-------- 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 568981374 1490 hdaLYVVGALDEAMELRGMRYHPIDIETSVIRahksvtECAVFTWTNLLVVVVELDGSE 1548
Cdd:PRK05691 444 ---LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1031-1562 |
7.76e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 136.23 E-value: 7.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1031 VLQWRAQTTPDHLLYTLLNCR---GTIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1108 CVPITVRPPHPQN--------IATTLPTVkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA 1179
Cdd:PRK05850 84 LIAVPLSVPQGGAhdervsavLRDTSPSV-----------VLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1180 QIYKPSNPDTlAYLDFSVSTTGMLAGVKMSHAATSAFCRsiKLQCELYPSREVAICLD-------P-YCGLGFVLWCLCS 1251
Cdd:PRK05850 153 DARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1252 VYSGHQSILIPPSELETNPALW--LLAVSQYkvrdtfcSYSV-----MELCTKglgsQTESLKARGLDLSRVRTcVVVAE 1324
Cdd:PRK05850 230 ILGGCPAVLTSPVAFLQRPARWmqLLASNPH-------AFSAapnfaFELAVR----KTSDDDMAGLDLGGVLG-IISGS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1325 ERPRIALTQSFSKLFKDLGLHPRAVSTSFG---CRVNLAIclqGTSGPDPTTVYVDMRALRHDRVR---------LVERG 1392
Cdd:PRK05850 298 ERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1393 SPHSlplmesgkilPGVRIIiaNPETKGPLGDSHLGEIWVHSAHNASGYFTiyGDESLQSDhFNSRL---SFGDTQTIWA 1469
Cdd:PRK05850 375 SPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAAGYWQ--KPEETERT-FGATLvdpSPGTPEGPWL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1470 RTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVirahKSVT--ECAVFT----WTNLLVVVVE 1543
Cdd:PRK05850 440 RTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATI----QEITggRVAAISvpddGTEKLVAIIE 504
|
570 580
....*....|....*....|..
gi 568981374 1544 L---DGSEQEALDLVPLVTNVV 1562
Cdd:PRK05850 505 LkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1028-1555 |
9.15e-32 |
|
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: 130.70 E-value: 9.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1028 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:COG0318 1 LADLLRRAAARHPDR---PALVFGGR---RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1108 CVPITVrpphpqNIATTLPTVKMIVEVSRSACLMTtqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnp 1187
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1188 dtlAYLDFSvS-TTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPpsel 1266
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1267 ETNPALWLLAVSQYKVrdTFCSYS---VMELCtkglgsqtESLKARGLDLSRVRTCVVVAEerpriALTQSFSKLFKDLg 1343
Cdd:COG0318 175 RFDPERVLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1344 lhpravstsFGCRVNLA-----ICLQGTSGPDpttvyvDMRALRHDRVrlvergsphslplmesGKILPGVRIIIANPET 1418
Cdd:COG0318 239 ---------FGVRIVEGyglteTSPVVTVNPE------DPGERRPGSV----------------GRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1419 KgPLGDSHLGEIWVHSAHNASGYftiYGDESLqsdhfnSRLSFGDTqtiWARTGYLGFLrrteltDANGErhdaLYVVGA 1498
Cdd:COG0318 288 R-ELPPGEVGEIVVRGPNVMKGY---WNDPEA------TAEAFRDG---WLRTGDLGRL------DEDGY----LYIVGR 344
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981374 1499 LDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLVVVVEL-DGSEQEALDLV 1555
Cdd:COG0318 345 KKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
373-961 |
2.19e-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: 131.25 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 373 PPSLEAALQRWGTISPKAPClTTMDTNGKPlYILTYGKLWTRsmkvAYNILHKLGTKQepmVRPGDRVALVFPNNDpaAF 452
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSE-EFQSYQDLLED----ARRLAAGLRQLG---LRPGDSVILQFDDNE--DF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 453 MVAFYGCLLAEVVPVPIEVPLTRKDAGSQ-----QIGFLLGSCgvtVALTSDACHKGLpksptgeIPQFKGWPKLLWFVT 527
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSP---VVLTDAELVAEF-------AGLETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 528 ESKHLSKPPRDWFPHIKDAnNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHG 607
Cdd:cd05906 148 SIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 608 ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKV------ACVKSRDmhwaLVAHRDQRDVNLSSLRMLIVADGANp 681
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 682 wSISSCDAFLNVFQSKGLRQEVICPCASSPEalTVAirrptddsnqppgrgvlsmhGLTYGviRVDSEEKLS-VLTVQDV 760
Cdd:cd05906 302 -VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS--------------------GVIYS--RSFPTYDHSqALEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 761 GLVMPGAIMCSVKPDGipQLCRTDEIGELCVCavatGTS----YYGLSGMTKNTFevfpmTSSGapiseypFIRTGLLGF 836
Cdd:cd05906 357 GRPIPGVSMRIVDDEG--QLLPEGEVGRLQVR----GPVvtkgYYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 837 VGPGGLVFvVGKMDGLMVVSGRRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHD--ERIVIVAeqrpdSTEEDSFQW 914
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFF-----VPEYDLQDA 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 568981374 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 |
1.87e-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: 123.77 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 376 LEAALQRWGTISPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVA 455
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS--PEFVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 456 FYGCLLAEVVPVPIEVPLTRKdagsqQIGFLLGSCGVTVALTSDACH----KGLPKsptgeipqfkgwpkllwfvteskh 531
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 532 lskpprdwfphikdanndtayieyktckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTS 611
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 612 VMNMMHVISIPyslmKVNPLSWIQKVCQYKA-KVACVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAF 690
Cdd:COG0318 164 LLAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 691 LNVFQSkglrqeVICPC-ASSpEALTVAIRRPTDDSNQPPGRgvlsmhgltygvirvdseeklsvltvqdVGLVMPGAIM 769
Cdd:COG0318 236 EERFGV------RIVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 770 CSVKPDGIPqlCRTDEIGELCVC--AVATGtsYYGLSGMTKNTFEVfpmtssgapiseyPFIRTGLLGFVGPGGLVFVVG 847
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVVRgpNVMKG--YWNDPEATAEAFRD-------------GWLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 848 KMDGLMVVSGRRHNADDIVATALAVEPMKfvyrgRIAVFSVTV-LHDERIV--IVAEQRPDSTEEDSFQWMSRVL---QA 921
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 568981374 922 IDSIHQVGvyclalvpanTLPKTPLGGIHLSETKQLFLEGSL 963
Cdd:COG0318 419 PRRVEFVD----------ELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
406-965 |
6.37e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 123.96 E-value: 6.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAYNILhKLGtkqepmVRPGDRVALVfPNNDPAaFMVAFYGCLLAEVVPVPIEVP--LTRKDAGSQQI 483
Cdd:PRK09192 50 LPYQTLRARAEAGARRLL-ALG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 484 GFLLGSCGVTVALTSDACHKGLPKSPTGEIPQFKGWPKLLwfvteskHLSKPPRDWFPHIKDanNDTAYIEYKTckdGSV 563
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWF-------KALPEADVALPRPTP--DDIAYLQYSS---GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 564 ---LGVTVTRIALLTHCQALTQ-ACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQ 639
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 640 YKAKVAcvKSRDMHWALVAHR----DQRDVNLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlT 715
Cdd:PRK09192 269 NRGTIS--YSPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 716 VAIrrptddSNQPPGRGV----LSMHGLTYGVIRVDSEEK-LSVLTVQDVGLVMPGAIMCSVKPDGIPQLCRtdEIGELC 790
Cdd:PRK09192 344 LAV------SFSPLGSGIvveeVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPLPER--VVGHIC 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 791 VcavatgtsyYGLSGMTkntfEVFPMTSSGAPISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATAl 870
Cdd:PRK09192 416 V---------RGPSLMS----GYFRDEESQDVLAADGWLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIA- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 871 avEPMKFVYRGRIAVFSVTVLHDERIVIVAEQRPdSTEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLGGI 949
Cdd:PRK09192 481 --EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKL 555
|
570
....*....|....*.
gi 568981374 950 HLSETKQLFLEGSLHP 965
Cdd:PRK09192 556 SRAKAKKRYLSGAFAS 571
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1055-1526 |
5.84e-27 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 118.31 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1055 ANSLTCVQLHKRAEKIAVMLMErgHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNIATTLPTVkmiVEV 1134
Cdd:PRK12476 66 AVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTA---LRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1135 SRSACLMTTQLICKLLRSREAAAAVDVRtwPLILDTDDLPKkRPAQIYKPSNPDT--LAYLDFSVSTTGMLAGVKMSHAA 1212
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPD-SAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1213 TSA----FCRSIKLqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHqSILIPPSELETNPALWLLAVSQ-YKVRDTFC 1287
Cdd:PRK12476 218 VGTnlvqMILSIDL---LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1288 SYS--VMELCT-KGLGSQTEslkarGLDLSRVrtCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrVNLAICLQ 1364
Cdd:PRK12476 294 AAPnfAYEWAAqRGLPAEGD-----DIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1365 GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYF 1442
Cdd:PRK12476 365 ATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYW 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1443 TiYGDESLQSDH--FNSRLSFG------DTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGALDEAMELRGMRYHPID 1514
Cdd:PRK12476 445 G-RPEETERTFGakLQSRLAEGshadgaADDGTWLRTGDLGVYL-------DGE----LYITGRIADLIVIDGRNHYPQD 512
|
490
....*....|..
gi 568981374 1515 IETSVIRAHKSV 1526
Cdd:PRK12476 513 IEATVAEASPMV 524
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
435-963 |
8.17e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 114.83 E-value: 8.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 435 RPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPltrKDAG-SQQIGFLLGSCGVTVALTSDACHKGLPKSptgei 513
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP---AEPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKF----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 514 pqFKGWPKllwfvteskhlSKPPR-------------DWFPhiKDANNDT-AYIEYKTckdGSV---LGVTVTRIALLTH 576
Cdd:PRK07769 147 --FRARPA-----------KERPRviavdavpdevgaTWVP--PEANEDTiAYLQYTS---GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 577 CQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNmmHVISI--PYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHW 654
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 655 A--LVAHR-----DQRDVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEALTVAIRRPTDDSNQ 727
Cdd:PRK07769 286 AfeHAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 728 ppgrgvlsmhgltygVIRVDSEEkLSVLTVQDVGLVMPGAI-------------MCSVKPDGIPQLcRTDEIGELCVCAV 794
Cdd:PRK07769 364 ---------------VIYVDRDE-LNAGRFVEVPADAPNAVaqvsagkvgvsewAVIVDPETASEL-PDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 795 ATGTSYYGLSGMTKNTFE------VFPMTSSGAPiSEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVAT 868
Cdd:PRK07769 427 NIGTGYWGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 869 ALavEPMKFVYRGRIAVFSV-------TVLHD-------------ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQV 928
Cdd:PRK07769 505 AQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGV 582
|
570 580 590
....*....|....*....|....*....|....*
gi 568981374 929 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSL 963
Cdd:PRK07769 583 TVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1032-1526 |
3.24e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 112.90 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1032 LQWRAQTTPDHLLYTLLNC---RGTIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAGC 1108
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDFsteRDGVARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1109 VPITVRPPHPQNIATTLPTVkmIVEVSRSACLMTT---QLICKLLRSREAAAAvdvrtwPLILDTDDLPKKRPAQIYKPS 1185
Cdd:PRK07769 105 IAVPLFDPAEPGHVGRLHAV--LDDCTPSAILTTTdsaEGVRKFFRARPAKER------PRVIAVDAVPDEVGATWVPPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1186 -NPDTLAYLDFSVSTTGMLAGVKMSH--AATSAF--CRSIKLQcelYPSREVAiCLDPYCGLGFVLWCLCSVYSGHQSIL 1260
Cdd:PRK07769 177 aNEDTIAYLQYTSGSTRIPAGVQITHlnLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1261 IPPSELEtNPALWLLAVSQyKVRDTFCSYSV-----MELCT-KGLGSQTESlkarGLDLSRVRtCVVVAEERPRIALTQS 1334
Cdd:PRK07769 253 SPAAFVR-RPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNGSEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1335 FSKLFKDLGLHPRAVSTSFGcrVNLAICLQGTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRII 1412
Cdd:PRK07769 326 FNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1413 IANPETKGPLGDSHLGEIWVHSAHNASGYftiYG--DESLQSDH--FNSRLSFGDTQ-----TIWARTGYLGflrrtelT 1483
Cdd:PRK07769 404 IVDPETASELPDGQIGEIWLHGNNIGTGY---WGkpEETAATFQniLKSRLSESHAEgapddALWVRTGDYG-------V 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568981374 1484 DANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSV 1526
Cdd:PRK07769 474 YFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1028-1541 |
3.67e-25 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 111.99 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1028 LSEVLQWRAQTTPDHLLYTllncrgtIANSLTCV-----QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYG 1102
Cdd:cd05906 12 LLELLLRAAERGPTKGITY-------IDADGSEEfqsyqDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1103 CLYAGCVPITVRPPHP-QNIATTLPTVKMIVEVSRSA-CLMTTQLICKLLRSREAA--AAVDVRTWPLILDTDDLPKKRP 1178
Cdd:cd05906 84 CVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPvVLTDAELVAEFAGLETLSglPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1179 AQiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSiKLQCELYPSREVA---ICLDPYCGLGFVlwCLCSVYSG 1255
Cdd:cd05906 164 SR------PDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1256 HQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSvmeLCTKgLGSQTESLKARGLDLSRVRtCVVVAEERPRIALTQSF 1335
Cdd:cd05906 235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1336 SKLFKDLGLHPRAVSTSFG----CrvnlaiclqgtSGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKILPGVRI 1411
Cdd:cd05906 310 LRLLEPYGLPPDAIRPAFGmtetC-----------SG---VIYSRSFPTYDH----------SQALEFVSLGRPIPGVSM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1412 IIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaNGErhd 1491
Cdd:cd05906 366 RIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFLD-------NGN--- 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 568981374 1492 aLYVVGALDEAMELRGMRYHPIDIETSV----IRAHKSVTECAVF---TWTNLLVVV 1541
Cdd:cd05906 424 -LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRdpgAETEELAIF 479
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1018-1551 |
1.57e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 110.48 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1018 DNDQARK---FLFLSEVLQWRAQTTPDHLLYTLlncRGTIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGI 1094
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFYDR---RGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1095 DLIAAFYGCLYAGCVPITVrpPHPQNI---ATTLPTVKMIVEVSRSACLMTTQLICKLLrsREAAAAVDVRtWPLILDTD 1171
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLL-HVLSHAWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1172 DLPKKRPAQIYKPSnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQ-CELYPSREVAICLDPYCGLGFVlWCLC 1250
Cdd:PRK09192 161 KALPEADVALPRPT-PDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGLV-GFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1251 SVYSGHQSI-LIPPSELETNPALWLLAVSqyKVRDTFcSYSV---MELCTKGLGSQTESlkarGLDLSRVRTCVVVAEE- 1325
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGADMi 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1326 RPRIalTQSFSKLFKDLGLHPRAVSTSFG-CRVNLAIclqgtSGPDPTTvyvDMRALRHDRVRLVERGspHSLPLMES-- 1402
Cdd:PRK09192 312 RPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAV-----SFSPLGS---GIVVEEVDRDRLEYQG--KAVAPGAEtr 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1403 --------GKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESlqsdhfnsrlsfgDTQTI----WAR 1470
Cdd:PRK09192 380 rvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYF---RDEE-------------SQDVLaadgWLD 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1471 TGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSV-----IRAHksvtECAVFTWTN----LLVVV 1541
Cdd:PRK09192 443 TGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqepeLRSG----DAAAFSIAQengeKIVLL 507
|
570
....*....|
gi 568981374 1542 VELDGSEQEA 1551
Cdd:PRK09192 508 VQCRISDEER 517
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
399-961 |
2.53e-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: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 399 NGKPLYIlTYGKLWTrsmkvayNILHKLGTKQEPMVRPGDRValVFPNNDPAAFMVAFYGCLLAEVVPVPievpltrkda 478
Cdd:cd05908 10 DKKEKFV-SYRHLRE-------EALGYLGALQELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVP---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 479 gsqqigfllgscgvtVALTSDACHKglpksptgeIPQFKGWPKLL--WFVTESKHLSKPPrdwfphikdanNDTAYIEYK 556
Cdd:cd05908 70 ---------------VSIGSNEEHK---------LKLNKVWNTLKnpYLITEEEVLCELA-----------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 557 TCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQK 636
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 637 VCQYKAKVACVKSRDMHWALVAHRDQR--DVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAl 714
Cdd:cd05908 195 ASEHKATIVSSPNFGYKYFLKTLKPEKanDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 715 TVAIRRPTDDSNQPPgrgvLSMH--GLTYG--VIRVDSEEKlSVLTVQDVGLVMPgaiMCSVK-PDGIPQLCRTDEIGEL 789
Cdd:cd05908 272 SVGASLPKAQSPFKT----ITLGrrHVTHGepEPEVDKKDS-ECLTFVEVGKPID---ETDIRiCDEDNKILPDGYIGHI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 790 CVCAVATGTSYYGLSGMTKNTfevfpMTSSGapiseypFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATA 869
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKV-----FTDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIA 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 870 LAVEPmkfVYRGRIAVFSV--TVLHDERIVIVAEQRpdsTEEDSFQWMSRVLQAID------SIHQVgvyclalVPANTL 941
Cdd:cd05908 411 EELEG---VELGRVVACGVnnSNTRNEEIFCFIEHR---KSEDDFYPLGKKIKKHLnkrggwQINEV-------LPIRRI 477
|
570 580
....*....|....*....|
gi 568981374 942 PKTPLGGIHLSETKQLFLEG 961
Cdd:cd05908 478 PKTTSGKVKRYELAQRYQSG 497
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1062-1531 |
3.10e-24 |
|
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: 107.35 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1062 QLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITvrPPHPQN-IATtlptvkmIVEVSRSA 1138
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAayVPLD--PAYPAErLAF-------ILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1139 CLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAqiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCR 1218
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1219 SIklqCELYPSREVAICLDpYCGLGF------VLWCLcsvYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVM 1292
Cdd:TIGR01733 151 WL---ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1293 ELCtkglgsqtesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLHpravstsfgcrvNlaiclqgTSGPDPT 1372
Cdd:TIGR01733 224 ALL----------AAALPPALASLRL-VILGGEALTPALVDRWRARGPGARLI------------N-------LYGPTET 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1373 TVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYFtiyGDESLQS 1452
Cdd:TIGR01733 274 TVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGYL---NRPELTA 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568981374 1453 DHFNSRLSFGDTQTIWARTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1531
Cdd:TIGR01733 342 ERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
380-856 |
9.34e-24 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 105.86 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 380 LQRWGTISPKAPCLTTMDTngkplYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGC 459
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG-----RRLTYRELDERANRLA-AGLRALG------VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 460 LLAEVVPVPIEVpltrkDAGSQQIGFLLGSCGVTVALTSD--------ACHKGLPKSPTGEIPQFKGWPKLLWFVTESKH 531
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 532 LSKPPRdwfPHIKDANNDTAYIEY--------KtckdgsvlGVTVTRIALLTHCQALTQAC----GYTEAETIVNVLDFK 599
Cdd:pfam00501 142 ADVPPP---PPPPPDPDDLAYIIYtsgttgkpK--------GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 600 KDVGLWHGILTSVMNMMHVISIPYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHwALVAHRDQRDVNLSSLRMLIVadGA 679
Cdd:pfam00501 211 HDFGLSLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERYKVTVLYGVPTLLN-MLLEAGAPKRALLSSLRLVLS--GG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 680 NPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptddsnqppGRGVLSMHGLT--YGVIRVDSEEKLSVLTV 757
Cdd:pfam00501 287 APLPPELARRFRELF-----------------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 758 QDVGLVMPGAIMCSVKPDGIpQLCRTDEIGELCV--CAVATGtsYYGLSGMTKNTFEvfpmtssgapisEYPFIRTGLLG 835
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCVrgPGVMKG--YLNDPELTAEAFD------------EDGWYRTGDLG 396
|
490 500
....*....|....*....|.
gi 568981374 836 FVGPGGLVFVVGKMDGLMVVS 856
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
375-949 |
5.33e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 105.79 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 375 SLEAALQRWGTISPKAPCLTTMDTNGKPLYI---LTYGKLWTRSMKVAYNiLHKLGtkqepmvRPGDRVALVFPNNdpAA 451
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIDYEQDPAGVaetLTWSQLYRRTLNVAEE-LRRHG-------STGDRAVILAPQG--LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 452 FMVAFYGCLLAEVVPVPIEVPLTRkdAGSQQIGFLLGSCGVTVALTS----DACHKGLPKSPTGEIPqfkgwpkllWFVT 527
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQSAP---------PVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 528 ------ESKHLSKPPRDWFPhikdannDTAYIEYKTCKDGSVLGVTVTRIALLTHC-QALTQACGYTEAE-----TIVNV 595
Cdd:PRK05850 141 vdlldlDSPRGSDARPRDLP-------STAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 596 LDFKKDVGLWHGILTSVMNMMH-VISIPYSLMKvNPLSWIQKVCQYKAKVACVKSrdmhWAL-VAHRDQRDVNLSSL--- 670
Cdd:PRK05850 214 LPFYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQLLASNPHAFSAAPN----FAFeLAVRKTSDDDMAGLdlg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 671 RMLIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIRRPtddsNQPPGrgvlsmhgltygVIRVDSE 749
Cdd:PRK05850 289 GVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP----GQPPE------------SVRFDYE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 750 eKLSVLTVQ----DVG--LVMPGAIMCS----VKPDGIPQlCRTDEIGELCVCA--VATGtsYYGLSGMTKNTFE---VF 814
Cdd:PRK05850 353 -KLSAGHAKrcetGGGtpLVSYGSPRSPtvriVDPDTCIE-CPAGTVGEIWVHGdnVAAG--YWQKPEETERTFGatlVD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 815 PmtSSGAPISeyPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalavepMKFVYRGRIAVFSVTVLHDE 894
Cdd:PRK05850 429 P--SPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTE 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 895 RIVIVAE-QRPDSTEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 949
Cdd:PRK05850 498 KLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-174 |
6.15e-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: 6.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 8 GMALPLEVRARLAELELELSEGDITQKGYEKKRSKLIGAYLPQPptangaavvrcrlqpgegvprrpfrsahigvcdire 87
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHP------------------------------------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 88 aaareraasaagnrplfyfrfgvdqalpqerRAPVTPSSASRYHR-RRSSGSRDERYRSDVHTEAVQAALAKHKERKMAV 166
Cdd:pfam06464 46 -------------------------------ETPTKLSAEAQNQLaSLETKLRDEELSEEVYLEKVKALLAKELERENGL 94
|
....*...
gi 568981374 167 PMPSKRRS 174
Cdd:pfam06464 95 NAPTKEQS 102
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1052-1532 |
9.75e-23 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 103.83 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1052 GTIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCvpitvrPPHPQNIATTLPTVKMI 1131
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1132 VEVSRSACLMTTQliCKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSN--------------PDTLAYLDFSV 1197
Cdd:cd05911 78 LKISKPKVIFTDP--DGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLgeededlppplkdgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1198 STTGMLAGVKMSHaatSAFCRSIKLQC----ELYPSREVAICLDPY---CGLgfvLWCLCSVYSGHQSILIPpselETNP 1270
Cdd:cd05911 156 GTTGLPKGVCLSH---RNLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMP----KFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1271 ALWLLAVSQYKVRDTFCSYSVMELctkgLGSQTESLKArglDLSRVRTCVVVAEerpriALTQSFSKLFKdlglhpravs 1350
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGGA-----PLSKELQELLA---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1351 tsfgCRVNLAICLQG-----TSGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVRIIIANPETKGPLGDS 1425
Cdd:cd05911 284 ----KRFPNATIKQGygmteTGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKDSLGPN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1426 HLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMEL 1505
Cdd:cd05911 341 EPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYF------DEDGY----LYIVDRKKELIKY 399
|
490 500
....*....|....*....|....*..
gi 568981374 1506 RGMRYHPIDIEtSVIRAHKSVTECAVF 1532
Cdd:cd05911 400 KGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
397-965 |
2.44e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 103.67 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 397 DTNGKPLYiLTYGKLWTRsmkvayniLHKLGTKQEPMVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPI---EVPl 473
Cdd:PRK12476 61 SAAGCAVE-LTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfapELP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 474 trkdAGSQQIGFLLGSCGVTVALTSDAChkglpkspTGEIPQFkgwpkllwfvteskhLSKPPRDWFPH------IKDA- 546
Cdd:PRK12476 129 ----GHAERLDTALRDAEPTVVLTTTAA--------AEAVEGF---------------LRNLPRLRRPRviaidaIPDSa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 547 ----------NNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETI-VNVLDFKKDVGLWHGILTSVMNM 615
Cdd:PRK12476 182 gesfvpveldTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 616 MHVISIPYSLMKvNPLSWIQKV---CQYKAKVACVKSRDMHWAlvAHR----DQRDVNLSSLRMLIvadGANPWSISSCD 688
Cdd:PRK12476 262 HSTLMSPTAFVR-RPQRWIKALsegSRTGRVVTAAPNFAYEWA--AQRglpaEGDDIDLSNVVLII---GSEPVSIDAVT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 689 AFLNVFQSKGLRQEVICPCASSPEA-LTVAirrpTDDSNQPPGRGVLSMHGLTYG-VIRVDSEEKLSVLTVQdVGLVMPG 766
Cdd:PRK12476 336 TFNKAFAPYGLPRTAFKPSYGIAEAtLFVA----TIAPDAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 767 AIMCSVKPDGIPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFEV-----FPMTS--SGAPISEyPFIRTGLLGFVGP 839
Cdd:PRK12476 411 QWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDG-TWLRTGDLGVYLD 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 840 GGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVL 919
Cdd:PRK12476 489 GEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 568981374 920 QAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 965
Cdd:PRK12476 566 AAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1055-1534 |
3.47e-21 |
|
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: 99.37 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1055 ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPItvrpphPQNIATTLPTVKMIVEV 1134
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1135 SRSACLMTTQLICKLLRSREAAAAVDVRT----------WPLILDTDDLPKKRPAQIYKPSNPDTLAYLDFSVSTTGMLA 1204
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1205 GVKMSHAatsafcrSIKLQCELYPSREVAICLDPYC----------GLGFVLWCLCSVysGHQSILIPpsELETnPALWL 1274
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP--ERPT-PAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1275 LAVSQYKvRDTFcsYSVMELCTKGLGSqtESLKARglDLSRVRTCVVVAEerpriALTQSFSKLFKDLglhpravstsFG 1354
Cdd:cd05959 248 KRIRRYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGE-----ALPAEVGERWKAR----------FG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1355 CRVnlaicLQGTSGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHS 1434
Cdd:cd05959 306 LDI-----LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELYVRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1435 AHNASGYFTIYGDeslqsdhfnSRLSFgdtQTIWARTGYlGFLRrteltDANGerhdALYVVGALDEAMELRGMRYHPID 1514
Cdd:cd05959 366 PSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLKVSGIWVSPFE 423
|
490 500
....*....|....*....|
gi 568981374 1515 IEtSVIRAHKSVTECAVFTW 1534
Cdd:cd05959 424 VE-SALVQHPAVLEAAVVGV 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1057-1554 |
1.64e-18 |
|
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: 90.28 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSR 1136
Cdd:cd05930 12 SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE------RLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1137 SACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1216
Cdd:cd05930 85 AKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1217 CRSIKlqcELYP--SREVAICLDPYcglGF------VLWCLCSvysGHQsILIPPSELETNPALWLLAVSQYKVRDTFCS 1288
Cdd:cd05930 122 LLWMQ---EAYPltPGDRVLQFTSF---SFdvsvweIFGALLA---GAT-LVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1289 YSVMELCTKGLGSQteslkarglDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLhpravstsfgcrVNLaiclqgtSG 1368
Cdd:cd05930 192 PSLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1369 PDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDE 1448
Cdd:cd05930 243 PTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---LNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1449 SLQSDHFNSrLSFGDTQTIWaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTE 1528
Cdd:cd05930 310 ELTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLAHPGVRE 376
|
490 500 510
....*....|....*....|....*....|..
gi 568981374 1529 CAVFTWTN------LLVVVVELDGSEQEALDL 1554
Cdd:cd05930 377 AAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
373-993 |
1.87e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.99 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 373 PPSLEAALQRWGTISPKAPCLTTMDTNGKPLYILTYGKLWTRSMKVAYNIlhklgtkqEPMVRPGDRVALVFPNNdpAAF 452
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 453 MVAFYGCLLAEVVPVPIEVPLTRKDAGSQQIGFLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkGWPKLLwfvTESKHL 532
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPELL---CVDTLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 533 SKPPRDWF-PHIKDanNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACG--YTEAETIVNVLDFKKDVGLWHGIL 609
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 610 TSVMNmmhviSIPYSLMKVN-----PLSWIQKVCQYKAKVAcvKSRDMHWALVAHRdQRDVNLSSL---RMLIVADGANP 681
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 682 WSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAirrptddsNQPPGRGVlsmhgltyGVIRVDSE-------EKLS 753
Cdd:PRK05691 302 IRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS--------GGRRGQGI--------PALELDAEalarnraEPGT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 754 VLTVQDVGLVMPGAIMCSVKPDGIPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFevfpMTSSGApiseyPFIRTGL 833
Cdd:PRK05691 366 GSVLMSCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 834 LGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalAVEPMKFVYRGRIAVFSVTVLHDERIVIVAE-----QRPDSTE 908
Cdd:PRK05691 436 LGFLRDGEL-FVTGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 909 EdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLhpcnvlmcphTCVTNLPKPRQKQPE 988
Cdd:PRK05691 513 A----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAA 578
|
....*
gi 568981374 989 IGPAS 993
Cdd:PRK05691 579 QTAAS 583
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1062-1531 |
1.31e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 78.65 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1062 QLHKRAEKIAVMLMERGhlqDGDHVALVYPPGIDLIAAFYGCLYAG----CVPITVRPPHPQNIA-TTLptvkmivevSR 1136
Cdd:PRK05851 36 EVHGRAENVAARLLDRD---RPGAVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWAdATL---------TR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1137 SACLMTTQLIC-----KLLRSREAAAAV-DVRTWPlildtddlpKKRPAQIYKPSNPDTLAYLDFSVSTTGMLAGVKMSH 1210
Cdd:PRK05851 104 FAGIGVRTVLShgshlERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1211 AATSAFCRSIKLQCELYPSREVAICLDPY---CGLGFVLwclCSVYSGHQSILIPPSELETNPALWLLAVSQykVRDTFC 1287
Cdd:PRK05851 175 GAVLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSD--SRATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1288 SYSVMELCTKGLGSQteslKARGLDLSRVRTCVVVAEerP-RIALTQSFSKLFKDLGLHPRAVSTSFGcrvnLAICLQGT 1366
Cdd:PRK05851 250 AAPNFAYNLIGKYAR----RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG----LAESTCAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1367 SGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYFtiyG 1446
Cdd:PRK05851 320 TVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYL---G 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1447 DESLQSDHfnsrlsfgdtqtiWARTGYLGFlrrteLTDangerhDALYVVGALDEAMELRGMRYHPIDIETSVIRAhKSV 1526
Cdd:PRK05851 389 QAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGV 443
|
....*
gi 568981374 1527 TECAV 1531
Cdd:PRK05851 444 REGAV 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1186-1516 |
1.26e-13 |
|
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: 75.60 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1186 NPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSE 1265
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1266 LETNPALWLLAVSQYKVRDTFCSysvmELCTKGLGSQTESLKARGLDLSRVRTCVVVAEErprIA--LTQSFSKLFKDLG 1343
Cdd:cd05908 184 FIRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1344 LHPRAVSTSFGcrvnLAICLQGTSGPDP----TTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVRIIIANPET 1418
Cdd:cd05908 257 LKRNAILPVYG----LAEASVGASLPKAqspfKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1419 KGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGA 1498
Cdd:cd05908 333 KI-LPDGYIGHIQIRGKNVTPGY---YNNPEATAKVF--------TDDGWLKTGDLGFIR-------NGR----LVITGR 389
|
330
....*....|....*...
gi 568981374 1499 LDEAMELRGMRYHPIDIE 1516
Cdd:cd05908 390 EKDIIFVNGQNVYPHDIE 407
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1057-1531 |
3.97e-13 |
|
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: 73.81 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1057 SLTCVQLHKRAEKIAVMLMERGHLQdGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqniATTLPTVKMIVEVSR 1136
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1137 SACLMTT-QLICKLlrsreAAAAVDVrtwpLILDTDD---LPKKRPAQIYKPSNP-------DTLAYLDFSVSTTGMLAG 1205
Cdd:cd05904 105 AKLAFTTaELAEKL-----ASLALPV----VLLDSAEfdsLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1206 VKMSH----AATSAFCRSIKLQCElypSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPSELETnpalWLLAVSQY 1280
Cdd:cd05904 176 VMLTHrnliAMVAQFVAGEGSNSD---SEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1281 KVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPRiALTQSFSKLFKDlglhpravstsfgcrVNLa 1360
Cdd:cd05904 249 KVTHLPVVPPIVLALVK-------SPIVDKYDLSSLRQIMSGAAPLGK-ELIEAFRAKFPN---------------VDL- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1361 icLQG----TSGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAH 1436
Cdd:cd05904 305 --GQGygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1437 NASGYFtiyGDESlqsdhfnsrlsfgDTQ-TI----WARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYH 1511
Cdd:cd05904 368 IMKGYL---NNPE-------------ATAaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVA 421
|
490 500
....*....|....*....|
gi 568981374 1512 PIDIEtSVIRAHKSVTECAV 1531
Cdd:cd05904 422 PAELE-ALLLSHPEILDAAV 440
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1028-1531 |
2.11e-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: 71.44 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1028 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:cd05936 1 LADLLEEAARRFPDK---TALIFMGR---KLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1108 CVPITVRPphpqniattlptvkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWplildTDDLPKKRPAQIYKPSNP 1187
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1188 DTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsIKLQC-----ELYPSREVAICLDP-YCGLGFVLWCLCSVYSGHQSILI 1261
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1262 P-PSeletnPALWLLAVSQYKVrDTFCS----YSVMelctkglgsqTESLKARGLDLSRVRTCVvvaeerprialtqsfs 1336
Cdd:cd05936 201 PrFR-----PIGVLKEIRKHRV-TIFPGvptmYIAL----------LNAPEFKKRDFSSLRLCI---------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1337 klfkdlglhpravstsfgcrvnlaiclqgtSGPDPTTVYVDMRALRHDRVRLVErG------SP--HSLPLMES------ 1402
Cdd:cd05936 249 ------------------------------SGGAPLPVEVAERFEELTGVPIVE-GygltetSPvvAVNPLDGPrkpgsi 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1403 GKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSrlsfGdtqtiWARTGYLGFLrrtel 1482
Cdd:cd05936 298 GIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGY---WNRPEETAEAFVD----G-----WLRTGDIGYM----- 359
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568981374 1483 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1531
Cdd:cd05936 360 -DEDGY----FFIVDRKKDMIIVGGFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
435-947 |
3.64e-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: 70.55 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 435 RPGDRVALVFPNNDPA---AFMVAFYGCLLAEVVpvpieVPLTrKDAGSQQIGFLLGSCGVTVALTS----DACHKGLPK 507
Cdd:cd05922 16 VRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADagaaDRLRDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 508 SPTGEipqfkgwpklLWFVTESKHLSKPPRDWFPHIKDannDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYT 587
Cdd:cd05922 90 SPDPG----------TVLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 588 EAETIVNVLDFKKDVGLwhgiltSVMNMmH-------VISIPYSLmkvnPLSWIQKVCQYKAK-VACVKSrdmHWALVAH 659
Cdd:cd05922 157 ADDRALTVLPLSYDYGL------SVLNT-HllrgatlVLTNDGVL----DDAFWEDLREHGATgLAGVPS---TYAMLTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 660 RDQRDVNLSSLRMLIVADGANPwsisscDAFLNVFQSKGlrqevicpcasspealtvairrptddsnqpPGRGVLSMHGL 739
Cdd:cd05922 223 LGFDPAKLPSLRYLTQAGGRLP------QETIARLRELL------------------------------PGAQVYVMYGQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 740 TYGVIR---VDSEEKLSVLTvqDVGLVMPGAIMCSVKPDGipQLCRTDEIGELcvcaVATGTSYYgLSGMTKNTFEVFPM 816
Cdd:cd05922 267 TEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDG--TPTPPGEPGEI----VHRGPNVM-KGYWNDPPYRRKEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 817 TSSGApiseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDERI 896
Cdd:cd05922 338 RGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKL 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 568981374 897 VIVAEqRPDSTEEDSfqwMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 947
Cdd:cd05922 406 ALFVT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1036-1557 |
5.37e-12 |
|
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: 69.97 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1036 AQTTPDHLLYTllnCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITV 1113
Cdd:cd05945 1 AAANPDRPAVV---EGGR---TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1114 RPPHPQniattlptVKMIVEVSRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYL 1193
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIAD-------------------------------------------GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1194 DFSVSTTGMLAGVKMSHAATSAFCRSIkLQCELYPSREVAICLDPYcglGF---VLWCLCSVYSGhQSILIPPSELETNP 1270
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPF---SFdlsVMDLYPALASG-ATLVPVPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1271 ALWLLAVSQYKVRDTFCSYSVMELCTkGLGSQTESLkargldLSRVRTCVVVAEERPrIALTQSFSKLFkdlglhPravs 1350
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPES------LPSLRHFLFCGEVLP-HKTARALQQRF------P---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1351 tsfGCRV-NlaiclqgTSGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVRIIIANPETKgPLGDSHLGE 1429
Cdd:cd05945 240 ---DARIyN-------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILDEDGR-PVPPGEKGE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1430 IWVHSAHNASGYFtiyGDEslqsDHFNSRLSFGDTQTiWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMR 1509
Cdd:cd05945 301 LVISGPSVSKGYL---NNP----EKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRLDFQVKLNGYR 362
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568981374 1510 YHPIDIETSViRAHKSVTECAVFTWTNL-----LVVVVELDGSEqEALDLVPL 1557
Cdd:cd05945 363 IELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1036-1531 |
1.88e-11 |
|
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: 68.52 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1036 AQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG--CVPITV 1113
Cdd:cd17651 5 AARTPDA---PALVAEGR---RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1114 RPPhPQNIAttlptvkMIVEVSRSACLMTTQlickllrsREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSNPDTLAYL 1193
Cdd:cd17651 78 AYP-AERLA-------FMLADAGPVLVLTHP--------ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1194 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF--VLWCLCSVYSGHQSILIPPSELETNPA 1271
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTL----QFAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1272 LWLLAVSQYKVRDTFCSYSVME-LCtkglgsqtESLKARGLDLSRVRtCVVVAEERPRIAltqsfsklfkdlGLHPRAVS 1350
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGEQLVLT------------EDLREFCA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1351 TSFGCRvnlaicLQGTSGPDPTTVyVDMRALRHDRVRlveRGSPHSLplmesGKILPGVRIIIANPETKgPLGDSHLGEI 1430
Cdd:cd17651 277 GLPGLR------LHNHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLDAALR-PVPPGVPGEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1431 WVHSAHNASGYFTIYG--DESLQSDHF--NSRLSfgdtqtiwaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELR 1506
Cdd:cd17651 341 YIGGAGLARGYLNRPEltAERFVPDPFvpGARMY---------RTGDLA--RW----LPDGE----LEFLGRADDQVKIR 401
|
490 500
....*....|....*....|....*
gi 568981374 1507 GMRYHPIDIEtSVIRAHKSVTECAV 1531
Cdd:cd17651 402 GFRIELGEIE-AALARHPGVREAVV 425
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1034-1531 |
5.68e-11 |
|
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: 66.92 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1034 WRAQT--TPDH--LLYTllncrgtiANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1109
Cdd:cd17646 4 VAEQAarTPDApaVVDE--------GRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1110 PITVRPPHPQniattlPTVKMIVEVSRSACLMTTQlickllRSREAAAAVDVRTWPLILDTDDLPKKRPAQiykPSNPDT 1189
Cdd:cd17646 75 YLPLDPGYPA------DRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLV---PPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1190 LAYLDFSVSTTGMLAGVKMSHAatsAFCRSIKLQCELYP--SREVAICLDPycgLGF------VLWCLCsvySGhQSILI 1261
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPlgPGDRVLQKTP---LSFdvsvweLFWPLV---AG-ARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1262 PPSELETNPALWLLAVSQYKVrdTFCSY--SVMELCtkglgsqteslkargLDLSRVRTC-----VVVAEErpriALTQS 1334
Cdd:cd17646 210 ARPGGHRDPAYLAALIREHGV--TTCHFvpSMLRVF---------------LAEPAAGSCaslrrVFCSGE----ALPPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1335 FSKLFKDLglhpravstsFGCR-VNLaiclqgtSGPDPTTVYVDmralrHDRVRlvERGSPHSLPLmesGKILPGVRIII 1413
Cdd:cd17646 269 LAARFLAL----------PGAElHNL-------YGPTEAAIDVT-----HWPVR--GPAETPSVPI---GRPVPNTRLYV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1414 ANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHF-------NSRLSfgdtqtiwaRTGYLGflRRTeltdAN 1486
Cdd:cd17646 322 LDDALR-PVPVGVPGELYLGGVQLARGY---LGRPALTAERFvpdpfgpGSRMY---------RTGDLA--RWR----PD 382
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 568981374 1487 GerhdALYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAV 1531
Cdd:cd17646 383 G----ALEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVV 422
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1035-1554 |
6.05e-11 |
|
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: 67.57 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1035 RAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPIT 1112
Cdd:COG1020 485 QAARTPDA---VAVVFGDQ---SLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVPLD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1113 vrPPHPQN-IAttlptvkMIVEVSRSACLMTTQlickLLRSREAAAAVDVrtwpLILDTDDLPKKRPAQIYKPSNPDTLA 1191
Cdd:COG1020 558 --PAYPAErLA-------YMLEDAGARLVLTQS----ALAARLPELGVPV----LALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1192 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF------VLWCLCsvySGHQSILIPPsE 1265
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSFdasvweIFGALL---SGATLVLAPP-E 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1266 LETNPALWLLAVSQYKVrdtfcsySVMELcTKGLGSQTesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLH 1345
Cdd:COG1020 693 ARRDPAALAELLARHRV-------TVLNL-TPSLLRAL--LDAAPEALPSLRL-VLVGGEALPPELVRRWRARLPGARLV 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1346 pravstsfgcrvNLaiclqgtSGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVRIIIAnpetkgplgDS 1425
Cdd:COG1020 762 ------------NL-------YGPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL---------DA 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1426 HL--------GEIWVHSAHNASGYFtiyGDESLQSDHF--NsrlSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYV 1495
Cdd:COG1020 805 HLqpvpvgvpGELYIGGAGLARGYL---NRPELTAERFvaD---PFGFPGARLYRTGDLA--RWL----PDGN----LEF 868
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981374 1496 VGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVFTWTN-----LLVVVVELDGSEQEALDL 1554
Cdd:COG1020 869 LGRADDQVKIRGFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAAL 931
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
565-949 |
3.14e-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: 63.46 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 565 GVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV 644
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 645 ACVkSRDMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptdd 724
Cdd:cd04433 92 LLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP------------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 725 snqppGRGVLSMHGLT-----YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGIPqlCRTDEIGELCVcavatgTS 799
Cdd:cd04433 139 -----GIKLVNGYGLTetggtVATGPPDDDARKPG----SVGRPVPGVEVRIVDPDGGE--LPPGEIGELVV------RG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 800 YYGLSGMTKNTFEVFPMTSSGapiseypFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvy 879
Cdd:cd04433 202 PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA--- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568981374 880 rgRIAVFSVTvlhDER------IVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 949
Cdd:cd04433 272 --EAAVVGVP---DPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1057-1282 |
9.07e-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: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPhPQNIATtlptvkmIVEV 1134
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARREA-------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1135 SRSACLMTTQLICKLLRSREAAAAVDvrtwpliLDTDDLPKKRPAQiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1214
Cdd:cd12114 83 AGARLVLTDGPDAQLDVAVFDVLILD-------LDALAAPAPPPPV---DVAPDDLAYVIFTSGSTGTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981374 1215 AFCRSIKLQCELYPSREVaICLDPycgLGFVLwclcSVY------SGHQSILIPPSELETNPALWLLAVSQYKV 1282
Cdd:cd12114 153 NTILDINRRFAVGPDDRV-LALSS---LSFDL----SVYdifgalSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
566-958 |
9.70e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.09 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 566 VTVTRIALLTHCQALTQACGYT-EAETIVNVLDFKKDVGLWhGILTSVMNM-MHVISI-PYSLMkVNPLSWIQKVCQYKA 642
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMV-GFLTVPMYFgAELVKVtPMDFL-RDPLLWAELISKYRG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 643 KVACvkSRDMHWALVAHR-----DQRDVNLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVA 717
Cdd:PRK07768 248 TMTA--APNFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEA-TLA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 718 IrrptddSNQPPGRGvlsmhgLTYGVIRVD--SEEKLSVLTVQD-------VGLVMPGAIMCSVKPDGipQLCRTDEIGE 788
Cdd:PRK07768 323 V------SFSPCGAG------LVVDEVDADllAALRRAVPATKGntrrlatLGPPLPGLEVRVVDEDG--QVLPPRGVGV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 789 LCVCAVATgTSYYglsgmtkntfevfpMTSSG--APISEYPFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIV 866
Cdd:PRK07768 389 IELRGESV-TPGY--------------LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 867 ATALAVEPmkfVYRGRIAVFSVTVLHD-ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPK 943
Cdd:PRK07768 454 RAAARVEG---VRPGNAVAVRLDAGHSrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPK 528
|
410
....*....|....*
gi 568981374 944 TPLGGIHLSETKQLF 958
Cdd:PRK07768 529 TPSGKLRRANAAELV 543
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1032-1552 |
3.68e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.45 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1032 LQWRAQTTPDHLLYTLLNCRGTIAN----SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADGKlaydELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1108 CVPITVRP-------------PHPQ--------NIATTL-----PTVKMIVEVSRSACLMTTQLickllrsreaaaavdv 1161
Cdd:PRK09274 91 AVPVLVDPgmgiknlkqclaeAQPDafigipkaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTL---------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1162 rtwplildtDDLPKKRPAQIYKP--SNPDTLAYLDFSVSTTGMLAGVKMSHaatSAFCRSIKLQCELYPSR--EVAIC-- 1235
Cdd:PRK09274 155 ---------ATLLRDGAAAPFPMadLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQIEALREDYGIEpgEIDLPtf 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1236 -----LDPYCGlgfvlwcLCSVysghqsilIPPSEL----ETNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSL 1306
Cdd:PRK09274 223 plfalFGPALG-------MTSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1307 KARGLDLSRVRTcVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLqgtsgpdpttvyVDMRALRHDR 1385
Cdd:PRK09274 281 EANGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFAT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1386 VRLVERGSPHSLplmesGKILPGVRI-IIA---NP-----ETKgPLGDSHLGEIWVHSAHNASGYFtiygdeslQSDHFN 1456
Cdd:PRK09274 343 RAATDNGAGICV-----GRPVDGVEVrIIAisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYY--------NRPEAT 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1457 --SRLSFGDTQtIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAvftw 1534
Cdd:PRK09274 409 rlAKIPDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA---- 472
|
570
....*....|....*...
gi 568981374 1535 tnllVVVVELDGSEQEAL 1552
Cdd:PRK09274 473 ----LVGVGVPGAQRPVL 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1057-1548 |
9.10e-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: 60.00 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSR 1136
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1137 SACLMTTQlickllrSREAAAAVDVRTWPLILDTDDLPkkrPAQIYKPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1216
Cdd:cd12116 85 PALVLTDD-------ALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1217 CRSIklqcelypsREvaicldpycglgfvlwclcsvysghqsilippsELETNPALWLLAVSQYkvrdTFcSYSVMEL-- 1294
Cdd:cd12116 155 LHSM---------RE---------------------------------RLGLGPGDRLLAVTTY----AF-DISLLELll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1295 ----------CTKGLGSQTESLKARgldLSRVRTCVVVAeerprialTQSFSKLFKDLGLHPRAvstsfGCRV------- 1357
Cdd:cd12116 188 pllagarvviAPRETQRDPEALARL---IEAHSITVMQA--------TPATWRMLLDAGWQGRA-----GLTAlcggeal 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1358 --NLAICLQGTS-------GPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLG 1428
Cdd:cd12116 252 ppDLAARLLSRVgslwnlyGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVLDAALR-PVPPGVPG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1429 EIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWARTGYLgfLRRteltDANGErhdaLYVVGALDEAMELRGM 1508
Cdd:cd12116 319 ELYIGGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR----RADGR----LEYLGRADGQVKIRGH 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 568981374 1509 RYHPIDIETsVIRAHKSVTECAVFTWTN----LLVVVVELDGSE 1548
Cdd:cd12116 385 RIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1058-1556 |
2.71e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1058 LTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRS 1137
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPE-VLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1138 ACLMTTQLICKLLRSREAAAAVDV---RTWplildtDDLPKKRPAqiyKPSNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1214
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDGLASLALdrdEDW------EGFPAHDPA---VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV 4720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1215 AFCRSIKLQCELYPSREVaICLDPYCGLGFVL---WCLCSvysgHQSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSV 1291
Cdd:PRK12316 4721 NHLHATGERYELTPDDRV-LQFMSFSFDGSHEglyHPLIN----GASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1292 MELCTKGlgsqteslKARGLDLSRVRTCVVVAEERPRIALTQSFSKLfKDLGLHpravstsfgcrvnlaiclqGTSGPDP 1371
Cdd:PRK12316 4795 LQQLAEH--------AERDGEPPSLRVYCFGGEAVAQASYDLAWRAL-KPVYLF-------------------NGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1372 TTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVRIII----ANPETKGPLGDSHLGEIWVhsahnASGYFTiygD 1447
Cdd:PRK12316 4847 TTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVldgqLNPLPVGVAGELYLGGEGV-----ARGYLE---R 4910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1448 ESLQSDHFNSRlSFGDTQTIWARTGYLGFLRRTELTDangerhdalyVVGALDEAMELRGMRYHPIDIETSvIRAHKSVT 1527
Cdd:PRK12316 4911 PALTAERFVPD-PFGAPGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEAR-LREHPAVR 4978
|
490 500
....*....|....*....|....*....
gi 568981374 1528 ECavftwtnlLVVVVELDGSEQEALDLVP 1556
Cdd:PRK12316 4979 EA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1057-1531 |
3.25e-08 |
|
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: 58.09 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPHPQNIAttlptvkmIVEV 1134
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERIAF--------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1135 SRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATS 1214
Cdd:cd17643 83 SGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1215 AFCRSIKLQCELYPSREVAICldPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAVSQYKVrdtfcsySVMel 1294
Cdd:cd17643 120 ALFAATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV-------TVL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1295 ctkglgSQT--------ESLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDlgLHPRAvstsfgcrVNLaiclqgt 1366
Cdd:cd17643 189 ------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1367 SGPDPTTVYVDMRALRHDRVRLVErGSPhslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyG 1446
Cdd:cd17643 245 YGITETTVHVTFRPLDAADLPAAA-ASP-------IGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYL---G 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1447 DESLQSDHFNSrLSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSV 1526
Cdd:cd17643 313 RPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE-AALATHPSV 380
|
....*
gi 568981374 1527 TECAV 1531
Cdd:cd17643 381 RDAAV 385
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
369-674 |
5.06e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 57.61 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 369 VTNWPPSLEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNd 448
Cdd:PRK07656 4 WMTLPELLARAARRF----GDKEAYVFGDQR------LTYAELNARVRRAA-AALAALG------IGKGDRVAIWAPNS- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 449 pAAFMVAFYGCLLAEVVPVPIEvplTRKDAGsqQIGFLLGSCGVTVALTSD-------ACHKGLPK----------SPTG 511
Cdd:PRK07656 66 -PHWVIAALGALKAGAVVVPLN---TRYTAD--EAAYILARGDAKALFVLGlflgvdySATTRLPAlehvviceteEDDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 512 EIPQFKGWPKLLwfvteskhLSKPPRDWFPHIKDanNDTAYIEYKTCKDGSVLGVtvtriaLLTHCQALTQA------CG 585
Cdd:PRK07656 140 HTEKMKTFTDFL--------AAGDPAERAPEVDP--DDVADILFTSGTTGRPKGA------MLTHRQLLSNAadwaeyLG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 586 YTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV-ACVKSrdMHWALVAHRDQRD 664
Cdd:PRK07656 204 LTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERITVlPGPPT--MYNSLLQHPDRSA 277
|
330
....*....|
gi 568981374 665 VNLSSLRMLI 674
Cdd:PRK07656 278 EDLSSLRLAV 287
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1032-1555 |
7.55e-08 |
|
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: 56.85 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1032 LQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPi 1111
Cdd:cd17631 1 LRRRARRHPDR---TALVFGGR---SLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVF- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1112 tvrppHPQNIATTLPTVKMIVEVSRSACLMttqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnpDTLA 1191
Cdd:cd17631 73 -----VPLNFRLTPPEVAYILADSGAKVLF----------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1192 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELyPSREVAICLDPYC---GLGfvLWCLCSVYSGHQSILIPpselET 1268
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILR----KF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1269 NPALWLLAVSQYKVRDTFCSYSVME-LCTKGlgsqteslKARGLDLSRVRtCVVVAEERPRIALTQSFsklfKDLGLhpr 1347
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1348 AVSTSFGcrvnlaiclQGTSGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVRIIIANPETKgPLGDSHL 1427
Cdd:cd17631 239 KFVQGYG---------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR-EVPPGEV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1428 GEIWVHSAHNASGYftiYGDESLQSDhfnsrlSFGDTqtiWARTGYLGFLrrteltDANGerhdALYVVGALDEAMELRG 1507
Cdd:cd17631 293 GEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRKKDMIISGG 350
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568981374 1508 MRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLV-VVVELDGSEQEALDLV 1555
Cdd:cd17631 351 ENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
407-857 |
8.69e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 56.73 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 407 TYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGCLLAEVVPVPIEVPLTrkdagSQQIGFL 486
Cdd:PRK06187 33 TYAELDERVNRLA-NALRALG------VKKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 487 LGSCGVTVALTSDAcHKGLPKSPTGEIPQFKGW--------PKLLWFVTESKHL--SKPPRDWFPHIKDanNDTAYIEYK 556
Cdd:PRK06187 99 LNDAEDRVVLVDSE-FVPLLAAILPQLPTVRTVivegdgpaAPLAPEVGEYEELlaAASDTFDFPDIDE--NDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 557 TCKDGSVLGVTVTRIALLTHCQALTQACGYTEaetivnvldfkKDVGLwhgiltSVMNMMHV--ISIPY-SLM------- 626
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR-----------DDVYL------VIVPMFHVhaWGLPYlALMagakqvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 627 --KVNPlswiQKVCQY--KAKV---ACVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFqskgl 699
Cdd:PRK06187 239 prRFDP----ENLLDLieTERVtffFAVPT--IWQMLLKAPRAYFVDFSSLRLVIY--GGAALPPALLREFKEKF----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 700 rqevicpcasspealtvairrptddsnqppGRGVLSMHGL--TYGVIRVD--SEEKLSVLTVQ-DVGLVMPG---AImcs 771
Cdd:PRK06187 306 ------------------------------GIDLVQGYGMteTSPVVSVLppEDQLPGQWTKRrSAGRPLPGveaRI--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 772 VKPDGIPQLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEvfpmtsSGapiseypFIRTGLLGFVGPGGLVFVVGKMDG 851
Cdd:PRK06187 353 VDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------GG-------WLHTGDVGYIDEDGYLYITDRIKD 419
|
....*.
gi 568981374 852 lMVVSG 857
Cdd:PRK06187 420 -VIISG 424
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
376-497 |
1.14e-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: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 376 LEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVA 455
Cdd:cd05936 5 LEEAARRF----PDKTALIFMGRK------LTYRELDALAEAFA-AGLQNLG------VQPGDRVALMLPNC--PQFPIA 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568981374 456 FYGCLLAEVVPVPIEVPLTrkdagSQQIGFLLGSCGVTVALT 497
Cdd:cd05936 66 YFGALKAGAVVVPLNPLYT-----PRELEHILNDSGAKALIV 102
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
337-873 |
1.35e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 337 FEELLEVQQPDPNQPKPEGAqmLATRGEQLGVVTNWPPSLEAALQRWGT---------ISPKAPCLTTMDTNgkplyiLT 407
Cdd:PRK12316 1959 LLHLLEQMAEDAQAALGELA--LLDAGERQRILADWDRTPEAYPRGPGVhqriaeqaaRAPEAIAVVFGDQH------LS 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 408 YGKLWTRSMKVAYNILhKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLA--EVVPVPIEVPLTRkdagsqqIGF 485
Cdd:PRK12316 2031 YAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERS--FELVVALLAVLKAggAYVPLDPNYPAER-------LAY 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 486 LLGSCGVTVALTSDACHKGLPksPTGEIPQFKGWPKLLWFVTESKHlskpprdwfPHIKDANNDTAYIEYKTCKDGSVLG 565
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWADYPDTA---------PAVQLAGENLAYVIYTSGSTGLPKG 2163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 566 VTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPYSLMkvNPLSWIQKVCQYKAKVA 645
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELW--DPEQLYDEMERHGVTIL 2240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 646 CVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLN------VFQSKGLRQEVICP-----CASSPE-A 713
Cdd:PRK12316 2241 DFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPllwkcRPQDPCgA 2316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 714 LTVAIRRPTDDsnqppgrgvlsmhgltygvirvdseEKLSVLtvqDVGLvmpgaimcsvkpdgipQLCRTDEIGELCVCA 793
Cdd:PRK12316 2317 AYVPIGRALGN-------------------------RRAYIL---DADL----------------NLLAPGMAGELYLGG 2352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 794 VATGTSYYGLSGMTKNTFEVFPMTSSGAPIseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVE 873
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1062-1229 |
1.93e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1062 QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLM 1141
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1142 T-TQLICKLLRSREAAAavdvrtwpLILDTD----DLPKKRPAQiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1216
Cdd:PRK12316 2106 TqRHLLERLPLPAGVAR--------LPLDRDaewaDYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170
....*....|...
gi 568981374 1217 CRSIKLQCELYPS 1229
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 |
2.23e-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: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 400 GKPLYI-----LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFpnNDPAAFMVAFYGCLLAEVVPVPIEVPLT 474
Cdd:cd05959 19 DKTAFIddagsLTYAELEAEARRVA-GALRALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 568981374 475 rkdagSQQIGFLLGSCGVTVALTSDACH 502
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGELA 112
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1184-1531 |
7.74e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.85 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1184 PSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYC-GLGFVLWCLCSVYSGHQSILIP 1262
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1263 PSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGSQTESlkaRGLDLSRVRtCVVVAEERPRIALTQSFSKLFKDL 1342
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1343 GLHPRAVSTSFG-CRVNLAICLqGTSGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPG--VRIIIANPEtk 1419
Cdd:PRK07768 304 GLRPEAILPAYGmAEATLAVSF-SPCGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGleVRVVDEDGQ-- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1420 gPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDHfnsrlsfGdtqtiWARTGYLGFLrrTEltdaNGErhdaLYVVGAL 1499
Cdd:PRK07768 380 -VLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE----EGE----VVVCGRV 436
|
330 340 350
....*....|....*....|....*....|..
gi 568981374 1500 DEAMELRGMRYHPIDIETSVIRAHKSVTECAV 1531
Cdd:PRK07768 437 KDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1030-1565 |
7.81e-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: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1030 EVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1109
Cdd:cd12117 1 ELFEEQAARTPDA---VAVVYGDR---SLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1110 PITVRPPHPQNiattlpTVKMIVEVSRSACLMTtqlickllrSREAAAAVDVRTWPLILDtDDLPKKRPAQIYKPSNPDT 1189
Cdd:cd12117 74 YVPLDPELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGLEVAVVID-EALDAGPAGNPAVPVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1190 LAYLDFSVSTTGMLAGVKMSHAATSAFCRS---IKLQcelypSREVAICLDPYC--GLGFVLWclCSVYSGHQSILIPPS 1264
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtnyVTLG-----PDDRVLQTSPLAfdASTFEIW--GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1265 ELETNPALwLLAVSQYKVrdtfcsySVMELcTKGLGSQteslkargldlsrvrtcvvVAEERPrialtQSFSKLfkdlgl 1344
Cdd:cd12117 211 TLLDPDAL-GALIAEEGV-------TVLWL-TAALFNQ-------------------LADEDP-----ECFAGL------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1345 hpRAVSTSfGCRVN-------LAIC----LQGTSGPDPTTVYvdmrALRHdrvrLVERG--SPHSLPLmesGKILPGVRI 1411
Cdd:cd12117 252 --RELLTG-GEVVSpphvrrvLAACpglrLVNGYGPTENTTF----TTSH----VVTELdeVAGSIPI---GRPIANTRV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1412 IIANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWaRTGYLGFLRrteltdANGErhd 1491
Cdd:cd12117 318 YVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNRPALTAERF-VADPFGPGERLY-RTGDLARWL------PDGR--- 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568981374 1492 aLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAvftwtnllVVVVELDGSEQEaldlvpLVTNVVLEE 1565
Cdd:cd12117 383 -LEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAV--------VVVREDAGGDKR------LVAYVVAEG 440
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
406-500 |
8.95e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 53.40 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 485
Cdd:PRK08316 37 WTYAELDAAVNRVA-AALLDLG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAY 102
|
90
....*....|....*
gi 568981374 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 ... |
1030-1210 |
1.93e-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: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1030 EVLQWRAQTTPDHllyTLLNCRGtiaNSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC- 1108
Cdd:cd17655 1 ELFEEQAEKTPDH---TAVVFED---QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1109 -VPITvrPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAaavdvrtwpLILDTDDLPKKRPAQIYKPSNP 1187
Cdd:cd17655 74 yLPID--PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKS 136
|
170 180
....*....|....*....|...
gi 568981374 1188 DTLAYLDFSVSTTGMLAGVKMSH 1210
Cdd:cd17655 137 DDLAYVIYTSGSTGKPKGVMIEH 159
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
377-500 |
5.37e-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: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 377 EAALQRWGTISPKAPCLTTMDTNGKPlYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdPAAfMVAF 456
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-PEA-VIAM 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568981374 457 YGCLLAEVVPVPIeVPLTRKDAgsqqIGFLLGSCGVTVALTSDA 500
Cdd:COG0365 82 LACARIGAVHSPV-FPGFGAEA----LADRIEDAEAKVLITADG 120
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
406-497 |
6.36e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAYNILHKLGtkqepmVRPGDRVALvFPNNDPAaFMVAFYGCLLAEVVPVPIEvPLTRkdagSQQIGF 485
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSPQ-FVIAYYAILRANAVVVPVN-PMNR----EEELAH 102
|
90
....*....|..
gi 568981374 486 LLGSCGVTVALT 497
Cdd:PRK08314 103 YVTDSGARVAIV 114
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
596-961 |
1.03e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.15 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 596 LDFKKDVG-----LWHG-----ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKVacVKSRDMHWALVAH--RDQR 663
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATL--TAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 664 DVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVAIRRPTddsnqpPGRGVLsmhgltygV 743
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV------PGIGLR--------V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 744 IRVDSEEKLSVLTVQDVGLVMPGA---IMCSVKPDGIPQlcrtDEIGELCVCAVATGTSYYGlsgmtkntfevfpmtssG 820
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMevrISPGDGAAGVAG----REIGEIEIRGASMMSGYLG-----------------Q 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 821 APISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfVYRGRIavfsVTVLHDE-----R 895
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRG---VREGAV----VAVGTGEgsarpG 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568981374 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 |
1.12e-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: 49.92 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 380 LQRWGTISPKAPCLTTMDTngkplyILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGC 459
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLA-HALRALG------VAKGDRVAVLSKNSP--EFLELLFAA 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 568981374 460 LLAEVVPVPIEVPLTRKDagsqqIGFLLGSCGVTVAL 496
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSGAKVLF 97
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
986-1212 |
1.27e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.43 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 986 QPEIGPASVmvgNLVSGKRIAQasgrdLGQIEDNDQARKFLFLSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHK 1065
Cdd:PRK10252 426 DPALLCGDV---DILLPGEYAQ-----LAQVNATAVEIPETTLSALVAQQAAKTPDA---PALADARY---QFSYREMRE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1066 RAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLMTTQl 1145
Cdd:PRK10252 492 QVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTA- 563
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568981374 1146 ickLLRSREAAAAVDVRTWPLILDTDdlPKKRPAQIYKPSNPdtlAYLDFSVSTTGMLAGVKMSHAA 1212
Cdd:PRK10252 564 ---DQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHT---AYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
372-500 |
1.53e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 49.65 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 372 WPP-------------SLEAALQRWGTISPKAPCLttmDTNGkplYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGD 438
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568981374 439 RVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKdagsQQIGFLLGSCGVTVALTSDA 500
Cdd:PRK06178 85 RVAVFLPNC--PQFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1058-1477 |
1.54e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.38 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1058 LTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP-PHPQNIATtlptvkmivevsr 1136
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQ------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1137 saCLmttqlickllrsREAAaavdvrtwplildtddlPKkrpAQIYKPSNPDTLAYLdFSVSTTGMLAGVKMSHaatSAF 1216
Cdd:cd05910 69 --CL------------QEAE-----------------PD---AFIGIPKADEPAAIL-FTSGSTGTPKGVVYRH---GTF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1217 CRSIKLQCELYPSREVAICLDpycglGFVLWCLCSVYSGHQSIlIPPSE----LETNPALWLLAVSQYKVRDTFCSYSVM 1292
Cdd:cd05910 111 AAQIDALRQLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1293 ELCTkglgsqtESLKARGLDLSRVRtCVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLQGTsgpdp 1371
Cdd:cd05910 185 ERVA-------RYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGS----- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1372 ttvyvdmRALRHDRVRLVERGSPHSLplmesGKILPGV--RIIIANPETKGPLGDSH------LGEIWVHSAHNASGYFT 1443
Cdd:cd05910 247 -------RELLATTTAATSGGAGTCV-----GRPIPGVrvRIIEIDDEPIAEWDDTLelprgeIGEITVTGPTVTPTYVN 314
|
410 420 430
....*....|....*....|....*....|....
gi 568981374 1444 IYGDESLQSDHFNSrlsfgdtQTIWARTGYLGFL 1477
Cdd:cd05910 315 RPVATALAKIDDNS-------EGFWHRMGDLGYL 341
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1036-1531 |
2.31e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 49.39 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1036 AQTTPDHLLYTLLNCRgtiansLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP 1115
Cdd:PRK12467 522 ARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPD-VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1116 PHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTDDLPKKRPAQIYKPSNPDTLAYLDF 1195
Cdd:PRK12467 595 EYPQD------RLAYMLDDSGVRLLLTQSHLLAQL-----PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1196 SVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAIcLDPYCGLGFVLWCLCSVYSGHQSILIPPSEletnpalwll 1275
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM-VSTFAFDLGVTELFGALASGATLHLLPPDC---------- 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1276 avsqykVRDTFCSYSVMelCTKGLG--SQTES-----LKARGLDLSRVRTCVVVAEErpriALTQSFSKLFKDLGLhpra 1348
Cdd:PRK12467 733 ------ARDAEAFAALM--ADQGVTvlKIVPShlqalLQASRVALPRPQRALVCGGE----ALQVDLLARVRALGP---- 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1349 vstsfGCRvnlaicLQGTSGPDPTTVYVDMRALRHDRVrlVERGSPHSLPLMESgkilpGVRIIIA--NPETKGPLGDSH 1426
Cdd:PRK12467 797 -----GAR------LINHYGPTETTVGVSTYELSDEER--DFGNVPIGQPLANL-----GLYILDHylNPVPVGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1427 LGeiwvhSAHNASGYftiYGDESLQSDHFNSRLSFGDTQTIWaRTGYLGflRRTeltdANGErhdaLYVVGALDEAMELR 1506
Cdd:PRK12467 859 IG-----GAGLARGY---HRRPALTAERFVPDPFGADGGRLY-RTGDLA--RYR----ADGV----IEYLGRMDHQVKIR 919
|
490 500
....*....|....*....|....*
gi 568981374 1507 GMRYHPIDIETSvIRAHKSVTECAV 1531
Cdd:PRK12467 920 GFRIELGEIEAR-LLAQPGVREAVV 943
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1030-1217 |
3.17e-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: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1030 EVLQWRAQTTPDHLLYTLlncRGtiaNSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCV 1109
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD---RG---QSLTYKQLNEKANQLARHLRGKGVKPD-DQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1110 PITVRPPHPQniattlptvkmivevsrsaclmttQLICKLLRSREAAaavdvrtwpLILdtddlpkkrpaqiykpSNPDT 1189
Cdd:cd17645 75 YVPIDPDYPG------------------------ERIAYMLADSSAK---------ILL----------------TNPDD 105
|
170 180
....*....|....*....|....*...
gi 568981374 1190 LAYLDFSVSTTGMLAGVKMSHAATSAFC 1217
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1057-1216 |
4.41e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.98 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIATTLPT--VKMI-- 1131
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALfv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1132 ------VEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDlPKKRPAQIykpsNPDTLAYLDFSVSTTGMLAG 1205
Cdd:PRK07656 109 lglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD-PAERAPEV----DPDDVADILFTSGTTGRPKG 183
|
170
....*....|..
gi 568981374 1206 VKMSHAAT-SAF 1216
Cdd:PRK07656 184 AMLTHRQLlSNA 195
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1028-1117 |
6.22e-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: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1028 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:COG1021 27 LGDLLRRRAERHPDR---IAVVDGER---RLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 568981374 1108 CVPITVRPPH 1117
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
406-467 |
8.76e-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: 8.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568981374 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 |
1.67e-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: 46.10 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 407 TYGKLWTRSMKVAYNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEV--PLTRkdagsqqIG 484
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981374 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 |
1.87e-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: 46.11 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 388 PKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDPAafMVAFYGCLLAEVVPV 467
Cdd:cd12114 1 PDATAVICGDGT------LTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQ--VVAVLGILAAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 468 PIEV--PLTRKDAgsqqigfLLGSCGVTVALTSDACHKGLPKSPTgeipqfkgwpkllwFVTESKHLSKPPRDwFPHIKD 545
Cdd:cd12114 66 PVDIdqPAARREA-------ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDV 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568981374 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 |
2.06e-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: 46.39 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPI--EVPLTRkdagsqqI 483
Cdd:COG1020 502 LTYAELNARANRLA-HHLRALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER-------L 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 484 GFLLGSCGVTVALTSDACHKGLPKSptgeipqfkgwpKLLWFVTESKHLSKPPRDWfPHIKDANNDTAYIEY-------- 555
Cdd:COG1020 566 AYMLEDAGARLVLTQSALAARLPEL------------GVPVLALDALALAAEPATN-PPVPVTPDDLAYVIYtsgstgrp 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568981374 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 ... |
1039-1210 |
3.37e-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: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1039 TPDHLLYTLLNCrgtianSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAG--CVPITvrpP 1116
Cdd:cd17656 1 TPDAVAVVFENQ------KLTYRELNERSNQLARFLREKGVKKD-SIVAIMMERSAEMIVGILGILKAGgaFVPID---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1117 HpqniattLPTVKMIVEVSRSAC-LMTTQLICKLLRSREAAaaVDVRTWPLILDTDDlpkkrpAQIYKPSNPDTLAYLDF 1195
Cdd:cd17656 71 E-------YPEERRIYIMLDSGVrVVLTQRHLKSKLSFNKS--TILLEDPSISQEDT------SNIDYINNSDDLLYIIY 135
|
170
....*....|....*
gi 568981374 1196 SVSTTGMLAGVKMSH 1210
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 |
3.40e-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: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALvFPNNDPaAFMVAFYGCLLAEVVPVPIevpltRKDAGSQQIGF 485
Cdd:cd05907 6 ITWAEFAEEVRALA-KGLIALG------VEPGDRVAI-LSRNRP-EWTIADLAILAIGAVPVPI-----YPTSSAEQIAY 71
|
90
....*....|....*
gi 568981374 486 LLGSCGVTVALTSDA 500
Cdd:cd05907 72 ILNDSEAKALFVEDP 86
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1036-1211 |
4.83e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 44.50 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1036 AQTTPDHLLYtllNCRGTianSLTCVQLHKRAEKIAVMLMERgHLQDGDHVaLVY----PpgiDLIAAFYGCLYAGC--V 1109
Cdd:PRK04813 12 AQTQPDFPAY---DYLGE---KLTYGQLKEDSDALAAFIDSL-KLPDKSPI-IVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1110 PITVRPPhpqniattLPTVKMIVEVSRSACLMTTqlickllrSREAAAAVDVRTwpLILD--TDDLPKKRPAQIYKPSNP 1187
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIPV--ITLDelKDIFATGNPYDFDHAVKG 142
|
170 180
....*....|....*....|....
gi 568981374 1188 DTLAYLDFSVSTTGMLAGVKMSHA 1211
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
406-945 |
6.17e-04 |
|
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: 44.06 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEV--PLTRkdagsqqI 483
Cdd:cd05930 13 LTYAELDARANRLA-RYLRERG------VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDPsyPAER-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 484 GFLLGSCGVTVALTSDachkglpksptgeipqfkgwpkllwfvteskhlskpprdwfphikdanNDTAYIEY-------- 555
Cdd:cd05930 77 AYILEDSGAKLVLTDP------------------------------------------------DDLAYVIYtsgstgkp 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 556 KtckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMN--MMHVISipySLMKVNPLSW 633
Cdd:cd05930 109 K--------GVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAgaTLVVLP---EEVRKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 634 IQKVCQYKAKVA-CVKSrdmHW-ALVAHRDQRDvnLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcassp 711
Cdd:cd05930 177 ADLLAEEGITVLhLTPS---LLrLLLQELELAA--LPSLRLVLVG-G--------------------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 712 EALTVAIRRPTDDSNqpPGRGVLSMHGLT-------YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGipQLCRTD 784
Cdd:cd05930 218 EALPPDLVRRWRELL--PGARLVNLYGPTeatvdatYYRVPPDDEEDGRV----PIGRPIPNTRVYVLDENL--RPVPPG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 785 EIGELCVC--AVATGtsYYGLSGMTKntfEVFPMTSSGAPISEYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNA 862
Cdd:cd05930 290 VPGELYIGgaGLARG--YLNRPELTA---ERFVPNPFGPGERMY---RTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 863 DDIVATALAVEPMkfvyrgRIAVfsVTVLHD----ERIV--IVAEQRPDSTEEDSFQWMSRVLQAidsihqvgvYCL--A 934
Cdd:cd05930 362 GEIEAALLAHPGV------REAA--VVAREDgdgeKRLVayVVPDEGGELDEEELRAHLAERLPD---------YMVpsA 424
|
570
....*....|.
gi 568981374 935 LVPANTLPKTP 945
Cdd:cd05930 425 FVVLDALPLTP 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
406-499 |
7.22e-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: 44.23 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 485
Cdd:cd05926 15 LTYADLAELVDDLA-RQLAALG------IKKGDRVAIALPNG--LEFVVAFLAAARAGAVVAPLN-PAYKKA----EFEF 80
|
90
....*....|....
gi 568981374 486 LLGSCGVTVALTSD 499
Cdd:cd05926 81 YLADLGSKLVLTPK 94
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
406-500 |
9.50e-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: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALvFPNNDPaAFMVAFYGCLLAEVVPVPIEVpltrkDAGSQQIGF 485
Cdd:COG1022 41 LTWAEFAERVRALAAG-LLALG------VKPGDRVAI-LSDNRP-EWVIADLAILAAGAVTVPIYP-----TSSAEEVAY 106
|
90
....*....|....*
gi 568981374 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 |
9.73e-04 |
|
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: 9.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPnnDPAAFMVAFYGCLLAEVVPVPIEVPLTRKD 477
Cdd:cd05919 11 VTYGQLHDGANRLG-SALRNLG------VSSGDRVLLLML--DSPELVQLFLGCLARGAIAVVINPLLHPDD 73
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
406-595 |
1.43e-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: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvpltrKDAGSQQIGF 485
Cdd:cd12116 13 LSYAELDERANRLA-ARLRARG------VGPGDRVAVYLPRS--ARLVAAMLAVLKAGAAYVPLD-----PDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 486 LLGSCGVTVALTSDACHKGLPKSPTgeipqfkGWPKLLWFVTESKHLSKPPrdwfphikDANNDTAYIEYKTCKDGSVLG 565
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLP-------VLLLALAAAAAAPAAPRTP--------VSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190
....*....|....*....|....*....|
gi 568981374 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 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 485
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 568981374 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 ... |
1403-1545 |
2.82e-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: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1403 GKILPGVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFTIYGDEsLQSDHFNSRLsfgdtqtiwaRTGYLGFLrrtel 1482
Cdd:cd05922 289 GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL----------HTGDLARR----- 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568981374 1483 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSvIRAHKSVTECAVF----TWTNLLVVVVELD 1545
Cdd:cd05922 352 -DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
407-467 |
2.87e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 42.29 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568981374 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 ... |
1403-1531 |
3.70e-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: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1403 GKILPGVRIIIANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLRrtel 1482
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568981374 1483 tdangeRHDALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1531
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1408-1532 |
5.51e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.41 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1408 GVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLrrteltDANG 1487
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---GDPTITAANFTDG---------WLRTGDLGSL------SAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568981374 1488 ErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1532
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1062-1206 |
5.74e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 1062 QLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSRSACLM 1141
Cdd:PRK05691 3750 ELNRAANRLGHALRAAGVGVD-QPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP------AQRLQRIIELSRTPVLV 3822
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568981374 1142 TTQlICkLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQ----IYkpSNPDTLAYLDFSVSTTGMLAGV 1206
Cdd:PRK05691 3823 CSA-AC-REQARALLDELGCANRPRLLVWEEVQAGEVAShnpgIY--SGPDNLAYVIYTSGSTGLPKGV 3887
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
407-501 |
6.21e-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: 41.12 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 407 TYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVplTRKDAGSQQIgfl 486
Cdd:cd05934 5 TYAELLRESARIA-AALAALG------IRPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPINT--ALRGDELAYI--- 70
|
90
....*....|....*
gi 568981374 487 LGSCGVTVALTSDAC 501
Cdd:cd05934 71 IDHSGAQLVVVDPAS 85
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
406-555 |
6.62e-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: 41.03 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAYNILHKlGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLA--EVVPVPIEVPLTRkdagsqqI 483
Cdd:cd12117 23 LTYAELNERANRLARRLRAA-G------VGPGDVVGVLAERS--PELVVALLAVLKAgaAYVPLDPELPAER-------L 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568981374 484 GFLLGSCGVTVALTsdacHKGLPKSPTGEIPqfkgwpkLLWFVTESKHLSKPPrdwfPHIKDANNDTAYIEY 555
Cdd:cd12117 87 AFMLADAGAKVLLT----DRSLAGRAGGLEV-------AVVIDEALDAGPAGN----PAVPVSPDDLAYVMY 143
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
406-523 |
7.42e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 40.66 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568981374 406 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 485
Cdd:PRK08276 12 VTYGELEARSNRLA-HGLRALG------LREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLTAAE-----IAY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568981374 486 LLGSCGVTVALTS----DACHKGLPKSP---------TGEIPQFKGWPKLL 523
Cdd:PRK08276 78 IVDDSGAKVLIVSaalaDTAAELAAELPagvplllvvAGPVPGFRSYEEAL 128
|
|
| |
