|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1044-1618 |
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: 791.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1044 LYTLLNCRGAIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIA 1122
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1123 TTLPTVKMivEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA-----QICKPCNPDTLAYLDFSV 1197
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1198 STTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAV 1277
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1278 SQYKVRDTFCSYSVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGCRV 1357
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1358 NLAICLqphrlwtlaeQGTSGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHL 1437
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1438 GEIWVHSAHNASGYFTIYGDESLQSDHFNS-RLSFGDTQTIWARTGYLGFLRRTELTDANGERHDALYVVGALDEAMELR 1516
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1517 GMRYHPIDIETSVIRAHKSVTECAVFTWTNLLVVVVELD-GSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINS 1595
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 530392110 1596 RGEKQRMHLRDGFLADQLDPIYV 1618
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
392-968 |
0e+00 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 741.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 392 CLTTMDTNGKPLYILTYGKLWTRSMKVAYSILHKLGTKqepmvrPGDRVALVFPnnDPAAFMAAFYGCLLAEVVPVPIEV 471
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLK------PGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 472 PLtrkdaGSQQIGFLLGSCGVTVALTSDACHKGLPKS-----PTGEIPQFKGWPKLLWFVTESKHLSKPPRDWFPHIKDA 546
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 547 NNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLM 626
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 627 KVNPLSWIQKVCQYKAKVACVKSRDMHWAL------VAHRDQRDINLSSLRMLIVADGaNPWSISSCDAFLNVFQSKGLR 700
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 701 QEvicpcASSPEALTVAIRRPTD--DSNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQDVGLVMPGAIMCSVKPDGVP 778
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWqgTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 779 qLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEVFPMTSSGAPISEYPFIRTGLLGFVGPG----------GLVFVVGK 848
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 849 MDGLMVVSGRRHNADDIVATALAVEPmkfvYRGRIAVFSVTvlhdERIVIVAEQRPDStEEDSFQWMSRVLQAIDSIHQV 928
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPPGS-EEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 530392110 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 ... |
1034-1576 |
1.28e-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: 244.84 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1034 WRAQTTPDHILYTLLNCRGAIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITV 1113
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1114 RPPHPqniATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKPcNPDTLAYL 1193
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSP-DPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1194 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALW 1273
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1274 LLAVSQYkvRDTFcsySVM-----ELCTKglgsQTESLKARGLDLSRVRTCVVVAEeRPRIALTQSFSKLFKDLGLHPRA 1348
Cdd:cd05931 235 LRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFRPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1349 VSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVRII 1422
Cdd:cd05931 305 FRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1423 IANPETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRLSFGDtqTIWARTGYLGFLrrteltdANGErhda 1502
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDE--GGWLRTGDLGFL-------HDGE---- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1503 LYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTW----TNLLVVVVELDGSeQEALDLVPLVTNV---VL 1573
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVA 510
|
...
gi 530392110 1574 EEH 1576
Cdd:cd05931 511 REH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
406-959 |
2.63e-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: 217.49 E-value: 2.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAYSILHKLgtkqepmvRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVPLTRKDAgsQQIGF 485
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVG--------KPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPPPTPGRHA--ERLAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 486 LLGSCGVTVALTSDACHKGLPKSptgeIPQFKGWPKLLWFVTESKHLSkPPRDWFPHIKDANnDTAYIEYKTCKDGSVLG 565
Cdd:cd05931 93 ILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPPPSPDPD-DIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 566 VTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISI-PYSLMKvNPLSWIQKVCQYKAKV 644
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 645 ACVKsrDMHWALVAHR----DQRDINLSSLRMLIVadGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIR 719
Cdd:cd05931 246 SAAP--NFAYDLCVRRvrdeDLEGLDLSSWRVALN--GAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 720 RPtddsNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQdVGLVMPG---AIMCsvkPDGVpQLCRTDEIGELCVC--AV 794
Cdd:cd05931 322 PP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDqevRIVD---PETG-RELPDGEVGEIWVRgpSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 795 ATGtsYYGLSGMTKNTFEVFpmtssgAPISEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEP 874
Cdd:cd05931 393 ASG--YWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 875 MkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSET 954
Cdd:cd05931 464 A--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRAC 541
|
....*
gi 530392110 955 KQLFL 959
Cdd:cd05931 542 RAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1032-1516 |
2.51e-56 |
|
AMP-binding enzyme;
Pssm-ID: 425722 [Multi-domain] Cd Length: 417 Bit Score: 202.15 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1032 LQWRAQTTPDHILYTllncrGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPI 1111
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1112 TVRPphpqniATTLPTVKMIVEVSRSACLMTTQlICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICK-------- 1183
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDD-ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1184 ---PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCE----LYPSREVAICLDPYCGLGFVLWCLCSVYSGH 1256
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLAIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1257 QSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSVMELCtkglgsqTESLKARGLDLSRVRTCVVVAeERPRIALTQSFS 1336
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1337 KLFkdlglhPRAVSTSFGcrvnlaiclqphrlwtLAEqgTSGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 1416
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDDDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1417 PGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDAN 1496
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCIRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 530392110 1497 GErhdaLYVVGALDEAMELR 1516
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1189-1563 |
2.46e-38 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 147.05 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1189 TLAYLDFSVSTTGMLAGVKMSH---AATSAFCRSIKlqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSe 1265
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnlLAAAAALAASG----GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1266 letNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPrIALTQSFSKLfkdlglh 1345
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1346 pravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVRIIIAN 1425
Cdd:cd04433 138 -------PGIKL--------VNGYGLTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1426 PETkGPLGDSHLGEIWVHSAHNASGYFTiygdeslqsdhfNSRLSFGDTQTIWARTGYLGFLrrteltDANGErhdaLYV 1505
Cdd:cd04433 184 PDG-GELPPGEIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------DEDGY----LYI 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392110 1506 VGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 1563
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1028-1558 |
1.23e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 146.08 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1028 LSEVLQWRAQTTPDHILYTLLNCRGAIANSLTCVQLHKRAEKIAVMLMERGHLqdGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1108 CV------PITVRPPHPQNIATtlptvkmIVEVSRSACLMTTQLICKLLRSREAAAAVDVrtwPLILDTDDLPKKRPAQI 1181
Cdd:PRK05691 89 VIavpaypPESARRHHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1182 CKP-CNPDTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsiklqCELYPSREVAICLDP----------YCGLGFVLWCLC 1250
Cdd:PRK05691 159 QEPaLQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1251 SVYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGsqtESLKARgLDLSRVRtcVVVAEERP-RI 1329
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVS---ESALER-LDLSRWR--VAYSGSEPiRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1330 ALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHDRVRLVErGS 1403
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-GS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1404 phslPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgDTQTiWARTGY 1483
Cdd:PRK05691 368 ----VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGY---WRNPEASAKTFVEH----DGRT-WLRTGD 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530392110 1484 LGFLRRTEltdangerhdaLYVVGALDEAMELRGMRYHPIDIETSVIRahksvtECAVFTWTNLLVVVVELDGSE 1558
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| CaiC |
COG0318 |
Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II [Lipid transport and metabolism, ... |
1028-1563 |
2.91e-34 |
|
Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 223395 [Multi-domain] Cd Length: 534 Bit Score: 139.90 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1028 LSEVLQWRAQTTPDHILYTllncRGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:COG0318 13 LASLLERAARRNPDRPALI----FLGRGGRLTYRELDRRANRLAAALQALG-VKPGDRVAILLPNSPEFLIAFLAALRAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1108 CVPITVRPP-HPQNIATTLPTVKM-IVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPK-KRPAQICKP 1184
Cdd:COG0318 88 AVAVPLNPRlTPRELAYILNDAGAkVLITSAEFAALLEAVAEALPVVLVVLLVGDADDRLPITLEALAAEgPGPDADARP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1185 CNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSRE--VAICLDPYCGLGFVLWCLCSVYSGHQSILIP 1262
Cdd:COG0318 168 VDPDDLAFLLYTSGTTGLPKGVVLTHRNLLANAAGIAAALGGGLTPDdvVLSWLPLFHIFGLIVGLLAPLLGGGTLVLLS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1263 PSELETNPALWLLAvsQYKVrdtfcsySVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFkdl 1342
Cdd:COG0318 248 PEPFDPEEVLWLIE--KYKV-------TVLSGVPTFLRELLDNPEKDDDDLSSSLRLVLSGGAPLPPELLERFEERF--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1343 glHPRAVSTSFGcrvnlaiclqphrlwtLAEqgTSGPDpTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVRII 1422
Cdd:COG0318 316 --GPIAILEGYG----------------LTE--TSPVV-TINPPDDLLAKPGSV----------------GRPLPGVEVR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1423 IANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNsrlsfGDTqtiWARTGYLGFLrrteltDANGErhda 1502
Cdd:COG0318 359 IVDPDGGEVLPGEV-GEIWVRGPNVMKGY---WNRPEATAEAFD-----EDG---WLRTGDLGYV------DEDGY---- 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530392110 1503 LYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 1563
Cdd:COG0318 417 LYIVGRLKDLIISGGENIYPEEIE-AVLAEHPAVAEAAVVgvpdeRWGERVVAVVVLKPGGDAELT 481
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1031-1572 |
1.01e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 135.84 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1031 VLQWRAQTTPDHILYTLLNCR---GAIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1108 CVPITVRPPH----------------PQNIATTLPTVKMIVEVSRSACLMTTQLIckllrsreaaAAVDVrtwpLILDTD 1171
Cdd:PRK05850 84 LIAVPLSVPQggahdervsavlrdtsPSVVLTTSAVVDDVTEYVAPQPGQSAPPV----------IEVDL----LDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1172 DLPKKRPAQIckpcnPDTlAYLDFSVSTTGMLAGVKMSHAATSAFCRsiKLQCELYPSREVAICLD-------P-YCGLG 1243
Cdd:PRK05850 150 RGSDARPRDL-----PST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1244 FVLWCLCSVYSGHQSILIPPSELETNPALW--LLAVSQYkvrdtfcSYSV-----MELCTKglgsQTESLKARGLDLSRV 1316
Cdd:PRK05850 222 LVLGVCAPILGGCPAVLTSPVAFLQRPARWmqLLASNPH-------AFSAapnfaFELAVR----KTSDDDMAGLDLGGV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1317 RTcVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAE------QGTSGPDPTTVYVDMRA 1390
Cdd:PRK05850 291 LG-IISGSERVHPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1391 LRHDRVR---------LVERGSPHSlplmesgkilPGVRIIiaNPETKGPLGDSHLGEIWVHSAHNASGYFTiyGDESLQ 1461
Cdd:PRK05850 354 LSAGHAKrcetgggtpLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAAGYWQ--KPEETE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1462 SDhFNSRL---SFGDTQTIWARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVirahKSVT- 1537
Cdd:PRK05850 420 RT-FGATLvdpSPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATI----QEITg 483
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 530392110 1538 -ECAVFT----WTNLLVVVVEL---DGSEQEALDLVPLVTNVV 1572
Cdd:PRK05850 484 gRVAAISvpddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| CaiC |
COG0318 |
Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II [Lipid transport and metabolism, ... |
373-964 |
2.33e-32 |
|
Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 223395 [Multi-domain] Cd Length: 534 Bit Score: 134.13 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 373 PPSLEAALQRWGTISPKAPCLTTMDTNGKplyiLTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAF 452
Cdd:COG0318 10 ELTLASLLERAARRNPDRPALIFLGRGGR----LTYRELDRRANRLA-AALQALG------VKPGDRVAILLPNS--PEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 453 MAAFYGCLLAEVVPVPIEVPLTRKdagsqQIGFLLGSCGVTVALTSDA----CHKGLPKSPTGEIPQFKGWPKLLWFVTE 528
Cdd:COG0318 77 LIAFLAALRAGAVAVPLNPRLTPR-----ELAYILNDAGAKVLITSAEfaalLEAVAEALPVVLVVLLVGDADDRLPITL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 529 SKHLSKPPRDWFPHIKDANNDTAYIEY--------KtckdgsvlGVTVTRTALLTHCQALTQACG--YTEAETIVNVLDF 598
Cdd:COG0318 152 EALAAEGPGPDADARPVDPDDLAFLLYtsgttglpK--------GVVLTHRNLLANAAGIAAALGggLTPDDVVLSWLPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 599 KKDVGLWHGILTSVMNMMHVisIPYSLMKVNPLSWIQKVCQYKAKV-ACVKsrDMHWALVAHRDQRDINLSS-LRMLIVa 676
Cdd:COG0318 224 FHIFGLIVGLLAPLLGGGTL--VLLSPEPFDPEEVLWLIEKYKVTVlSGVP--TFLRELLDNPEKDDDDLSSsLRLVLS- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 677 dGANPWSISSCDAFLNVFQSKglrqeVICPCASSPEALTVAIRRPTDDSNQPPGRGVLSMHGLTYGVIRVDSEEklsvlt 756
Cdd:COG0318 299 -GGAPLPPELLERFEERFGPI-----AILEGYGLTETSPVVTINPPDDLLAKPGSVGRPLPGVEVRIVDPDGGE------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 757 vqdvglVMPGaimcsvkpdgvpqlcrtdEIGELCVC--AVATGtsYYGLSGMTKNTFEvfpmtssgapisEYPFIRTGLL 834
Cdd:COG0318 367 ------VLPG------------------EVGEIWVRgpNVMKG--YWNRPEATAEAFD------------EDGWLRTGDL 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 835 GFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEpmkfvYRGRIAVFSVTVLH-DERIVIVAEQRPDSTEEDSFQ 913
Cdd:COG0318 409 GYVDEDGYLYIVGRLKDLIISGGENIYPEEIEAVLAEHP-----AVAEAAVVGVPDERwGERVVAVVVLKPGGDAELTAE 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 530392110 914 WMSRVLQAIDSIHQVGVYclaLVPANTLPKTPLGGIHLSETKQLFLEGSLH 964
Cdd:COG0318 484 ELRAFLRKRLALYKVPRI---VVFVDELPRTASGKIDRRALREEYRAEPRL 531
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
373-961 |
3.68e-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: 130.48 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 373 PPSLEAALQRWGTISPKAPClTTMDTNGKPlYILTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAF 452
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSE-EFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDDNE--DF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 453 MAAFYGCLLAEVVPVPIEVPLTRKDAGSQ-----QIGFLLGSCgvtVALTSDACHKGLpksptgeIPQFKGWPKLLWFVT 527
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSP---VVLTDAELVAEF-------AGLETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 528 ESKHLSKPPRDWFPHIKDAnNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHG 607
Cdd:cd05906 148 SIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 608 ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKV------ACVKSRDmhwaLVAHRDQRDINLSSLRMLIVADGANp 681
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 682 wSISSCDAFLNVFQSKGLRQEVICPCASSPEalTVAirrptddsnqppgrgvlsmhGLTYGviRVDSEEKLS-VLTVQDV 760
Cdd:cd05906 302 -VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS--------------------GVIYS--RSFPTYDHSqALEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 761 GLVMPGAIMCSVKPDGvpQLCRTDEIGELCVCavatGTS----YYGLSGMTKNTFevfpmTSSGapiseypFIRTGLLGF 836
Cdd:cd05906 357 GRPIPGVSMRIVDDEG--QLLPEGEVGRLQVR----GPVvtkgYYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 837 VGPGGLVFvVGKMDGLMVVSGRRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHD--ERIVIVAeqrpdSTEEDSFQW 914
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFF-----VPEYDLQDA 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 530392110 915 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHLSETKQLFLEG 961
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
406-965 |
2.83e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 125.12 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAYSILhKLGtkqepmVRPGDRVALVfPNNDPAaFMAAFYGCLLAEVVPVPIEVP--LTRKDAGSQQI 483
Cdd:PRK09192 50 LPYQTLRARAEAGARRLL-ALG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 484 GFLLGSCGVTVALTSDACHKGLPKSPTGEIPQFKGWPKLLwfvteskHLSKPPRDWFPHIKDanNDTAYIEYKTckdGSV 563
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWF-------KALPEADVALPRPTP--DDIAYLQYSS---GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 564 ---LGVTVTRTALLTHCQALTQ-ACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQ 639
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 640 YKAKVAcvKSRDMHWALVAHR----DQRDINLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlT 715
Cdd:PRK09192 269 NRGTIS--YSPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 716 VAIrrptddSNQPPGRGV----LSMHGLTYGVIRVDSEEK-LSVLTVQDVGLVMPGAIMCSVKPDG--VPQLcrtdEIGE 788
Cdd:PRK09192 344 LAV------SFSPLGSGIvveeVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGmpLPER----VVGH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 789 LCVcavatgtsyYGLSGMTkntfEVFPMTSSGAPISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVAT 868
Cdd:PRK09192 414 ICV---------RGPSLMS----GYFRDEESQDVLAADGWLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 869 AlavEPMKFVYRGRIAVFSVTVLHDERIVIVAEQRPdSTEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLG 947
Cdd:PRK09192 480 A---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSG 553
|
570
....*....|....*...
gi 530392110 948 GIHLSETKQLFLEGSLHP 965
Cdd:PRK09192 554 KLSRAKAKKRYLSGAFAS 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
435-963 |
2.28e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 113.29 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 435 RPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVPltrKDAG-SQQIGFLLGSCGVTVALTSDACHKGLPKSptgei 513
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP---AEPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKF----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 514 pqFKGWPKllwfvteskhlSKPPR-------------DWFPhiKDANNDT-AYIEYKTckdGSV---LGVTVTRTALLTH 576
Cdd:PRK07769 147 --FRARPA-----------KERPRviavdavpdevgaTWVP--PEANEDTiAYLQYTS---GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 577 CQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNmmHVISI--PYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHW 654
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 655 A--LVAHR-----DQRDINLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEALTVAIRRPTDDSNQ 727
Cdd:PRK07769 286 AfeHAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 728 ppgrgvlsmhgltygVIRVDSEEkLSVLTVQDVGLVMPGAI-------------MCSVKPDGVPQLcRTDEIGELCVCAV 794
Cdd:PRK07769 364 ---------------VIYVDRDE-LNAGRFVEVPADAPNAVaqvsagkvgvsewAVIVDPETASEL-PDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 795 ATGTSYYGLSGMTKNTFE------VFPMTSSGAPiSEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVAT 868
Cdd:PRK07769 427 NIGTGYWGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 869 ALavEPMKFVYRGRIAVFSV-------TVLHD-------------ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQV 928
Cdd:PRK07769 505 AQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGV 582
|
570 580 590
....*....|....*....|....*....|....*
gi 530392110 929 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSL 963
Cdd:PRK07769 583 TVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1028-1551 |
6.80e-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: 111.22 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1028 LSEVLQWRAQTTPDHILYTllncrgaIANSLTCV-----QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYG 1102
Cdd:cd05906 12 LLELLLRAAERGPTKGITY-------IDADGSEEfqsyqDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1103 CLYAGCVPITVRPPHP-QNIATTLPTVKMIVEVSRSA-CLMTTQLICKLLRSREAA--AAVDVRTWPLILDTDDLPKKRP 1178
Cdd:cd05906 84 CVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPvVLTDAELVAEFAGLETLSglPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1179 AQickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSiKLQCELYPSREVA---ICLDPYCGLGFVlwCLCSVYSG 1255
Cdd:cd05906 164 SR------PDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1256 HQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSvmeLCTKgLGSQTESLKARGLDLSRVRtCVVVAEERPRIALTQSF 1335
Cdd:cd05906 235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1336 SKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQGtSGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKI 1415
Cdd:cd05906 310 LRLLEPYGLPPDAIRPAFG----------------MTETC-SG---VIYSRSFPTYDH----------SQALEFVSLGRP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1416 LPGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltda 1495
Cdd:cd05906 360 IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFLD------- 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392110 1496 NGErhdaLYVVGALDEAMELRGMRYHPIDIETSV----IRAHKSVTECAVF---TWTNLLVVV 1551
Cdd:cd05906 421 NGN----LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1055-1536 |
1.57e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 110.60 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1055 ANSLTCVQLHKRAEKIAVMLMErgHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNIATTLPTVkmiVEV 1134
Cdd:PRK12476 66 AVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTA---LRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1135 SRSACLMTTQLICKLLRSREAAAAVDVRtwPLILDTDDLPKkRPAQICKPCNPDT--LAYLDFSVSTTGMLAGVKMSHAA 1212
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPD-SAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1213 TSA----FCRSIKLqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHqSILIPPSELETNPALWLLAVSQ-YKVRDTFC 1287
Cdd:PRK12476 218 VGTnlvqMILSIDL---LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1288 SYS--VMELCT-KGLGSQTEslkarGLDLSRVrtCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclq 1364
Cdd:PRK12476 294 AAPnfAYEWAAqRGLPAEGD-----DIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG---------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1365 phrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLG 1438
Cdd:PRK12476 357 ------IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1439 EIWVHSAHNASGYFTiYGDESLQSDH--FNSRLSFG------DTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGALD 1510
Cdd:PRK12476 431 EIWLHGDNIGRGYWG-RPEETERTFGakLQSRLAEGshadgaADDGTWLRTGDLGVYL-------DGE----LYITGRIA 498
|
490 500
....*....|....*....|....*.
gi 530392110 1511 EAMELRGMRYHPIDIETSVIRAHKSV 1536
Cdd:PRK12476 499 DLIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1032-1536 |
3.00e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.82 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1032 LQWRAQTTPDHILYTLLNC---RGAIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAGC 1108
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDFsteRDGVARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1109 VPITVRPPHPQNIATTLPTVkmIVEVSRSACLMTT---QLICKLLRSREAAAAvdvrtwPLILDTDDLPKKRPAQICKP- 1184
Cdd:PRK07769 105 IAVPLFDPAEPGHVGRLHAV--LDDCTPSAILTTTdsaEGVRKFFRARPAKER------PRVIAVDAVPDEVGATWVPPe 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1185 CNPDTLAYLDFSVSTTGMLAGVKMSH--AATSAF--CRSIKLQcelYPSREVAiCLDPYCGLGFVLWCLCSVYSGHQSIL 1260
Cdd:PRK07769 177 ANEDTIAYLQYTSGSTRIPAGVQITHlnLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1261 IPPSELEtNPALWLLAVSQyKVRDTFCSYSV-----MELCT-KGLGSQTESlkarGLDLSRVRtCVVVAEERPRIALTQS 1334
Cdd:PRK07769 253 SPAAFVR-RPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNGSEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1335 FSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLP 1408
Cdd:PRK07769 326 FNEAFAPYGLPPTAIKPSYG----------------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1409 LMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYG--DESLQSDH--FNSRLSFGDTQ-----TIWA 1479
Cdd:PRK07769 390 QVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGY---WGkpEETAATFQniLKSRLSESHAEgapddALWV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 530392110 1480 RTGYLGflrrtelTDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSV 1536
Cdd:PRK07769 467 RTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1018-1561 |
4.43e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 108.94 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1018 DNDQARK---FLFLSEVLQWRAQTTPDHILYTLlncRGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGI 1094
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFYDR---RGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1095 DLIAAFYGCLYAGCVPITVrpPHPQNI---ATTLPTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTD 1171
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV-----NEATHGNPLLHVLSHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1172 DLpKKRPAQICK--PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQ-CELYPSREVAICLDPYCGLGFVlWC 1248
Cdd:PRK09192 159 WF-KALPEADVAlpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGLV-GF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1249 LCSVYSGHQSI-LIPPSELETNPALWLLAVSqyKVRDTFcSYSV---MELCTKGLGSQTESlkarGLDLSRVRTCVVVAE 1324
Cdd:PRK09192 237 LLTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1325 E-RPRIalTQSFSKLFKDLGLHPRAVSTSFG-CRVNLAICLQPHrlwtlaEQGtsgpdpttvyvdMRALRHDRVRLVERG 1402
Cdd:PRK09192 310 MiRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPL------GSG------------IVVEEVDRDRLEYQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1403 spHSLPLMES----------GKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESlqsdhfnsrlsfg 1472
Cdd:PRK09192 370 --KAVAPGAEtrrvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYF---RDEE------------- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1473 DTQTI----WARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSV-----IRAHksvtECAVFT 1543
Cdd:PRK09192 431 SQDVLaadgWLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqepeLRSG----DAAAFS 495
|
570 580
....*....|....*....|..
gi 530392110 1544 WTN----LLVVVVELDGSEQEA 1561
Cdd:PRK09192 496 IAQengeKIVLLVQCRISDEER 517
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
399-961 |
6.12e-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: 107.57 E-value: 6.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 399 NGKPLYIlTYGKLWTRSMKVaysilhkLGTKQEPMVRPGDRValVFPNNDPAAFMAAFYGCLLAEVVPVPievpltrkda 478
Cdd:cd05908 10 DKKEKFV-SYRHLREEALGY-------LGALQELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVP---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 479 gsqqigfllgscgvtVALTSDACHKglpksptgeIPQFKGWPKLL--WFVTESKHLSKPPrdwfphikdanNDTAYIEYK 556
Cdd:cd05908 70 ---------------VSIGSNEEHK---------LKLNKVWNTLKnpYLITEEEVLCELA-----------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 557 TCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQK 636
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 637 VCQYKAKVACVKSRDMHWALVAHRDQR--DINLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAl 714
Cdd:cd05908 195 ASEHKATIVSSPNFGYKYFLKTLKPEKanDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 715 TVAIRRPTDDSNQPPgrgvLSMH--GLTYG--VIRVDSEEKlSVLTVQDVGLVMPgaiMCSVK-PDGVPQLCRTDEIGEL 789
Cdd:cd05908 272 SVGASLPKAQSPFKT----ITLGrrHVTHGepEPEVDKKDS-ECLTFVEVGKPID---ETDIRiCDEDNKILPDGYIGHI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 790 CVCAVATGTSYYGLSGMTKNTfevfpMTSSGapiseypFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATA 869
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKV-----FTDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIA 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 870 LAVEPmkfVYRGRIAVFSV--TVLHDERIVIVAEQRpdsTEEDSFQWMSRVLQAID------SIHQVgvyclalVPANTL 941
Cdd:cd05908 411 EELEG---VELGRVVACGVnnSNTRNEEIFCFIEHR---KSEDDFYPLGKKIKKHLnkrggwQINEV-------LPIRRI 477
|
570 580
....*....|....*....|
gi 530392110 942 PKTPLGGIHLSETKQLFLEG 961
Cdd:cd05908 478 PKTTSGKVKRYELAQRYQSG 497
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-174 |
5.82e-23 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 Cd Length: 104 Bit Score: 94.79 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 8 GMALPLEVRARLAELELELSEGDITQKGYEKKRSKLIGAYLPQPptangaavvrcrlqhsegaprrtfrsahigvcdvre 87
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHP------------------------------------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 88 aaarervastagnrplfyfrfgvdqalpqerRAPVTPSSASRYHR-RRSSGSRDERYRSDVHTEAVQAALAKHKERKMAV 166
Cdd:pfam06464 46 -------------------------------ETPTKLSAEAQNQLaSLETKLRDEELSEEVYLEKVKALLAKELERENGL 94
|
....*...
gi 530392110 167 PMPSKRRS 174
Cdd:pfam06464 95 NAPTKEQS 102
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
375-949 |
6.65e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 105.41 E-value: 6.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 375 SLEAALQRWGTISPKAPCLTTMDTNGKPLYI---LTYGKLWTRSMKVAYSiLHKLGtkqepmvRPGDRVALVFPNNdpAA 451
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIDYEQDPAGVaetLTWSQLYRRTLNVAEE-LRRHG-------STGDRAVILAPQG--LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 452 FMAAFYGCLLAEVVPVPIEVPLTRkdAGSQQIGFLLGSCGVTVALTS----DACHKGLPKSPTGEIPqfkgwpkllWFVT 527
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQSAP---------PVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 528 ------ESKHLSKPPRDWFPhikdannDTAYIEYKTCKDGSVLGVTVTRTALLTHC-QALTQACGYTEAE-----TIVNV 595
Cdd:PRK05850 141 vdlldlDSPRGSDARPRDLP-------STAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 596 LDFKKDVGLWHGILTSVMNMMH-VISIPYSLMKvNPLSWIQKVCQYKAKVACVKSrdmhWAL-VAHRDQRDINLSSL--- 670
Cdd:PRK05850 214 LPFYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQLLASNPHAFSAAPN----FAFeLAVRKTSDDDMAGLdlg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 671 RMLIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIRRPtddsNQPPGrgvlsmhgltygVIRVDSE 749
Cdd:PRK05850 289 GVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP----GQPPE------------SVRFDYE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 750 eKLSVLTVQ----DVG--LVMPGAIMCS----VKPDGVPQlCRTDEIGELCVCA--VATGtsYYGLSGMTKNTFE---VF 814
Cdd:PRK05850 353 -KLSAGHAKrcetGGGtpLVSYGSPRSPtvriVDPDTCIE-CPAGTVGEIWVHGdnVAAG--YWQKPEETERTFGatlVD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 815 PmtSSGAPISeyPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalavepMKFVYRGRIAVFSVTVLHDE 894
Cdd:PRK05850 429 P--SPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTE 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 895 RIVIVAE-QRPDSTEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 949
Cdd:PRK05850 498 KLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
380-856 |
7.37e-23 |
|
AMP-binding enzyme;
Pssm-ID: 425722 [Multi-domain] Cd Length: 417 Bit Score: 103.16 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 380 LQRWGTISPKAPCLTTMDTngkplYILTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGC 459
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG-----RRLTYRELDERANRLAAG-LRALG------VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 460 LLAEVVPVPIEVpltrkDAGSQQIGFLLGSCGVTVALTSD--------ACHKGLPKSPTGEIPQFKGWPKLLWFVTESKH 531
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 532 LSKPPRdwfPHIKDANNDTAYIEY--------KtckdgsvlGVTVTRTALLTHCQALTQAC----GYTEAETIVNVLDFK 599
Cdd:pfam00501 142 ADVPPP---PPPPPDPDDLAYIIYtsgttgkpK--------GVMLTHRNLVANVLAIKRVRprgfGLGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 600 KDVGLWHGILTSVMNMMHVISIPYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHwALVAHRDQRDINLSSLRMLIVadGA 679
Cdd:pfam00501 211 HDFGLSLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERYKVTVLYGVPTLLN-MLLEAGAPKRALLSSLRLVLS--GG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 680 NPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptddsnqppGRGVLSMHGLT--YGVIRVDSEEKLSVLTV 757
Cdd:pfam00501 287 APLPPELARRFRELF-----------------------------------GGALVNGYGLTetTGVVTTPLPLDDDLRSL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 758 QDVGLVMPGAIMCSVKPDGVpQLCRTDEIGELCV--CAVATGtsYYGLSGMTKNTFEvfpmtssgapisEYPFIRTGLLG 835
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCIrgPGVMKG--YLNDPELTAEAFD------------EDGWYRTGDLG 396
|
490 500
....*....|....*....|.
gi 530392110 836 FVGPGGLVFVVGKMDGLMVVS 856
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1062-1541 |
7.66e-23 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 103.11 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1062 QLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITvrPPHPQN-IATtlptvkmIVEVSRSA 1138
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAayVPLD--PAYPAErLAF-------ILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1139 CLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAqickPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCR 1218
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1219 SIklqCELYPSREVAICLDpYCGLGF------VLWCLcsvYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVM 1292
Cdd:TIGR01733 151 WL---ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1293 ELCtkglgsqtesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLglhpravstsfgcrvnlaiclqphRLWTla 1372
Cdd:TIGR01733 224 ALL----------AAALPPALASLRL-VILGGEALTPALVDRWRARGPGA------------------------RLIN-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1373 eqgTSGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYF 1452
Cdd:TIGR01733 267 ---LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGYL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1453 tiyGDESLQSDHFNSRLSFGDTQTIWARTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRA 1532
Cdd:TIGR01733 335 ---NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLR 400
|
....*....
gi 530392110 1533 HKSVTECAV 1541
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
397-965 |
1.11e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 104.82 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 397 DTNGKPLYiLTYGKLWTRsmkvaysiLHKLGTKQEPMVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPI---EVPl 473
Cdd:PRK12476 61 SAAGCAVE-LTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfapELP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 474 trkdAGSQQIGFLLGSCGVTVALTSDAChkglpkspTGEIPQFkgwpkllwfvteskhLSKPPRDWFPH------IKDA- 546
Cdd:PRK12476 129 ----GHAERLDTALRDAEPTVVLTTTAA--------AEAVEGF---------------LRNLPRLRRPRviaidaIPDSa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 547 ----------NNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETI-VNVLDFKKDVGLWHGILTSVMNM 615
Cdd:PRK12476 182 gesfvpveldTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 616 MHVISIPYSLMKvNPLSWIQKV---CQYKAKVACVKSRDMHWAlvAHR----DQRDINLSSLRMLIvadGANPWSISSCD 688
Cdd:PRK12476 262 HSTLMSPTAFVR-RPQRWIKALsegSRTGRVVTAAPNFAYEWA--AQRglpaEGDDIDLSNVVLII---GSEPVSIDAVT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 689 AFLNVFQSKGLRQEVICPCASSPEA-LTVAirrpTDDSNQPPGRGVLSMHGLTYG-VIRVDSEEKLSVLTVQdVGLVMPG 766
Cdd:PRK12476 336 TFNKAFAPYGLPRTAFKPSYGIAEAtLFVA----TIAPDAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 767 AIMCSVKPDGVPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFEV-----FPMTS--SGAPISEyPFIRTGLLGFVGP 839
Cdd:PRK12476 411 QWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDG-TWLRTGDLGVYLD 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 840 GGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVL 919
Cdd:PRK12476 489 GEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 530392110 920 QAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 965
Cdd:PRK12476 566 AAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1057-1542 |
3.66e-22 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 101.91 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVpitVRPPHPQNIATTL--------PTV 1128
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGI---FSAANPIYTADELahqlkiskPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1129 kMIVEVSrsaCLMTTQLICK---------LLRSREAAAA--VDVRTWPLILDTDDLPkkrpaqICKPCNPDTLAYLDFSV 1197
Cdd:cd05911 86 -IFTDPD---GLEKVKEAAKelgpkdkiiVLDDKPDGVLsiEDLLSPTLGEEDEDLP------PPLKDGKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1198 STTGMLAGVKMSHaatSAFCRSIKLQC----ELYPSREVAICLDPY---CGLgfvLWCLCSVYSGHQSILIPpselETNP 1270
Cdd:cd05911 156 GTTGLPKGVCLSH---RNLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMP----KFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1271 ALWLLAVSQYKVRDTFCSYSVMELctkgLGSQTESLKArglDLSRVRTCVVVAEerpriALTQSFSKLFKdlglhpravs 1350
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGGA-----PLSKELQELLA---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1351 tsfgCRVNLAICLQphrLWTLAEqgTSGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVRIIIANPETKG 1430
Cdd:cd05911 284 ----KRFPNATIKQ---GYGMTE--TGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1431 PLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALD 1510
Cdd:cd05911 336 SLGPNEPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYF------DEDGY----LYIVDRKK 394
|
490 500 510
....*....|....*....|....*....|..
gi 530392110 1511 EAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1542
Cdd:cd05911 395 ELIKYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1055-1544 |
1.27e-18 |
|
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: 91.28 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1055 ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPItvrpphPQNIATTLPTVKMIVEV 1134
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1135 SRSACLMTTQLICKLLRSREAAAAVDVRT----------WPLILDTDDLPKKRPAQICKPCNPDTLAYLDFSVSTTGMLA 1204
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1205 GVKMSHAatsafcrSIKLQCELYPSREVAICLDPYC----------GLGFVLWCLCSVysGHQSILIPpsELETnPALWL 1274
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP--ERPT-PAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1275 LAVSQYKvRDTFcsYSVMELCTKGLGSqtESLKARglDLSRVRTCVVVAEerpriALTQSFSKLFKDLglhpravstsFG 1354
Cdd:cd05959 248 KRIRRYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGE-----ALPAEVGERWKAR----------FG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1355 CRVnlaiclqphrlwtlaEQGTSGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVRIIIANpETKGPLGD 1434
Cdd:cd05959 306 LDI---------------LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1435 SHLGEIWVHSAHNASGYFTIYGDeslqsdhfnSRLSFgdtQTIWARTGYlGFLRrteltDANGerhdALYVVGALDEAME 1514
Cdd:cd05959 356 GEPGELYVRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLK 413
|
490 500 510
....*....|....*....|....*....|
gi 530392110 1515 LRGMRYHPIDIEtSVIRAHKSVTECAVFTW 1544
Cdd:cd05959 414 VSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
373-993 |
2.29e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.07 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 373 PPSLEAALQRWGTISPKAPCLTTMDTNGKPLYILTYGKLWTRSMKVAYSIlhklgtkqEPMVRPGDRVALVFPNNdpAAF 452
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 453 MAAFYGCLLAEVVPVPIEVPLTRKDAGSQQIGFLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkGWPKLLwfvTESKHL 532
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPELL---CVDTLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 533 SKPPRDWF-PHIKDanNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACG--YTEAETIVNVLDFKKDVGLWHGIL 609
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 610 TSVMNmmhviSIPYSLMKVN-----PLSWIQKVCQYKAKVAcvKSRDMHWALVAHRdQRDINLSSL---RMLIVADGANP 681
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 682 WSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAirrptddsNQPPGRGVlsmhgltyGVIRVDSE-------EKLS 753
Cdd:PRK05691 302 IRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS--------GGRRGQGI--------PALELDAEalarnraEPGT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 754 VLTVQDVGLVMPGAIMCSVKPDGVPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFevfpMTSSGApiseyPFIRTGL 833
Cdd:PRK05691 366 GSVLMSCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 834 LGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalAVEPMKFVYRGRIAVFSVTVLHDERIVIVAE-----QRPDSTE 908
Cdd:PRK05691 436 LGFLRDGEL-FVTGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 909 EdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLhpcnvlmcphTCVTNLPKPRQKQPE 988
Cdd:PRK05691 513 A----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAA 578
|
....*
gi 530392110 989 IGPAS 993
Cdd:PRK05691 579 QTAAS 583
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1057-1564 |
2.72e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 86.43 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSR 1136
Cdd:cd05930 12 SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE------RLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1137 SACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1216
Cdd:cd05930 85 AKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1217 CRSIKlqcELYP--SREVAICLDPYcglGF------VLWCLCsvySGHQsILIPPSELETNPALWLLAVSQYKVRDTFCS 1288
Cdd:cd05930 122 LLWMQ---EAYPltPGDRVLQFTSF---SFdvsvweIFGALL---AGAT-LVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1289 YSVMELCTKGLGSQteslkarglDLSRVRTcVVVAEERPRIALTQSFSKLFKDlglhpravstsfgcrvnlaiclqpHRL 1368
Cdd:cd05930 192 PSLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPG------------------------ARL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1369 WTLaeqgtSGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNA 1448
Cdd:cd05930 238 VNL-----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1449 SGYftiYGDESLQSDHFNsRLSFGDTQTIWaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIETs 1528
Cdd:cd05930 303 RGY---LNRPELTAERFV-PNPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA- 366
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 530392110 1529 VIRAHKSVTECAVFTWTN------LLVVVVELDGSEQEALDL 1564
Cdd:cd05930 367 ALLAHPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| EntF |
COG1020 |
Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport ... |
1028-1533 |
1.30e-13 |
|
Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 223951 [Multi-domain] Cd Length: 642 Bit Score: 75.76 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1028 LSEVLQWRAQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:COG1020 229 IHLLFEEQAATTPDAVA---LVRGGQ---QLTYAELDARANRLARLLISLG-VGPGETVAILADRSLELVVALLAVLKAG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1108 CVPITVRPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVdvrtWPLILDTDDLPKKRPAQickpcnP 1187
Cdd:COG1020 302 AAYVPLDPLYPAE------RLAYILEDSRPTLLLTQAHLRVDDVGLPGLALD----DALSEIPDTDPIPQALL------G 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1188 DTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGF--VLWCLCsvySGhQSILIPPSE 1265
Cdd:COG1020 366 DALAYIIYTSGSTGQPKGVRIEHRALANLLNDAGARFGLDADDRVLALASLSFDASVfeIFGALL---EG-ARLVLAPAL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1266 LETNPALWLLAVSQYKVrdtfcsySVMeLCTKGLGSQ---TESLKARGLDLSRVRTCVVVAEerpriALTQSFSKLFkdl 1342
Cdd:COG1020 442 LQVDPAALLELLEAQGI-------TVL-LLVPLLLRLlllAALAPDLISPCERLRQLLSGGE-----ALPLALVQRL--- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1343 glhpravstsfgcrvnLAICLQPHRLWTLaeqgtSGPDPTTVYVDMRALRHDRVRLVERGSPhslplmesgkiLPGVRII 1422
Cdd:COG1020 506 ----------------LQLAALARRLLNL-----YGPTEATLDAPSFPISAELESRVPIGRP-----------VANTQLY 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1423 IANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRLSFgdtqtiwaRTGYLGFLrrteltDANGERHda 1502
Cdd:COG1020 554 ILD-QGLRPLPLGVPGELYIAGLGLALGY---LNRPDLTAERFIALRLY--------RTGDLARP------LADGALE-- 613
|
490 500 510
....*....|....*....|....*....|.
gi 530392110 1503 lyVVGALDEAMELRGMRyhpidIETSVIRAH 1533
Cdd:COG1020 614 --YLGRKDSQVKIRGFR-----IELGEIEAA 637
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1062-1541 |
2.49e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 74.42 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1062 QLHKRAEKIAVMLMERGhlqDGDHVALVYPPGIDLIAAFYGCLYAG----CVPITVRPPHPQNIA-TTLptvkmivevSR 1136
Cdd:PRK05851 36 EVHGRAENVAARLLDRD---RPGAVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWAdATL---------TR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1137 SACLMTTQLIC-----KLLRSREAAAAV-DVRTWPlildtddlPKKRPAQIcKPCNPDTLAYLDFSVSTTGMLAGVKMSH 1210
Cdd:PRK05851 104 FAGIGVRTVLShgshlERLRAVDSSVTVhDLATAA--------HTNRSASL-TPPDSGGPAVLQGTAGSTGTPRTAILSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1211 AATSAFCRSIKLQCELYPSREVAICLDPY---CGLGFVLwclCSVYSGHQSILIPPSELETNPALWLLAVSQykVRDTFC 1287
Cdd:PRK05851 175 GAVLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSD--SRATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1288 SYSVMELCTKGLGSQteslKARGLDLSRVRTCVVVAEerP-RIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqph 1366
Cdd:PRK05851 250 AAPNFAYNLIGKYAR----RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG------------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1367 rlwtLAEQ--GTSGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVRIIIANPETKGPLGDSHLGEIWVHS 1444
Cdd:PRK05851 312 ----LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1445 AHNASGYFtiyGDESLQSDHfnsrlsfgdtqtiWARTGYLGFlrrteLTDangerhDALYVVGALDEAMELRGMRYHPID 1524
Cdd:PRK05851 380 ASMMSGYL---GQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTE 432
|
490
....*....|....*..
gi 530392110 1525 IETSVIRAhKSVTECAV 1541
Cdd:PRK05851 433 IERVAAQV-RGVREGAV 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1186-1526 |
1.10e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 72.52 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1186 NPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSE 1265
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1266 LETNPALWLLAVSQYKVRDTFCSysvmELCTKGLGSQTESLKARGLDLSRVRTCVVVAEErprIA--LTQSFSKLFKDLG 1343
Cdd:cd05908 184 FIRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1344 LHPRAVSTSFGcrvnlaiclqphrlwtLAEQ--GTSGPDP----TTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKIL 1416
Cdd:cd05908 257 LKRNAILPVYG----------------LAEAsvGASLPKAqspfKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1417 PGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaN 1496
Cdd:cd05908 321 DETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGY---YNNPEATAKVF--------TDDGWLKTGDLGFIR-------N 381
|
330 340 350
....*....|....*....|....*....|
gi 530392110 1497 GErhdaLYVVGALDEAMELRGMRYHPIDIE 1526
Cdd:cd05908 382 GR----LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
419-947 |
4.49e-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: 70.16 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 419 AYSILHKLGTkqepmvRPGDRVALVFPNNDPA---AFMAAFYGCLLAEVVpvpieVPLTrKDAGSQQIGFLLGSCGVTVA 495
Cdd:cd05922 6 AASALLEAGG------VRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 496 LTS----DACHKGLPKSPTGEipqfkgwpklLWFVTESKHLSKPPRDWFPHIKDannDTAYIEYKTCKDGSVLGVTVTRT 571
Cdd:cd05922 74 LADagaaDRLRDALPASPDPG----------TVLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 572 ALLTHCQALTQACGYTEAETIVNVLDFKKDVGLwhgiltSVMNMmH-------VISIPYSLmkvnPLSWIQKVCQYKAK- 643
Cdd:cd05922 141 NLLANARSIAEYLGITADDRALTVLPLSYDYGL------SVLNT-HllrgatlVLTNDGVL----DDAFWEDLREHGATg 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 644 VACVKSrdmHWALVAHRDQRDINLSSLRMLIVADGANPwsisscDAFLNVFQSKGlrqevicpcasspealtvairrptd 723
Cdd:cd05922 210 LAGVPS---TYAMLTRLGFDPAKLPSLRYLTQAGGRLP------QETIARLRELL------------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 724 dsnqpPGRGVLSMHGLTYGVIR---VDSEEKLSVLTvqDVGLVMPGAIMCSVKPDGvpQLCRTDEIGELcvcaVATGTSY 800
Cdd:cd05922 256 -----PGAQVYVMYGQTEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDG--TPTPPGEPGEI----VHRGPNV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 801 YgLSGMTKNTFEVFPMTSSGApiseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfvyr 880
Cdd:cd05922 323 M-KGYWNDPPYRRKEGRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI----- 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530392110 881 GRIAVFSVTVLHDERIVIVAEqRPDSTEEDSfqwMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 947
Cdd:cd05922 390 IEAAAVGLPDPLGEKLALFVT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1028-1262 |
5.96e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 69.90 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1028 LSEVLQWRAQTTPDHilyTLLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:cd05936 1 LADLLEEAARRFPDK---TALIFMGR---KLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1108 CVPITVRPphpqniattlptvkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQickpcNP 1187
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVAL-----TP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1188 DTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsIKLQC-----ELYPSREVAICLDP-YCGLGFVLWCLCSVYSGHQSILI 1261
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 530392110 1262 P 1262
Cdd:cd05936 201 P 201
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1057-1541 |
1.12e-11 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 69.19 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1057 SLTCVQLHKRAEKIAVMLMERGHLQdGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqniATTLPTVKMIVEVSR 1136
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1137 SACLMTT-QLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKP-CNPDTLAYLDFSVSTTGMLAGVKMSH---- 1210
Cdd:cd05904 105 AKLAFTTaELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVvIKQDDVAALLYSSGTTGRSKGVMLTHrnli 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1211 AATSAFCRSIKLQCElypSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPSELETnpalWLLAVSQYKVRDTFCSY 1289
Cdd:cd05904 185 AMVAQFVAGEGSNSD---SEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVTHLPVVP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1290 SVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPRiALTQSFSKLFKDlglhpravstsfgcrVNLaicLQPHRLW 1369
Cdd:cd05904 258 PIVLALVK-------SPIVDKYDLSSLRQIMSGAAPLGK-ELIEAFRAKFPN---------------VDL---GQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1370 TLAEQGTSGPDPTtvyvdmralrHDRVRlveRGSphslplmeSGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNAS 1449
Cdd:cd05904 312 ESTGVVAMCFAPE----------KDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1450 GYFtiyGDESlqsdhfnsrlsfgDTQ-TI----WARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPID 1524
Cdd:cd05904 371 GYL---NNPE-------------ATAaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVAPAE 424
|
490
....*....|....*..
gi 530392110 1525 IEtSVIRAHKSVTECAV 1541
Cdd:cd05904 425 LE-ALLLSHPEILDAAV 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1036-1567 |
7.32e-11 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 66.50 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1036 AQTTPDHILYTllnCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITV 1113
Cdd:cd05945 1 AAANPDRPAVV---EGGR---TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1114 RPPHPQniattlptVKMIVEVSRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYL 1193
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIAD-------------------------------------------GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1194 DFSVSTTGMLAGVKMSHAATSAFCRSIkLQCELYPSREVAICLDPYcglGF---VLWCLCSVYSGhQSILIPPSELETNP 1270
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPF---SFdlsVMDLYPALASG-ATLVPVPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1271 ALWLLAVSQYKVRDTFCSYSVMELCTkGLGSQTESLkargldLSRVRTCVVVAEERPrIALTQSFSKLFkdlglhPravs 1350
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPES------LPSLRHFLFCGEVLP-HKTARALQQRF------P---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1351 tsfGCRV-NlaiclqphrlwtlaeqgTSGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVRIIIANPETK 1429
Cdd:cd05945 240 ---DARIyN-----------------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILDEDGR 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1430 gPLGDSHLGEIWVHSAHNASGYFtiyGDEslqsDHFNSRLSFGDTQTiWARTGYLGFLrrteltDANGErhdaLYVVGAL 1509
Cdd:cd05945 292 -PVPPGEKGELVISGPSVSKGYL---NNP----EKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRL 352
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392110 1510 DEAMELRGMRYHPIDIETSViRAHKSVTECAVFTWTNL-----LVVVVELDGSEqEALDLVPL 1567
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1036-1541 |
3.22e-10 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 64.67 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1036 AQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG--CVPITV 1113
Cdd:cd17651 5 AARTPDAPA---LVAEGR---RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1114 RPPhPQNIAttlptvkMIVEVSRSACLMTTQlickllrsREAAAAVDVRTWPLILDTDDLPKKRPAQICKPCNPDTLAYL 1193
Cdd:cd17651 78 AYP-AERLA-------FMLADAGPVLVLTHP--------ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1194 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF--VLWCLCSVYSGHQSILIPPSELETNPA 1271
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTL----QFAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1272 LWLLAVSQYKVRDTFCSYSVME-LCtkglgsqtESLKARGLDLSRVRtCVVVAEERprialtqsfsklfkdLGLHPRavs 1350
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGEQ---------------LVLTED--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1351 tsfgcrvnlaiclqpHRLWTLAEQG-----TSGPDPTTVyVDMRALRHDRVRlveRGSPHSLplmesGKILPGVRIIIAN 1425
Cdd:cd17651 271 ---------------LREFCAGLPGlrlhnHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1426 PETKgPLGDSHLGEIWVHSAHNASGYFTIYG--DESLQSDHF--NSRLSfgdtqtiwaRTGYLGflRRteltDANGErhd 1501
Cdd:cd17651 327 AALR-PVPPGVPGELYIGGAGLARGYLNRPEltAERFVPDPFvpGARMY---------RTGDLA--RW----LPDGE--- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 530392110 1502 aLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1541
Cdd:cd17651 388 -LEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVV 425
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
565-949 |
5.68e-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: 62.69 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 565 GVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV 644
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 645 ACVkSRDMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptdd 724
Cdd:cd04433 92 LLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP------------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 725 snqppGRGVLSMHGLT-----YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGVPqlCRTDEIGELCVcavatgTS 799
Cdd:cd04433 139 -----GIKLVNGYGLTetggtVATGPPDDDARKPG----SVGRPVPGVEVRIVDPDGGE--LPPGEIGELVV------RG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 800 YYGLSGMTKNTFEVFPMTSSGapiseypFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvy 879
Cdd:cd04433 202 PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA--- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530392110 880 rgRIAVFSVTvlhDER------IVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 949
Cdd:cd04433 272 --EAAVVGVP---DPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
566-958 |
7.69e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.48 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 566 VTVTRTALLTHCQALTQACGYT-EAETIVNVLDFKKDVGLWhGILTSVMNM-MHVISI-PYSLMkVNPLSWIQKVCQYKA 642
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMV-GFLTVPMYFgAELVKVtPMDFL-RDPLLWAELISKYRG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 643 KVACvkSRDMHWALVAHR-----DQRDINLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVA 717
Cdd:PRK07768 248 TMTA--APNFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEA-TLA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 718 IrrptddSNQPPGRGvlsmhgLTYGVIRVD--SEEKLSVLTVQD-------VGLVMPGAIMCSVKPDGvpQLCRTDEIGE 788
Cdd:PRK07768 323 V------SFSPCGAG------LVVDEVDADllAALRRAVPATKGntrrlatLGPPLPGLEVRVVDEDG--QVLPPRGVGV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 789 LCVCAVATgTSYYglsgmtkntfevfpMTSSG--APISEYPFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIV 866
Cdd:PRK07768 389 IELRGESV-TPGY--------------LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 867 ATALAVEPmkfVYRGRIAVFSVTVLHD-ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPK 943
Cdd:PRK07768 454 RAAARVEG---VRPGNAVAVRLDAGHSrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPK 528
|
410
....*....|....*
gi 530392110 944 TPLGGIHLSETKQLF 958
Cdd:PRK07768 529 TPSGKLRRANAAELV 543
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1057-1282 |
2.79e-09 |
|
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: 61.52 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPhPQNIATTLptvkmiveV 1134
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARREAIL--------A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1135 SRSACLMTTQLICkllrSREAAAAVDVRTWPLILD-TDDLPKKRPAQickpcnPDTLAYLDFSVSTTGMLAGVKMSHAAT 1213
Cdd:cd12114 82 DAGARLVLTDGPD----AQLDVAVFDVLILDLDALaAPAPPPPVDVA------PDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530392110 1214 SAFCRSIKLQCELYPSREVaICLDPycgLGFVLwclcSVY------SGHQSILIPPSELETNPALWLLAVSQYKV 1282
Cdd:cd12114 152 LNTILDINRRFAVGPDDRV-LALSS---LSFDL----SVYdifgalSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1057-1558 |
3.01e-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: 61.15 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSR 1136
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1137 SACLMTTQlickllrSREAAAAVDVRTWPLILDTDDLPkkrPAQICKPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1216
Cdd:cd12116 85 PALVLTDD-------ALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1217 CRSIklqcelypsREvaicldpycglgfvlwclcsvysghqsilippsELETNPALWLLAVSQYkvrdTFcSYSVMEL-- 1294
Cdd:cd12116 155 LHSM---------RE---------------------------------RLGLGPGDRLLAVTTY----AF-DISLLELll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1295 ----------CTKGLGSQTESLKARgldLSRVRTCVVVAeerprialTQSFSKLFKDLGLHPRAvstsfGCRV------- 1357
Cdd:cd12116 188 pllagarvviAPRETQRDPEALARL---IEAHSITVMQA--------TPATWRMLLDAGWQGRA-----GLTAlcggeal 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1358 --NLA--ICLQPHRLWTLaeqgtSGPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVRIIIANPETKgPLG 1433
Cdd:cd12116 252 ppDLAarLLSRVGSLWNL-----YGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVLDAALR-PVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1434 DSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWARTGYLgfLRRteltDANGErhdaLYVVGALDEAM 1513
Cdd:cd12116 314 PGVPGELYIGGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR----RADGR----LEYLGRADGQV 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 530392110 1514 ELRGMRYHPIDIETsVIRAHKSVTECAVFTWTN----LLVVVVELDGSE 1558
Cdd:cd12116 380 KIRGHRIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1034-1541 |
3.25e-09 |
|
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: 61.14 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1034 WRAQT--TPDH--ILYTllncrgaiANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1109
Cdd:cd17646 4 VAEQAarTPDApaVVDE--------GRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1110 PITVRPPHPQniattlPTVKMIVEVSRSACLMTTQlickllRSREAAAAVDVRTWPLILDTDDLPKKRPAQickPCNPDT 1189
Cdd:cd17646 75 YLPLDPGYPA------DRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLV---PPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1190 LAYLDFSVSTTGMLAGVKMSHAatsAFCRSIKLQCELYP--SREVAICLDPycgLGF------VLWCLCsvySGhQSILI 1261
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPlgPGDRVLQKTP---LSFdvsvweLFWPLV---AG-ARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1262 PPSELETNPALWLLAVSQYKVrdTFCSY--SVMELCtkglgsqteslkargLDLSRVRTC-----VVVAEErpriALTQS 1334
Cdd:cd17646 210 ARPGGHRDPAYLAALIREHGV--TTCHFvpSMLRVF---------------LAEPAAGSCaslrrVFCSGE----ALPPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1335 FSKLFKDLglhpravstsFGCRVnlaiclqpHRLWtlaeqgtsGPDPTTVYVDmralrHDRVRlvERGSPHSLPLmesGK 1414
Cdd:cd17646 269 LAARFLAL----------PGAEL--------HNLY--------GPTEAAIDVT-----HWPVR--GPAETPSVPI---GR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1415 ILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHF-------NSRLSfgdtqtiwaRTGYLGfl 1487
Cdd:cd17646 313 PVPNTRLYVLDDALR-PVPVGVPGELYLGGVQLARGY---LGRPALTAERFvpdpfgpGSRMY---------RTGDLA-- 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 530392110 1488 RRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAV 1541
Cdd:cd17646 378 RWR----PDGA----LEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVV 422
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1032-1562 |
3.76e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.99 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1032 LQWRAQTTPDHILYTLLNCRGAIAN----SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1107
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADGKlaydELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1108 CVPITVRP-------------PHPQ--------NIATTL-----PTVKMIVEVSRSACLMTTQLIcKLLRSREAAAAvdv 1161
Cdd:PRK09274 91 AVPVLVDPgmgiknlkqclaeAQPDafigipkaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTLA-TLLRDGAAAPF--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1162 rtwplildtddlpkkrpaqICKPCNPDTLAYLDFSVSTTGMLAGVKMSHaatSAFCRSIKLQCELYPSR--EVAIC---- 1235
Cdd:PRK09274 167 -------------------PMADLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQIEALREDYGIEpgEIDLPtfpl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1236 ---LDPYCGlgfvlwcLCSVysghqsilIPPSEL----ETNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKA 1308
Cdd:PRK09274 225 falFGPALG-------MTSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YGEA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1309 RGLDLSRVRTcVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLqphrlwtlaeqgtsgpdpttvyVD 1387
Cdd:PRK09274 283 NGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS----------------------IE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1388 MRALRHDRVRLVERGSPHSLplmesGKILPGVRI-IIA---NP-----ETKgPLGDSHLGEIWVHSAHNASGYFtiygde 1458
Cdd:PRK09274 335 SREILFATRAATDNGAGICV-----GRPVDGVEVrIIAisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYY------ 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1459 slQSDHFN--SRLSFGDTQtIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSV 1536
Cdd:PRK09274 403 --NRPEATrlAKIPDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGV 468
|
570 580
....*....|....*....|....*.
gi 530392110 1537 TECAvftwtnllVVVVELDGSEQEAL 1562
Cdd:PRK09274 469 KRSA--------LVGVGVPGAQRPVL 486
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
376-674 |
6.44e-08 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 57.19 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 376 LEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAA 455
Cdd:cd05936 5 LEEAARRF----PDKTALIFMGRK------LTYRELDALAEAFA-AGLQNLG------VQPGDRVALMLPNC--PQFPIA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 456 FYGCLLAEVVPVPIEVPLTrkdagSQQIGFLLGSCGVTVALTsdachkglpksptgeipqfkgwpkLLWFvtesKHLSKP 535
Cdd:cd05936 66 YFGALKAGAVVVPLNPLYT-----PRELEHILNDSGAKALIV------------------------AVSF----TDLLAA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 536 PRDWFPHIKDANNDTAYIEYKTckdgsvlGVT-VTRTALLTH---------CQALTQACGyTEAETIVNVLDFKKDVGLW 605
Cdd:cd05936 113 GAPLGERVALTPEDVAVLQYTS-------GTTgVPKGAMLTHrnlvanalqIKAWLEDLL-EGDDVVLAALPLFHVFGLT 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 606 HGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKVAC-VKSrdMHWALVAHRDQRDINLSSLRMLI 674
Cdd:cd05936 185 VALLLPLALGATIVLIP----RFRPIGVLKEIRKHRVTIFPgVPT--MYIALLNAPEFKKRDFSSLRLCI 248
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
369-679 |
1.42e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 56.07 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 369 VTNWPPSLEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNd 448
Cdd:PRK07656 4 WMTLPELLARAARRF----GDKEAYVFGDQR------LTYAELNARVRRAA-AALAALG------IGKGDRVAIWAPNS- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 449 pAAFMAAFYGCLLAEVVPVPIEvplTRKDAGsqQIGFLLGSCGVTVALTSD-------ACHKGLPK----------SPTG 511
Cdd:PRK07656 66 -PHWVIAALGALKAGAVVVPLN---TRYTAD--EAAYILARGDAKALFVLGlflgvdySATTRLPAlehvviceteEDDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 512 EIPQFKGWPKLLwfvteskhLSKPPRDWFPHIKDanNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAET 591
Cdd:PRK07656 140 HTEKMKTFTDFL--------AAGDPAERAPEVDP--DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 592 IVNVLDFKKDVGLWHGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV-ACVKSrdMHWALVAHRDQRDINLSSL 670
Cdd:PRK07656 210 YLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERITVlPGPPT--MYNSLLQHPDRSAEDLSSL 283
|
....*....
gi 530392110 671 RmLIVADGA 679
Cdd:PRK07656 284 R-LAVTGAA 291
|
|
| EntF |
COG1020 |
Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport ... |
406-859 |
1.60e-07 |
|
Non-ribosomal peptide synthetase component F [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 223951 [Multi-domain] Cd Length: 642 Bit Score: 56.11 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAYsILHKLGtkqepmVRPGDRVALVFPNndPAAFMAAFYGCLLAEVVPVPIEVpltrkDAGSQQIGF 485
Cdd:COG1020 253 LTYAELDARANRLAR-LLISLG------VGPGETVAILADR--SLELVVALLAVLKAGAAYVPLDP-----LYPAERLAY 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 486 LLGSCGVTVALTSDACHKGLPKSPTGEIPQfkgwpkLLWFVTESKhlskpprdwFPHIKDANNDTAYIEYKTCKDGSVLG 565
Cdd:COG1020 319 ILEDSRPTLLLTQAHLRVDDVGLPGLALDD------ALSEIPDTD---------PIPQALLGDALAYIIYTSGSTGQPKG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 566 VTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVIsIPYSLMKVNPLSWIQKVCQYKAKVa 645
Cdd:COG1020 384 VRIEHRALANLLNDAGARFGLDADDRVLALASLSFDASVF-EIFGALLEGARLV-LAPALLQVDPAALLELLEAQGITV- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 646 cvksrdMHWalvahrdqrdinLSSLRMLIVADGANPWSISSCDAflnvfqskgLRQEVIcpcasSPEALTVAIRRPTDDS 725
Cdd:COG1020 461 ------LLL------------VPLLLRLLLLAALAPDLISPCER---------LRQLLS-----GGEALPLALVQRLLQL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 726 NqPPGRGVLSMHGLTYGVI-----RVDSEEKLSVLtvqdVGLVMPGAIMCSVkpDGVPQLCRTDEIGELCV--CAVATGt 798
Cdd:COG1020 509 A-ALARRLLNLYGPTEATLdapsfPISAELESRVP----IGRPVANTQLYIL--DQGLRPLPLGVPGELYIagLGLALG- 580
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530392110 799 sYYGLSGMTKntfEVFpmtssgapiSEYPFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRR 859
Cdd:COG1020 581 -YLNRPDLTA---ERF---------IALRLYRTGDLARPLADGALEYLGRKDSQVKIRGFR 628
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1058-1566 |
1.90e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1058 LTCVQLHKRAEKIAVMLMERGHLQDGdHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRS 1137
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEV-LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1138 ACLMTTQLICKLLRSREAAAAVDV---RTWplildtDDLPKKRPAqicKPCNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1214
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDGLASLALdrdEDW------EGFPAHDPA---VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV 4720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1215 AFCRSIKLQCELYPSREVaICLDPYCGLGFVL---WCLCSvysgHQSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSV 1291
Cdd:PRK12316 4721 NHLHATGERYELTPDDRV-LQFMSFSFDGSHEglyHPLIN----GASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1292 MELCTKGlgsqteslKARGLDLSRVRTCVVVAEERPRIALTQSFSKlfkdlglhpravstsfgcrvnlaicLQPHRLWTl 1371
Cdd:PRK12316 4795 LQQLAEH--------AERDGEPPSLRVYCFGGEAVAQASYDLAWRA-------------------------LKPVYLFN- 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1372 aeqgTSGPDPTTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVRIII----ANPETKGPLGDSHLGEIWVhsahn 1447
Cdd:PRK12316 4841 ----GYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVldgqLNPLPVGVAGELYLGGEGV----- 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1448 ASGYFTiygDESLQSDHFNSRlSFGDTQTIWARTGYLGFLRRTELTDangerhdalyVVGALDEAMELRGMRYHPIDIET 1527
Cdd:PRK12316 4904 ARGYLE---RPALTAERFVPD-PFGAPGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEA 4969
|
490 500 510
....*....|....*....|....*....|....*....
gi 530392110 1528 SvIRAHKSVTECavftwtnlLVVVVELDGSEQEALDLVP 1566
Cdd:PRK12316 4970 R-LREHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1062-1229 |
2.54e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1062 QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLM 1141
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1142 T-TQLICKLLRSREAAAavdvrtwpLILDTD----DLPKKRPAQickPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1216
Cdd:PRK12316 2106 TqRHLLERLPLPAGVAR--------LPLDRDaewaDYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170
....*....|...
gi 530392110 1217 CRSIKLQCELYPS 1229
Cdd:PRK12316 2175 CQAAGERYELSPA 2187
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
407-857 |
4.11e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 54.42 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 407 TYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAFMAAFYGCLLAEVVPVPIEVPLTrkdagSQQIGFL 486
Cdd:PRK06187 33 TYAELDERVNRLA-NALRALG------VKKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 487 LGSCGVTVALTSDAcHKGLPKSPTGEIPQFKGW--------PKLLWFVTESKHL--SKPPRDWFPHIKDanNDTAYIEYK 556
Cdd:PRK06187 99 LNDAEDRVVLVDSE-FVPLLAAILPQLPTVRTVivegdgpaAPLAPEVGEYEELlaAASDTFDFPDIDE--NDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 557 TCKDGSVLGVTVTRTALLTHCQALTQACGYTEaetivnvldfkKDVGLwhgiltSVMNMMHV--ISIPY-SLM------- 626
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR-----------DDVYL------VIVPMFHVhaWGLPYlALMagakqvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 627 --KVNPlswiQKVCQY--KAKV---ACVKSrdMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAFLNVFqskgl 699
Cdd:PRK06187 239 prRFDP----ENLLDLieTERVtffFAVPT--IWQMLLKAPRAYFVDFSSLRLVIY--GGAALPPALLREFKEKF----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 700 rqevicpcasspealtvairrptddsnqppGRGVLSMHGL--TYGVIRVD--SEEKLSVLTVQ-DVGLVMPG---AImcs 771
Cdd:PRK06187 306 ------------------------------GIDLVQGYGMteTSPVVSVLppEDQLPGQWTKRrSAGRPLPGveaRI--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 772 VKPDGVPQLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEvfpmtsSGapiseypFIRTGLLGFVGPGGLVFVVGKMDG 851
Cdd:PRK06187 353 VDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------GG-------WLHTGDVGYIDEDGYLYITDRIKD 419
|
....*.
gi 530392110 852 lMVVSG 857
Cdd:PRK06187 420 -VIISG 424
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
400-502 |
4.70e-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: 54.30 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 400 GKPLYI-----LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFpnNDPAAFMAAFYGCLLAEVVPVPIEVPLT 474
Cdd:cd05959 19 DKTAFIddagsLTYAELEAEARRVA-GALRALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 530392110 475 rkdagSQQIGFLLGSCGVTVALTSDACH 502
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGELA 112
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
337-873 |
5.24e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.96 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 337 FEELLEVQQPDPNQPKPEGAqmLAMRGEQLGVVTNWPPSLEAALQRWGT---------ISPKAPCLTTMDTNgkplyiLT 407
Cdd:PRK12316 1959 LLHLLEQMAEDAQAALGELA--LLDAGERQRILADWDRTPEAYPRGPGVhqriaeqaaRAPEAIAVVFGDQH------LS 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 408 YGKLWTRSMKVAYSILhKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLA--EVVPVPIEVPLTRkdagsqqIGF 485
Cdd:PRK12316 2031 YAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERS--FELVVALLAVLKAggAYVPLDPNYPAER-------LAY 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 486 LLGSCGVTVALTSDACHKGLPksPTGEIPQFKGWPKLLWFVTESKHlskpprdwfPHIKDANNDTAYIEYKTCKDGSVLG 565
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWADYPDTA---------PAVQLAGENLAYVIYTSGSTGLPKG 2163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 566 VTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPYSLMkvNPLSWIQKVCQYKAKVA 645
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELW--DPEQLYDEMERHGVTIL 2240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 646 CVKSrdMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAFLN------VFQSKGLRQEVICP-----CASSPE-A 713
Cdd:PRK12316 2241 DFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPllwkcRPQDPCgA 2316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 714 LTVAIRRPTDDsnqppgrgvlsmhgltygvirvdseEKLSVLtvqDVGLvmpgaimcsvkpdgvpQLCRTDEIGELCVCA 793
Cdd:PRK12316 2317 AYVPIGRALGN-------------------------RRAYIL---DADL----------------NLLAPGMAGELYLGG 2352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 794 VATGTSYYGLSGMTKNTFEVFPMTSSGAPIseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVE 873
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1057-1541 |
5.26e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 54.24 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1057 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPHPQNIAttlptvkmIVEV 1134
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERIAF--------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1135 SRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATS 1214
Cdd:cd17643 83 SGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1215 AFCRSIKLQCELYPSREVAICldPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAVSQYKVrdtfcsySVMel 1294
Cdd:cd17643 120 ALFAATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV-------TVL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1295 ctkglgSQT--------ESLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDlgLHPRAvstsfgcrVNLaiclqph 1366
Cdd:cd17643 189 ------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1367 rlwtlaeqgtSGPDPTTVYVDMRALRHDRVRLVErGSPhslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHSAH 1446
Cdd:cd17643 245 ----------YGITETTVHVTFRPLDAADLPAAA-ASP-------IGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1447 NASGYFtiyGDESLQSDHFNSrLSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIE 1526
Cdd:cd17643 306 VARGYL---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE 371
|
490
....*....|....*
gi 530392110 1527 tSVIRAHKSVTECAV 1541
Cdd:cd17643 372 -AALATHPSVRDAAV 385
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1030-1575 |
5.82e-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: 54.13 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1030 EVLQWRAQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1109
Cdd:cd12117 1 ELFEEQAARTPDAVA---VVYGDR---SLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1110 PITVRPPHPQNiattlpTVKMIVEVSRSACLMTtqlickllrSREAAAAVDVRTWPLILDTDDLPKKRPAQICkPCNPDT 1189
Cdd:cd12117 74 YVPLDPELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGLEVAVVIDEALDAGPAGNPAV-PVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1190 LAYLDFSVSTTGMLAGVKMSHAATSAFCRS---IKLQcelypSREVAICLDPYC--GLGFVLWclCSVYSGHQSILIPPS 1264
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtnyVTLG-----PDDRVLQTSPLAfdASTFEIW--GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1265 ELETNPALwLLAVSQYKVrdtfcsySVMELcTKGLGSQteslkargldlsrvrtcvvVAEERPrialtQSFSKLfkdlgl 1344
Cdd:cd12117 211 TLLDPDAL-GALIAEEGV-------TVLWL-TAALFNQ-------------------LADEDP-----ECFAGL------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1345 hpRAVSTSfGCRVNLAIClqphRLWTLAEQGTS-----GPDPTTVYvdmrALRHdrvrLVERG--SPHSLPLmesGKILP 1417
Cdd:cd12117 252 --RELLTG-GEVVSPPHV----RRVLAACPGLRlvngyGPTENTTF----TTSH----VVTELdeVAGSIPI---GRPIA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1418 GVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWaRTGYLgfLRRteltDANG 1497
Cdd:cd12117 314 NTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNRPALTAERF-VADPFGPGERLY-RTGDL--ARW----LPDG 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530392110 1498 ErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAvftwtnllVVVVELDGSEQEaldlvpLVTNVVLEE 1575
Cdd:cd12117 382 R----LEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAV--------VVVREDAGGDKR------LVAYVVAEG 440
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1032-1565 |
6.47e-07 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 53.77 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1032 LQWRAQTTPDHilyTLLNCRGaiaNSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPi 1111
Cdd:cd17631 1 LRRRARRHPDR---TALVFGG---RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVF- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1112 tvrppHPQNIATTLPTVKMIVEVSRSACLMttqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnpDTLA 1191
Cdd:cd17631 73 -----VPLNFRLTPPEVAYILADSGAKVLF----------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1192 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELyPSREVAICLDPYC---GLGfvLWCLCSVYSGHQSILIPpselET 1268
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILR----KF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1269 NPALWLLAVSQYKVRDTFCSYSVME-LCTKGlgsqteslKARGLDLSRVRtCVVVAEERPRIALTQSFSKlfkdlglhpr 1347
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRALQA---------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1348 avstsFGCRvnlaiclqphrLWTLAEQGTSGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVRIIIANPE 1427
Cdd:cd17631 236 -----RGVK-----------FVQGYGMTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPD 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1428 TKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDhfnsrlSFGDTqtiWARTGYLGFLrrteltDANGerhdALYVVG 1507
Cdd:cd17631 284 GR-EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVD 340
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530392110 1508 ALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLV-VVVELDGSEQEALDLV 1565
Cdd:cd17631 341 RKKDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1030-1210 |
7.29e-07 |
|
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: 53.87 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1030 EVLQWRAQTTPDHIlytllncrgAIA---NSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYA 1106
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1107 GC--VPITvrPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAaavdvrtwpLILDTDDLPKKRPAQICKP 1184
Cdd:cd17655 71 GGayLPID--PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPV 133
|
170 180
....*....|....*....|....*.
gi 530392110 1185 CNPDTLAYLDFSVSTTGMLAGVKMSH 1210
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
406-500 |
4.11e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 51.47 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAFMAAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 485
Cdd:PRK08316 37 WTYAELDAAVNRVA-AALLDLG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAY 102
|
90
....*....|....*
gi 530392110 486 LLGSCGVTVALTSDA 500
Cdd:PRK08316 103 ILDHSGARAFLVDPA 117
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1184-1541 |
1.03e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 49.99 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1184 PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYC-GLGFVLWCLCSVYSGHQSILIP 1262
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1263 PSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGSQTESlkaRGLDLSRVRtCVVVAEERPRIALTQSFSKLFKDL 1342
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1343 GLHPRAVSTSFG-CRVNLAICLQPhrlwtlaeqgtSGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPG--V 1419
Cdd:PRK07768 304 GLRPEAILPAYGmAEATLAVSFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGleV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1420 RIIIANPEtkgPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDHfnsrlsfGdtqtiWARTGYLGFLrrTEltdaNGEr 1499
Cdd:PRK07768 372 RVVDEDGQ---VLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE----EGE- 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530392110 1500 hdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTECAV 1541
Cdd:PRK07768 430 ---VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
406-497 |
1.24e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 49.96 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAYSILHKLGtkqepmVRPGDRVALvFPNNDPaAFMAAFYGCLLAEVVPVPIEvPLTRkdagSQQIGF 485
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNR----EEELAH 102
|
90
....*....|..
gi 530392110 486 LLGSCGVTVALT 497
Cdd:PRK08314 103 YVTDSGARVAIV 114
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
986-1212 |
1.57e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.04 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 986 QPEIGPASVmvgNLVSGKRIAQasgrdLGQIEDNDQARKFLFLSEVLQWRAQTTPDhilytllncRGAIA---NSLTCVQ 1062
Cdd:PRK10252 426 DPALLCGDV---DILLPGEYAQ-----LAQVNATAVEIPETTLSALVAQQAAKTPD---------APALAdarYQFSYRE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1063 LHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLMT 1142
Cdd:PRK10252 489 MREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLIT 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1143 TQlickLLRSREAAAAVDVRTWPLILDTDdlPKKRPAQICKPCNPdtlAYLDFSVSTTGMLAGVKMSHAA 1212
Cdd:PRK10252 562 TA----DQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHT---AYIIFTSGSTGRPKGVMVGQTA 622
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
380-496 |
1.77e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 49.15 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 380 LQRWGTISPKAPCLTTMDTngkplyILTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAFMAAFYGC 459
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLA-HALRALG------VAKGDRVAVLSKNSP--EFLELLFAA 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 530392110 460 LLAEVVPVPIEVPLTRKDagsqqIGFLLGSCGVTVAL 496
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSGAKVLF 97
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
596-961 |
2.65e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.61 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 596 LDFKKDVG-----LWHG-----ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKVacVKSRDMHWALVAH--RDQR 663
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATL--TAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 664 DINLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVAIRRPTddsnqpPGRGVLsmhgltygV 743
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV------PGIGLR--------V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 744 IRVDSEEKLSVLTVQDVGLVMPGA---IMCSVKPDGVPQlcrtDEIGELCVCAVATGTSYYGlsgmtkntfevfpmtssG 820
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMevrISPGDGAAGVAG----REIGEIEIRGASMMSGYLG-----------------Q 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 821 APISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfVYRGRIavfsVTVLHDE-----R 895
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRG---VREGAV----VAVGTGEgsarpG 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392110 896 IVIVAEQRpdSTEEDSFQwmSRVLQAIDSihQVGVyclalVPAN-------TLPKTPLGGIHLSETKQLFLEG 961
Cdd:PRK05851 462 LVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDvvfvapgSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1028-1216 |
2.92e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 48.75 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1028 LSEVLQWRAQTTPDHIlytllncrgAIA---NSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCL 1104
Cdd:PRK07656 7 LPELLARAARRFGDKE---------AYVfgdQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1105 YAGCVPITVRPPH-PQNIATTLPT--VKMI--------VEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDl 1173
Cdd:PRK07656 77 KAGAVVVPLNTRYtADEAAYILARgdAKALfvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530392110 1174 PKKRPAQIckpcNPDTLAYLDFSVSTTGMLAGVKMSHAAT-SAF 1216
Cdd:PRK07656 156 PAERAPEV----DPDDVADILFTSGTTGRPKGAMLTHRQLlSNA 195
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1030-1217 |
5.89e-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: 47.55 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1030 EVLQWRAQTTPDHILYTLlncRGaiaNSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCV 1109
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD---RG---QSLTYKQLNEKANQLARHLRGKGVKPD-DQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1110 PITVRPPHPQniattlptvkmivevsrsaclmttQLICKLLRSREAAaavdvrtwpLILDtddlpkkrpaqickpcNPDT 1189
Cdd:cd17645 75 YVPIDPDYPG------------------------ERIAYMLADSSAK---------ILLT----------------NPDD 105
|
170 180
....*....|....*....|....*...
gi 530392110 1190 LAYLDFSVSTTGMLAGVKMSHAATSAFC 1217
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
372-500 |
5.91e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 47.73 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 372 WPP-------------SLEAALQRWGTISPKAPCLttmDTNGkplYILTYGKLWTRSMKVAySILHKLGtkqepmVRPGD 438
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392110 439 RVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEvPLTRKdagsQQIGFLLGSCGVTVALTSDA 500
Cdd:PRK06178 85 RVAVFLPNC--PQFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1036-1211 |
1.67e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.04 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1036 AQTTPDHILYtllNCRGAianSLTCVQLHKRAEKIAVMLMERgHLQDGDHVaLVY----PpgiDLIAAFYGCLYAGC--V 1109
Cdd:PRK04813 12 AQTQPDFPAY---DYLGE---KLTYGQLKEDSDALAAFIDSL-KLPDKSPI-IVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1110 PITVRPPhpqniattLPTVKMIVEVSRSACLMTTqlickllrSREAAAAVDVRTwpLILD--TDDLPKKRPAQICKPCNP 1187
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIPV--ITLDelKDIFATGNPYDFDHAVKG 142
|
170 180
....*....|....*....|....
gi 530392110 1188 DTLAYLDFSVSTTGMLAGVKMSHA 1211
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
406-500 |
2.45e-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: 45.28 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALvFPNNDPAAFMAAFyGCLLAEVVPVPIevpltRKDAGSQQIGF 485
Cdd:cd05907 6 ITWAEFAEEVRALAKG-LIALG------VEPGDRVAI-LSRNRPEWTIADL-AILAIGAVPVPI-----YPTSSAEQIAY 71
|
90
....*....|....*
gi 530392110 486 LLGSCGVTVALTSDA 500
Cdd:cd05907 72 ILNDSEAKALFVEDP 86
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
406-595 |
3.05e-04 |
|
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: 45.36 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEvpltrKDAGSQQIGF 485
Cdd:cd12116 13 LSYAELDERANRLA-ARLRARG------VGPGDRVAVYLPRS--ARLVAAMLAVLKAGAAYVPLD-----PDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 486 LLGSCGVTVALTSDACHKGLPKSPTgeipqfkGWPKLLWFVTESKHLSKPPrdwfphikDANNDTAYIEYKTCKDGSVLG 565
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLP-------VLLLALAAAAAAPAAPRTP--------VSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190
....*....|....*....|....*....|
gi 530392110 566 VTVTRTALLTHCQALTQACGYTEAETIVNV 595
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDRLLAV 173
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1039-1210 |
3.20e-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: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1039 TPDHILYTLLNCrgaianSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAG--CVPITvrpP 1116
Cdd:cd17656 1 TPDAVAVVFENQ------KLTYRELNERSNQLARFLREKGVKKD-SIVAIMMERSAEMIVGILGILKAGgaFVPID---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1117 HpqniattLPTVKMIVEVSRSAC-LMTTQLICKLLRSREAAaaVDVRTWPLILDTDDlpkkrpAQICKPCNPDTLAYLDF 1195
Cdd:cd17656 71 E-------YPEERRIYIMLDSGVrVVLTQRHLKSKLSFNKS--TILLEDPSISQEDT------SNIDYINNSDDLLYIIY 135
|
170
....*....|....*
gi 530392110 1196 SVSTTGMLAGVKMSH 1210
Cdd:cd17656 136 TSGTTGKPKGVQLEH 150
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
407-859 |
3.79e-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: 44.95 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 407 TYGKLWTRSMKVAYSILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEV--PLTRkdagsqqIG 484
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 485 FLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkgwPKLLWFVTESKHLSKPPRDWFPHikdaNNDTAYIEY--------K 556
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSG----PDDLAYVIYtsgstgrpK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 557 tckdgsvlGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHgILTSVMNMMHVISIPYSLMKVNPLSWIQK 636
Cdd:TIGR01733 137 --------GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 637 VCQYKAKVAC-VKSrdmHWALVAhrDQRDINLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcasspEALT 715
Cdd:TIGR01733 208 IAEHPVTVLNlTPS---LLALLA--AALPPALASLRLVILG-G---------------------------------EALT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 716 VA-IRRPtddSNQPPGRGVLSMHGLTYGVI-----RVDSEEkLSVLTVQDVGLVMPGAIMCSVKPDGvpQLCRTDEIGEL 789
Cdd:TIGR01733 249 PAlVDRW---RARGPGARLINLYGPTETTVwstatLVDPDD-APRESPVPIGRPLANTRLYVLDDDL--RPVPVGVVGEL 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392110 790 CVCA--VATGtsYYGLSGMTKNTF-EVFPMTSSGAPIseYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRR 859
Cdd:TIGR01733 323 YIGGpgVARG--YLNRPELTAERFvPDPFAGGDGARL--Y---RTGDLVRYLPDGNLEFLGRIDDQVKIRGYR 388
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
388-598 |
4.07e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 44.95 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 388 PKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNDPAafMAAFYGCLLAEVVPV 467
Cdd:cd12114 1 PDATAVICGDGT------LTYGELAERARRVAGA-LKAAG------VRPGDLVAVTLPKGPEQ--VVAVLGILAAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 468 PIEV--PLTRKDAgsqqigfLLGSCGVTVALTSDACHKGLPKSPTgeipqfkgwpkllwFVTESKHLSKPPRDwFPHIKD 545
Cdd:cd12114 66 PVDIdqPAARREA-------ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDV 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530392110 546 ANNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNV--LDF 598
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALssLSF 178
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1036-1541 |
4.54e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1036 AQTTPDHILYTLLNCRgaiansLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP 1115
Cdd:PRK12467 522 ARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPD-VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1116 PHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTDDLPKKRPAQICKPCNPDTLAYLDF 1195
Cdd:PRK12467 595 EYPQD------RLAYMLDDSGVRLLLTQSHLLAQL-----PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1196 SVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAIcLDPYCGLGFVLWCLCSVYSGHQSILIPPSEletnpalwll 1275
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM-VSTFAFDLGVTELFGALASGATLHLLPPDC---------- 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1276 avsqykVRDTFCSYSVMelCTKGLG--SQTES-----LKARGLDLSRVRTCVVVAEErpriALTQSFSKLFKDLGLhpra 1348
Cdd:PRK12467 733 ------ARDAEAFAALM--ADQGVTvlKIVPShlqalLQASRVALPRPQRALVCGGE----ALQVDLLARVRALGP---- 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1349 vstsfGCrvnlaiclqphRLWTLaeqgtSGPDPTTVYVDMRALRHDRVrlVERGSPHSLPLMESgkilpGVRIIIA--NP 1426
Cdd:PRK12467 797 -----GA-----------RLINH-----YGPTETTVGVSTYELSDEER--DFGNVPIGQPLANL-----GLYILDHylNP 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1427 ETKGPLGDSHLGeiwvhSAHNASGYftiYGDESLQSDHFNSRLSFGDTQTIWaRTGYLGflRRTeltdANGErhdaLYVV 1506
Cdd:PRK12467 849 VPVGVVGELYIG-----GAGLARGY---HRRPALTAERFVPDPFGADGGRLY-RTGDLA--RYR----ADGV----IEYL 909
|
490 500 510
....*....|....*....|....*....|....*
gi 530392110 1507 GALDEAMELRGMRYHPIDIETSvIRAHKSVTECAV 1541
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEAR-LLAQPGVREAVV 943
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1054-1282 |
9.14e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 43.87 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1054 IANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP------------------ 1115
Cdd:PRK06710 46 LGKDITFSVFHDKVKRFANYLQKLG-VEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPlytereleyqlhdsgakv 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1116 --------PHPQNIATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKPCNP 1187
Cdd:PRK06710 125 ilcldlvfPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1188 DT-LAYLDFSVSTTGMLAGVKMSHA-ATSAFCRSIKLQCELYPSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPS 1264
Cdd:PRK06710 205 ENdLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVyGMTAVMNLSIMQGYKMVLIPKF 284
|
250
....*....|....*...
gi 530392110 1265 ELEtnpaLWLLAVSQYKV 1282
Cdd:PRK06710 285 DMK----MVFEAIKKHKV 298
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
406-945 |
9.31e-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: 43.67 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAYSILHKLgtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEV--PLTRkdagsqqI 483
Cdd:cd05930 13 LTYAELDARANRLARYLRERG-------VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDPsyPAER-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 484 GFLLGSCGVTVALTSDachkglpksptgeipqfkgwpkllwfvteskhlskpprdwfphikdanNDTAYIEY-------- 555
Cdd:cd05930 77 AYILEDSGAKLVLTDP------------------------------------------------DDLAYVIYtsgstgkp 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 556 KtckdgsvlGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMN--MMHVISipySLMKVNPLSW 633
Cdd:cd05930 109 K--------GVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAgaTLVVLP---EEVRKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 634 IQKVCQYKAKVA-CVKSrdmHW-ALVAHRDQRDinLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcassp 711
Cdd:cd05930 177 ADLLAEEGITVLhLTPS---LLrLLLQELELAA--LPSLRLVLVG-G--------------------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 712 EALTVAIRRPTDDSNqpPGRGVLSMHGLT-------YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGvpQLCRTD 784
Cdd:cd05930 218 EALPPDLVRRWRELL--PGARLVNLYGPTeatvdatYYRVPPDDEEDGRV----PIGRPIPNTRVYVLDENL--RPVPPG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 785 EIGELCVC--AVATGtsYYGLSGMTKntfEVFPMTSSGAPISEYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNA 862
Cdd:cd05930 290 VPGELYIGgaGLARG--YLNRPELTA---ERFVPNPFGPGERMY---RTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 863 DDIVATALAVEPMkfvyrgRIAVfsVTVLHD----ERIV--IVAEQRPDSTEEDSFQWMSRVLQAidsihqvgvYCL--A 934
Cdd:cd05930 362 GEIEAALLAHPGV------REAA--VVAREDgdgeKRLVayVVPDEGGELDEEELRAHLAERLPD---------YMVpsA 424
|
570
....*....|.
gi 530392110 935 LVPANTLPKTP 945
Cdd:cd05930 425 FVVLDALPLTP 435
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
406-497 |
1.16e-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: 43.24 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 485
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 530392110 486 LLGSCGVTVALT 497
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
406-477 |
1.41e-03 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 42.83 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392110 406 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPnnDPAAFMAAFYGCLLAEVVPVPIEVPLTRKD 477
Cdd:cd05919 11 VTYGQLHDGANRLG-SALRNLG------VSSGDRVLLLML--DSPELVQLFLGCLARGAIAVVINPLLHPDD 73
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1413-1555 |
2.94e-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: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1413 GKILPGVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFTIYGDEsLQSDHFNSRLsfgdtqtiwaRTGYLGFLrrtel 1492
Cdd:cd05922 289 GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL----------HTGDLARR----- 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530392110 1493 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSvIRAHKSVTECAVF----TWTNLLVVVVELD 1555
Cdd:cd05922 352 -DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
407-467 |
3.12e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 41.91 E-value: 3.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530392110 407 TYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdPaAFMAAFYGCLLAEVVPV 467
Cdd:PRK05605 59 TYAELGKQVRRAA-AGLRALG------VRPGDRVAIVLPNC-P-QHIVAFYAVLRLGAVVV 110
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1413-1541 |
3.57e-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: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1413 GKILPGVRIIIANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLRrtel 1492
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530392110 1493 tdangeRHDALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1541
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
406-523 |
5.09e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 41.43 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 406 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 485
Cdd:PRK08276 12 VTYGELEARSNRLA-HGLRALG------LREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLTAAE-----IAY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 530392110 486 LLGSCGVTVALTS----DACHKGLPKSP---------TGEIPQFKGWPKLL 523
Cdd:PRK08276 78 IVDDSGAKVLIVSaalaDTAAELAAELPagvplllvvAGPVPGFRSYEEAL 128
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1418-1542 |
6.42e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.03 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392110 1418 GVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLrrteltDANG 1497
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---GDPTITAANFTDG---------WLRTGDLGSL------SAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530392110 1498 ErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1542
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
|