|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
992-1556 |
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: 793.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 992 LYTLLNCRGTIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIA 1070
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1071 TTLPTVKMivEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA-----QIYKPSNPDTLAYLDFSV 1145
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1146 STTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAV 1225
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1226 SQYKVRDTFCSYSVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGCRV 1305
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1306 NLAICLQGTSGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHN 1385
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1386 ASGYFTIYGDESLQSDHFNS-RLSFGDTQTIWARTGYLGFLRRTELTDANGERHDALYVVGALDEAMELRGMRYHPIDIE 1464
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1465 TSVIRAHKSVTECAVFTWTNLLVVVVELD-GSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINSRGEKQRMHLR 1543
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 1537992864 1544 DGFLADQLDPIYV 1556
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
336-912 |
0e+00 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 736.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 336 CLTTMDTNGKPLYILTYGKLWTRSMKVAYNILHKLGTKqepmvrPGDRVALVFPnnDPAAFMVAFYGCLLAEVVPVPIEV 415
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLK------PGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 416 PLtrkdaGSQQIGFLLGSCGVTVALTSDACHKGLPKS-----PTGEIPQFKGWPKLLWFVTESKHLSKPPRDWFPHIKDA 490
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 491 NNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLM 570
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 571 KVNPLSWIQKVCQYKAKVACVKSRDMHWAL------VAHRDQRDVNLSSLRMLIVADGaNPWSISSCDAFLNVFQSKGLR 644
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 645 QEvicpcASSPEALTVAIRRPTD--DSNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQDVGLVMPGAIMCSVKPDGIP 722
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWqgTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 723 qLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEVFPMTSSGAPISEYPFIRTGLLGFVGPG----------GLVFVVGK 792
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 793 MDGLMVVSGRRHNADDIVATALAVEPmkfvYRGRIAVFSVTvlhdERIVIVAEQRPDStEEDSFQWMSRVLQAIDSIHQV 872
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPPGS-EEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1537992864 873 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHPCNV 912
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
982-1514 |
9.29e-70 |
|
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: 245.23 E-value: 9.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 982 WRAQTTPDHLLYTLLNCRGTIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITV 1061
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1062 RPPHPqniATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSnPDTLAYL 1141
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1142 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPY--CGLGFVLwcLCSVYSGHQSILIPPSELETNPA 1219
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1220 LWLLAVSQYkvRDTFcsySVM-----ELCTKglgsQTESLKARGLDLSRVRTCVVVAEeRPRIALTQSFSKLFKDLGLHP 1294
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFRP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1295 RAVSTSFGcrvnLA-ICL---QGTSGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPL 1370
Cdd:cd05931 303 EAFRPSYG----LAeATLfvsGGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGREL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1371 GDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRLSFGDtqTIWARTGYLGFLRRteltdanGErhdaLYVVGALDEA 1450
Cdd:cd05931 378 PDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDE--GGWLRTGDLGFLHD-------GE----LYITGRLKDL 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1537992864 1451 MELRGMRYHPIDIETSVIRAHKSVTE--CAVFTW----TNLLVVVVELDGSeQEALDLVPLVTNV---VLEEH 1514
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
350-903 |
5.51e-60 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 216.72 E-value: 5.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAYNILHKLgtkqepmvRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPLTRKDAgsQQIGF 429
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVG--------KPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPPPTPGRHA--ERLAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 430 LLGSCGVTVALTSDACHKGLPKSptgeIPQFKGWPKLLWFVTESKHLSkPPRDWFPHIKDANnDTAYIEYKTCKDGSVLG 509
Cdd:cd05931 93 ILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPPPSPDPD-DIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 510 VTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISI-PYSLMKvNPLSWIQKVCQYKAKV 588
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 589 ACVKsrDMHWALVAHR----DQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIR 663
Cdd:cd05931 246 SAAP--NFAYDLCVRRvrdeDLEGLDLSSWRVALN--GAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 664 RPtddsNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQdVGLVMPG---AIMCsvkPDGiPQLCRTDEIGELCVC--AV 738
Cdd:cd05931 322 PP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDqevRIVD---PET-GRELPDGEVGEIWVRgpSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 739 ATGtsYYGLSGMTKNTFEVFpmtssgAPISEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEP 818
Cdd:cd05931 393 ASG--YWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 819 MkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSET 898
Cdd:cd05931 464 A--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRAC 541
|
....*
gi 1537992864 899 KQLFL 903
Cdd:cd05931 542 RAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
980-1454 |
1.10e-58 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 209.09 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 980 LQWRAQTTPDHLLYTllNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPI 1059
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGR---RLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1060 TVRPphpqniATTLPTVKMIVEVSRSACLMTTQlICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSN----- 1134
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDD-ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1135 ------PDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCE----LYPSREVAICLDPYCGLGFVLWCLCSVYSGH 1204
Cdd:pfam00501 148 pppppdPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1205 QSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSVMELCTkglgsqtESLKARGLDLSRVRTCVVVAEeRPRIALTQSFS 1284
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLL-------EAGAPKRALLSSLRLVLSGGA-PLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1285 KLFkdlglhPRAVSTSFGCRVNLAICLQGTSGPDPTTVYvdmralrhdrvrlverGSPhslplmesGKILPGVRIIIANP 1364
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLRSL----------------GSV--------GRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1365 ETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVV 1444
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DEDGY----LEIV 407
|
490
....*....|
gi 1537992864 1445 GALDEAMELR 1454
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1137-1501 |
4.90e-39 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 149.36 E-value: 4.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1137 TLAYLDFSVSTTGMLAGVKMSH---AATSAFCRSIKlqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSe 1213
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnlLAAAAALAASG----GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1214 letNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPrIALTQSFSKLFKD---- 1289
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGIklvn 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1290 -LGLHPRAVSTSFGCRVNLAIclqgtsgpDPTTVyvdmralrhdrvrlvergsphslplmesGKILPGVRIIIANPETkG 1368
Cdd:cd04433 145 gYGLTETGGTVATGPPDDDAR--------KPGSV----------------------------GRPVPGVEVRIVDPDG-G 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1369 PLGDSHLGEIWVHSAHNASGYFTiygdeslqsdhfNSRLSFGDTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALD 1448
Cdd:cd04433 188 ELPPGEIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------DEDGY----LYIVGRLK 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1537992864 1449 EAMELRGMRYHPIDIETsVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 1501
Cdd:cd04433 246 DMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
976-1554 |
4.88e-36 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 150.70 E-value: 4.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 976 LSEVLQWRAQTTPDHLLYTLLNCRGTIANSLTCVQLHKRAEKIAVMLMERGHLqdGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1056 CV------PITVRPPHPQNIATtlptvkmIVEVSRSACLMTTQLICKLLRSREAAAAVDVrtwPLILDTDDLPKKRPAQI 1129
Cdd:PRK05691 89 VIavpaypPESARRHHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1130 YKPS-NPDTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsiklqCELYPSREVAICLDP----------YCGLGFVLWCLC 1198
Cdd:PRK05691 159 QEPAlQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1199 SVYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGsqtESLKARgLDLSRVRtcVVVAEERP-RI 1277
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVS---ESALER-LDLSRWR--VAYSGSEPiRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1278 ALTQSFSKLFKDLGLHPRAVSTSFGCRVNLAICLQGTSGPDPTTVYVDMRALRHDRVRLVErGSphslPLMESGKILPGV 1357
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGT-GS----VLMSCGRSQPGH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1358 RIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgDTQTiWARTGYLGFLRRTEltdanger 1437
Cdd:PRK05691 380 AVLIVDPQSLEVLGDNRVGEIWASGPSIAHGY---WRNPEASAKTFVEH----DGRT-WLRTGDLGFLRDGE-------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1438 hdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTWTNL----LVVVVELDGSEQEAL---DLVPLVTN 1508
Cdd:PRK05691 444 ---LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKgrVAAFAVNHQgeegIGIAAEISRSVQKILppqALIKSIRQ 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1537992864 1509 VVLEEHYLIVGVVVVVDIGVIPINSRGEKQRMHLRDGFLADQLDPI 1554
Cdd:PRK05691 521 AVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDSY 566
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
979-1510 |
6.41e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 136.23 E-value: 6.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 979 VLQWRAQTTPDHLLYTLLNCR---GTIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1056 CVPITVRPPHPQN--------IATTLPTVkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA 1127
Cdd:PRK05850 84 LIAVPLSVPQGGAhdervsavLRDTSPSV-----------VLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1128 QIYKPSNPDTlAYLDFSVSTTGMLAGVKMSHAATSAFCRsiKLQCELYPSREVAICLD-------P-YCGLGFVLWCLCS 1199
Cdd:PRK05850 153 DARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1200 VYSGHQSILIPPSELETNPALW--LLAVSQYkvrdtfcSYSV-----MELCTKglgsQTESLKARGLDLSRVRTcVVVAE 1272
Cdd:PRK05850 230 ILGGCPAVLTSPVAFLQRPARWmqLLASNPH-------AFSAapnfaFELAVR----KTSDDDMAGLDLGGVLG-IISGS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1273 ERPRIALTQSFSKLFKDLGLHPRAVSTSFG---CRVNLAIclqGTSGPDPTTVYVDMRALRHDRVR---------LVERG 1340
Cdd:PRK05850 298 ERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1341 SPHSlplmesgkilPGVRIIiaNPETKGPLGDSHLGEIWVHSAHNASGYFTiyGDESLQSDhFNSRL---SFGDTQTIWA 1417
Cdd:PRK05850 375 SPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAAGYWQ--KPEETERT-FGATLvdpSPGTPEGPWL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1418 RTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVirahKSVT--ECAVFT----WTNLLVVVVE 1491
Cdd:PRK05850 440 RTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATI----QEITggRVAAISvpddGTEKLVAIIE 504
|
570 580
....*....|....*....|..
gi 1537992864 1492 L---DGSEQEALDLVPLVTNVV 1510
Cdd:PRK05850 505 LkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
976-1503 |
5.84e-32 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 131.09 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 976 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:COG0318 1 LADLLRRAAARHPDR---PALVFGGR---RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1056 CVPITVrpphpqNIATTLPTVKMIVEVSRSACLMTtqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnp 1135
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1136 dtlAYLDFSvS-TTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPpsel 1214
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1215 ETNPALWLLAVSQYKVrdTFCSYS---VMELCtkglgsqtESLKARGLDLSRVRTCVVVAEerpriALTQSFSKLFKDLg 1291
Cdd:COG0318 175 RFDPERVLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1292 lhpravstsFGCRVNLA-----ICLQGTSGPDpttvyvDMRALRHDRVrlvergsphslplmesGKILPGVRIIIANPET 1366
Cdd:COG0318 239 ---------FGVRIVEGyglteTSPVVTVNPE------DPGERRPGSV----------------GRPLPGVEVRIVDEDG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1367 KgPLGDSHLGEIWVHSAHNASGYftiYGDESLqsdhfnSRLSFGDTqtiWARTGYLGFLrrteltDANGErhdaLYVVGA 1446
Cdd:COG0318 288 R-ELPPGEVGEIVVRGPNVMKGY---WNDPEA------TAEAFRDG---WLRTGDLGRL------DEDGY----LYIVGR 344
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1537992864 1447 LDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLVVVVEL-DGSEQEALDLV 1503
Cdd:COG0318 345 KKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
317-905 |
2.11e-31 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 131.25 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 317 PPSLEAALQRWGTISPKAPClTTMDTNGKPlYILTYGKLWTRsmkvAYNILHKLGTKQepmVRPGDRVALVFPNNDpaAF 396
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSE-EFQSYQDLLED----ARRLAAGLRQLG---LRPGDSVILQFDDNE--DF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 397 MVAFYGCLLAEVVPVPIEVPLTRKDAGSQ-----QIGFLLGSCgvtVALTSDACHKGLpksptgeIPQFKGWPKLLWFVT 471
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSP---VVLTDAELVAEF-------AGLETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 472 ESKHLSKPPRDWFPHIKDAnNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHG 551
Cdd:cd05906 148 SIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 552 ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKV------ACVKSRDmhwaLVAHRDQRDVNLSSLRMLIVADGANp 625
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 626 wSISSCDAFLNVFQSKGLRQEVICPCASSPEalTVAirrptddsnqppgrgvlsmhGLTYGviRVDSEEKLS-VLTVQDV 704
Cdd:cd05906 302 -VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS--------------------GVIYS--RSFPTYDHSqALEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 705 GLVMPGAIMCSVKPDGipQLCRTDEIGELCVCavatGTS----YYGLSGMTKNTFevfpmTSSGapiseypFIRTGLLGF 780
Cdd:cd05906 357 GRPIPGVSMRIVDDEG--QLLPEGEVGRLQVR----GPVvtkgYYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 781 VGPGGLVFvVGKMDGLMVVSGRRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHD--ERIVIVAeqrpdSTEEDSFQW 858
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFF-----VPEYDLQDA 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1537992864 859 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHLSETKQLFLEG 905
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-118 |
1.55e-30 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 116.75 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 8 GMALPLEVRARLAELELELSEGDITQKGYEKKRSKLIGAYLPQPprvdqalpqerRAPVTPSSASRYHR-RRSSGSRDER 86
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHP-----------ETPTKLSAEAQNQLaSLETKLRDEE 70
|
90 100 110
....*....|....*....|....*....|..
gi 1537992864 87 YRSDVHTEAVQAALAKHKERKMAVPMPSKRRS 118
Cdd:pfam06464 71 LSEEVYLEKVKALLAKELERENGLNAPTKEQS 102
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
320-907 |
1.22e-29 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 124.15 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 320 LEAALQRWGTISPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVA 399
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS--PEFVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 400 FYGCLLAEVVPVPIEVPLTRKdagsqQIGFLLGSCGVTVALTSDACH----KGLPKsptgeipqfkgwpkllwfvteskh 475
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 476 lskpprdwfphikdanndtayieyktckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTS 555
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 556 VMNMMHVISIPyslmKVNPLSWIQKVCQYKA-KVACVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAF 634
Cdd:COG0318 164 LLAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 635 LNVFQSkglrqeVICPC-ASSpEALTVAIRRPTDDSNQPPGRgvlsmhgltygvirvdseeklsvltvqdVGLVMPGAIM 713
Cdd:COG0318 236 EERFGV------RIVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 714 CSVKPDGIPqlCRTDEIGELCVC--AVATGtsYYGLSGMTKNTFEVfpmtssgapiseyPFIRTGLLGFVGPGGLVFVVG 791
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVVRgpNVMKG--YWNDPEATAEAFRD-------------GWLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 792 KMDGLMVVSGRRHNADDIVATALAVEPMKfvyrgRIAVFSVTV-LHDERIV--IVAEQRPDSTEEDSFQWMSRVL---QA 865
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1537992864 866 IDSIHQVGvyclalvpanTLPKTPLGGIHLSETKQLFLEGSL 907
Cdd:COG0318 419 PRRVEFVD----------ELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
350-909 |
4.92e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 124.35 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAYNILhKLGtkqepmVRPGDRVALVfPNNDPAaFMVAFYGCLLAEVVPVPIEVP--LTRKDAGSQQI 427
Cdd:PRK09192 50 LPYQTLRARAEAGARRLL-ALG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 428 GFLLGSCGVTVALTSDACHKGLPKSPTGEIPQFKGWPKLLwfvteskHLSKPPRDWFPHIKDanNDTAYIEYKTckdGSV 507
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWF-------KALPEADVALPRPTP--DDIAYLQYSS---GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 508 ---LGVTVTRIALLTHCQALTQ-ACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQ 583
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 584 YKAKVAcvKSRDMHWALVAHR----DQRDVNLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlT 659
Cdd:PRK09192 269 NRGTIS--YSPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 660 VAIrrptddSNQPPGRGV----LSMHGLTYGVIRVDSEEK-LSVLTVQDVGLVMPGAIMCSVKPDGIPQLCRtdEIGELC 734
Cdd:PRK09192 344 LAV------SFSPLGSGIvveeVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPLPER--VVGHIC 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 735 VcavatgtsyYGLSGMTkntfEVFPMTSSGAPISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATAl 814
Cdd:PRK09192 416 V---------RGPSLMS----GYFRDEESQDVLAADGWLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIA- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 815 avEPMKFVYRGRIAVFSVTVLHDERIVIVAEQRPdSTEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLGGI 893
Cdd:PRK09192 481 --EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKL 555
|
570
....*....|....*.
gi 1537992864 894 HLSETKQLFLEGSLHP 909
Cdd:PRK09192 556 SRAKAKKRYLSGAFAS 571
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1003-1474 |
4.17e-27 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 118.69 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1003 ANSLTCVQLHKRAEKIAVMLMErgHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNIATTLPTVkmiVEV 1082
Cdd:PRK12476 66 AVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTA---LRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1083 SRSACLMTTQLICKLLRSREAAAAVDVRtwPLILDTDDLPKkRPAQIYKPSNPDT--LAYLDFSVSTTGMLAGVKMSHAA 1160
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPD-SAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1161 TSA----FCRSIKLqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHqSILIPPSELETNPALWLLAVSQ-YKVRDTFC 1235
Cdd:PRK12476 218 VGTnlvqMILSIDL---LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1236 SYS--VMELCT-KGLGSQTEslkarGLDLSRVrtCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrVNLAICLQ 1312
Cdd:PRK12476 294 AAPnfAYEWAAqRGLPAEGD-----DIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1313 GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYF 1390
Cdd:PRK12476 365 ATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYW 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1391 TiYGDESLQSDH--FNSRLSFG------DTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGALDEAMELRGMRYHPID 1462
Cdd:PRK12476 445 G-RPEETERTFGakLQSRLAEGshadgaADDGTWLRTGDLGVYL-------DGE----LYITGRIADLIVIDGRNHYPQD 512
|
490
....*....|..
gi 1537992864 1463 IETSVIRAHKSV 1474
Cdd:PRK12476 513 IEATVAEASPMV 524
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
379-907 |
7.81e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 114.83 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 379 RPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPltrKDAG-SQQIGFLLGSCGVTVALTSDACHKGLPKSptgei 457
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP---AEPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKF----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 458 pqFKGWPKllwfvteskhlSKPPR-------------DWFPhiKDANNDT-AYIEYKTckdGSV---LGVTVTRIALLTH 520
Cdd:PRK07769 147 --FRARPA-----------KERPRviavdavpdevgaTWVP--PEANEDTiAYLQYTS---GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 521 CQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNmmHVISI--PYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHW 598
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 599 A--LVAHR-----DQRDVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEALTVAIRRPTDDSNQ 671
Cdd:PRK07769 286 AfeHAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 672 ppgrgvlsmhgltygVIRVDSEEkLSVLTVQDVGLVMPGAI-------------MCSVKPDGIPQLcRTDEIGELCVCAV 738
Cdd:PRK07769 364 ---------------VIYVDRDE-LNAGRFVEVPADAPNAVaqvsagkvgvsewAVIVDPETASEL-PDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 739 ATGTSYYGLSGMTKNTFE------VFPMTSSGAPiSEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVAT 812
Cdd:PRK07769 427 NIGTGYWGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 813 ALavEPMKFVYRGRIAVFSV-------TVLHD-------------ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQV 872
Cdd:PRK07769 505 AQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGV 582
|
570 580 590
....*....|....*....|....*....|....*
gi 1537992864 873 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSL 907
Cdd:PRK07769 583 TVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
980-1474 |
3.10e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 112.90 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 980 LQWRAQTTPDHLLYTLLNC---RGTIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAGC 1056
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDFsteRDGVARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1057 VPITVRPPHPQNIATTLPTVkmIVEVSRSACLMTT---QLICKLLRSREAAAAvdvrtwPLILDTDDLPKKRPAQIYKPS 1133
Cdd:PRK07769 105 IAVPLFDPAEPGHVGRLHAV--LDDCTPSAILTTTdsaEGVRKFFRARPAKER------PRVIAVDAVPDEVGATWVPPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1134 -NPDTLAYLDFSVSTTGMLAGVKMSH--AATSAF--CRSIKLQcelYPSREVAiCLDPYCGLGFVLWCLCSVYSGHQSIL 1208
Cdd:PRK07769 177 aNEDTIAYLQYTSGSTRIPAGVQITHlnLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1209 IPPSELEtNPALWLLAVSQyKVRDTFCSYSV-----MELCT-KGLGSQTESlkarGLDLSRVRtCVVVAEERPRIALTQS 1282
Cdd:PRK07769 253 SPAAFVR-RPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNGSEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1283 FSKLFKDLGLHPRAVSTSFGcrVNLAICLQGTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRII 1360
Cdd:PRK07769 326 FNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1361 IANPETKGPLGDSHLGEIWVHSAHNASGYftiYG--DESLQSDH--FNSRLSFGDTQ-----TIWARTGYLGflrrtelT 1431
Cdd:PRK07769 404 IVDPETASELPDGQIGEIWLHGNNIGTGY---WGkpEETAATFQniLKSRLSESHAEgapddALWVRTGDYG-------V 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1537992864 1432 DANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSV 1474
Cdd:PRK07769 474 YFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
976-1489 |
3.57e-25 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 111.99 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 976 LSEVLQWRAQTTPDHLLYTllncrgtIANSLTCV-----QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYG 1050
Cdd:cd05906 12 LLELLLRAAERGPTKGITY-------IDADGSEEfqsyqDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1051 CLYAGCVPITVRPPHP-QNIATTLPTVKMIVEVSRSA-CLMTTQLICKLLRSREAA--AAVDVRTWPLILDTDDLPKKRP 1126
Cdd:cd05906 84 CVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPvVLTDAELVAEFAGLETLSglPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1127 AQiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSiKLQCELYPSREVA---ICLDPYCGLGFVlwCLCSVYSG 1203
Cdd:cd05906 164 SR------PDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1204 HQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSvmeLCTKgLGSQTESLKARGLDLSRVRtCVVVAEERPRIALTQSF 1283
Cdd:cd05906 235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1284 SKLFKDLGLHPRAVSTSFG----CrvnlaiclqgtSGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKILPGVRI 1359
Cdd:cd05906 310 LRLLEPYGLPPDAIRPAFGmtetC-----------SG---VIYSRSFPTYDH----------SQALEFVSLGRPIPGVSM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1360 IIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaNGErhd 1439
Cdd:cd05906 366 RIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFLD-------NGN--- 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1537992864 1440 aLYVVGALDEAMELRGMRYHPIDIETSV----IRAHKSVTECAVF---TWTNLLVVV 1489
Cdd:cd05906 424 -LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRdpgAETEELAIF 479
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
962-1499 |
4.44e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 112.02 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 962 DNDQARKvRTEFLFLSEVLQWRAQTTPDHLLYTLlncRGTIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPG 1041
Cdd:PRK09192 10 TSSLPRR-YADFPTLVEALDYAALGEAGMNFYDR---RGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1042 IDLIAAFYGCLYAGCVPITVrpPHPQNI---ATTLPTVKMIVEVSRSACLMTTQLICKLLrsREAAAAVDVRtWPLILDT 1118
Cdd:PRK09192 85 GDFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLL-HVLSHAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1119 DDLPKKRPAQIYKPSnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQ-CELYPSREVAICLDPYCGLGFVlWCL 1197
Cdd:PRK09192 160 FKALPEADVALPRPT-PDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGLV-GFL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1198 CSVYSGHQSI-LIPPSELETNPALWLLAVSqyKVRDTFcSYSV---MELCTKGLGSQTESlkarGLDLSRVRTCVVVAEE 1273
Cdd:PRK09192 238 LTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGADM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1274 -RPRIalTQSFSKLFKDLGLHPRAVSTSFG-CRVNLAIclqgtSGPDPTTvyvDMRALRHDRVRLVERGspHSLPLMES- 1350
Cdd:PRK09192 311 iRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAV-----SFSPLGS---GIVVEEVDRDRLEYQG--KAVAPGAEt 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1351 ---------GKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESlqsdhfnsrlsfgDTQTI----WA 1417
Cdd:PRK09192 379 rrvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYF---RDEE-------------SQDVLaadgWL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1418 RTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSV-----IRAHksvtECAVFTWTN----LLVV 1488
Cdd:PRK09192 442 DTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqepeLRSG----DAAAFSIAQengeKIVL 506
|
570
....*....|.
gi 1537992864 1489 VVELDGSEQEA 1499
Cdd:PRK09192 507 LVQCRISDEER 517
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1010-1479 |
2.26e-24 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 107.74 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1010 QLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITvrPPHPQN-IATtlptvkmIVEVSRSA 1086
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAayVPLD--PAYPAErLAF-------ILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1087 CLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAqiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCR 1166
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1167 SIklqCELYPSREVAICLDpYCGLGF------VLWCLcsvYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVM 1240
Cdd:TIGR01733 151 WL---ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1241 ELCtkglgsqtesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLHpravstsfgcrvNlaiclqgTSGPDPT 1320
Cdd:TIGR01733 224 ALL----------AAALPPALASLRL-VILGGEALTPALVDRWRARGPGARLI------------N-------LYGPTET 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1321 TVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYFtiyGDESLQS 1400
Cdd:TIGR01733 274 TVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGYL---NRPELTA 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1537992864 1401 DHFNSRLSFGDTQTIWARTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1479
Cdd:TIGR01733 342 ERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
343-905 |
2.43e-24 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 109.11 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 343 NGKPLYIlTYGKLWTrsmkvayNILHKLGTKQEPMVRPGDRValVFPNNDPAAFMVAFYGCLLAEVVPVPievpltrkda 422
Cdd:cd05908 10 DKKEKFV-SYRHLRE-------EALGYLGALQELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVP---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 423 gsqqigfllgscgvtVALTSDACHKglpksptgeIPQFKGWPKLL--WFVTESKHLSKPPrdwfphikdanNDTAYIEYK 500
Cdd:cd05908 70 ---------------VSIGSNEEHK---------LKLNKVWNTLKnpYLITEEEVLCELA-----------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 501 TCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQK 580
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 581 VCQYKAKVACVKSRDMHWALVAHRDQR--DVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAl 658
Cdd:cd05908 195 ASEHKATIVSSPNFGYKYFLKTLKPEKanDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 659 TVAIRRPTDDSNQPPgrgvLSMH--GLTYG--VIRVDSEEKlSVLTVQDVGLVMPgaiMCSVK-PDGIPQLCRTDEIGEL 733
Cdd:cd05908 272 SVGASLPKAQSPFKT----ITLGrrHVTHGepEPEVDKKDS-ECLTFVEVGKPID---ETDIRiCDEDNKILPDGYIGHI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 734 CVCAVATGTSYYGLSGMTKNTfevfpMTSSGapiseypFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATA 813
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKV-----FTDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIA 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 814 LAVEPmkfVYRGRIAVFSV--TVLHDERIVIVAEQRpdsTEEDSFQWMSRVLQAID------SIHQVgvyclalVPANTL 885
Cdd:cd05908 411 EELEG---VELGRVVACGVnnSNTRNEEIFCFIEHR---KSEDDFYPLGKKIKKHLnkrggwQINEV-------LPIRRI 477
|
570 580
....*....|....*....|
gi 1537992864 886 PKTPLGGIHLSETKQLFLEG 905
Cdd:cd05908 478 PKTTSGKVKRYELAQRYQSG 497
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
324-800 |
7.60e-24 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 106.24 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 324 LQRWGTISPKAPCLTTMDTngkplYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGC 403
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG-----RRLTYRELDERANRLA-AGLRALG------VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 404 LLAEVVPVPIEVpltrkDAGSQQIGFLLGSCGVTVALTSD--------ACHKGLPKSPTGEIPQFKGWPKLLWFVTESKH 475
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 476 LSKPPRdwfPHIKDANNDTAYIEY--------KtckdgsvlGVTVTRIALLTHCQALTQAC----GYTEAETIVNVLDFK 543
Cdd:pfam00501 142 ADVPPP---PPPPPDPDDLAYIIYtsgttgkpK--------GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 544 KDVGLWHGILTSVMNMMHVISIPYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHwALVAHRDQRDVNLSSLRMLIVadGA 623
Cdd:pfam00501 211 HDFGLSLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERYKVTVLYGVPTLLN-MLLEAGAPKRALLSSLRLVLS--GG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 624 NPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptddsnqppGRGVLSMHGLT--YGVIRVDSEEKLSVLTV 701
Cdd:pfam00501 287 APLPPELARRFRELF-----------------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 702 QDVGLVMPGAIMCSVKPDGIpQLCRTDEIGELCV--CAVATGtsYYGLSGMTKNTFEvfpmtssgapisEYPFIRTGLLG 779
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCVrgPGVMKG--YLNDPELTAEAFD------------EDGWYRTGDLG 396
|
490 500
....*....|....*....|.
gi 1537992864 780 FVGPGGLVFVVGKMDGLMVVS 800
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
319-893 |
4.59e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 105.79 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 319 SLEAALQRWGTISPKAPCLTTMDTNGKPLYI---LTYGKLWTRSMKVAYNiLHKLGtkqepmvRPGDRVALVFPNNdpAA 395
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIDYEQDPAGVaetLTWSQLYRRTLNVAEE-LRRHG-------STGDRAVILAPQG--LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 396 FMVAFYGCLLAEVVPVPIEVPLTRkdAGSQQIGFLLGSCGVTVALTS----DACHKGLPKSPTGEIPqfkgwpkllWFVT 471
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQSAP---------PVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 472 ------ESKHLSKPPRDWFPhikdannDTAYIEYKTCKDGSVLGVTVTRIALLTHC-QALTQACGYTEAE-----TIVNV 539
Cdd:PRK05850 141 vdlldlDSPRGSDARPRDLP-------STAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 540 LDFKKDVGLWHGILTSVMNMMH-VISIPYSLMKvNPLSWIQKVCQYKAKVACVKSrdmhWAL-VAHRDQRDVNLSSL--- 614
Cdd:PRK05850 214 LPFYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQLLASNPHAFSAAPN----FAFeLAVRKTSDDDMAGLdlg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 615 RMLIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIRRPtddsNQPPGrgvlsmhgltygVIRVDSE 693
Cdd:PRK05850 289 GVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP----GQPPE------------SVRFDYE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 694 eKLSVLTVQ----DVG--LVMPGAIMCS----VKPDGIPQlCRTDEIGELCVCA--VATGtsYYGLSGMTKNTFE---VF 758
Cdd:PRK05850 353 -KLSAGHAKrcetGGGtpLVSYGSPRSPtvriVDPDTCIE-CPAGTVGEIWVHGdnVAAG--YWQKPEETERTFGatlVD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 759 PmtSSGAPISeyPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalavepMKFVYRGRIAVFSVTVLHDE 838
Cdd:PRK05850 429 P--SPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTE 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 839 RIVIVAE-QRPDSTEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 893
Cdd:PRK05850 498 KLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1000-1480 |
1.02e-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: 103.83 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1000 GTIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCvpitvrPPHPQNIATTLPTVKMI 1079
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1080 VEVSRSACLMTTQliCKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSN--------------PDTLAYLDFSV 1145
Cdd:cd05911 78 LKISKPKVIFTDP--DGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLgeededlppplkdgKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1146 STTGMLAGVKMSHaatSAFCRSIKLQC----ELYPSREVAICLDPY---CGLgfvLWCLCSVYSGHQSILIPpselETNP 1218
Cdd:cd05911 156 GTTGLPKGVCLSH---RNLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMP----KFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1219 ALWLLAVSQYKVRDTFCSYSVMELctkgLGSQTESLKArglDLSRVRTCVVVAEerpriALTQSFSKLFKdlglhpravs 1298
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGGA-----PLSKELQELLA---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1299 tsfgCRVNLAICLQG-----TSGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVRIIIANPETKGPLGDS 1373
Cdd:cd05911 284 ----KRFPNATIKQGygmteTGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKDSLGPN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1374 HLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMEL 1453
Cdd:cd05911 341 EPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYF------DEDGY----LYIVDRKKELIKY 399
|
490 500
....*....|....*....|....*..
gi 1537992864 1454 RGMRYHPIDIEtSVIRAHKSVTECAVF 1480
Cdd:cd05911 400 KGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
341-909 |
1.63e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 104.44 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 341 DTNGKPLYiLTYGKLWTRsmkvayniLHKLGTKQEPMVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPI---EVPl 417
Cdd:PRK12476 61 SAAGCAVE-LTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfapELP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 418 trkdAGSQQIGFLLGSCGVTVALTSDAChkglpkspTGEIPQFkgwpkllwfvteskhLSKPPRDWFPH------IKDA- 490
Cdd:PRK12476 129 ----GHAERLDTALRDAEPTVVLTTTAA--------AEAVEGF---------------LRNLPRLRRPRviaidaIPDSa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 491 ----------NNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETI-VNVLDFKKDVGLWHGILTSVMNM 559
Cdd:PRK12476 182 gesfvpveldTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 560 MHVISIPYSLMKvNPLSWIQKV---CQYKAKVACVKSRDMHWAlvAHR----DQRDVNLSSLRMLIvadGANPWSISSCD 632
Cdd:PRK12476 262 HSTLMSPTAFVR-RPQRWIKALsegSRTGRVVTAAPNFAYEWA--AQRglpaEGDDIDLSNVVLII---GSEPVSIDAVT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 633 AFLNVFQSKGLRQEVICPCASSPEA-LTVAirrpTDDSNQPPGRGVLSMHGLTYG-VIRVDSEEKLSVLTVQdVGLVMPG 710
Cdd:PRK12476 336 TFNKAFAPYGLPRTAFKPSYGIAEAtLFVA----TIAPDAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 711 AIMCSVKPDGIPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFEV-----FPMTS--SGAPISEyPFIRTGLLGFVGP 783
Cdd:PRK12476 411 QWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDG-TWLRTGDLGVYLD 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 784 GGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVL 863
Cdd:PRK12476 489 GEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1537992864 864 QAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 909
Cdd:PRK12476 566 AAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1003-1482 |
3.32e-21 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 99.37 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1003 ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPItvrpphPQNIATTLPTVKMIVEV 1082
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1083 SRSACLMTTQLICKLLRSREAAAAVDVRT----------WPLILDTDDLPKKRPAQIYKPSNPDTLAYLDFSVSTTGMLA 1152
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1153 GVKMSHAatsafcrSIKLQCELYPSREVAICLDPYC----------GLGFVLWCLCSVysGHQSILIPpsELETnPALWL 1222
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP--ERPT-PAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1223 LAVSQYKvRDTFcsYSVMELCTKGLGSqtESLKARglDLSRVRTCVVVAEerpriALTQSFSKLFKDLglhpravstsFG 1302
Cdd:cd05959 248 KRIRRYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGE-----ALPAEVGERWKAR----------FG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1303 CRVnlaicLQGTSGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHS 1382
Cdd:cd05959 306 LDI-----LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELYVRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1383 AHNASGYFTIYGDeslqsdhfnSRLSFgdtQTIWARTGYlGFLRrteltDANGerhdALYVVGALDEAMELRGMRYHPID 1462
Cdd:cd05959 366 PSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLKVSGIWVSPFE 423
|
490 500
....*....|....*....|
gi 1537992864 1463 IEtSVIRAHKSVTECAVFTW 1482
Cdd:cd05959 424 VE-SALVQHPAVLEAAVVGV 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1005-1502 |
1.49e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 90.28 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1005 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSR 1084
Cdd:cd05930 12 SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE------RLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1085 SACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1164
Cdd:cd05930 85 AKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1165 CRSIKlqcELYP--SREVAICLDPYcglGF------VLWCLCSvysGHQsILIPPSELETNPALWLLAVSQYKVRDTFCS 1236
Cdd:cd05930 122 LLWMQ---EAYPltPGDRVLQFTSF---SFdvsvweIFGALLA---GAT-LVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1237 YSVMELCTKGLGSQteslkarglDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLhpravstsfgcrVNLaiclqgtSG 1316
Cdd:cd05930 192 PSLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1317 PDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDE 1396
Cdd:cd05930 243 PTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---LNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1397 SLQSDHFNSrLSFGDTQTIWaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTE 1476
Cdd:cd05930 310 ELTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLAHPGVRE 376
|
490 500 510
....*....|....*....|....*....|..
gi 1537992864 1477 CAVFTWTN------LLVVVVELDGSEQEALDL 1502
Cdd:cd05930 377 AAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
317-937 |
1.66e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.38 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 317 PPSLEAALQRWGTISPKAPCLTTMDTNGKPLYILTYGKLWTRSMKVAYNIlhklgtkqEPMVRPGDRVALVFPNNdpAAF 396
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 397 MVAFYGCLLAEVVPVPIEVPLTRKDAGSQQIGFLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkGWPKLLwfvTESKHL 476
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPELL---CVDTLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 477 SKPPRDWF-PHIKDanNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACG--YTEAETIVNVLDFKKDVGLWHGIL 553
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 554 TSVMNmmhviSIPYSLMKVN-----PLSWIQKVCQYKAKVAcvKSRDMHWALVAHRdQRDVNLSSL---RMLIVADGANP 625
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 626 WSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAirrptddsNQPPGRGVlsmhgltyGVIRVDSE-------EKLS 697
Cdd:PRK05691 302 IRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS--------GGRRGQGI--------PALELDAEalarnraEPGT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 698 VLTVQDVGLVMPGAIMCSVKPDGIPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFevfpMTSSGApiseyPFIRTGL 777
Cdd:PRK05691 366 GSVLMSCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 778 LGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalAVEPMKFVYRGRIAVFSVTVLHDERIVIVAE-----QRPDSTE 852
Cdd:PRK05691 436 LGFLRDGEL-FVTGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 853 EdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLhpcnvlmcphTCVTNLPKPRQKQPE 932
Cdd:PRK05691 513 A----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAA 578
|
....*
gi 1537992864 933 IGPAS 937
Cdd:PRK05691 579 QTAAS 583
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1010-1479 |
8.89e-15 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 79.04 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1010 QLHKRAEKIAVMLMERGhlqDGDHVALVYPPGIDLIAAFYGCLYAG----CVPITVRPPHPQNIA-TTLptvkmivevSR 1084
Cdd:PRK05851 36 EVHGRAENVAARLLDRD---RPGAVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWAdATL---------TR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1085 SACLMTTQLIC-----KLLRSREAAAAV-DVRTWPlildtddlpKKRPAQIYKPSNPDTLAYLDFSVSTTGMLAGVKMSH 1158
Cdd:PRK05851 104 FAGIGVRTVLShgshlERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1159 AATSAFCRSIKLQCELYPSREVAICLDPY---CGLGFVLwclCSVYSGHQSILIPPSELETNPALWLLAVSQykVRDTFC 1235
Cdd:PRK05851 175 GAVLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSD--SRATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1236 SYSVMELCTKGLGSQteslKARGLDLSRVRTCVVVAEerP-RIALTQSFSKLFKDLGLHPRAVSTSFGcrvnLAICLQGT 1314
Cdd:PRK05851 250 AAPNFAYNLIGKYAR----RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG----LAESTCAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1315 SGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYFtiyG 1394
Cdd:PRK05851 320 TVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYL---G 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1395 DESLQSDHfnsrlsfgdtqtiWARTGYLGFlrrteLTDangerhDALYVVGALDEAMELRGMRYHPIDIETSVIRAhKSV 1474
Cdd:PRK05851 389 QAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGV 443
|
....*
gi 1537992864 1475 TECAV 1479
Cdd:PRK05851 444 REGAV 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1134-1464 |
1.21e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 75.60 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1134 NPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSE 1213
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1214 LETNPALWLLAVSQYKVRDTFCSysvmELCTKGLGSQTESLKARGLDLSRVRTCVVVAEErprIA--LTQSFSKLFKDLG 1291
Cdd:cd05908 184 FIRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1292 LHPRAVSTSFGcrvnLAICLQGTSGPDP----TTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVRIIIANPET 1366
Cdd:cd05908 257 LKRNAILPVYG----LAEASVGASLPKAqspfKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1367 KGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGA 1446
Cdd:cd05908 333 KI-LPDGYIGHIQIRGKNVTPGY---YNNPEATAKVF--------TDDGWLKTGDLGFIR-------NGR----LVITGR 389
|
330
....*....|....*...
gi 1537992864 1447 LDEAMELRGMRYHPIDIE 1464
Cdd:cd05908 390 EKDIIFVNGQNVYPHDIE 407
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1005-1479 |
3.78e-13 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 73.81 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1005 SLTCVQLHKRAEKIAVMLMERGHLQdGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqniATTLPTVKMIVEVSR 1084
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1085 SACLMTT-QLICKLlrsreAAAAVDVrtwpLILDTDD---LPKKRPAQIYKPSNP-------DTLAYLDFSVSTTGMLAG 1153
Cdd:cd05904 105 AKLAFTTaELAEKL-----ASLALPV----VLLDSAEfdsLSFSDLLFEADEAEPpvvvikqDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1154 VKMSH----AATSAFCRSIKLQCElypSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPSELETnpalWLLAVSQY 1228
Cdd:cd05904 176 VMLTHrnliAMVAQFVAGEGSNSD---SEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1229 KVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPRiALTQSFSKLFKDlglhpravstsfgcrVNLa 1308
Cdd:cd05904 249 KVTHLPVVPPIVLALVK-------SPIVDKYDLSSLRQIMSGAAPLGK-ELIEAFRAKFPN---------------VDL- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1309 icLQG----TSGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAH 1384
Cdd:cd05904 305 --GQGygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1385 NASGYFtiyGDESlqsdhfnsrlsfgDTQ-TI----WARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYH 1459
Cdd:cd05904 368 IMKGYL---NNPE-------------ATAaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVA 421
|
490 500
....*....|....*....|
gi 1537992864 1460 PIDIEtSVIRAHKSVTECAV 1479
Cdd:cd05904 422 PAELE-ALLLSHPEILDAAV 440
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
976-1479 |
1.59e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 71.83 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 976 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:cd05936 1 LADLLEEAARRFPDK---TALIFMGR---KLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1056 CVPITVRPphpqniattlptvkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWplildTDDLPKKRPAQIYKPSNP 1135
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1136 DTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsIKLQC-----ELYPSREVAICLDP-YCGLGFVLWCLCSVYSGHQSILI 1209
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1210 P-PSeletnPALWLLAVSQYKVrDTFCS----YSVMelctkglgsqTESLKARGLDLSRVRTCVvvaeerprialtqsfs 1284
Cdd:cd05936 201 PrFR-----PIGVLKEIRKHRV-TIFPGvptmYIAL----------LNAPEFKKRDFSSLRLCI---------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1285 klfkdlglhpravstsfgcrvnlaiclqgtSGPDPTTVYVDMRALRHDRVRLVErG------SP--HSLPLMES------ 1350
Cdd:cd05936 249 ------------------------------SGGAPLPVEVAERFEELTGVPIVE-GygltetSPvvAVNPLDGPrkpgsi 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1351 GKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSrlsfGdtqtiWARTGYLGFLrrtel 1430
Cdd:cd05936 298 GIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGY---WNRPEETAEAFVD----G-----WLRTGDIGYM----- 359
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1537992864 1431 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1479
Cdd:cd05936 360 -DEDGY----FFIVDRKKDMIIVGGFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
379-891 |
3.07e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 70.93 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 379 RPGDRVALVFPNNDPA---AFMVAFYGCLLAEVVpvpieVPLTrKDAGSQQIGFLLGSCGVTVALTS----DACHKGLPK 451
Cdd:cd05922 16 VRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADagaaDRLRDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 452 SPTGEipqfkgwpklLWFVTESKHLSKPPRDWFPHIKDannDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYT 531
Cdd:cd05922 90 SPDPG----------TVLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 532 EAETIVNVLDFKKDVGLwhgiltSVMNMmH-------VISIPYSLmkvnPLSWIQKVCQYKAK-VACVKSrdmHWALVAH 603
Cdd:cd05922 157 ADDRALTVLPLSYDYGL------SVLNT-HllrgatlVLTNDGVL----DDAFWEDLREHGATgLAGVPS---TYAMLTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 604 RDQRDVNLSSLRMLIVADGANPwsisscDAFLNVFQSKGlrqevicpcasspealtvairrptddsnqpPGRGVLSMHGL 683
Cdd:cd05922 223 LGFDPAKLPSLRYLTQAGGRLP------QETIARLRELL------------------------------PGAQVYVMYGQ 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 684 TYGVIR---VDSEEKLSVLTvqDVGLVMPGAIMCSVKPDGipQLCRTDEIGELcvcaVATGTSYYgLSGMTKNTFEVFPM 760
Cdd:cd05922 267 TEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDG--TPTPPGEPGEI----VHRGPNVM-KGYWNDPPYRRKEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 761 TSSGApiseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDERI 840
Cdd:cd05922 338 RGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKL 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1537992864 841 VIVAEqRPDSTEEDSfqwMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 891
Cdd:cd05922 406 ALFVT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
984-1505 |
4.49e-12 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 70.35 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 984 AQTTPDHLLYTllnCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITV 1061
Cdd:cd05945 1 AAANPDRPAVV---EGGR---TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1062 RPPHPQniattlptVKMIVEVSRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYL 1141
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIAD-------------------------------------------GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1142 DFSVSTTGMLAGVKMSHAATSAFCRSIkLQCELYPSREVAICLDPYcglGF---VLWCLCSVYSGhQSILIPPSELETNP 1218
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPF---SFdlsVMDLYPALASG-ATLVPVPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1219 ALWLLAVSQYKVRDTFCSYSVMELCTkGLGSQTESLkargldLSRVRTCVVVAEERPrIALTQSFSKLFkdlglhPravs 1298
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPES------LPSLRHFLFCGEVLP-HKTARALQQRF------P---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1299 tsfGCRV-NlaiclqgTSGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVRIIIANPETKgPLGDSHLGE 1377
Cdd:cd05945 240 ---DARIyN-------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILDEDGR-PVPPGEKGE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1378 IWVHSAHNASGYFtiyGDEslqsDHFNSRLSFGDTQTiWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMR 1457
Cdd:cd05945 301 LVISGPSVSKGYL---NNP----EKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRLDFQVKLNGYR 362
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1537992864 1458 YHPIDIETSViRAHKSVTECAVFTWTNL-----LVVVVELDGSEqEALDLVPL 1505
Cdd:cd05945 363 IELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
984-1479 |
1.52e-11 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 68.91 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 984 AQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG--CVPITV 1061
Cdd:cd17651 5 AARTPDA---PALVAEGR---RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1062 RPPhPQNIAttlptvkMIVEVSRSACLMTTQlickllrsREAAAAVDVRTWPLILDTDDLPKKRPAQIYKPSNPDTLAYL 1141
Cdd:cd17651 78 AYP-AERLA-------FMLADAGPVLVLTHP--------ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1142 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF--VLWCLCSVYSGHQSILIPPSELETNPA 1219
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTL----QFAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1220 LWLLAVSQYKVRDTFCSYSVME-LCtkglgsqtESLKARGLDLSRVRtCVVVAEERPRIAltqsfsklfkdlGLHPRAVS 1298
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGEQLVLT------------EDLREFCA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1299 TSFGCRvnlaicLQGTSGPDPTTVyVDMRALRHDRVRlveRGSPHSLplmesGKILPGVRIIIANPETKgPLGDSHLGEI 1378
Cdd:cd17651 277 GLPGLR------LHNHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLDAALR-PVPPGVPGEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1379 WVHSAHNASGYFTIYG--DESLQSDHF--NSRLSfgdtqtiwaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELR 1454
Cdd:cd17651 341 YIGGAGLARGYLNRPEltAERFVPDPFvpGARMY---------RTGDLA--RW----LPDGE----LEFLGRADDQVKIR 401
|
490 500
....*....|....*....|....*
gi 1537992864 1455 GMRYHPIDIEtSVIRAHKSVTECAV 1479
Cdd:cd17651 402 GFRIELGEIE-AALARHPGVREAVV 425
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
982-1479 |
3.48e-11 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 67.69 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 982 WRAQT--TPDH--LLYTllncrgtiANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1057
Cdd:cd17646 4 VAEQAarTPDApaVVDE--------GRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1058 PITVRPPHPQniattlPTVKMIVEVSRSACLMTTQlickllRSREAAAAVDVRTWPLILDTDDLPKKRPAQiykPSNPDT 1137
Cdd:cd17646 75 YLPLDPGYPA------DRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLV---PPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1138 LAYLDFSVSTTGMLAGVKMSHAatsAFCRSIKLQCELYP--SREVAICLDPycgLGF------VLWCLCsvySGhQSILI 1209
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPlgPGDRVLQKTP---LSFdvsvweLFWPLV---AG-ARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1210 PPSELETNPALWLLAVSQYKVrdTFCSY--SVMELCtkglgsqteslkargLDLSRVRTC-----VVVAEErpriALTQS 1282
Cdd:cd17646 210 ARPGGHRDPAYLAALIREHGV--TTCHFvpSMLRVF---------------LAEPAAGSCaslrrVFCSGE----ALPPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1283 FSKLFKDLglhpravstsFGCR-VNLaiclqgtSGPDPTTVYVDmralrHDRVRlvERGSPHSLPLmesGKILPGVRIII 1361
Cdd:cd17646 269 LAARFLAL----------PGAElHNL-------YGPTEAAIDVT-----HWPVR--GPAETPSVPI---GRPVPNTRLYV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1362 ANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHF-------NSRLSfgdtqtiwaRTGYLGflRRTeltdAN 1434
Cdd:cd17646 322 LDDALR-PVPVGVPGELYLGGVQLARGY---LGRPALTAERFvpdpfgpGSRMY---------RTGDLA--RWR----PD 382
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1537992864 1435 GErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAV 1479
Cdd:cd17646 383 GA----LEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVV 422
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
983-1502 |
4.95e-11 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 67.96 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 983 RAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPIT 1060
Cdd:COG1020 485 QAARTPDA---VAVVFGDQ---SLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVPLD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1061 vrPPHPQN-IAttlptvkMIVEVSRSACLMTTQlickLLRSREAAAAVDVrtwpLILDTDDLPKKRPAQIYKPSNPDTLA 1139
Cdd:COG1020 558 --PAYPAErLA-------YMLEDAGARLVLTQS----ALAARLPELGVPV----LALDALALAAEPATNPPVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1140 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF------VLWCLCsvySGHQSILIPPsE 1213
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSFdasvweIFGALL---SGATLVLAPP-E 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1214 LETNPALWLLAVSQYKVrdtfcsySVMELcTKGLGSQTesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLGLH 1293
Cdd:COG1020 693 ARRDPAALAELLARHRV-------TVLNL-TPSLLRAL--LDAAPEALPSLRL-VLVGGEALPPELVRRWRARLPGARLV 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1294 pravstsfgcrvNLaiclqgtSGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVRIIIAnpetkgplgDS 1373
Cdd:COG1020 762 ------------NL-------YGPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL---------DA 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1374 HL--------GEIWVHSAHNASGYFtiyGDESLQSDHF--NsrlSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYV 1443
Cdd:COG1020 805 HLqpvpvgvpGELYIGGAGLARGYL---NRPELTAERFvaD---PFGFPGARLYRTGDLA--RWL----PDGN----LEF 868
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1537992864 1444 VGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVFTWTN-----LLVVVVELDGSEQEALDL 1502
Cdd:COG1020 869 LGRADDQVKIRGFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAAL 931
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
509-893 |
2.94e-10 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 63.84 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 509 GVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV 588
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 589 ACVkSRDMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptdd 668
Cdd:cd04433 92 LLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP------------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 669 snqppGRGVLSMHGLT-----YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGIPqlCRTDEIGELCVcavatgTS 743
Cdd:cd04433 139 -----GIKLVNGYGLTetggtVATGPPDDDARKPG----SVGRPVPGVEVRIVDPDGGE--LPPGEIGELVV------RG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 744 YYGLSGMTKNTFEVFPMTSSGapiseypFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvy 823
Cdd:cd04433 202 PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA--- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1537992864 824 rgRIAVFSVTvlhDER------IVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 893
Cdd:cd04433 272 --EAAVVGVP---DPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1005-1230 |
7.87e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 63.06 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1005 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPhPQNIATtlptvkmIVEV 1082
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARREA-------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1083 SRSACLMTTQLICKLLRSREAAAAVDvrtwpliLDTDDLPKKRPAQiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1162
Cdd:cd12114 83 AGARLVLTDGPDAQLDVAVFDVLILD-------LDALAAPAPPPPV---DVAPDDLAYVIFTSGSTGTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1537992864 1163 AFCRSIKLQCELYPSREVaICLDPycgLGFVLwclcSVY------SGHQSILIPPSELETNPALWLLAVSQYKV 1230
Cdd:cd12114 153 NTILDINRRFAVGPDDRV-LALSS---LSFDL----SVYdifgalSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
510-902 |
8.06e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.48 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 510 VTVTRIALLTHCQALTQACGYT-EAETIVNVLDFKKDVGLWhGILTSVMNM-MHVISI-PYSLMkVNPLSWIQKVCQYKA 586
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMV-GFLTVPMYFgAELVKVtPMDFL-RDPLLWAELISKYRG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 587 KVACvkSRDMHWALVAHR-----DQRDVNLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVA 661
Cdd:PRK07768 248 TMTA--APNFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEA-TLA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 662 IrrptddSNQPPGRGvlsmhgLTYGVIRVD--SEEKLSVLTVQD-------VGLVMPGAIMCSVKPDGipQLCRTDEIGE 732
Cdd:PRK07768 323 V------SFSPCGAG------LVVDEVDADllAALRRAVPATKGntrrlatLGPPLPGLEVRVVDEDG--QVLPPRGVGV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 733 LCVCAVATgTSYYglsgmtkntfevfpMTSSG--APISEYPFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIV 810
Cdd:PRK07768 389 IELRGESV-TPGY--------------LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 811 ATALAVEPmkfVYRGRIAVFSVTVLHD-ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPK 887
Cdd:PRK07768 454 RAAARVEG---VRPGNAVAVRLDAGHSrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPK 528
|
410
....*....|....*
gi 1537992864 888 TPLGGIHLSETKQLF 902
Cdd:PRK07768 529 TPSGKLRRANAAELV 543
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
980-1500 |
2.90e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 61.45 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 980 LQWRAQTTPDHLLYTLLNCRGTIAN----SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADGKlaydELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1056 CVPITVRP-------------PHPQ--------NIATTL-----PTVKMIVEVSRSACLMTTQLickllrsreaaaavdv 1109
Cdd:PRK09274 91 AVPVLVDPgmgiknlkqclaeAQPDafigipkaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTL---------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1110 rtwplildtDDLPKKRPAQIYKP--SNPDTLAYLDFSVSTTGMLAGVKMSHaatSAFCRSIKLQCELYPSR--EVAIC-- 1183
Cdd:PRK09274 155 ---------ATLLRDGAAAPFPMadLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQIEALREDYGIEpgEIDLPtf 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1184 -----LDPYCGlgfvlwcLCSVysghqsilIPPSEL----ETNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSL 1254
Cdd:PRK09274 223 plfalFGPALG-------MTSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1255 KARGLDLSRVRTcVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLqgtsgpdpttvyVDMRALRHDR 1333
Cdd:PRK09274 281 EANGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFAT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1334 VRLVERGSPHSLplmesGKILPGVRI-IIA---NP-----ETKgPLGDSHLGEIWVHSAHNASGYFtiygdeslQSDHFN 1404
Cdd:PRK09274 343 RAATDNGAGICV-----GRPVDGVEVrIIAisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYY--------NRPEAT 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1405 --SRLSFGDTQtIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAvftw 1482
Cdd:PRK09274 409 rlAKIPDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA---- 472
|
570
....*....|....*...
gi 1537992864 1483 tnllVVVVELDGSEQEAL 1500
Cdd:PRK09274 473 ----LVGVGVPGAQRPVL 486
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1005-1496 |
7.30e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 60.00 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1005 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSR 1084
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1085 SACLMTTQlickllrSREAAAAVDVRTWPLILDTDDLPkkrPAQIYKPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1164
Cdd:cd12116 85 PALVLTDD-------ALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1165 CRSIklqcelypsREvaicldpycglgfvlwclcsvysghqsilippsELETNPALWLLAVSQYkvrdTFcSYSVMEL-- 1242
Cdd:cd12116 155 LHSM---------RE---------------------------------RLGLGPGDRLLAVTTY----AF-DISLLELll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1243 ----------CTKGLGSQTESLKARgldLSRVRTCVVVAeerprialTQSFSKLFKDLGLHPRAvstsfGCRV------- 1305
Cdd:cd12116 188 pllagarvviAPRETQRDPEALARL---IEAHSITVMQA--------TPATWRMLLDAGWQGRA-----GLTAlcggeal 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1306 --NLAICLQGTS-------GPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLG 1376
Cdd:cd12116 252 ppDLAARLLSRVgslwnlyGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVLDAALR-PVPPGVPG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1377 EIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWARTGYLgfLRRteltDANGErhdaLYVVGALDEAMELRGM 1456
Cdd:cd12116 319 ELYIGGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR----RADGR----LEYLGRADGQVKIRGH 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1537992864 1457 RYHPIDIETsVIRAHKSVTECAVFTWTN----LLVVVVELDGSE 1496
Cdd:cd12116 385 RIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1006-1504 |
2.60e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1006 LTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRS 1085
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPE-VLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1086 ACLMTTQLICKLLRSREAAAAVDV---RTWplildtDDLPKKRPAqiyKPSNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1162
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDGLASLALdrdEDW------EGFPAHDPA---VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV 4720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1163 AFCRSIKLQCELYPSREVaICLDPYCGLGFVL---WCLCSvysgHQSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSV 1239
Cdd:PRK12316 4721 NHLHATGERYELTPDDRV-LQFMSFSFDGSHEglyHPLIN----GASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1240 MELCTKGlgsqteslKARGLDLSRVRTCVVVAEERPRIALTQSFSKLfKDLGLHpravstsfgcrvnlaiclqGTSGPDP 1319
Cdd:PRK12316 4795 LQQLAEH--------AERDGEPPSLRVYCFGGEAVAQASYDLAWRAL-KPVYLF-------------------NGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1320 TTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVRIII----ANPETKGPLGDSHLGEIWVhsahnASGYFTiygD 1395
Cdd:PRK12316 4847 TTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVldgqLNPLPVGVAGELYLGGEGV-----ARGYLE---R 4910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1396 ESLQSDHFNSRlSFGDTQTIWARTGYLGFLRRTELTDangerhdalyVVGALDEAMELRGMRYHPIDIETSvIRAHKSVT 1475
Cdd:PRK12316 4911 PALTAERFVPD-PFGAPGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEAR-LREHPAVR 4978
|
490 500
....*....|....*....|....*....
gi 1537992864 1476 ECavftwtnlLVVVVELDGSEQEALDLVP 1504
Cdd:PRK12316 4979 EA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1005-1479 |
2.68e-08 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 58.09 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1005 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPHPQNIAttlptvkmIVEV 1082
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERIAF--------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1083 SRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnPDTLAYLDFSVSTTGMLAGVKMSHAATS 1162
Cdd:cd17643 83 SGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1163 AFCRSIKLQCELYPSREVAICldPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAVSQYKVrdtfcsySVMel 1242
Cdd:cd17643 120 ALFAATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV-------TVL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1243 ctkglgSQT--------ESLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDlgLHPRAvstsfgcrVNLaiclqgt 1314
Cdd:cd17643 189 ------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1315 SGPDPTTVYVDMRALRHDRVRLVErGSPhslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyG 1394
Cdd:cd17643 245 YGITETTVHVTFRPLDAADLPAAA-ASP-------IGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYL---G 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1395 DESLQSDHFNSrLSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSV 1474
Cdd:cd17643 313 RPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE-AALATHPSV 380
|
....*
gi 1537992864 1475 TECAV 1479
Cdd:cd17643 381 RDAAV 385
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
313-623 |
4.71e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 57.61 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 313 VTNWPPSLEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNd 392
Cdd:PRK07656 4 WMTLPELLARAARRF----GDKEAYVFGDQR------LTYAELNARVRRAA-AALAALG------IGKGDRVAIWAPNS- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 393 pAAFMVAFYGCLLAEVVPVPIEvplTRKDAGsqQIGFLLGSCGVTVALTSD-------ACHKGLPK----------SPTG 455
Cdd:PRK07656 66 -PHWVIAALGALKAGAVVVPLN---TRYTAD--EAAYILARGDAKALFVLGlflgvdySATTRLPAlehvviceteEDDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 456 EIPQFKGWPKLLwfvteskhLSKPPRDWFPHIKDanNDTAYIEYKTCKDGSVLGVtvtriaLLTHCQALTQA------CG 529
Cdd:PRK07656 140 HTEKMKTFTDFL--------AAGDPAERAPEVDP--DDVADILFTSGTTGRPKGA------MLTHRQLLSNAadwaeyLG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 530 YTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV-ACVKSrdMHWALVAHRDQRD 608
Cdd:PRK07656 204 LTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERITVlPGPPT--MYNSLLQHPDRSA 277
|
330
....*....|....*
gi 1537992864 609 VNLSSLRmLIVADGA 623
Cdd:PRK07656 278 EDLSSLR-LAVTGAA 291
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
980-1503 |
6.32e-08 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 56.85 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 980 LQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPi 1059
Cdd:cd17631 1 LRRRARRHPDR---TALVFGGR---SLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVF- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1060 tvrppHPQNIATTLPTVKMIVEVSRSACLMttqlickllrsreaaaavdvrtwplildtddlpkkrpaqiykpsnpDTLA 1139
Cdd:cd17631 73 -----VPLNFRLTPPEVAYILADSGAKVLF----------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1140 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELyPSREVAICLDPYC---GLGfvLWCLCSVYSGHQSILIPpselET 1216
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILR----KF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1217 NPALWLLAVSQYKVRDTFCSYSVME-LCTKGlgsqteslKARGLDLSRVRtCVVVAEERPRIALTQSFsklfKDLGLhpr 1295
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1296 AVSTSFGcrvnlaiclQGTSGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVRIIIANPETKgPLGDSHL 1375
Cdd:cd17631 239 KFVQGYG---------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR-EVPPGEV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1376 GEIWVHSAHNASGYftiYGDESLQSDhfnsrlSFGDTqtiWARTGYLGFLrrteltDANGerhdALYVVGALDEAMELRG 1455
Cdd:cd17631 293 GEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRKKDMIISGG 350
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1537992864 1456 MRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLV-VVVELDGSEQEALDLV 1503
Cdd:cd17631 351 ENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
351-801 |
8.51e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 56.73 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 351 TYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGCLLAEVVPVPIEVPLTrkdagSQQIGFL 430
Cdd:PRK06187 33 TYAELDERVNRLA-NALRALG------VKKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 431 LGSCGVTVALTSDAcHKGLPKSPTGEIPQFKGW--------PKLLWFVTESKHL--SKPPRDWFPHIKDanNDTAYIEYK 500
Cdd:PRK06187 99 LNDAEDRVVLVDSE-FVPLLAAILPQLPTVRTVivegdgpaAPLAPEVGEYEELlaAASDTFDFPDIDE--NDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 501 TCKDGSVLGVTVTRIALLTHCQALTQACGYTEaetivnvldfkKDVGLwhgiltSVMNMMHV--ISIPY-SLM------- 570
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR-----------DDVYL------VIVPMFHVhaWGLPYlALMagakqvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 571 --KVNPlswiQKVCQY--KAKV---ACVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLNVFqskgl 643
Cdd:PRK06187 239 prRFDP----ENLLDLieTERVtffFAVPT--IWQMLLKAPRAYFVDFSSLRLVIY--GGAALPPALLREFKEKF----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 644 rqevicpcasspealtvairrptddsnqppGRGVLSMHGL--TYGVIRVD--SEEKLSVLTVQ-DVGLVMPG---AImcs 715
Cdd:PRK06187 306 ------------------------------GIDLVQGYGMteTSPVVSVLppEDQLPGQWTKRrSAGRPLPGveaRI--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 716 VKPDGIPQLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEvfpmtsSGapiseypFIRTGLLGFVGPGGLVFVVGKMDG 795
Cdd:PRK06187 353 VDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------GG-------WLHTGDVGYIDEDGYLYITDRIKD 419
|
....*.
gi 1537992864 796 lMVVSG 801
Cdd:PRK06187 420 -VIISG 424
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
320-459 |
9.89e-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: 56.42 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 320 LEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVA 399
Cdd:cd05936 5 LEEAARRF----PDKTALIFMGRK------LTYRELDALAEAFA-AGLQNLG------VQPGDRVALMLPNC--PQFPIA 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1537992864 400 FYGCLLAEVVPVPIEVPLTrkdagSQQIGFLLGSCGVTVALTSDA-CHKGLPKSPTGEIPQ 459
Cdd:cd05936 66 YFGALKAGAVVVPLNPLYT-----PRELEHILNDSGAKALIVAVSfTDLLAAGAPLGERVA 121
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
281-817 |
1.29e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 281 FEELLEVQQPDPNQPKPEGAqmLATRGEQLGVVTNWPPSLEAALQRWGT---------ISPKAPCLTTMDTNgkplyiLT 351
Cdd:PRK12316 1959 LLHLLEQMAEDAQAALGELA--LLDAGERQRILADWDRTPEAYPRGPGVhqriaeqaaRAPEAIAVVFGDQH------LS 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 352 YGKLWTRSMKVAYNILhKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLA--EVVPVPIEVPLTRkdagsqqIGF 429
Cdd:PRK12316 2031 YAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERS--FELVVALLAVLKAggAYVPLDPNYPAER-------LAY 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 430 LLGSCGVTVALTSDACHKGLPksPTGEIPQFKGWPKLLWFVTESKHlskpprdwfPHIKDANNDTAYIEYKTCKDGSVLG 509
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWADYPDTA---------PAVQLAGENLAYVIYTSGSTGLPKG 2163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 510 VTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPYSLMkvNPLSWIQKVCQYKAKVA 589
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELW--DPEQLYDEMERHGVTIL 2240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 590 CVKSrdMHWALVAHRDQRDVNLSSLRMLIVadGANPWSISSCDAFLN------VFQSKGLRQEVICP-----CASSPE-A 657
Cdd:PRK12316 2241 DFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPllwkcRPQDPCgA 2316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 658 LTVAIRRPTDDsnqppgrgvlsmhgltygvirvdseEKLSVLtvqDVGLvmpgaimcsvkpdgipQLCRTDEIGELCVCA 737
Cdd:PRK12316 2317 AYVPIGRALGN-------------------------RRAYIL---DADL----------------NLLAPGMAGELYLGG 2352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 738 VATGTSYYGLSGMTKNTFEVFPMTSSGAPIseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVE 817
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1010-1177 |
1.86e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1010 QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLM 1089
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1090 T-TQLICKLLRSREAAAavdvrtwpLILDTD----DLPKKRPAQiykPSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1164
Cdd:PRK12316 2106 TqRHLLERLPLPAGVAR--------LPLDRDaewaDYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170
....*....|...
gi 1537992864 1165 CRSIKLQCELYPS 1177
Cdd:PRK12316 2175 CQAAGERYELSPA 2187
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
344-446 |
2.15e-07 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 55.45 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 344 GKPLYI-----LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFpnNDPAAFMVAFYGCLLAEVVPVPIEVPLT 418
Cdd:cd05959 19 DKTAFIddagsLTYAELEAEARRVA-GALRALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 1537992864 419 rkdagSQQIGFLLGSCGVTVALTSDACH 446
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGELA 112
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
978-1513 |
6.12e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 53.74 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 978 EVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1057
Cdd:cd12117 1 ELFEEQAARTPDA---VAVVYGDR---SLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1058 PITVRPPHPQNiattlpTVKMIVEVSRSACLMTtqlickllrSREAAAAVDVRTWPLILDtDDLPKKRPAQIYKPSNPDT 1137
Cdd:cd12117 74 YVPLDPELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGLEVAVVID-EALDAGPAGNPAVPVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1138 LAYLDFSVSTTGMLAGVKMSHAATSAFCRS---IKLQcelypSREVAICLDPYC--GLGFVLWclCSVYSGHQSILIPPS 1212
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtnyVTLG-----PDDRVLQTSPLAfdASTFEIW--GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1213 ELETNPALwLLAVSQYKVrdtfcsySVMELcTKGLGSQteslkargldlsrvrtcvvVAEERPrialtQSFSKLfkdlgl 1292
Cdd:cd12117 211 TLLDPDAL-GALIAEEGV-------TVLWL-TAALFNQ-------------------LADEDP-----ECFAGL------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1293 hpRAVSTSfGCRVN-------LAIC----LQGTSGPDPTTVYvdmrALRHdrvrLVERG--SPHSLPLmesGKILPGVRI 1359
Cdd:cd12117 252 --RELLTG-GEVVSpphvrrvLAACpglrLVNGYGPTENTTF----TTSH----VVTELdeVAGSIPI---GRPIANTRV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1360 IIANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWaRTGYLgfLRRteltDANGErhd 1439
Cdd:cd12117 318 YVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNRPALTAERF-VADPFGPGERLY-RTGDL--ARW----LPDGR--- 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1537992864 1440 aLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAvftwtnllVVVVELDGSEQEaldlvpLVTNVVLEE 1513
Cdd:cd12117 383 -LEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAV--------VVVREDAGGDKR------LVAYVVAEG 440
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1132-1479 |
6.45e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.85 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1132 PSNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYC-GLGFVLWCLCSVYSGHQSILIP 1210
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1211 PSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGSQTESlkaRGLDLSRVRtCVVVAEERPRIALTQSFSKLFKDL 1290
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1291 GLHPRAVSTSFG-CRVNLAICLqGTSGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPG--VRIIIANPEtk 1367
Cdd:PRK07768 304 GLRPEAILPAYGmAEATLAVSF-SPCGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGleVRVVDEDGQ-- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1368 gPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDHfnsrlsfGdtqtiWARTGYLGFLrrTEltdaNGErhdaLYVVGAL 1447
Cdd:PRK07768 380 -VLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE----EGE----VVVCGRV 436
|
330 340 350
....*....|....*....|....*....|..
gi 1537992864 1448 DEAMELRGMRYHPIDIETSVIRAHKSVTECAV 1479
Cdd:PRK07768 437 KDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
350-444 |
8.54e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 53.40 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 429
Cdd:PRK08316 37 WTYAELDAAVNRVA-AALLDLG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAY 102
|
90
....*....|....*
gi 1537992864 430 LLGSCGVTVALTSDA 444
Cdd:PRK08316 103 ILDHSGARAFLVDPA 117
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
978-1158 |
1.86e-06 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 52.33 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 978 EVLQWRAQTTPDHllyTLLNCRGtiaNSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC- 1056
Cdd:cd17655 1 ELFEEQAEKTPDH---TAVVFED---QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1057 -VPITvrPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAaavdvrtwpLILDTDDLPKKRPAQIYKPSNP 1135
Cdd:cd17655 74 yLPID--PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKS 136
|
170 180
....*....|....*....|...
gi 1537992864 1136 DTLAYLDFSVSTTGMLAGVKMSH 1158
Cdd:cd17655 137 DDLAYVIYTSGSTGKPKGVMIEH 159
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
321-444 |
4.79e-06 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 51.27 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 321 EAALQRWGTISPKAPCLTTMDTNGKPlYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdPAAfMVAF 400
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-PEA-VIAM 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1537992864 401 YGCLLAEVVPVPIeVPLTRKDAgsqqIGFLLGSCGVTVALTSDA 444
Cdd:COG0365 82 LACARIGAVHSPV-FPGFGAEA----LADRIEDAEAKVLITADG 120
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
350-441 |
6.08e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAYNILHKLGtkqepmVRPGDRVALvFPNNDPAaFMVAFYGCLLAEVVPVPIEvPLTRkdagSQQIGF 429
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSPQ-FVIAYYAILRANAVVVPVN-PMNR----EEELAH 102
|
90
....*....|..
gi 1537992864 430 LLGSCGVTVALT 441
Cdd:PRK08314 103 YVTDSGARVAIV 114
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
540-905 |
7.84e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.53 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 540 LDFKKDVG-----LWHG-----ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKVacVKSRDMHWALVAH--RDQR 607
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATL--TAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 608 DVNLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVAIRRPTddsnqpPGRGVLsmhgltygV 687
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV------PGIGLR--------V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 688 IRVDSEEKLSVLTVQDVGLVMPGA---IMCSVKPDGIPQlcrtDEIGELCVCAVATGTSYYGlsgmtkntfevfpmtssG 764
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMevrISPGDGAAGVAG----REIGEIEIRGASMMSGYLG-----------------Q 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 765 APISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfVYRGRIavfsVTVLHDE-----R 839
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRG---VREGAV----VAVGTGEgsarpG 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1537992864 840 IVIVAEQRpdSTEEDSFQwmSRVLQAIDSihQVGVyclalVPAN-------TLPKTPLGGIHLSETKQLFLEG 905
Cdd:PRK05851 462 LVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDvvfvapgSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
324-440 |
1.02e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 49.92 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 324 LQRWGTISPKAPCLTTMDTngkplyILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDpaAFMVAFYGC 403
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLA-HALRALG------VAKGDRVAVLSKNSP--EFLELLFAA 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 1537992864 404 LLAEVVPVPIEVPLTRKDagsqqIGFLLGSCGVTVAL 440
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSGAKVLF 97
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1006-1425 |
1.27e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.77 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1006 LTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP-PHPQNIATtlptvkmivevsr 1084
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQ------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1085 saCLmttqlickllrsREAAaavdvrtwplildtddlPKkrpAQIYKPSNPDTLAYLdFSVSTTGMLAGVKMSHaatSAF 1164
Cdd:cd05910 69 --CL------------QEAE-----------------PD---AFIGIPKADEPAAIL-FTSGSTGTPKGVVYRH---GTF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1165 CRSIKLQCELYPSREVAICLDpycglGFVLWCLCSVYSGHQSIlIPPSE----LETNPALWLLAVSQYKVRDTFCSYSVM 1240
Cdd:cd05910 111 AAQIDALRQLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1241 ELCTkglgsqtESLKARGLDLSRVRtCVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLQGTsgpdp 1319
Cdd:cd05910 185 ERVA-------RYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGS----- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1320 ttvyvdmRALRHDRVRLVERGSPHSLplmesGKILPGV--RIIIANPETKGPLGDSH------LGEIWVHSAHNASGYFT 1391
Cdd:cd05910 247 -------RELLATTTAATSGGAGTCV-----GRPIPGVrvRIIEIDDEPIAEWDDTLelprgeIGEITVTGPTVTPTYVN 314
|
410 420 430
....*....|....*....|....*....|....
gi 1537992864 1392 IYGDESLQSDHFNSrlsfgdtQTIWARTGYLGFL 1425
Cdd:cd05910 315 RPVATALAKIDDNS-------EGFWHRMGDLGYL 341
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
316-444 |
1.44e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 49.65 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 316 WPP-------------SLEAALQRWGTISPKAPCLttmDTNGkplYILTYGKLWTRSMKVAyNILHKLGtkqepmVRPGD 382
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1537992864 383 RVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKdagsQQIGFLLGSCGVTVALTSDA 444
Cdd:PRK06178 85 RVAVFLPNC--PQFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
976-1160 |
2.12e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 49.27 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 976 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:PRK10252 460 LSALVAQQAAKTPDA---PALADARY---QFSYREMREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAG 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1056 CVPITVRPPHPQNiattlpTVKMIVEVSRSACLMTTQlickLLRSREAAAAVDVRTWPLILDTDdlPKKRPAQIYKPSNP 1135
Cdd:PRK10252 533 AAWLPLDTGYPDD------RLKMMLEDARPSLLITTA----DQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHT 600
|
170 180
....*....|....*....|....*
gi 1537992864 1136 dtlAYLDFSVSTTGMLAGVKMSHAA 1160
Cdd:PRK10252 601 ---AYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
984-1479 |
2.22e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 49.39 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 984 AQTTPDHLLYTLLNCRgtiansLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP 1063
Cdd:PRK12467 522 ARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPD-VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1064 PHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTDDLPKKRPAQIYKPSNPDTLAYLDF 1143
Cdd:PRK12467 595 EYPQD------RLAYMLDDSGVRLLLTQSHLLAQL-----PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1144 SVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAIcLDPYCGLGFVLWCLCSVYSGHQSILIPPSEletnpalwll 1223
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM-VSTFAFDLGVTELFGALASGATLHLLPPDC---------- 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1224 avsqykVRDTFCSYSVMelCTKGLG--SQTES-----LKARGLDLSRVRTCVVVAEErpriALTQSFSKLFKDLGLhpra 1296
Cdd:PRK12467 733 ------ARDAEAFAALM--ADQGVTvlKIVPShlqalLQASRVALPRPQRALVCGGE----ALQVDLLARVRALGP---- 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1297 vstsfGCRvnlaicLQGTSGPDPTTVYVDMRALRHDRVrlVERGSPHSLPLMESgkilpGVRIIIA--NPETKGPLGDSH 1374
Cdd:PRK12467 797 -----GAR------LINHYGPTETTVGVSTYELSDEER--DFGNVPIGQPLANL-----GLYILDHylNPVPVGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1375 LGeiwvhSAHNASGYftiYGDESLQSDHFNSRLSFGDTQTIWaRTGYLGflRRTeltdANGErhdaLYVVGALDEAMELR 1454
Cdd:PRK12467 859 IG-----GAGLARGY---HRRPALTAERFVPDPFGADGGRLY-RTGDLA--RYR----ADGV----IEYLGRMDHQVKIR 919
|
490 500
....*....|....*....|....*
gi 1537992864 1455 GMRYHPIDIETSvIRAHKSVTECAV 1479
Cdd:PRK12467 920 GFRIELGEIEAR-LLAQPGVREAVV 943
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
978-1165 |
3.11e-05 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 48.32 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 978 EVLQWRAQTTPDHLLYTLlncRGtiaNSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCV 1057
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD---RG---QSLTYKQLNEKANQLARHLRGKGVKPD-DQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1058 PITVRPPHPQniattlptvkmivevsrsaclmttQLICKLLRSREAAaavdvrtwpLILdtddlpkkrpaqiykpSNPDT 1137
Cdd:cd17645 75 YVPIDPDYPG------------------------ERIAYMLADSSAK---------ILL----------------TNPDD 105
|
170 180
....*....|....*....|....*...
gi 1537992864 1138 LAYLDFSVSTTGMLAGVKMSHAATSAFC 1165
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1005-1164 |
4.33e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.98 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1005 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIATTLPT--VKMI-- 1079
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALfv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1080 ------VEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDlPKKRPAQIykpsNPDTLAYLDFSVSTTGMLAG 1153
Cdd:PRK07656 109 lglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD-PAERAPEV----DPDDVADILFTSGTTGRPKG 183
|
170
....*....|..
gi 1537992864 1154 VKMSHAAT-SAF 1164
Cdd:PRK07656 184 AMLTHRQLlSNA 195
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
976-1065 |
5.65e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 47.83 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 976 LSEVLQWRAQTTPDHllyTLLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1055
Cdd:COG1021 27 LGDLLRRRAERHPDR---IAVVDGER---RLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 1537992864 1056 CVPITVRPPH 1065
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
350-411 |
8.09e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 47.06 E-value: 8.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1537992864 350 LTYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPV 411
Cdd:COG1021 51 LSYAELDRRADRLAAG-LLALG------LRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
351-499 |
1.44e-04 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 46.10 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 351 TYGKLWTRSMKVAYNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEV--PLTRkdagsqqIG 428
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1537992864 429 FLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkgwPKLLWFVTESKHLSKPPRDWFPHikdaNNDTAYIEY 499
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSG----PDDLAYVIY 127
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
332-542 |
1.69e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 46.11 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 332 PKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNDPAafMVAFYGCLLAEVVPV 411
Cdd:cd12114 1 PDATAVICGDGT------LTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQ--VVAVLGILAAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 412 PIEV--PLTRKDAgsqqigfLLGSCGVTVALTSDACHKGLPKSPTgeipqfkgwpkllwFVTESKHLSKPPRDwFPHIKD 489
Cdd:cd12114 66 PVDIdqPAARREA-------ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDV 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1537992864 490 ANNDTAYIEYKTCKDGSVLGVTVTRIALLTHCQALTQACGYTEAETIVNV--LDF 542
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALssLSF 178
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
350-549 |
1.85e-04 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 46.39 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPI--EVPLTRkdagsqqI 427
Cdd:COG1020 502 LTYAELNARANRLA-HHLRALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER-------L 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 428 GFLLGSCGVTVALTSDACHKGLPKSptgeipqfkgwpKLLWFVTESKHLSKPPRDWfPHIKDANNDTAYIEY-------- 499
Cdd:COG1020 566 AYMLEDAGARLVLTQSALAARLPEL------------GVPVLALDALALAAEPATN-PPVPVTPDDLAYVIYtsgstgrp 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1537992864 500 KtckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNV--LDFkkDVGLW 549
Cdd:COG1020 633 K--------GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
350-444 |
3.25e-04 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 44.89 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALvFPNNDPaAFMVAFYGCLLAEVVPVPIevpltRKDAGSQQIGF 429
Cdd:cd05907 6 ITWAEFAEEVRALA-KGLIALG------VEPGDRVAI-LSRNRP-EWTIADLAILAIGAVPVPI-----YPTSSAEQIAY 71
|
90
....*....|....*
gi 1537992864 430 LLGSCGVTVALTSDA 444
Cdd:cd05907 72 ILNDSEAKALFVEDP 86
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
987-1158 |
3.42e-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: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 987 TPDHLLYTLLNCrgtianSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAG--CVPITvrpP 1064
Cdd:cd17656 1 TPDAVAVVFENQ------KLTYRELNERSNQLARFLREKGVKKD-SIVAIMMERSAEMIVGILGILKAGgaFVPID---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1065 HpqniattLPTVKMIVEVSRSAC-LMTTQLICKLLRSREAAaaVDVRTWPLILDTDDlpkkrpAQIYKPSNPDTLAYLDF 1143
Cdd:cd17656 71 E-------YPEERRIYIMLDSGVrVVLTQRHLKSKLSFNKS--TILLEDPSISQEDT------SNIDYINNSDDLLYIIY 135
|
170
....*....|....*
gi 1537992864 1144 SVSTTGMLAGVKMSH 1158
Cdd:cd17656 136 TSGTTGKPKGVQLEH 150
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
984-1159 |
4.66e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 44.50 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 984 AQTTPDHLLYtllNCRGTianSLTCVQLHKRAEKIAVMLMERgHLQDGDHVaLVY----PpgiDLIAAFYGCLYAGC--V 1057
Cdd:PRK04813 12 AQTQPDFPAY---DYLGE---KLTYGQLKEDSDALAAFIDSL-KLPDKSPI-IVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1058 PITVRPPhpqniattLPTVKMIVEVSRSACLMTTqlickllrSREAAAAVDVRTwpLILD--TDDLPKKRPAQIYKPSNP 1135
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIPV--ITLDelKDIFATGNPYDFDHAVKG 142
|
170 180
....*....|....*....|....
gi 1537992864 1136 DTLAYLDFSVSTTGMLAGVKMSHA 1159
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
350-889 |
5.32e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 44.44 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEV--PLTRkdagsqqI 427
Cdd:cd05930 13 LTYAELDARANRLA-RYLRERG------VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDPsyPAER-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 428 GFLLGSCGVTVALTSDachkglpksptgeipqfkgwpkllwfvteskhlskpprdwfphikdanNDTAYIEY-------- 499
Cdd:cd05930 77 AYILEDSGAKLVLTDP------------------------------------------------DDLAYVIYtsgstgkp 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 500 KtckdgsvlGVTVTRIALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMN--MMHVISipySLMKVNPLSW 577
Cdd:cd05930 109 K--------GVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAgaTLVVLP---EEVRKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 578 IQKVCQYKAKVA-CVKSrdmHW-ALVAHRDQRDvnLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcassp 655
Cdd:cd05930 177 ADLLAEEGITVLhLTPS---LLrLLLQELELAA--LPSLRLVLVG-G--------------------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 656 EALTVAIRRPTDDSNqpPGRGVLSMHGLT-------YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGipQLCRTD 728
Cdd:cd05930 218 EALPPDLVRRWRELL--PGARLVNLYGPTeatvdatYYRVPPDDEEDGRV----PIGRPIPNTRVYVLDENL--RPVPPG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 729 EIGELCVC--AVATGtsYYGLSGMTKntfEVFPMTSSGAPISEYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNA 806
Cdd:cd05930 290 VPGELYIGgaGLARG--YLNRPELTA---ERFVPNPFGPGERMY---RTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 807 DDIVATALAVEPMkfvyrgRIAVfsVTVLHD----ERIV--IVAEQRPDSTEEDSFQWMSRVLQAidsihqvgvYCL--A 878
Cdd:cd05930 362 GEIEAALLAHPGV------REAA--VVAREDgdgeKRLVayVVPDEGGELDEEELRAHLAERLPD---------YMVpsA 424
|
570
....*....|.
gi 1537992864 879 LVPANTLPKTP 889
Cdd:cd05930 425 FVVLDALPLTP 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
350-443 |
6.72e-04 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 44.23 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 429
Cdd:cd05926 15 LTYADLAELVDDLA-RQLAALG------IKKGDRVAIALPNG--LEFVVAFLAAARAGAVVAPLN-PAYKKA----EFEF 80
|
90
....*....|....
gi 1537992864 430 LLGSCGVTVALTSD 443
Cdd:cd05926 81 YLADLGSKLVLTPK 94
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
350-421 |
8.76e-04 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 43.60 E-value: 8.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPnnDPAAFMVAFYGCLLAEVVPVPIEVPLTRKD 421
Cdd:cd05919 11 VTYGQLHDGANRLG-SALRNLG------VSSGDRVLLLML--DSPELVQLFLGCLARGAIAVVINPLLHPDD 73
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
350-444 |
9.24e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 43.94 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALvFPNNDPaAFMVAFYGCLLAEVVPVPIEVpltrkDAGSQQIGF 429
Cdd:COG1022 41 LTWAEFAERVRALAAG-LLALG------VKPGDRVAI-LSDNRP-EWVIADLAILAAGAVTVPIYP-----TSSAEEVAY 106
|
90
....*....|....*
gi 1537992864 430 LLGSCGVTVALTSDA 444
Cdd:COG1022 107 ILNDSGAKVLFVEDQ 121
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
350-539 |
1.32e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 43.05 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvpltrKDAGSQQIGF 429
Cdd:cd12116 13 LSYAELDERANRLA-ARLRARG------VGPGDRVAVYLPRS--ARLVAAMLAVLKAGAAYVPLD-----PDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 430 LLGSCGVTVALTSDACHKGLPKSPTgeipqfkGWPKLLWFVTESKHLSKPPrdwfphikDANNDTAYIEYKTCKDGSVLG 509
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLP-------VLLLALAAAAAAPAAPRTP--------VSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190
....*....|....*....|....*....|
gi 1537992864 510 VTVTRIALLTHCQALTQACGYTEAETIVNV 539
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDRLLAV 173
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
350-441 |
1.40e-03 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 42.85 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 429
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 1537992864 430 LLGSCGVTVALT 441
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1351-1493 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1351 GKILPGVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFTIYGDEsLQSDHFNSRLsfgdtqtiwaRTGYLGFLrrtel 1430
Cdd:cd05922 289 GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL----------HTGDLARR----- 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1537992864 1431 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSvIRAHKSVTECAVF----TWTNLLVVVVELD 1493
Cdd:cd05922 352 -DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
351-411 |
2.76e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 42.29 E-value: 2.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1537992864 351 TYGKLWTRSMKVAYNiLHKLGtkqepmVRPGDRVALVFPNNdPaAFMVAFYGCLLAEVVPV 411
Cdd:PRK05605 59 TYAELGKQVRRAAAG-LRALG------VRPGDRVAIVLPNC-P-QHIVAFYAVLRLGAVVV 110
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1351-1479 |
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 1537992864 1351 GKILPGVRIIIANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLRrtel 1430
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1537992864 1431 tdangeRHDALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1479
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1356-1480 |
4.92e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.41 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1356 GVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLrrteltDANG 1435
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---GDPTITAANFTDG---------WLRTGDLGSL------SAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1537992864 1436 ErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1480
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1010-1154 |
5.49e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1010 QLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSRSACLM 1089
Cdd:PRK05691 3750 ELNRAANRLGHALRAAGVGVD-QPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP------AQRLQRIIELSRTPVLV 3822
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1537992864 1090 TTQlICkLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQ----IYkpSNPDTLAYLDFSVSTTGMLAGV 1154
Cdd:PRK05691 3823 CSA-AC-REQARALLDELGCANRPRLLVWEEVQAGEVAShnpgIY--SGPDNLAYVIYTSGSTGLPKGV 3887
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
351-445 |
5.64e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 41.12 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 351 TYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVplTRKDAGSQQIgfl 430
Cdd:cd05934 5 TYAELLRESARIA-AALAALG------IRPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPINT--ALRGDELAYI--- 70
|
90
....*....|....*
gi 1537992864 431 LGSCGVTVALTSDAC 445
Cdd:cd05934 71 IDHSGAQLVVVDPAS 85
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
350-499 |
5.67e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 41.03 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAYNILHKlGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLA--EVVPVPIEVPLTRkdagsqqI 427
Cdd:cd12117 23 LTYAELNERANRLARRLRAA-G------VGPGDVVGVLAERS--PELVVALLAVLKAgaAYVPLDPELPAER-------L 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1537992864 428 GFLLGSCGVTVALTsdacHKGLPKSPTGEIPqfkgwpkLLWFVTESKHLSKPPrdwfPHIKDANNDTAYIEY 499
Cdd:cd12117 87 AFMLADAGAKVLLT----DRSLAGRAGGLEV-------AVVIDEALDAGPAGN----PAVPVSPDDLAYVMY 143
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
350-467 |
6.97e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 40.66 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 350 LTYGKLWTRSMKVAyNILHKLGtkqepmVRPGDRVALVFPNNdpAAFMVAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 429
Cdd:PRK08276 12 VTYGELEARSNRLA-HGLRALG------LREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLTAAE-----IAY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1537992864 430 LLGSCGVTVALTS----DACHKGLPKSP---------TGEIPQFKGWPKLL 467
Cdd:PRK08276 78 IVDDSGAKVLIVSaalaDTAAELAAELPagvplllvvAGPVPGFRSYEEAL 128
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
983-1168 |
9.56e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.92 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 983 RAQTTPDHLLytlLNCRGTianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVR 1062
Cdd:PRK05691 2197 QAARTPQAPA---LTFAGQ---TLSYAELDARANRLARALRERG-VGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537992864 1063 PPHPqniattLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAvdvrTWPLILDTDDLPKKRPAQIYKPSNPDTLAYLD 1142
Cdd:PRK05691 2270 PEYP------LERLHYMIEDSGIGLLLSDRALFEALGELPAGVA----RWCLEDDAAALAAYSDAPLPFLSLPQHQAYLI 2339
|
170 180
....*....|....*....|....*.
gi 1537992864 1143 FSVSTTGMLAGVKMSHAATSAFCRSI 1168
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIAMHCQAV 2365
|
|
| |
