|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1004-1578 |
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: 722.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1004 LFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 1082
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1083 TTLPTVKMivEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFR-----PPSPDVLAYLDFSV 1157
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKwgphpPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1158 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1237
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1238 SQYKARVTFCSYSVMEMCTKGLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRV 1317
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1318 NVAICLqpnrlgklaeQGTAGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHL 1397
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1398 GEIWVSSPHNATGYYTVYGEEALHADHF-SARLSFGDTQTIWARTGYLGFLRRTELTDASGGRHDALYVVGSLDETLELR 1476
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFpSTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1477 GMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELD-GLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINS 1555
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 2217337420 1556 RGEKQRMHLRDGFLADQLDPIYV 1578
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
352-928 |
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: 656.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 352 CLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 431
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 432 PLtrkdaGSQQVGFLLGSCGVFLALTTDACQKGLPKA-----QTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDT 506
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 507 GTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALM 586
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 587 KANPLSWIQKVCFYKARAALVKSRDMHWSL------LAQRGQRDVSLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 660
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 661 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEgTP 738
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPE-TK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 739 YLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGP----------DNLVFIVGK 808
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 809 LDGLMVTGVRRHNADDVVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 888
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2217337420 889 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 928
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
994-1536 |
6.63e-68 |
|
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: 239.83 E-value: 6.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 994 WRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRlsVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1073
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1074 RPPHPqnlGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRtwPTILDTDDIPKKKIASVFRP-PSPDVLAY 1152
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGT--PRLLVVDLLPDTSAADWPPPsPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1153 LDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESNV 1230
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1231 SLWLSAVSQYKARVT----FcSYsvmEMCTK-GLGAQTGvlrmkGVNLSCVRTCMVVAEeRPRIALTQSFSKLFKDLGLP 1305
Cdd:cd05931 232 LRWLRLISRYRATISaapnF-AY---DLCVRrVRDEDLE-----GLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1306 ARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTAGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGV 1379
Cdd:cd05931 302 PEAFRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1380 KVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEEALHADHFSARLSFGDtqTIWARTGYLGFLRRTEltdasggr 1459
Cdd:cd05931 365 EVRIVDPETGRELPDGEVGEIWVRGPSVASGY---WGRPEATAETFGALAATDE--GGWLRTGDLGFLHDGE-------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1460 hdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAE--CAVFTW----TNLLVVVVELDGLeQDALDLVALVTNV-- 1531
Cdd:cd05931 432 ---LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIra 507
|
....*.
gi 2217337420 1532 -VLEEH 1536
Cdd:cd05931 508 aVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
342-919 |
2.29e-64 |
|
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: 229.43 E-value: 2.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 342 RWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLnkltsknePLLKPGDRVALVFPNSdpVMFMVAFYGCLL 421
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 422 AELVPVPIEVPLTRKDAgsQQVGFLLGSCGVFLALTTDACQKGLPKAqtgeVAAFKGWPPLSWLVIDGKHLAkPPKDWHP 501
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 502 LAQDTGTgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHV 578
Cdd:cd05931 144 PSPDPDD-IAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 579 VsvpyaLMK-----ANPLSWIQKVCFYKAR--AAlvksRDMHWSLLAQRGQR----DVSLSSLRMLIVadGANPWSISSC 647
Cdd:cd05931 220 V-----LMSpaaflRRPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 648 DAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPG 726
Cdd:cd05931 289 RRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 727 ANVCVVKLEGTPyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGapifdrPFTRTGLLGFIGPDNLvFIV 806
Cdd:cd05931 364 QEVRIVDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YIT 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 807 GKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIH 886
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREH 513
|
570 580 590
....*....|....*....|....*....|...
gi 2217337420 887 QVGVYCLALVPANTLPKAPLGGIHISETKQRFL 919
Cdd:cd05931 514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
992-1476 |
5.74e-48 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 177.50 E-value: 5.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 992 LQWRAHTTPDHPLFlllnAKGTVTSTaTCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1071
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1072 TVrpphpqNLGTTLPTVKMIVEVSKSACVLtTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPK-----------KKIAS 1140
Cdd:pfam00501 75 PL------NPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1141 VFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1216
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1217 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAeERPRIALTQSFS 1296
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1297 KLFkdlglpARAVSTTFGCRVN-VAICLQPNRLGKLAEQGTAgpdpttvyvdmralrhdrvrlvergsphslplmesGKI 1375
Cdd:pfam00501 299 ELF------GGALVNGYGLTETtGVVTTPLPLDEDLRSLGSV-----------------------------------GRP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1376 LPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEEALHADHFsarlsfgdTQTIWARTGYLGFLrrteltDA 1455
Cdd:pfam00501 338 LPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DE 400
|
490 500
....*....|....*....|.
gi 2217337420 1456 SGgrhdALYVVGSLDETLELR 1476
Cdd:pfam00501 401 DG----YLEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
988-1518 |
6.11e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 137.22 E-value: 6.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEkgRLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQA--RASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1068 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIrtwPTILDTDDIPkKKIASV 1141
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD-PALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1142 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1216
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1217 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEMCTKGLgaqtgvlrmkgvNLSCVRTCMVVAEerP- 1287
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSESALERL------------DLSRWRVAYSGSE--Pi 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1288 RIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTAGPDPTTVYVDMRALRHDRVRLVEr 1361
Cdd:PRK05691 303 RQDSLERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1362 GSphslPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTvyGEEAlHADHFSARlsfgDTQTiWART 1441
Cdd:PRK05691 366 GS----VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-SAKTFVEH----DGRT-WLRT 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217337420 1442 GYLGFLRRTEltdasggrhdaLYVVGSLDETLELRGMRYHPIDIETSVIRahrsiaECAVFTWTNLLVVVVELDGLE 1518
Cdd:PRK05691 434 GDLGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1150-1528 |
3.58e-31 |
|
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: 126.25 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1150 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1226
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1227 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAEERPrIALTQSFSKLFKDlglpa 1306
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1307 rAVSTTFGcrvnvaiclqpnrlgkLAEqgtAGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVKVIIAHT 1386
Cdd:cd04433 141 -KLVNGYG----------------LTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1387 ETkGPLGDSHLGEIWVSSPHNATGYYTVygeealhadhfsARLSFGDTQTIWARTGYLGFLRrteltdasggRHDALYVV 1466
Cdd:cd04433 185 DG-GELPPGEIGELVVRGPSVMKGYWNN------------PEATAAVDEDGWYRTGDLGRLD----------EDGYLYIV 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217337420 1467 GSLDETLELRGMRYHPIDIETsVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1528
Cdd:cd04433 242 GRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHV 308
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
333-921 |
1.09e-28 |
|
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: 122.78 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 333 PPSLLATLQRWGTTQPKSPClTALDTTGkAVYTLTYGKLWSRSLKLAyTLLNKLTskneplLKPGDRVALVFP-NSDpvm 411
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 412 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVflaLTTDACQkglpkAQTGEVAAFKGWPPLSWLV 486
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 487 IDGKHLAKPPKDWHPLAQDtgtgTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAG 563
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 564 LWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKA------RAALVKSRDmhwsLLAQRGQRDVSLSSLRMLIVAD 637
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 638 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 714
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 715 LTVQDVGQVMPGANVCVVKLEGTpyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLL 794
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDG-------WFRTGDL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 795 GFIGPDNLVFIVGKLDGLMVTGVrRHNADDVVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSfqw 874
Cdd:cd05906 417 GFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDA--- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2217337420 875 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 921
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
988-1528 |
2.86e-28 |
|
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: 120.30 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRLTYA---ELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1068 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLTtqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsp 1147
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1148 dvlAYLDFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1226
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1227 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAEerpriALTQSFSKLFKDLglpa 1306
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1307 ravsttFGCRVNvaiclqpNRLGkLAEqgtAGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVKVIIAHT 1386
Cdd:COG0318 239 ------FGVRIV-------EGYG-LTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRIVDE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1387 ETKgPLGDSHLGEIWVSSPHNATGYYTvyGEEALhadhfsaRLSFGDTqtiWARTGYLGFLrrteltDASGgrhdALYVV 1466
Cdd:COG0318 286 DGR-ELPPGEVGEIVVRGPNVMKGYWN--DPEAT-------AEAFRDG---WLRTGDLGRL------DEDG----YLYIV 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217337420 1467 GSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1528
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELRAFL 409
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-123 |
6.85e-28 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 109.05 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 10 AAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIpliqgidpsLQAENripgPSQTTAAAPKQQKSRPTASRD 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFL---------LHPET----PTKLSAEAQNQLASLETKLRD 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217337420 90 ERFRSDVHTEAVQAALAKYKERKM--PMPSKRRSVL 123
Cdd:pfam06464 69 EELSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
335-919 |
1.34e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.05 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 335 SLLATLQRWGTTQPKSPCLT----ALDTTGKAvYTLTYGKLWSRSLKLAYTLlNKLTSknepllkPGDRVALVFPNSdpV 410
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVA-ETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 411 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVFLALTTDACqkglpkaqTGEVAAF----KGWPPLSWLV 486
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 487 IDGKHLAKPPKDwhPLAQDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQA----CGYSEAETLTNV--LD 557
Cdd:PRK05850 141 VDLLDLDSPRGS--DARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFEQLMSDyfgdTGGVPPPDTTVVswLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 558 FKRDAGLWHGVLTSVMNRMHVV-SVPYALMkANPLSWIQkvcfykaraaLVKSRDMHWSL-------LAQRGQRDVSLSS 629
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPAVlTSPVAFL-QRPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 630 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 705
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 706 VDTEeKLSVltvqdvGQVMPGANVcvvklEGTPYL--------------------CKTDEVGEICVSSSATGTAYYGLLG 765
Cdd:PRK05850 349 FDYE-KLSA------GHAKRCETG-----GGTPLVsygsprsptvrivdpdtcieCPAGTVGEIWVHGDNVAAGYWQKPE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 766 ITKNVFEAVPVT-TGGAPifDRPFTRTGLLGFIGPDNLvFIVGKL-DGLMVTGvRRHNADDVVATalavepMKFVYRGRI 843
Cdd:PRK05850 417 ETERTFGATLVDpSPGTP--EGPWLRTGDLGFISEGEL-FIVGRIkDLLIVDG-RNHYPDDIEAT------IQEITGGRV 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 844 AVFSVTVLHDDRIVLVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRF 918
Cdd:PRK05850 487 AAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQY 566
|
.
gi 2217337420 919 L 919
Cdd:PRK05850 567 R 567
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
340-816 |
1.58e-26 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 114.33 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 340 LQRWGTTQPKSPCLTALDTTgkavyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 419
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR-----RLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 420 LLAELVPVPIEVpltrkDAGSQQVGFLLGSCGVFLALTTD--------ACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKH 491
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 492 LAKPPKDWHPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQAC----GYSEAETLTNVLDFKRDAGL 564
Cdd:pfam00501 142 ADVPPPPPPPPDPDD---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 565 WHGVLTSVMNRMHVVSVP--YALMKANPLSWIQKvcfYKARAALVKSRDMHWsLLAQRGQRDVSLSSLRMLIVadGANPW 642
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPPgfPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 643 SISSCDAFLNVFqsrglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQ 722
Cdd:pfam00501 290 PPELARRFRELF------GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 723 VMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvttggapiFDRPFTRTGLLGFIGPDNL 802
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAF------------DEDGWYRTGDLGRRDEDGY 403
|
490
....*....|....
gi 2217337420 803 VFIVGKLDGLMVTG 816
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
336-825 |
2.92e-26 |
|
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: 114.14 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 336 LLATLQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSDPvmFMVA 415
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 416 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGvflalttdacqkglPKAqtgevaafkgwpplswlVIdgkhlakp 495
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSG--------------ARA-----------------LV-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 496 pkdwhplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSV 572
Cdd:COG0318 102 --------------TALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 573 MNRMHVVSVPyalmKANPLSWIQKVCFYKA-RAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFL 651
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 652 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGANVC 730
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 731 VVKLEGTPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttGGapifdrpFTRTGLLGFIGPDNLVFIVGKLD 810
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVGRKK 346
|
490
....*....|....*
gi 2217337420 811 GLMVTGVRRHNADDV 825
Cdd:COG0318 347 DMIISGGENVYPAEV 361
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
357-925 |
6.97e-26 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 114.72 E-value: 6.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 357 DTTGKAVYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LT 434
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 435 RKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEvaafkgwpPLSWlVIDGKHLAKPPKDWHPLAQDTGTGTAYIE 514
Cdd:PRK09192 112 GRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 515 YkTSkeGST---VGVTVSHASLLAQCRALTQ-ACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANP 590
Cdd:PRK09192 183 Y-SS--GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 591 LSWIQKVCfyKARAALVKSRDMHWSLLAQRGQ----RDVSLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICP 666
Cdd:PRK09192 260 LQWLDLIS--RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 667 CASSPEAlTVAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGANVCVVKLEGTPYlcKTDE 745
Cdd:PRK09192 336 SYGLAEA-TLAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 746 VGEICVSSSATGTAYYGllgitKNVFEAVPVTTGgapifdrpFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDV 825
Cdd:PRK09192 411 VGHICVRGPSLMSGYFR-----DEESQDVLAADG--------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 826 VATAlavEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKA 904
Cdd:PRK09192 477 EWIA---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRT 550
|
570 580
....*....|....*....|.
gi 2217337420 905 PLGGIHISETKQRFLEGTLHP 925
Cdd:PRK09192 551 SSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
988-1532 |
1.26e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 113.88 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCVQLHKRAERVAAALMEKGrlSVGDHVALVYPPGVDLIAAFYGCL 1064
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1065 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLTTQAVTRLLRskEAAAAVDIRTWPTI--LDTDDIPKKKIASVF 1142
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVT--EYVAPQPGQSAPPVieVDLLDLDSPRGSDAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1143 RPPSPDVlAYLDFSVSTTGILAGVKMSHAATSALCRSI------KLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1216
Cdd:PRK05850 156 PRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1217 QSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaQTGVLRMKGVNLSCVRTcMVVAEERPRIALTQSFS 1296
Cdd:PRK05850 235 PAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVR----KTSDDDMAGLDLGGVLG-IISGSERVHPATLKRFA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1297 KLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAE------QGTAGPDPTTVYVDMRALRHDRVR---------LVER 1361
Cdd:PRK05850 310 DRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1362 GSPHSlplmesgkilPGVKVIIAHTETKGPLGDshLGEIWVSSPHNATGYYTVYGEEalhADHFSARL---SFGDTQTIW 1438
Cdd:PRK05850 374 GSPRS----------PTVRIVDPDTCIECPAGT--VGEIWVHGDNVAAGYWQKPEET---ERTFGATLvdpSPGTPEGPW 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1439 ARTGYLGFLrrteltdaSGGrhdALYVVGSLDETLELRGMRYHPIDIETSV--IRAHRsiaeCAVFT----WTNLLVVVV 1512
Cdd:PRK05850 439 LRTGDLGFI--------SEG---ELFIVGRIKDLLIVDGRNHYPDDIEATIqeITGGR----VAAISvpddGTEKLVAII 503
|
570 580
....*....|....*....|...
gi 2217337420 1513 EL---DGLEQDALDLVALVTNVV 1532
Cdd:PRK05850 504 ELkkrGDSDEEAMDRLRTVKREV 526
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1022-1492 |
3.15e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 112.91 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGRLsvGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1093
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1094 vsksacVLTTQAVTRLLRSKEAAAAVDIRtwPTILDTDDIPKKkIASVFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1170
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDS-AGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1171 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1247
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1248 SYSVMEmctkgLGAQTGVLRM-KGVNLSCVrtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpn 1326
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG------------ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1327 rlgkLAEQ----GTAGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEI 1400
Cdd:PRK12476 357 ----IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1401 WVSSPHNATGYY-----TvygEEALHAdHFSARLSFG------DTQTIWARTGYLGFLRRTEltdasggrhdaLYVVGSL 1469
Cdd:PRK12476 433 WLHGDNIGRGYWgrpeeT---ERTFGA-KLQSRLAEGshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRI 497
|
490 500
....*....|....*....|...
gi 2217337420 1470 DETLELRGMRYHPIDIETSVIRA 1492
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEATVAEA 520
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
395-923 |
3.11e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 103.66 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 395 KPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVFLALTTDACQKG----- 464
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGvrkff 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 465 --LPKAQTGEVAAFKGWPP---LSWlvidgkhlaKPPkdwhPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQ 536
Cdd:PRK07769 148 raRPAKERPRVIAVDAVPDevgATW---------VPP----EANEDT---IAYLQY-TS--GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 537 CRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKaNPLSWIqkvcfykaRAALVKSRDMH--- 613
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWI--------RELARKPGGTGgtf 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 614 -------WSLLAQRG-----QRDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRR 680
Cdd:PRK07769 280 saapnfaFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 681 PPDlggpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTA 759
Cdd:PRK07769 358 MDE----EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 760 YYGLLGITKNVFEAV------PVTTGGAPIfDRPFTRTGLLGFIGPDNLvFIVGKLDGLMVTGVRRHNADDVVATALavE 833
Cdd:PRK07769 432 YWGKPEETAATFQNIlksrlsESHAEGAPD-DALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--E 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 834 PMKFVYRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCL 893
Cdd:PRK07769 508 ATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDV 587
|
570 580 590
....*....|....*....|....*....|
gi 2217337420 894 ALVPANTLPKAPLGGIHISETKQRFLEGTL 923
Cdd:PRK07769 588 LLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
332-953 |
6.08e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.01 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 332 RPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLlnkltsknEPLLKPGDRVALVFPnSDPvM 411
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 412 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLpkAQTGEVAAfKGWPPlsWLVIDGKh 491
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL--LQMEELAA-ANAPE--LLCVDTL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 492 LAKPPKDWHPLAQDtGTGTAYIEYkTSkeGSTV---GVTVSHASLLAQCRALTQACG--YSEAETLTNVLDFKRDAGLWH 566
Cdd:PRK05691 151 DPALAEAWQEPALQ-PDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 567 GVLTSVMNrmhvvSVPYALMK-----ANPLSWIQKVCFYkaRAALVKSRDMHWSLLAQRgqrdVSLSSLRML------IV 635
Cdd:PRK05691 227 GLLQPIFS-----GVPCVLMSpayflERPLRWLEAISEY--GGTISGGPDFAYRLCSER----VSESALERLdlsrwrVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 636 ADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSV 714
Cdd:PRK05691 296 YSGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 715 LTVQDVGQVM-------PGANVCVV---KLEGTPylckTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGapif 784
Cdd:PRK05691 360 RAEPGTGSVLmscgrsqPGHAVLIVdpqSLEVLG----DNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDG---- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 785 dRPFTRTGLLGFIgPDNLVFIVGKLDGLMVtgVRRHN--ADDVVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE- 861
Cdd:PRK05691 428 -RTWLRTGDLGFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEi 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 862 ----QRPDASEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVT 937
Cdd:PRK05691 502 srsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYA 567
|
650
....*....|....*.
gi 2217337420 938 NLPKPRQKQPEVGPAS 953
Cdd:PRK05691 568 LFPALQAVEAAQTAAS 583
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1022-1501 |
1.06e-19 |
|
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: 93.48 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1101
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1102 TTQAvTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1181
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAP---PPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1182 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1255
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1256 TKGLGAQTGVLRMkgvnlscvrtcMVVAEERPRIALTQSFSKLFKDLGLparavsttfgcrVNvaiclqpnrlgklaeqg 1335
Cdd:TIGR01733 227 AAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN----------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1336 TAGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYytvY 1415
Cdd:TIGR01733 267 LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---L 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1416 GEEALHADHFSARLSFGDTQTIWARTGYLGflRRteltdasggRHD-ALYVVGSLDETLELRGMRYHPIDIEtSVIRAHR 1494
Cdd:TIGR01733 335 NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY---------LPDgNLEFLGRIDDQVKIRGYRIELGEIE-AALLRHP 402
|
....*..
gi 2217337420 1495 SIAECAV 1501
Cdd:TIGR01733 403 GVREAVV 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1022-1511 |
3.30e-19 |
|
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: 93.50 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGRLSvGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1100
Cdd:cd05906 44 DLLEDARRLAAGLRQLGLRP-GDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1101 LTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSI 1180
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAA---DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1181 KLQCELYPSRQIA--ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVMEMC 1255
Cdd:cd05906 200 IQHNGLTPQDVFLnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWApnfAFALLNDL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1256 TKGLGAQTGvlrmkgvNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAEQG 1335
Cdd:cd05906 278 LEEIEDGTW-------DLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFG----------------MTETC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1336 tAGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvY 1415
Cdd:cd05906 334 -SG---VIYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIV-DDEGQLLPEGEVGRLQVRGPVVTKGY---Y 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1416 GEEALHADHFsarlsfgdTQTIWARTGYLGFLrrteltdasggRHDALYVVGSLDETLELRGMRYHPIDIETSV----IR 1491
Cdd:cd05906 396 NNPEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGV 456
|
490 500
....*....|....*....|...
gi 2217337420 1492 AHRSIAECAVF---TWTNLLVVV 1511
Cdd:cd05906 457 EPSFTAAFAVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
357-925 |
6.70e-19 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 92.88 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 357 DTTGKAVyTLTYGKLWSRslklaytlLNKLTSKNEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP---- 432
Cdd:PRK12476 61 SAAGCAV-ELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 433 -LTRKDAgsqqvgfLLGSCGVFLALTTDACQ-------KGLPKAQTGEVAAFKGWPplswlvidgkhlAKPPKDWHPLAQ 504
Cdd:PRK12476 130 hAERLDT-------ALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIP------------DSAGESFVPVEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 505 DTgTGTAYIEYkTSkeGST---VGVTVSHasllaqcRAltqACgyseaetlTNVLDFKRDAGLW----HGV--------- 568
Cdd:PRK12476 191 DT-DDVSHLQY-TS--GSTrppVGVEITH-------RA---VG--------TNLVQMILSIDLLdrntHGVswlplyhdm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 569 -LTSVM------NRMHVVSvPYALMKaNPLSWIQKVCfYKARAALV--KSRDMHWSLLAQRG----QRDVSLSSLRMLIv 635
Cdd:PRK12476 249 gLSMIGfpavygGHSTLMS-PTAFVR-RPQRWIKALS-EGSRTGRVvtAAPNFAYEWAAQRGlpaeGDDIDLSNVVLII- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 636 adGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSMNGLSYG-VIRVDTEEKLSV 714
Cdd:PRK12476 325 --GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPSVVYLDREQLGAGrAVRVAADAPNAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 715 LTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTT-------GGAPIfDRP 787
Cdd:PRK12476 400 AHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRlaegshaDGAAD-DGT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 788 FTRTGLLGFIgPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDAS 867
Cdd:PRK12476 477 WLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTS 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217337420 868 EEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHP 925
Cdd:PRK12476 554 RADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1022-1496 |
6.81e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 89.79 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGRlsVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1093
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1094 VSKSAcvlttQAVTRLLRSKEAAAAvdirtwPTILDTDDIPKKkIASVFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1170
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1171 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1244
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1245 tfcsYSVMEMCTKGLGAQTGVLR--MKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaic 1322
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARGLPKdgEPPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG-------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1323 lqpnrlgkLAEQ----GTAGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSH 1396
Cdd:PRK07769 346 --------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQ 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1397 LGEIWVSSPHNATGYytvYGEEALHADHFSARLSFGDTQT---------IWARTGYLGFLRRTEltdasggrhdaLYVVG 1467
Cdd:PRK07769 418 IGEIWLHGNNIGTGY---WGKPEETAATFQNILKSRLSEShaegapddaLWVRTGDYGVYFDGE-----------LYITG 483
|
490 500
....*....|....*....|....*....
gi 2217337420 1468 SLDETLELRGMRYHPIDIETSVIRAHRSI 1496
Cdd:PRK07769 484 RVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1019-1502 |
2.15e-16 |
|
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: 84.19 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1019 TCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1098
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1099 CVLTTQAVtrLLRSKEAAAAVDIRT----------WPTILDTDDIPKKKIASVFRPP----SPDVLAYLDFSVSTTGILA 1164
Cdd:cd05911 85 VIFTDPDG--LEKVKEAAKELGPKDkiivlddkpdGVLSIEDLLSPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1165 GVKMSHA---ATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQY 1240
Cdd:cd05911 163 GVCLSHRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1241 KARVTF------CSYSVMEMCTKGlgaqtgvlrmkgvNLSCVRTCMVVAEerpriALTQSFSKLFKDLGLPARAVSTtFG 1314
Cdd:cd05911 236 KITFLYlvppiaAALAKSPLLDKY-------------DLSSLRVILSGGA-----PLSKELQELLAKRFPNATIKQG-YG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1315 C-RVNVAICLQPNRLgklaeqgtagpdpttvyvdmralrhdrvrlVERGSphslplmeSGKILPGVKVIIAHTETKGPLG 1393
Cdd:cd05911 297 MtETGGILTVNPDGD------------------------------DKPGS--------VGRLLPNVEAKIVDDDGKDSLG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1394 DSHLGEIWVSSPHNATGYYTvyGEEALHADHfsarlsfgdTQTIWARTGYLGFLRRTELtdasggrhdaLYVVGSLDETL 1473
Cdd:cd05911 339 PNEPGEICVRGPQVMKGYYN--NPEATKETF---------DEDGWLHTGDIGYFDEDGY----------LYIVDRKKELI 397
|
490 500
....*....|....*....|....*....
gi 2217337420 1474 ELRGMRYHPIDIEtSVIRAHRSIAECAVF 1502
Cdd:cd05911 398 KYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
978-1489 |
5.63e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 83.13 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 978 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGV 1054
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1055 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLTTQAVTRLLrsKEAAAAVDIRTWPTILDTD 1131
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1132 DIPKKKIAsvFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1210
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1211 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTgvlrMKGVNLSCVRTCMVVAEE-RPR 1288
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKD----LAELDLSCWRVAGIGADMiRPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1289 IalTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPNRLGKLAEQgtagpdpttvyVDMRALRHDR--VRLVERGSPH 1365
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPLGSGIVVEE-----------VDRDRLEYQGkaVAPGAETRRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1366 SlPLMESGKILPGVKVIIaHTETKGPLGDSHLGEIWVSSPHNATGYYtvygeealhADHFSARLSFGDTqtiWARTGYLG 1445
Cdd:PRK09192 382 R-TFVNCGKALPGHEIEI-RNEAGMPLPERVVGHICVRGPSLMSGYF---------RDEESQDVLAADG---WLDTGDLG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217337420 1446 FLrrteltdaSGGRhdaLYVVGSLDETLELRGMRYHPIDIETSV 1489
Cdd:PRK09192 448 YL--------LDGY---LYITGRAKDLIIINGRNIWPQDIEWIA 480
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1019-1524 |
4.06e-14 |
|
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: 76.80 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1019 TCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSA 1098
Cdd:cd05930 14 TYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1099 CVLTTqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1178
Cdd:cd05930 87 LVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1179 SIKlqcELYPSR------QIAicldpycGLGF--ALWCL-CSVYSGHQSVLVPPlELESNVSLWLSAVSQYKARVTFCSY 1249
Cdd:cd05930 124 WMQ---EAYPLTpgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1250 SVMEMCTKGLGAQtgvlrmkgvNLSCVRTcMVVAEERPRIALTQSFSKLFKDLGLparavsttfgcrVNVaiclqpnrlg 1329
Cdd:cd05930 193 SLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL---------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1330 klaeqgtAGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNAT 1409
Cdd:cd05930 241 -------YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLAR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1410 GYytvYGEEALHADHFSArLSFGDTQTIWaRTGYLGflRRteltDASGGrhdaLYVVGSLDETLELRGMRYHPIDIETsV 1489
Cdd:cd05930 304 GY---LNRPELTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-A 367
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2217337420 1490 IRAHRSIAECAVFTWTN------LLVVVVELDGLEQDALDL 1524
Cdd:cd05930 368 LLAHPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
394-903 |
3.34e-13 |
|
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: 74.01 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 394 LKPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVFLALttdaCQKGL-PKAQ 469
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVL----ADAGAaDRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 470 TGEVAAFKgwpPLSWLVIDGKHLAKPPKDWHPLAQDTgtgTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEA 549
Cdd:cd05922 85 DALPASPD---PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 550 ETLTNVLDFKRDAGLwhGVLTS--------VMNRMHVVsvPYALMKAnplswiqkvcFYKARAALVKSRDMHWSLLAQRG 621
Cdd:cd05922 159 DRALTVLPLSYDYGL--SVLNThllrgatlVLTNDGVL--DDAFWED----------LREHGATGLAGVPSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 622 QRDVSLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavls 695
Cdd:cd05922 225 FDPAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 696 mnglsygvirvdteeklsvltvQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIcVSSSATGTAYYGllgiTKNVFEAVP 775
Cdd:cd05922 286 ----------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 776 VTTGGApifdrpfTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfvyrGRIAVFSVTVLHDDR 855
Cdd:cd05922 337 GRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEK 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2217337420 856 IVLVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 903
Cdd:cd05922 405 LALFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1015-1504 |
7.08e-13 |
|
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: 73.17 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1015 TSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1094
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1095 SKSACVLTTQAVTRLLRSKEAAAAVDIRT----------WPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILA 1164
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1165 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVPPLELESNVslwL 1234
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAV---F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1235 SAVSQYKARVTFCS---YSVMemctkglgaqTGVLRMKGVNLSCVRTCMVVAEerpriALTQSFSKLFKDLglparavst 1311
Cdd:cd05959 248 KRIRRYRPTVFFGVptlYAAM----------LAAPNLPSRDLSSLRLCVSAGE-----ALPAEVGERWKAR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1312 tFGCRVnvaiclqpnrlgklaEQGTAGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVIIAHtETKGP 1391
Cdd:cd05959 304 -FGLDI---------------LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1392 LGDSHLGEIWVSSPHNATGYYTVYGEealhadhfsARLSFgdtQTIWARTGYlGFLRRTEltdasgGRHdalYVVGSLDE 1471
Cdd:cd05959 353 VADGEPGELYVRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVRDDD------GFY---TYAGRADD 410
|
490 500 510
....*....|....*....|....*....|...
gi 2217337420 1472 TLELRGMRYHPIDIEtSVIRAHRSIAECAVFTW 1504
Cdd:cd05959 411 MLKVSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1022-1521 |
2.43e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.34 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGRLSVgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1097
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1098 acVLTTQAVTRLLRSKEAAAAVDirtwptilDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALC 1177
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVH--------DLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1178 RSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVMe 1253
Cdd:PRK05851 182 RGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1254 mctkGLGAQtgvlRMKGVNLSCVRTCmVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAE 1333
Cdd:PRK05851 260 ----GKYAR----RVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG----------------LAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1334 QGTAgpdpTTVYVDMRALRHDRVRLVERGSPHSLPLMesGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYyt 1413
Cdd:PRK05851 315 STCA----VTVPVPGIGLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1414 vYGEEALHADHfsarlsfgdtqtiWARTGYLGFlrrteLTDasggrhDALYVVGSLDETLELRGMRYHPIDIET--SVIR 1491
Cdd:PRK05851 387 -LGQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERvaAQVR 441
|
490 500 510
....*....|....*....|....*....|....
gi 2217337420 1492 AHRSIAECAVFTWTNL----LVVVVELDGLEQDA 1521
Cdd:PRK05851 442 GVREGAVVAVGTGEGSarpgLVIAAEFRGPDEAG 475
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
996-1178 |
5.09e-12 |
|
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: 70.45 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 996 AHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1075
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1076 PHPQnlgttlPTVKMIVEVSKSACVLTTQAVTrllrskeAAAAVDiRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDF 1155
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPALA-------GELAVE-LVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 2217337420 1156 SVSTTGILAGVKMSHAATSALCR 1178
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
988-1222 |
9.99e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 69.13 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLLLNAKGTVTstatcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1068 CVPVTVRPphpqnlgttlptvkmivevsksacVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIAsvfrpPSP 1147
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1148 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1221
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 2217337420 1222 P 1222
Cdd:cd05936 201 P 201
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1022-1501 |
9.19e-11 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 66.10 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVpvtVRPPHPQNlgtTLPTVKMIVEVSKSACVL 1101
Cdd:cd05904 37 ELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAV---VTTANPLS---TPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1102 TTQAVTrllrSKEAAAAVdirtwPTILdTDDIPKKKIASVFR--------PPSPDV----LAYLDFSVSTTGILAGVKMS 1169
Cdd:cd05904 110 TTAELA----EKLASLAL-----PVVL-LDSAEFDSLSFSDLlfeadeaePPVVVIkqddVAALLYSSGTTGRSKGVMLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1170 HA-ATSALCRSIKLQCELYPSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLVPPLELESnvslWLSAVSQYkaRVTFC 1247
Cdd:cd05904 180 HRnLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY--KVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1248 SYS---VMEMCTKGLGaqtgvlrmKGVNLSCVRTCMVVAeerprialtqsfSKLFKDLglpARAVSTTFGcrvNVAIClq 1324
Cdd:cd05904 254 PVVppiVLALVKSPIV--------DKYDLSSLRQIMSGA------------APLGKEL---IEAFRAKFP---NVDLG-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1325 pnrlgklaeQG----TAGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEI 1400
Cdd:cd05904 306 ---------QGygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1401 WVSSPHNATGYytVYGEEALHAdhfsarlsfgdtqTI----WARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELR 1476
Cdd:cd05904 362 WIRGPSIMKGY--LNNPEATAA-------------TIdkegWLHTGDLCYI------DEDG----YLFIVDRLKELIKYK 416
|
490 500
....*....|....*....|....*
gi 2217337420 1477 GMRYHPIDIEtSVIRAHRSIAECAV 1501
Cdd:cd05904 417 GFQVAPAELE-ALLLSHPEILDAAV 440
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
510-816 |
1.10e-10 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 65.00 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 510 TAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPyalm 586
Cdd:cd04433 2 PALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 587 KANPLSWIQKVCFYKARAALVkSRDMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVICP 666
Cdd:cd04433 74 KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 667 CASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPylCKTDEV 746
Cdd:cd04433 146 YGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGEI 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 747 GEICVSSsatgtaYYGLLGITKNVFEAVPVTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTG 816
Cdd:cd04433 195 GELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1147-1486 |
1.63e-10 |
|
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: 65.59 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1147 PDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1226
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1227 ESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTgvlrMKGVNLSCVRtcMVVAEERP-RIALTQSFSKLFKDLGLP 1305
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEK----ANDWDLSSIR--MILNGAEPiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1306 ARAVSTTFG-CRVNVAICLQPnrlgklaeqgtAGPDPTTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVKVII 1383
Cdd:cd05908 259 RNAILPVYGlAEASVGASLPK-----------AQSPFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1384 AHTETKGpLGDSHLGEIWVSSPHNATGYYTvyGEEAlhadhfSARLSFGDTqtiWARTGYLGFLRRTEltdasggrhdaL 1463
Cdd:cd05908 328 CDEDNKI-LPDGYIGHIQIRGKNVTPGYYN--NPEA------TAKVFTDDG---WLKTGDLGFIRNGR-----------L 384
|
330 340
....*....|....*....|...
gi 2217337420 1464 YVVGSLDETLELRGMRYHPIDIE 1486
Cdd:cd05908 385 VITGREKDIIFVNGQNVYPHDIE 407
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
367-810 |
1.83e-10 |
|
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: 64.98 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 367 TYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 444
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 445 FLLGSCGVFLALTTdacqkglpkAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYkTSkeGST- 523
Cdd:TIGR01733 66 FILEDAGARLLLTD---------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 524 --VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVVSVPYALMKANPLSWiqkvcfyk 601
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 602 arAALVKSRDM-HWSLLAqrgqrdvslSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 679
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 680 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIC 750
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRP--VPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 751 VSSSATGTAYYGLLGITKNVFEAVPVTTGGapifDRPFTRTGLLGFIGPDNLVFIVGKLD 810
Cdd:TIGR01733 324 IGGPGVARGYLNRPELTAERFVPDPFAGGD----GARLYRTGDLVRYLPDGNLEFLGRID 379
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1022-1527 |
1.84e-10 |
|
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: 65.39 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGRlSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1101
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1102 TTQAVtrllrskEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1181
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAAP---AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1182 LQCELYPSRQIaICLDPYCglgFALwclcSVysghqsvlvppleLESNVSLWlsavsqYKARVTFCSYSVmemcTKGLGA 1261
Cdd:cd12116 160 ERLGLGPGDRL-LAVTTYA---FDI----SL-------------LELLLPLL------AGARVVIAPRET----QRDPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1262 QTGVLRMKGVNlscvrtcMVVAeerprialTQSFSKLFKDLGLPARAVSTtfgcrvnvAIC----LQPNRLGKLAEQGTA 1337
Cdd:cd12116 209 LARLIEAHSIT-------VMQA--------TPATWRMLLDAGWQGRAGLT--------ALCggeaLPPDLAARLLSRVGS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1338 -----GPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------GEIWVSS 1404
Cdd:cd12116 266 lwnlyGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVL---------DAALrpvppgvpGELYIGG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1405 PHNATGYytvYGEEALHADHFSArLSFGDTQTIWARTGYLGFLRRteltdasGGRhdaLYVVGSLDETLELRGMRYHPID 1484
Cdd:cd12116 325 DGVAQGY---LGRPALTAERFVP-DPFAGPGSRLYRTGDLVRRRA-------DGR---LEYLGRADGQVKIRGHRIELGE 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2217337420 1485 IETsVIRAHRSIAECAVFTWTN----LLVVVVELDGLEqdALDLVAL 1527
Cdd:cd12116 391 IEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA--APDAAAL 434
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
357-814 |
3.20e-10 |
|
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: 64.54 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 357 DTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIevpltrk 436
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 437 DAGSQQ--VGFLLGSCGVFLALTTdacQKGLPKAQtgevAAFKGWPPLSWLVIDGKHLAK---PPKDWHPLA-------- 503
Cdd:cd05911 66 NPIYTAdeLAHQLKISKPKVIFTD---PDGLEKVK----EAAKELGPKDKIIVLDDKPDGvlsIEDLLSPTLgeededlp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 504 ---QDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCralTQACGYSEA-----ETLTNVLDFKRDAGLWhGVLTSV 572
Cdd:cd05911 139 pplKDGKDDTAAILY-SS--GTTglpKGVCLSHRNLIANL---SQVQTFLYGndgsnDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 573 MNRMHVVSVPyalmKANPLSWIQKVCFYKARAALVKSRDMHWslLAQRGQRDV-SLSSLRMLIVadGANPWSISSCDAFL 651
Cdd:cd05911 212 LNGATVIIMP----KFDSELFLDLIEKYKITFLYLVPPIAAA--LAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 652 NVFQSRGLRP-----EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPG 726
Cdd:cd05911 284 KRFPNATIKQgygmtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 727 ANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIV 806
Cdd:cd05911 324 VEAKIVDDDGKDSL-GPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIV 390
|
490
....*....|....
gi 2217337420 807 G------KLDGLMV 814
Cdd:cd05911 391 DrkkeliKYKGFQV 404
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1022-1245 |
7.66e-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: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1099
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1100 VLTTQAVtrllrskeAAAAVDIRTWPTILDTDDIPKKKIASvfRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1179
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217337420 1180 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1245
Cdd:cd12114 158 INRRFAVGPDdRVLAL-----SSLSFDL----SVYdifgalsAGATLVLPDEAR-RRDPAHWAELIERH--GVT 219
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
269-810 |
1.39e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 269 RVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSV-LRGEPLTAGVPRPPSLLATLQRwgttq 347
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVFGDQH----- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 348 pkspcltaldttgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPVMfmVAFYGCLLA--ELV 425
Cdd:PRK12316 2029 ------------------LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYV 2081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 426 PVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKgwPPLSWlvidgkhlakppKDW---HPL 502
Cdd:PRK12316 2082 PLDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLD--RDAEW------------ADYpdtAPA 2140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 503 AQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVvsvp 582
Cdd:PRK12316 2141 VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARV---- 2215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 583 yaLMKANPLsWIQKVCFYKARAALVKSRDM---HWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAflnvfQSRGL 659
Cdd:PRK12316 2216 --LIRDDEL-WDPEQLYDEMERHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEAL 2285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 660 RPEVIcpcasspealtvairrppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGANVCVvkLEGTPY 739
Cdd:PRK12316 2286 RPVYL-------------------FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLN 2338
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217337420 740 LCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 810
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLY-----RTGDLARYRADGVVEYLGRID 2404
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
996-1527 |
2.52e-09 |
|
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: 61.49 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 996 AHTTPDHPLFLLLNAkgtvtsTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1075
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1076 PHPqnlgttlptvkmivevsksacvlttqaVTRLLRSKEAAAavdirtwPTILDTDdipkkkiasvfrppsPDVLAYLDF 1155
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1156 SVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPY---CGLgFALWclCSVYSGHQSVLVPPLELEsNVSL 1232
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPFsfdLSV-MDLY--PALASGATLVPVPRDATA-DPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1233 WLSAVSQYKARVTFCSYSVMEMCT--KGLGAQtgvlrmkgvNLSCVRTCMVVAEERPrIALTQSFSKLFkdlglPARAVS 1310
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCLlsPTFTPE---------SLPSLRHFLFCGEVLP-HKTARALQQRF-----PDARIY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1311 TTFgcrvnvaiclqpnrlgklaeqgtaGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVKVIIAhTETKG 1390
Cdd:cd05945 245 NTY------------------------GPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVIL-DEDGR 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1391 PLGDSHLGEIWVSSPHNATGYytvYGEEALHADHFsarlsFGDTQTIWARTGYLGFLrrteltDASGGrhdaLYVVGSLD 1470
Cdd:cd05945 292 PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVRL------EADGL----LFYRGRLD 353
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217337420 1471 ETLELRGMRYHPIDIETSViRAHRSIAECAVFTWTNL-----LVVVVELDGlEQDALDLVAL 1527
Cdd:cd05945 354 FQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKP-GAEAGLTKAI 413
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1022-1538 |
3.13e-09 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 62.18 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1097
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1098 ACVLTTQAVTRLLRSKEAaaavdirtwPTI-LDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1176
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1177 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYKARVT 1245
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1246 FCSYSVMEMCTKGLGAQtgvlrmkgvnLSCVRTCMVVAEerpriALTQSfsklfkdlgLPARAVSTTFGCR-VNvaiclq 1324
Cdd:COG1020 713 NLTPSLLRALLDAAPEA----------LPSLRLVLVGGE-----ALPPE---------LVRRWRARLPGARlVN------ 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1325 pnrLGklaeqgtaGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL------- 1397
Cdd:COG1020 763 ---LY--------GPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL---------DAHLqpvpvgv 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1398 -GEIWVSSPHNATGYytvYGEEALHADHFSArLSFGDTQTIWARTGYLGflRRteltdasggRHD-ALYVVGSLDETLEL 1475
Cdd:COG1020 814 pGELYIGGAGLARGY---LNRPELTAERFVA-DPFGFPGARLYRTGDLA--RW---------LPDgNLEFLGRADDQVKI 878
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217337420 1476 RGMRYHPIDIEtSVIRAHRSIAECAVFTWTN-----LLVVVVELDGLEQDALDLVALVTNVVLEEHYL 1538
Cdd:COG1020 879 RGFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAALLRLALALLLPPYMV 945
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
354-539 |
4.10e-09 |
|
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: 61.04 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 354 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 433
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 434 TrkdagSQQVGFLLGSCGVFLALTtdacqkglpkaqtgeVAAFkgwpplswlvidgKHLAKPPKDWHPLAQDTGTGTAYI 513
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190
....*....|....*....|....*....|..
gi 2217337420 514 EYkTSkeGST---VGVTVSHASLLA---QCRA 539
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKA 159
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
365-565 |
4.65e-09 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.41 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 442
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 443 VGFLLGSCGVFLALTTDACQKGLPKAQtgevaafkgwppLSWLVIDGKHLAKPPKDWhPLAQDTGTGTAYIEYkTSkeGS 522
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217337420 523 T---VGVTVSHASLLAQCRALTQACGYSEAETLTNV--LDFkrDAGLW 565
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1022-1501 |
6.12e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.39 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgTTLP-----TVKMIVEVSK 1096
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPR---TDLAvwaedTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1097 SACVLTT--QAVTRLLRskeaAAAVDIRTWPTILDTDDIpkkkiasvfRPP--SPDVLAYLDFSVSTTGILAGVKMSHAA 1172
Cdd:PRK07768 110 KAVVVGEpfLAAAPVLE----EKGIRVLTVADLLAADPI---------DPVetGEDDLALMQLTSGSTGSPKAVQITHGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1173 TSALCRSIKLQCELYPSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC 1247
Cdd:PRK07768 177 LYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1248 SYSVMEMCTKGLGAQTgvlRMKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnr 1327
Cdd:PRK07768 253 PNFAYALLARRLRRQA---KPGAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYG------------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1328 lgkLAEQGTA------GPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIW 1401
Cdd:PRK07768 316 ---MAEATLAvsfspcGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGLEVRVV-DEDGQVLPPRGVGVIE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1402 VSSPHNATGYYTVYGEEALHADHfsarlsfGdtqtiWARTGYLGFLrrTEltdasGGRhdaLYVVGSLDETLELRGMRYH 1481
Cdd:PRK07768 391 LRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE-----EGE---VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 2217337420 1482 PIDIETSVIRAHRSIAECAV 1501
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
995-1172 |
6.51e-09 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 60.37 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 995 RAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1074
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1075 PPHPQnlgttlPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPkkkiasvfrPPSPDVLAYLD 1154
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 2217337420 1155 FSVSTTGILAGVKMSHAA 1172
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
365-552 |
8.93e-08 |
|
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: 56.53 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 444
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 445 FLLGSCGVFLALTTDACQKGLPkaqtgevaafkGWPPLSWLVIDGKHLAKPPkdwhPLAQDTGTGTAYIEYkTSkeGST- 523
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP-----------AGLPVLLLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GSTg 139
|
170 180 190
....*....|....*....|....*....|.
gi 2217337420 524 --VGVTVSHASLLAQCRALTQACGYSEAETL 552
Cdd:cd12116 140 rpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
995-1178 |
9.35e-08 |
|
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: 56.44 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 995 RAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1074
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1075 PPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEaaaavdirtwpTILDTDDIPKKKIASVFRPP-SPDVLAYL 1153
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLTDRSLAGRAGGLE-----------VAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 2217337420 1154 DFSVSTTGILAGVKMSHAATSALCR 1178
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1022-1528 |
1.56e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 55.78 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1101
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1102 TTqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1181
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1182 LQCELYPSRQIAICldPYCGLGFALWCLCSVYS-GHQSVLVPPLELESNVSLWLSAVSQykaRVTFCSysvmemctkglg 1260
Cdd:cd17643 127 RWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLhGGRLVVVPYEVARSPEDFARLLRDE---GVTVLN------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1261 aQTGvlrmkgvnlSCVRTCMVVAEERPRIALtqsfsklfkdlglPARAVstTFGCRVnvaicLQPNRLGKLAEQ-GTAGP 1339
Cdd:cd17643 190 -QTP---------SAFYQLVEAADRDGRDPL-------------ALRYV--IFGGEA-----LEAAMLRPWAGRfGLDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1340 D--------PTTVYVDMRALRHDRVRLVERGSphslplmeSGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGY 1411
Cdd:cd17643 240 QlvnmygitETTVHVTFRPLDAADLPAAAASP--------IGRPLPGLRVYVL-DADGRPVPPGVVGELYVSGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1412 YtvyGEEALHADHFSArLSFGDTQTIWARTGYLGflRRTeltdaSGGRhdaLYVVGSLDETLELRGMRYHPIDIEtSVIR 1491
Cdd:cd17643 311 L---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL-----PDGE---LEYLGRADEQVKIRGFRIELGEIE-AALA 375
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2217337420 1492 AHRSIAECAVFTWTN------LLVVVVELDGLEQDALDLVALV 1528
Cdd:cd17643 376 THPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRALL 418
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1017-1170 |
4.47e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 54.62 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1017 TATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 1075
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1076 -----PHPQNLGTTLP-----TVKMIvevskSACVLTTQAVTRL----LRSKEAA---AAVDIRTWPTILDTDDIPKKKI 1138
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 2217337420 1139 ASVFRpPSPDVLAYLDFSVSTTGILAGVKMSH 1170
Cdd:PRK05605 211 VSHPR-PTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
394-548 |
7.25e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 53.78 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 394 LKPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEV 473
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 474 AAFKGWPPL--------SWLVIDgkHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACG 545
Cdd:PRK08316 131 VDTLILSLVlggreapgGWLDFA--DWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
...
gi 2217337420 546 YSE 548
Cdd:PRK08316 209 MSA 211
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
365-631 |
8.78e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.19 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 442
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERS--AEMMVGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 443 VGFLLGSCGVFLALTTDACQKGLPKAqtgevaafKGwppLSWLVIDgkhlakPPKDW------HPLAQDTGTGTAYIEYK 516
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPIP--------DG---LASLALD------RDEDWegfpahDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 517 TSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPYALmkANPLSWIQK 596
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIRDDSL--WDPERLYAE 4779
|
250 260 270
....*....|....*....|....*....|....*
gi 2217337420 597 VcfYKARAALVKSRDMHWSLLAQRGQRDVSLSSLR 631
Cdd:PRK12316 4780 I--HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
328-460 |
4.27e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 51.20 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 328 AGVPRPP-------SLLATLQRWGTTQPKSPcltALDTTGkavYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRV 400
Cdd:PRK06178 20 AGIPREPeyphgerPLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFAALLRQRG-------VGAGDRV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 401 ALVFPNSdPvMFMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVFLALTTDA 460
Cdd:PRK06178 87 AVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
988-1502 |
4.51e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 51.25 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1068 CVPVTVrpphpqnlGTTLPT--VKMIVEVSKS-ACVLTTQA-VTRLLRSKEAAAAV---------------DIRTWPTIL 1128
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEqLDKLLEVRDELPSLrhivvldprglrddpRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1129 D--TDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS-RQIAIcldpycgLGFA 1205
Cdd:COG1022 162 AlgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGdRTLSF-------LPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1206 -----LWCLCSVYSGHQSVLVPPLE--------------------LE---SNVSLWLSAVSQYKARVtfcsysvMEMCTK 1257
Cdd:COG1022 235 hvferTVSYYALAAGATVAFAESPDtlaedlrevkptfmlavprvWEkvyAGIQAKAEEAGGLKRKL-------FRWALA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1258 gLGAQTGVLRMKGVNLScvrtcmvvAEERPRIALTQS--FSKLfkdlglpaRAVsttFGCRVNVAIC----LQPNrlgkL 1331
Cdd:COG1022 308 -VGRRYARARLAGKSPS--------LLLRLKHALADKlvFSKL--------REA---LGGRLRFAVSggaaLGPE----L 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1332 AE----------QG-----TAGPdpTTVYvdmralRHDRVRLverGSphslplmeSGKILPGVKVIIAHTetkgplgdsh 1396
Cdd:COG1022 364 ARffralgipvlEGyglteTSPV--ITVN------RPGDNRI---GT--------VGPPLPGVEVKIAED---------- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1397 lGEIWVSSPHNATGYY-----TvygEEALHADhfsarlsfGdtqtiWARTGYLGFLrrteltDASGgrHdaLYVVGSLDE 1471
Cdd:COG1022 415 -GEILVRGPNVMKGYYknpeaT---AEAFDAD--------G-----WLHTGDIGEL------DEDG--F--LRITGRKKD 467
|
570 580 590
....*....|....*....|....*....|..
gi 2217337420 1472 TLELR-GMRYHPIDIEtSVIRAHRSIAECAVF 1502
Cdd:COG1022 468 LIVTSgGKNVAPQPIE-NALKASPLIEQAVVV 498
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1015-1517 |
6.11e-06 |
|
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: 50.54 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1015 TSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPphpqnlgttlptvkmivev 1094
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1095 sksacVLTTQAVTRLLRSKEAAAavdirtwpTILDTDDIpkkkiasvfrppspdvlAYLDFSVSTTGILAGVKMSHAAT- 1173
Cdd:cd05919 68 -----LLHPDDYAYIARDCEARL--------VVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDPl 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1174 ---SALCRSIklqCELYPSRQIaicldpYC--------GLGFALWclCSVYSGHQSVLVPPLELESNVslwLSAVSQYKA 1242
Cdd:cd05919 118 lfaDAMAREA---LGLTPGDRV------FSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1243 RVTFcsysvmemctkglGAQTG---VLRMKGVN---LSCVRTCMVVAEERPRiALTQSFSKLFkdlGLParaVSTTFGCR 1316
Cdd:cd05919 184 TVLY-------------GVPTFyanLLDSCAGSpdaLRSLRLCVSAGEALPR-GLGERWMEHF---GGP---ILDGIGAT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1317 VNVAICLQpNRLGKlAEQGTAGpdpttvyvdmRALRHDRVRLVERgsphslplmesgkilpgvkviIAHTETKGPLGDsh 1396
Cdd:cd05919 244 EVGHIFLS-NRPGA-WRLGSTG----------RPVPGYEIRLVDE---------------------EGHTIPPGEEGD-- 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1397 lgeIWVSSPHNATGYYTVYGEEalhadhfSARLSFGdtqtiWARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELR 1476
Cdd:cd05919 289 ---LLVRGPSAAVGYWNNPEKS-------RATFNGG-----WYRTGDKFCR------DADG----WYTHAGRADDMLKVG 343
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2217337420 1477 GMRYHPIDIEtSVIRAHRSIAECAVftwtnllVVVVELDGL 1517
Cdd:cd05919 344 GQWVSPVEVE-SLIIQHPAVAEAAV-------VAVPESTGL 376
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
365-504 |
6.39e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 444
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217337420 445 FLLGSCGVFLALTT-DACQKGLPKAQTGE-----VAAFKGW-------PPLSWLVIDGKHLAKPPKDWHPLAQ 504
Cdd:PRK08314 102 HYVTDSGARVAIVGsELAPKVAPAVGNLRlrhviVAQYSDYlpaepeiAVPAWLRAEPPLQALAPGGVVAWKE 174
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
331-806 |
1.49e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 49.41 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 331 PRPPSLLATLQRWGTTQPKSpclTALDTTGKAVytlTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDpv 410
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 411 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVFLALTTDacqKGLPkaqtgEVAAFKGWPPL--SWLVID 488
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDS---EFVP-----LLAAILPQLPTvrTVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 489 GKHLAKPPKDWH------------PLAQDTGTGTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEaetlt 553
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 554 nvldfkRDAGLwhgVLTSvMNRMHVVSVPY-ALMKANPLSWIQKVCFYKARAALVKSR--------DMHWSLLAQRGQRD 624
Cdd:PRK06187 208 ------DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDPENLLDLIETERvtfffavpTIWQMLLKAPRAYF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 625 VSLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAVLSmngl 699
Cdd:PRK06187 278 VDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTKRR---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 700 sygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttG 779
Cdd:PRK06187 340 -------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------G 394
|
490 500
....*....|....*....|....*..
gi 2217337420 780 GapifdrpFTRTGLLGFIGPDNLVFIV 806
Cdd:PRK06187 395 G-------WLHTGDVGYIDEDGYLYIT 414
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1026-1515 |
1.72e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 49.36 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1026 RAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLTTQA 1105
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1106 vtrlLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE 1185
Cdd:cd05922 79 ----AADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1186 LYPSRQIAICLdpycglgfalwclcsvysghqsvlvpPLELESNVSLWLSAVSQYKARVTFCSY----SVMEMCTKglga 1261
Cdd:cd05922 155 ITADDRALTVL--------------------------PLSYDYGLSVLNTHLLRGATLVLTNDGvlddAFWEDLRE---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1262 qTGVLRMKGVnlscvrtcmvvaeerPRIaltqsFSKL----FKDLGLPARAVSTTFGCRvnvaicLQPNRLGKLAEqgtA 1337
Cdd:cd05922 205 -HGATGLAGV---------------PST-----YAMLtrlgFDPAKLPSLRYLTQAGGR------LPQETIARLRE---L 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1338 GPDpTTVYV---------DMRALRHDRVRlvERgsPHSLplmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNA 1408
Cdd:cd05922 255 LPG-AQVYVmygqteatrRMTYLPPERIL--EK--PGSI-----GLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVM 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1409 TGYytvygeealhadhfsarlsfgdtqtiWARTGYLGFLRRTELTDASG--GRHDA---LYVVGSLDETLELRGMRYHPI 1483
Cdd:cd05922 324 KGY--------------------------WNDPPYRRKEGRGGGVLHTGdlARRDEdgfLFIVGRRDRMIKLFGNRISPT 377
|
490 500 510
....*....|....*....|....*....|....*.
gi 2217337420 1484 DIETSvIRAHRSIAECAVF----TWTNLLVVVVELD 1515
Cdd:cd05922 378 EIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
995-1254 |
1.93e-05 |
|
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: 49.25 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 995 RAHTTPDHPLFLLLNakgtvtSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1074
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1075 PPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAaavdirtwpTILDTDDIPKKKIASVFRPPSPDVLAYLD 1154
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1155 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1226
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 2217337420 1227 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1254
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
995-1189 |
2.80e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 995 RAHTTPDHPLfLLLNAKgtvtsTATCVQLHKRAERVAAALMEKGrlsVGDH--VALVYPPGVDLIAAFYGCLYCGCVPVT 1072
Cdd:PRK12316 4560 RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEvlVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1073 VRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDI---RTWPTILDTDdiPKKKIAsvfrppsPDV 1149
Cdd:PRK12316 4631 LDPEYPRE------RLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDN 4695
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217337420 1150 LAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS 1189
Cdd:PRK12316 4696 LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPD 4735
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
971-1172 |
3.36e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.89 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 971 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatcvQLHKRAERVAAALMEKGrLSVGDHVALVY 1050
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1051 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDt 1130
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQG- 588
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217337420 1131 ddipkkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1172
Cdd:PRK10252 589 --------AAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
964-1189 |
3.48e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.80 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 964 RIAQASGRELAHLEDSDQARKFLFLADvlqWRAHTTP---DHPLFLLLNAKGTVTSTATCV----------QLHKRAERV 1030
Cdd:PRK12316 1965 QMAEDAQAALGELALLDAGERQRILAD---WDRTPEAyprGPGVHQRIAEQAARAPEAIAVvfgdqhlsyaELDSRANRL 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1031 AAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVT-RL 1109
Cdd:PRK12316 2042 AHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLLTQRHLLeRL 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1110 -----LRSKEAAAAVDIRTWPtildtDDIPKKKIAsvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQC 1184
Cdd:PRK12316 2115 plpagVARLPLDRDAEWADYP-----DTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
|
....*
gi 2217337420 1185 ELYPS 1189
Cdd:PRK12316 2183 ELSPA 2187
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
340-816 |
3.58e-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: 47.99 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 340 LQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPvmFMVAFYGC 419
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS------LTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 420 LLAELVPVPIEVPLTRKDagsqqVGFLLGSCGvflalttdacqkglpkaqtgevaafkgwpplSWLVIDgkhlakppkDw 499
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSG-------------------------------AKVLFD---------D- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 500 hplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETL--------TNVLDFKRDAGLWHGV 568
Cdd:cd17631 100 ----------LALLMY-TS--GTTgrpKGAMLTHRNLLWNAVNALAALDLGPDDVLlvvaplfhIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 569 LTSVMNRMHVVSVpyalmkanpLSWIQ--KVCFykarAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVADGANPwsiss 646
Cdd:cd17631 167 TVVILRKFDPETV---------LDLIErhRVTS----FFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMP----- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 647 cDAFLNVFQSRGLRpevICPCASSPEALTVAIRRPPDlggppprkavlsmnglsygvirvDTEEKLSvltvqDVGQVMPG 726
Cdd:cd17631 227 -ERLLRALQARGVK---FVQGYGMTETSPGVTFLSPE-----------------------DHRRKLG-----SAGRPVFF 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 727 ANVCVVKLEGTPylCKTDEVGEICVSSSATGTAYYGLlgitknvfeavPVTTGGApIFDRPFtRTGLLGFIGPDNLVFIV 806
Cdd:cd17631 275 VEVRIVDPDGRE--VPPGEVGEIVVRGPHVMAGYWNR-----------PEATAAA-FRDGWF-HTGDLGRLDEDGYLYIV 339
|
490
....*....|
gi 2217337420 807 GKLDGLMVTG 816
Cdd:cd17631 340 DRKKDMIISG 349
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
992-1528 |
8.92e-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: 46.83 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 992 LQWRAHTTPDHPLFLLLNakgtvtSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1071
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1072 tvrpphPQNLGTTLPTVKMIVEVSKSACVLttqavtrllrskeaaaavdirtwptildtDDipkkkiasvfrppspdvLA 1151
Cdd:cd17631 74 ------PLNFRLTPPEVAYILADSGAKVLF-----------------------------DD-----------------LA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1152 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELyPSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLVPPLELESnv 1230
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1231 slWLSAVSQYKARVTFCSYSVME-MCTKGlgaqtgvlRMKGVNLSCVRtCMVVAEERPRIALTQSFsklfKDLGLparAV 1309
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1310 STTFGcrvnvaiclqpnrlgklaeQGTAGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVKVIIAHTETK 1389
Cdd:cd17631 241 VQGYG-------------------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1390 gPLGDSHLGEIWVSSPHNATGYytvYGEEALHADhfsarlSFGDTqtiWARTGYLGFLrrteltDASGgrhdALYVVGSL 1469
Cdd:cd17631 286 -EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRK 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217337420 1470 DETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV-VVVELDGLEQDALDLVALV 1528
Cdd:cd17631 343 KDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELIAHC 406
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
529-905 |
9.30e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.07 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 529 SHASLLAQCRALTQACGyseaetltnvLDFKRDAG-----LWHG-----VLTSVMNRMHVVSVPYALMKANPLSWIQKVC 598
Cdd:PRK05851 173 SPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 599 fyKARAALVKSRDMHWSLLAQRGQR--DVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPC---ASSPEA 673
Cdd:PRK05851 243 --DSRATLTAAPNFAYNLIGKYARRvsDVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSyglAESTCA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 674 LTVairrppdlggPPPrkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSS 753
Cdd:PRK05851 319 VTV----------PVP--------GIGLRVDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIRG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 754 SATGTAYygllgitknvfeavpvtTGGAPIFDRPFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDVVATALAVE 833
Cdd:PRK05851 380 ASMMSGY-----------------LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217337420 834 PmkfVYRGRIavfsVTVLHDD-----RIVLVAEQRpdASEEDSFQwmSRVLQAIDSihQVGVyclalVPANTLPKAP 905
Cdd:PRK05851 442 G---VREGAV----VAVGTGEgsarpGLVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDVVFVAP 500
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
351-810 |
1.10e-04 |
|
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: 46.47 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 351 PCLTALDTTGKavyTLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVPIe 430
Cdd:cd05945 5 PDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVPL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 431 vpltrkDAGSqqvgfllgscgvflalttdacqkglPKAQTGEVAAfkgwpplswlvidgkhLAKPpkdwhPLAQDTGTGT 510
Cdd:cd05945 72 ------DASS-------------------------PAERIREILD----------------AAKP-----ALLIADGDDN 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 511 AYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLwHGVLTSVMNRMHVVSVPYAlMK 587
Cdd:cd05945 100 AYIIF-TS--GSTgrpKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPVPRD-AT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 588 ANPLSWIqkvcfykarAALVKSRDMHWsllaqrgqrdVSL-SSLRMLIVADGANPWSISSCDAFLnvFqsrglrpevicp 666
Cdd:cd05945 175 ADPKQLF---------RFLAEHGITVW----------VSTpSFAAMCLLSPTFTPESLPSLRHFL--F------------ 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 667 CAsspEALTVA-----IRRPPD-----LGGPPPrkavlSMNGLSYGVIrvdTEEKLSVLTVQDVGQVMPGANVCVVKLEG 736
Cdd:cd05945 222 CG---EVLPHKtaralQQRFPDariynTYGPTE-----ATVAVTYIEV---TPEVLDGYDRLPIGYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217337420 737 TPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 810
Cdd:cd05945 291 RP--VPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAY-----RTGDLVRLEADGLLFYRGRLD 353
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
988-1077 |
1.13e-04 |
|
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: 46.68 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 2217337420 1068 CVPVTVRPPH 1077
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
364-542 |
1.33e-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: 46.50 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 364 YTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsq 441
Cdd:cd12114 11 GTLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 442 qvgfLLGSCGVFLALTTDACQKGLPKAqtgevaafkgwPPLSWLVIDGKHLAKPPKDWHPLAQDTgtgtAYIEYkTSkeG 521
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAV-----------FDVLILDLDALAAPAPPPPVDVAPDDL----AYVIF-TS--G 136
|
170 180
....*....|....*....|....
gi 2217337420 522 ST---VGVTVSHASLLAQCRALTQ 542
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINR 160
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1022-1173 |
1.64e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 46.05 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1092
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1093 EVSKSA--CVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiasVFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1170
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 2217337420 1171 AAT 1173
Cdd:PRK07656 189 RQL 191
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
366-885 |
1.67e-04 |
|
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: 45.93 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 366 LTYGKLWSRSLKLAYTLLNKLTSKnepllkpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqQVGF 445
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 446 LLGSCGVFLALTTDACQKglpkaqtgevaafkgwpplswlvidgkhlakppkdwhplaqdtgtgTAYIEYKTSKEGSTVG 525
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 526 VTVSHASLLAQcrALTQACGY--SEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVVSVPYALMKanplSWIQKVcfykAR 603
Cdd:cd05935 102 CMHTHFSAAAN--ALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMA----RWDRET----AL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 604 AALVKSRDMHWS--------LLAQRGQRDVSLSSLRMLivADGANPWSISSCDAFLNVFqsrGLRPEVIcpcasspEALT 675
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL--TGGGAPMPPAVAEKLLKLT---GLRFVEG-------YGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 676 VAIrrPPDLGGPPPRKAVLSMnglsyGVIRVDTEEKlsVLTVQDVGQVMPGanvcvvklegtpylcktdEVGEICVSSSA 755
Cdd:cd05935 235 ETM--SQTHTNPPLRPKLQCL-----GIP*FGVDAR--VIDIETGRELPPN------------------EVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 756 TGTAYYGLLGITKNVFeavpVTTGGapifdRPFTRTGLLGFIGPDNLVFIVGKLDGLM-VTGVRRHNADdvVATALAVEP 834
Cdd:cd05935 288 IFKGYWNRPEETEESF----IEIKG-----RRFFRTGDLGYMDEEGYFFFVDRVKRMInVSGFKVWPAE--VEAKLYKHP 356
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 835 mkfvyrgriAVFSVTVLH--DDR--------IVLVAEQRPDASEEDSFQW----MS-----RVLQAIDSI 885
Cdd:cd05935 357 ---------AI*EVCVISvpDERvgeevkafIVLRPEYRGKVTEEDIIEWareqMAaykypREVEFVDEL 417
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
360-539 |
2.14e-04 |
|
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: 45.82 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 360 GKAVY-----TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLT 434
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 435 rkdagSQQVGFLLGSCGVFLALTTDACqkgLPKAQTgevAAFKGWPPLSWLVIDGKHLAKPPKDWhpLAQDTGTGT---- 510
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGEL---APVLAA---ALTKSEHTLVVLIVSGGAGPEAGALL--LAELVAAEAeqlk 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217337420 511 ---------AYIEYKTSKEGSTVGVTVSHASLLAQCRA 539
Cdd:cd05959 157 paathaddpAFWLYSSGSTGRPKGVVHLHADIYWTAEL 194
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
319-657 |
2.34e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.10 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 319 SVLRGEPLTAGVPRppSLLATLQRwgttQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGD 398
Cdd:PRK12316 502 ATAAEYPLQRGVHR--LFEEQVER----TPEAPALAFGEET------LDYAELNRRANRLAHALI-------ERGVGPDV 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 399 RVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAF 476
Cdd:PRK12316 563 LVGVAMERSIEMV--VALLAILKAggAYVPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDL 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 477 KgwPPLSWLviDGKHLAKPPKDWHPLaqdtgtGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVL 556
Cdd:PRK12316 634 D--RPAAWL--EGYSEENPGTELNPE------NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKT 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 557 DFKRDAGLWHGVLTsVMNRMHVVSVPYALMKaNPLSWIQkvcfYKARAAlVKSRDMHWSLLA--QRGQRDVSLSSLRMLI 634
Cdd:PRK12316 704 PFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVE----LINREG-VDTLHFVPSMLQafLQDEDVASCTSLRRIV 776
|
330 340
....*....|....*....|...
gi 2217337420 635 VADGANPWsisscDAFLNVFQSR 657
Cdd:PRK12316 777 CSGEALPA-----DAQEQVFAKL 794
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
990-1523 |
2.44e-04 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 45.58 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 990 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCV 1069
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1070 PVTVRPP-HPQNLGTTLPTVKM---IVEVSKSACVLTTQAVTRLLRskeaaAAVDIRTWPTILDTDDIPkkkiasvFRPP 1145
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMtaaVIAVDAQVMDAIFQSGVRVLA-----LSDLVGLGEPESAGPLIE-------DPPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1146 SPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCEL-YPSRQIAICLDP-YCGLGF-ALWCLCSVYSGhqsVLVP 1222
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrHGRHNVVLGLMPlYHVIGFfAVLVAALALDG---TYVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1223 PLELESNVSLWLSAvsqyKARVTfCSYSVMEMctkgLGAQTGVLRMKGVNLSCVRTcmvvaeerprialtqsfsklfkdL 1302
Cdd:cd05923 225 VEEFDPADALKLIE----QERVT-SLFATPTH----LDALAAAAEFAGLKLSSLRH-----------------------V 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1303 GLPARAVSTTFGCRVNVAIclqPNRlgKLAEQGTA-------GPDPTTVYVdMRALRHDRVRLVERG--SPHSLPLMESG 1373
Cdd:cd05923 273 TFAGATMPDAVLERVNQHL---PGE--KVNIYGTTeamnslyMRDARTGTE-MRPGFFSEVRIVRIGgsPDEALANGEEG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1374 KIlpgvkvIIAHTetkgplGDSHLGEIWvsSPHNATgyytvygeealhadhfSARLSFGdtqtiWARTGylgflrRTELT 1453
Cdd:cd05923 347 EL------IVAAA------ADAAFTGYL--NQPEAT----------------AKKLQDG-----WYRTG------DVGYV 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217337420 1454 DASGgrhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV--VVVELDGLEQDALD 1523
Cdd:cd05923 386 DPSG----DVRILGRVDDMIISGGENIHPSEIE-RVLSRHPGVTEVVVIgvadeRWGQSVTacVVPREGTLSADELD 457
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
720-823 |
2.50e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 45.72 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 720 VGQVMPGANVCVVKLEGT-PYL--CKTDEVGEICVSssatgtayygllgiTKNVFEA-VPVTTGGAPIFDRPFTRTGLLG 795
Cdd:PRK07529 388 VGLRLPYQRVRVVILDDAgRYLrdCAVDEVGVLCIA--------------GPNVFSGyLEAAHNKGLWLEDGWLNTGDLG 453
|
90 100
....*....|....*....|....*...
gi 2217337420 796 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 823
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLIIRG--GHNID 479
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1016-1500 |
2.57e-04 |
|
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: 45.53 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1016 STATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP-PHPQNLGTTLptvkmivev 1094
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQCL--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1095 sksacvlttqavtrllrsKEAAAAVDIrtwptildtdDIPKKkiasvfrppspDVLAYLDFSVSTTGILAGVKMSHAATS 1174
Cdd:cd05910 71 ------------------QEAEPDAFI----------GIPKA-----------DEPAAILFTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1175 ALCRSIKlqcELYPSRQIAICLDpycglGFALWCLCSVYSGHQSVlVPPLE----LESNVSLWLSAVSQYKARVTFCSYS 1250
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1251 VMEMCTKgLGAQtgvlrmKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDlglpARAVSTTFGCRVNVAICLqpnrlgk 1330
Cdd:cd05910 183 LLERVAR-YCAQ------HGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----EAEILTPYGATEALPVSS------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1331 laeqgtagpdpttvyVDMRALRHDRVRLVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWV 1402
Cdd:cd05910 244 ---------------IGSRELLATTTAATSGGAGTCV-----GRPIPGVRVrIIEIDDEPIAewddtleLPRGEIGEITV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1403 SSPHNATGYYTVYGEEALHADHFSArlsfgdtQTIWARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELRGMRYHP 1482
Cdd:cd05910 304 TGPTVTPTYVNRPVATALAKIDDNS-------EGFWHRMGDLGYL------DDEG----RLWFCGRKAHRVITTGGTLYT 366
|
490
....*....|....*...
gi 2217337420 1483 IDIEtSVIRAHRSIAECA 1500
Cdd:cd05910 367 EPVE-RVFNTHPGVRRSA 383
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1373-1501 |
2.63e-04 |
|
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: 44.94 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1373 GKILPGVKVIIAHTETKGPLGDSHlGEIWVSSPHNATGYYTvygEEALHADHFSARlsfgdtqtiWARTGYLGFLRrtel 1452
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2217337420 1453 tdasggRHDALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1501
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
355-437 |
3.65e-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: 45.00 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 355 ALDTTGKAVyTLTYGKLwsrsLKLAYTLLNKLTSKNeplLKPGDRVALVFPNSDPvmFMVAFYGCLLAELVPVPIEvPLT 434
Cdd:cd05926 5 ALVVPGSTP-ALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVAPLN-PAY 73
|
...
gi 2217337420 435 RKD 437
Cdd:cd05926 74 KKA 76
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
324-540 |
4.22e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 44.75 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 324 EPLTAGVPRP------PSLLATL----QRWGTtqpkSPCLTALdttGKavyTLTYGKLWSRSLKLAYTLlnkltsKNEPL 393
Cdd:PRK05677 8 DKYPAGIAAEinpdeyPNIQAVLkqscQRFAD----KPAFSNL---GK---TLTYGELYKLSGAFAAWL------QQHTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 394 LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV-------PIEVPLTRKDAGSQQVgfllgscgVFLALTTDACQKGLP 466
Cdd:PRK05677 72 LKPGDRIAVQLPNV--LQYPVAVFGAMRAGLIVVntnplytAREMEHQFNDSGAKAL--------VCLANMAHLAEKVLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 467 KAQ-----TGEVAAFKgwPPLSWLVIDG--KHLAKPPKDWH-------PLAQDTGTG------------TAYIEYKTSKE 520
Cdd:PRK05677 142 KTGvkhviVTEVADML--PPLKRLLINAvvKHVKKMVPAYHlpqavkfNDALAKGAGqpvteanpqaddVAVLQYTGGTT 219
|
250 260
....*....|....*....|...
gi 2217337420 521 GSTVGVTVSHASLLA---QCRAL 540
Cdd:PRK05677 220 GVAKGAMLTHRNLVAnmlQCRAL 242
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
988-1500 |
5.71e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 44.50 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLLLNAKGTVT----STATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGC 1063
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1064 LYCGCVPVTVRPphpqnlGTTLPTVKMIVEVSKSACVLT---TQAVTRLLRSKEAAA----AVDIRTWPTILDTDDIPKK 1136
Cdd:PRK09274 87 FKAGAVPVLVDP------GMGIKNLKQCLAEAQPDAFIGipkAHLARRLFGWGKPSVrrlvTVGGRLLWGGTTLATLLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1137 KIASVFRPP--SPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKlqcELYPSRQIAICL---------DPYCGLgfa 1205
Cdd:PRK09274 161 GAAAPFPMAdlAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfGPALGM--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1206 lwclCSVysghqsvlVPPLEL----ESNVSLWLSAVSQYKARVTFCSYSVMEMCTkglgaQTGvlRMKGVNLSCVRTcMV 1281
Cdd:PRK09274 235 ----TSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLG-----RYG--EANGIKLPSLRR-VI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1282 VAEERPRIALTQSFSKLfkdlgLPARA-VSTTFGCRVNVAICLqpnrlgklaeqgtagpdpttvyVDMRALRHDRVRLVE 1360
Cdd:PRK09274 295 SAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS----------------------IESREILFATRAATD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1361 RGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWVSSPHNATGYYTvyGEEALHAdhfsARLSFG 1432
Cdd:PRK09274 348 NGAGICV-----GRPVDGVEVrIIAISDAPIPewddalrLATGEIGEIVVAGPMVTRSYYN--RPEATRL----AKIPDG 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217337420 1433 DTQtIWARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECA 1500
Cdd:PRK09274 417 QGD-VWHRMGDLGYL------DAQG----RLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
354-582 |
5.83e-04 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 44.20 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 354 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLTSKnepllkPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI---- 429
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKDL------RGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLnpsy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 430 ---EVPLTRKDAGSQqvgfllgscgvflalttdacqkglpkaqtgevaafkgwpplswLVIDGkhlakppkdwhplaqdt 506
Cdd:cd05941 72 plaELEYVITDSEPS-------------------------------------------LVLDP----------------- 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217337420 507 gtgtAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVP 582
Cdd:cd05941 92 ----ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
364-427 |
1.10e-03 |
|
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: 43.60 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217337420 364 YTLTYGKLWSRSLKLAYTLLNkltsknepL-LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 427
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
988-1170 |
1.20e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 43.49 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1068 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLTTQAVTRLLRSKEAAAAV---DIRTWPTILDT 1130
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217337420 1131 DDI------PKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1170
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1338-1522 |
2.41e-03 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 42.30 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1338 GPDPTTVYVDMRALrhdrvrlvERGSPHSLplmesGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGE 1417
Cdd:cd17653 240 GPTECTISSTMTEL--------LPGQPVTI-----GKPIPNSTCYIL-DADLQPVPEGVVGEICISGVQVARGY---LGN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1418 EALHADHFsARLSFGDTQTIWaRTGYLGFLRRteltdaSGGrhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIA 1497
Cdd:cd17653 303 PALTASKF-VPDPFWPGSRMY-RTGDYGRWTE------DGG----LEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
|
170 180
....*....|....*....|....*
gi 2217337420 1498 ECAVFTWTNLLVVVVELDGLEQDAL 1522
Cdd:cd17653 371 QAAAIVVNGRLVAFVTPETVDVDGL 395
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1372-1501 |
2.97e-03 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 41.95 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1372 SGKILPGVKVIIAHtETKGPLGDshlGEIWVSSPHNATGYY--TVYGEEAlhadhfsarlsfgdTQTIWARTGYLGFLrr 1449
Cdd:cd05912 244 AGKPLFPVELKIED-DGQPPYEV---GEILLKGPNVTKGYLnrPDATEES--------------FENGWFKTGDIGYL-- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217337420 1450 teltDASGgrhdALYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAV 1501
Cdd:cd05912 304 ----DEEG----FLYVLDRRSDLIISGGENIYPAEIEE-VLLSHPAIKEAGV 346
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
365-427 |
3.10e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.96 E-value: 3.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 427
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1022-1073 |
3.12e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 42.02 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2217337420 1022 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1073
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
988-1171 |
3.91e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 41.67 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 988 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCVQlhkRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1067
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1068 CVPVtvrpphPQNLGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAA----------AVDIRTWPTILDTDDIPKKK 1137
Cdd:PRK06155 96 AIAV------PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwlldAPASVSVPAGWSTAPLPPLD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 2217337420 1138 IASVFRPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1171
Cdd:PRK06155 170 APAPAAAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
340-429 |
4.67e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 41.64 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 340 LQRWGTTQPKSPCLTALDTTGKAVyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 419
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA----NALRALG---VKKGDRVAIYLPNI--PEAVIAMLAC 84
|
90
....*....|
gi 2217337420 420 LLAELVPVPI 429
Cdd:COG0365 85 ARIGAVHSPV 94
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
329-533 |
5.10e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 329 GVPRPPSLLATL---QRWGTtqPKSPCLTAldttgkAVYTLTYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRVALVFP 405
Cdd:PRK10252 452 AVEIPETTLSALvaqQAAKT--PDAPALAD------ARYQFSYREMREQVVALANLL-------RERGVKPGDSVAVALP 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 406 NSdpVMFMVAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPls 483
Cdd:PRK10252 517 RS--VFLTLALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA-- 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217337420 484 wlvidgkhlakpPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASL 533
Cdd:PRK10252 586 ------------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
365-429 |
5.44e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 41.04 E-value: 5.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI 429
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPL 85
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
365-543 |
5.58e-03 |
|
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: 41.18 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 365 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQQVG 444
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARGV-------GPGDLVALCARRS--AELVVALLAILKAGAAYVPLDP-----AYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 445 FLLGSCGVFLALTTDACQKGLPkaqtgeVAAFKGWPplswlvIDGKHLAKPPKDWHPLAQDTGTgTAYIEYkTSkeGST- 523
Cdd:cd17651 86 FMLADAGPVLVLTHPALAGELA------VELVAVTL------LDQPGAAAGADAEPDPALDADD-LAYVIY-TS--GSTg 149
|
170 180
....*....|....*....|..
gi 2217337420 524 --VGVTVSHASLLAQCRALTQA 543
Cdd:cd17651 150 rpKGVVMPHRSLANLVAWQARA 171
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
995-1105 |
6.61e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 40.83 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 995 RAHTTPDHPLFlLLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVr 1074
Cdd:PRK13391 6 HAQTTPDKPAV-IMASTGEVVTYR---ELDERSNRLAHLFRSLG-LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV- 79
|
90 100 110
....*....|....*....|....*....|.
gi 2217337420 1075 pphpqNLGTTLPTVKMIVEVSKSACVLTTQA 1105
Cdd:PRK13391 80 -----NSHLTPAEAAYIVDDSGARALITSAA 105
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
720-834 |
6.90e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 40.54 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 720 VGQVMPGANVCVVKLEGTPYL---CKTDEVGEICVSSsatgtayygllgitKNVFEAVPVTTGGAPIFDRP-FTRTGLLG 795
Cdd:cd05944 176 VGLRLPYARVRIKVLDGVGRLlrdCAPDEVGEICVAG--------------PGVFGGYLYTEGNKNAFVADgWLNTGDLG 241
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2217337420 796 FIGPDNLVFIVGKLDGLMVTGvrRHNADDV-VATALAVEP 834
Cdd:cd05944 242 RLDADGYLFITGRAKDLIIRG--GHNIDPAlIEEALLRHP 279
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1372-1501 |
8.00e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 40.72 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1372 SGKILPGVKVIIAHTETKGPLGDShlGEIWVSSPHNATGYYtvYGEEALHAdhfsarlSFGDTqtiWARTGYLGFLrrte 1451
Cdd:PRK03640 309 AGKPLFPCELKIEKDGVVVPPFEE--GEIVVKGPNVTKGYL--NREDATRE-------TFQDG---WFKTGDIGYL---- 370
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1452 ltDASGgrhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1501
Cdd:PRK03640 371 --DEEG----FLYVLDRRSDLIISGGENIYPAEIE-EVLLSHPGVAEAGV 413
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1373-1502 |
8.44e-03 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 40.35 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217337420 1373 GKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYY-----TvygEEALHADHfsarlsfgdtqtiWARTGYLGFL 1447
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217337420 1448 rrteltDASGgrhdALYVVG-SLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF 1502
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVI 375
|
|
| |
