|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
994-1558 |
0e+00 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 736.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 994 LFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 1072
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1073 TTLPTVKMivEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVA-----SIFRPPSPDVLAYLDFSV 1147
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1148 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1227
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1228 SQYKARVTFCSYSVMEMCTKGLGAQTGALRMKGVNLSCVRTCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRV 1307
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1308 NVAICLQGTTGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHN 1387
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1388 ATGYYTVYGEETLHADHF-SARLSFGDTQTIWARTGYLGFLRRTELTDASGERHDALYVVGSLDETLELRGMRYHPIDIE 1466
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFpSTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1467 TSVIRAHRSIAECAVFTWTNLLVVVVELD-GLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINSRGEKQRMHLR 1545
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 359807008 1546 DGFLADQLDPIYV 1558
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
342-918 |
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 359807008 342 CLTALDTAGKATCTLTYGKLWSRSLKLAYTLLNKLTskneplLNPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 421
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 422 PLtrkdaGSQQVGFLLGSCGVTLALTTDACQKGLPKA-----PTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQDT 496
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 497 GSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIPYALM 576
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 577 KVNPLSWIQKVCSYKARAALVKSRDMHWSL------LAQRGQRDVCLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 650
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 651 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGASVCVVKVDGaP 728
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPET-K 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 729 YLCKTDEIGEICVNSVATGTAYYGLLGITKNTFETVPVTADGVPVSDRPFTRTGLLGFIGP----------DNLVFVVGK 798
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 799 LDGLMVVGVRRHNADDIVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 878
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 359807008 879 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 918
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
984-1516 |
1.62e-65 |
|
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: 232.90 E-value: 1.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 984 WRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1063
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1064 RPPHPqnlGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWptiLDTDDIPKKKVASIFRPPS--PDVLA 1141
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---LLVVDLLPDTSAADWPPPSpdPDDIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1142 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESN 1219
Cdd:cd05931 153 YLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1220 VSLWLSAVSQYKARVT----FcSYsvmEMCT-KGLGAQTGALrmkgvNLSCVRTCMVVAeERPRISLTQSFSKLFKDLGL 1294
Cdd:cd05931 231 PLRWLRLISRYRATISaapnF-AY---DLCVrRVRDEDLEGL-----DLSSWRVALNGA-EPVRPATLRRFAEAFAPFGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1295 PARAVSTTFG---CRVNVAIclqGTTGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGP 1371
Cdd:cd05931 301 RPEAFRPSYGlaeATLFVSG---GPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1372 LGDSHLGEIWVSSPHNATGYYTVyGEETlhADHFSARLSFGDtqTIWARTGYLGFLRRteltdasGErhdaLYVVGSLDE 1451
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGYWGR-PEAT--AETFGALAATDE--GGWLRTGDLGFLHD-------GE----LYITGRLKD 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359807008 1452 TLELRGMRYHPIDIETSVIRAHRSIAE--CAVFTW----TNLLVVVVELDGLeQDALDLVALVTNV---VLEEH 1516
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
333-909 |
2.09e-65 |
|
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: 232.51 E-value: 2.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 333 WGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLLnkltsknePLLNPGDRVALVFPNSdpVMFMVAFYGCLLA 412
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 413 ELVPVPIEVPLTRKDAgsQQVGFLLGSCGVTLALTTDACQKGLPKAptgeVATFKGWPPLAWLVIDGKHLTrPPKDWyPL 492
Cdd:cd05931 72 GAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADW-PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 493 AQDTGSRTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMH-V 568
Cdd:cd05931 144 PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPsV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 569 ITIPYALMKvNPLSWIQKVCSYKAR--AAlvksRDMHWSLLAQRGQR----DVCLSSLRMLIVadGANPWSISSCDAFLN 642
Cdd:cd05931 221 LMSPAAFLR-RPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 643 VFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPGASVCV 721
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 722 VKVDGAPyLCKTDEIGEICV--NSVATGtaYYGLLGITKNTFETVPVTADGvpvsdrPFTRTGLLGFIGPDNLvFVVGKL 799
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVrgPSVASG--YWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 800 DGLMVVGVRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVG 879
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVA 516
|
570 580 590
....*....|....*....|....*....|
gi 359807008 880 VYCLALVPANTLPKAPLGGIHISETKQRFL 909
Cdd:cd05931 517 PADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
982-1456 |
6.85e-50 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 183.28 E-value: 6.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 982 LQWRAHTTPDHPLFlllnAKGTVTSTaTCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1061
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1062 TVrpphpqNLGTTLPTVKMIVEVSKSACVLsTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPK-----------KKVAS 1130
Cdd:pfam00501 75 PL------NPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1131 IFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1206
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1207 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAeERPRISLTQSFS 1286
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1287 KLFkdlglpARAVSTTFGCRVNVAICLQGTTGPDPTTVYvdmralrhdrvrlverGSphslplmeSGKILPGVKVIIAHT 1366
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLRSL----------------GS--------VGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1367 ETKGPLGDSHLGEIWVSSPHNATGYytvYGEETLHADHFsarlsfgdTQTIWARTGYLGFLrrteltDASGErhdaLYVV 1446
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DEDGY----LEIV 407
|
490
....*....|
gi 359807008 1447 GSLDETLELR 1456
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
978-1498 |
1.50e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 139.15 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1058 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLSTQAITRLLKSKEAAAAVDVrtwPTILDTDDIPkKKVASI 1131
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD-PALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1132 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1206
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1207 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEmctkglgaqtGALrmKGVNLSCVRTCMVVAEERPR 1278
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSE----------SAL--ERLDLSRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1279 ISLtQSFSKLFKDLGLPARAVSTTFGCRVNVAICLQGTTGPDPTTVYVDMRALRHDRVRLVErGSphslPLMESGKILPG 1358
Cdd:PRK05691 305 DSL-ERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGT-GS----VLMSCGRSQPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1359 VKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTvYGEETlhADHFSARlsfgDTQTiWARTGYLGFLRRTEltdasge 1438
Cdd:PRK05691 379 HAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEAS--AKTFVEH----DGRT-WLRTGDLGFLRDGE------- 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1439 rhdaLYVVGSLDETLELRGMRYHPIDIETSVIRahrsiaECAVFTWTNLLVVVVELDGLE 1498
Cdd:PRK05691 444 ----LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1140-1508 |
2.66e-32 |
|
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: 129.33 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1140 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1216
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1217 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEERPrISLTQSFSKLFKDlglpa 1296
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1297 rAVSTTFGcrvnvaiclQGTTGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVKVIIAHTETkGPLGDSH 1376
Cdd:cd04433 141 -KLVNGYG---------LTETGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVDPDG-GELPPGE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1377 LGEIWVSSPHNATGYYTVygeetlhadhfsARLSFGDTQTIWARTGYLGFLRrteltdasgeRHDALYVVGSLDETLELR 1456
Cdd:cd04433 194 IGELVVRGPSVMKGYWNN------------PEATAAVDEDGWYRTGDLGRLD----------EDGYLYIVGRLKDMIKSG 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 359807008 1457 GMRYHPIDIETsVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1508
Cdd:cd04433 252 GENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHV 308
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
325-909 |
1.14e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 132.37 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 325 SLLAALQLWGTTQPKAPCLT----ALDTAGKATcTLTYGKLWSRSLKLAYTLlNKLTSknepllnPGDRVALVFPNSdpV 400
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVAE-TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 401 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVTLALTTDACqkglpkapTGEVATF----KGWPPLAWLV 476
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 477 IDGKHLTRPPKdwYPLAQDTGSRTAYIEYkTSkeGST---VGVTVSHSSLLAQC-QALTQACGYTEAE-----TLTNVLD 547
Cdd:PRK05850 141 VDLLDLDSPRG--SDARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 548 FKRDAGLWHGVLTSVMNRMH-VITIPYALMKvNPLSWIQkvcsykaraaLVKSRDMHWSL-------LAQRGQRDVCLSS 619
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 620 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 695
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 696 VDTeEKLSvltvqdVGQVMP-----GASVCVVKVDGAPYL----------CKTDEIGEICVN--SVATGtaYYGLLGITK 758
Cdd:PRK05850 349 FDY-EKLS------AGHAKRcetggGTPLVSYGSPRSPTVrivdpdtcieCPAGTVGEIWVHgdNVAAG--YWQKPEETE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 759 NTFETVPVT-ADGVPVSdrPFTRTGLLGFIGPDNLvFVVGKLDGLMVVGVRRHNADDIVATalavepMKFVYRGRIAVFS 837
Cdd:PRK05850 420 RTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAIS 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359807008 838 VTVLHDDRIVLVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFL 909
Cdd:PRK05850 491 VPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYR 567
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
978-1508 |
2.20e-29 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 123.38 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1058 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtddipkkkVASIFrppsp 1137
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALV------------------------------------TALIL----- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1138 dvlayldFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1216
Cdd:COG0318 107 -------YT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1217 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEerpriSLTQSFSKLFKDLglpa 1296
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1297 ravsttFGCRVnvaicLQG---T-TGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVKVIIAHTETKgPL 1372
Cdd:COG0318 239 ------FGVRI-----VEGyglTeTSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRIVDEDGR-EL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1373 GDSHLGEIWVSSPHNATGYYTvYGEETlhadhfsaRLSFGDTqtiWARTGYLGFLrrteltDASGErhdaLYVVGSLDET 1452
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWN-DPEAT--------AEAFRDG---WLRTGDLGRL------DEDGY----LYIVGRKKDM 348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359807008 1453 LELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1508
Cdd:COG0318 349 IISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELRAFL 409
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
326-815 |
7.49e-29 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 121.84 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 326 LLAALQLWGTTQPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSDPvmFMVA 405
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 406 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGVTLALTtdacqkglpkaptgevatfkgwpplawlvidgkhltrp 485
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVT-------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 486 pkdwyplaqdtgsrtAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSV 562
Cdd:COG0318 103 ---------------ALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 563 MNRMHVITIPyalmKVNPLSWIQKVCSYKA-RAALVKSrdMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFL 641
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 642 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGASVC 720
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 721 VVKVDGAPylCKTDEIGEICV--NSVATGtaYYGLLGITKNTFetvpvtADGvpvsdrpFTRTGLLGFIGPDNLVFVVGK 798
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVrgPNVMKG--YWNDPEATAEAF------RDG-------WLRTGDLGRLDEDGYLYIVGR 344
|
490
....*....|....*..
gi 359807008 799 LDGLMVVGVRRHNADDI 815
Cdd:COG0318 345 KKDMIISGGENVYPAEV 361
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
356-915 |
6.52e-28 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 120.88 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 356 LTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LTRKDAGSQQV 433
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 434 GFLLGSCGVTLALTTDACQKGLPKAPTGEvatfkgwpPLAWlVIDGKHLTRPPKDWYPLAQDTGSRTAYIEYkTSkeGST 513
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQY-SS--GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 514 ---VGVTVSHSSLLAQCQALTQ-ACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIPYALMKVNPLSWIQKVCs 589
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLIS- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 590 yKARAALVKSRDMHWSLLAQRGQ----RDVCLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEAlT 665
Cdd:PRK09192 268 -RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 666 VAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGASVCVVKVDGAPYlcKTDEIGEICVN-- 742
Cdd:PRK09192 344 LAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERVVGHICVRgp 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 743 SVATGtaYYGllgitkNTFETVPVTADGvpvsdrpFTRTGLLGFIGPDNLVfVVGKLDGLMVVGVRRHNADDIVATAlav 822
Cdd:PRK09192 420 SLMSG--YFR------DEESQDVLAADG-------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIA--- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 823 EPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKAPLGGIHI 901
Cdd:PRK09192 481 EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSR 557
|
570
....*....|....
gi 359807008 902 SETKQRFLEGTLHP 915
Cdd:PRK09192 558 AKAKKRYLSGAFAS 571
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
323-911 |
2.27e-26 |
|
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: 115.84 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 323 PLSLLAALQLWGTTQPKAPClTALDTAGKATcTLTYGKLWSRSLKLAyTLLNKLTskneplLNPGDRVALVFP-NSDpvm 401
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSEE-FQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 402 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVtlaLTTDACQkglpkAPTGEVATFKGWPPLAWLV 476
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 477 IDGKHLTRPPKDWYPLAQDtgsrTAYIEYKTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAG 553
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 554 LWHGVLTSVMNRMHVITIPYALMKVNPLSWIQKVCSYKA------RAALVKSRDmhwsLLAQRGQRDVCLSSLRMLIVAD 627
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 628 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 704
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 705 LTVQDVGQVMPGASVCVVKVDGApyLCKTDEIGE--ICVNSVATGtaYYGLLGITKNTFetvpvTADGvpvsdrpFTRTG 782
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRlqVRGPVVTKG--YYNNPEANAEAF-----TEDG-------WFRTG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 783 LLGFIGPDNLVFVVGKLDGLMVVGVrRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSf 862
Cdd:cd05906 415 DLGFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDA- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 359807008 863 qwMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 911
Cdd:cd05906 490 --LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1012-1472 |
4.57e-26 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 115.61 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1083
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1084 vsksacVLSTQAITRLLKSKEAAAAVDVRtwPTILDTDDIPKKkVASIFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1160
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDS-AGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1161 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1237
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1238 SYSVMEmctkgLGAQTGALRM-KGVNLSCVrtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrVNVAICLQGT 1316
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVAT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1317 TGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYY-- 1392
Cdd:PRK12476 367 IAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWgr 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1393 ---TvygEETLHAdHFSARLSFG------DTQTIWARTGYLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPI 1463
Cdd:PRK12476 447 peeT---ERTFGA-KLQSRLAEGshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNHYPQ 511
|
....*....
gi 359807008 1464 DIETSVIRA 1472
Cdd:PRK12476 512 DIEATVAEA 520
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
344-806 |
1.13e-24 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 108.55 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 344 TALDTAGkaTCTLTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpl 423
Cdd:pfam00501 12 TALEVGE--GRRLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 424 trkDAGSQQVGFLLGSCGVTLALTTD--------ACQKGLPKAPTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQD 495
Cdd:pfam00501 79 ---RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 496 TgsrTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQAC----GYTEAETLTNVLDFKRDAGLWHGVLTSVMN--RM 566
Cdd:pfam00501 156 D---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAgaTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 567 HVITIPYALMKVNPLSWIQKvcsYKARAALVKSRDMHWsLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqs 646
Cdd:pfam00501 230 VLPPGFPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 647 rglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQVMPGASVCVVKVDG 726
Cdd:pfam00501 302 ----GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGRPLPGTEVKIVDDET 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 727 APYLcKTDEIGEICV--NSVATGtaYYGLLGITKNTFetvpvTADGvpvsdrpFTRTGLLGFIGPDNLVFVVGKLDGLMV 804
Cdd:pfam00501 351 GEPV-PPGEPGELCVrgPGVMKG--YLNDPELTAEAF-----DEDG-------WYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
..
gi 359807008 805 VG 806
Cdd:pfam00501 416 LG 417
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
978-1512 |
3.56e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 109.26 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCIQLHKRAERVAAALMEKGrlDAGDHVALVYPPGVDLIAAFYGCL 1054
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1055 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLSTqaitrllkskeAAAAVDVRTW---------PTI--LDTDDI 1123
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVieVDLLDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1124 PKKKVASIFRPPSPDVlAYLDFSVSTTGILAGVKMSHAATSALCRSI------KLQCELYPSRQIAICLDPYCGLGFALW 1197
Cdd:PRK05850 147 DSPRGSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1198 CLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaQTGALRMKGVNLSCVRTcMVVAEERP 1277
Cdd:PRK05850 226 VCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVR----KTSDDDMAGLDLGGVLG-IISGSERV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1278 RISLTQSFSKLFKDLGLPARAVSTTFG---CRVNVAIclqGTTGPDPTTVYVDMRALRHDRVR---------LVERGSPH 1345
Cdd:PRK05850 301 HPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYGSPR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1346 SlplmesgkilPGVKVIIAHTETKGPLGDshLGEIWVSSPHNATGYYTVyGEETLHAdhFSARL---SFGDTQTIWARTG 1422
Cdd:PRK05850 378 S----------PTVRIVDPDTCIECPAGT--VGEIWVHGDNVAAGYWQK-PEETERT--FGATLvdpSPGTPEGPWLRTG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1423 YLGFLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV--IRAHRsiaeCAVFT----WTNLLVVVVEL-- 1494
Cdd:PRK05850 443 DLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIqeITGGR----VAAISvpddGTEKLVAIIELkk 507
|
570
....*....|....*....
gi 359807008 1495 -DGLEQDALDLVALVTNVV 1512
Cdd:PRK05850 508 rGDSDEEAMDRLRTVKREV 526
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
386-913 |
4.33e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.43 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 386 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVTLALTTDACQKGLPKapt 460
Cdd:PRK07769 78 PGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGVRK--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 461 gevaTFKGWPP------LAwlvID------GKHLTRPPKDwyplaQDTgsrTAYIEYkTSkeGST---VGVTVSHSSLLA 525
Cdd:PRK07769 146 ----FFRARPAkerprvIA---VDavpdevGATWVPPEAN-----EDT---IAYLQY-TS--GSTripAGVQITHLNLPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 526 QCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNrmHVITI--PYALMKvNPLSWIQKVCSYKARAALVKSR--D 601
Cdd:PRK07769 208 NVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAapN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 602 MHWSLLAQRG-----QRDVCLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPPDlg 675
Cdd:PRK07769 285 FAFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTPMDE-- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 676 gpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGASVCVVKVDGAPYLcKTDEIGEICVNSVATGTAYYGLL 754
Cdd:PRK07769 361 --EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 755 GITKNTFE------TVPVTADGVPvSDRPFTRTGLLGFIGPDNLvFVVGKLDGLMVVGVRRHNADDIVATALavEPMKFV 828
Cdd:PRK07769 437 EETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKAL 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 829 YRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPA 888
Cdd:PRK07769 513 RTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPA 592
|
570 580
....*....|....*....|....*
gi 359807008 889 NTLPKAPLGGIHISETKQRFLEGTL 913
Cdd:PRK07769 593 GSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-122 |
1.33e-23 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 96.72 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 10 AAPLPAEVLESLAELELELSEGDITQKGYEKKRAKLLARYipliqgvdpcLQTENRIPGPLltAATAKPQKSRATNSRDE 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKF----------LLHPETPTKLS--AEAQNQLASLETKLRDE 69
|
90 100 110
....*....|....*....|....*....|....*
gi 359807008 90 RFRSDVHTEAVQAALAKYKERKM--PMPSKRRSAL 122
Cdd:pfam06464 70 ELSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
386-915 |
6.77e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 99.05 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 386 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVTLALTTDACQ-------K 453
Cdd:PRK12476 91 PGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpghAERLDT-------ALRDAEPTVVLTTTAAAeavegflR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 454 GLPKAPTGEVATFKGWPPLAwlvidGKHLTRPPKDwyplAQDTgsrtAYIEYkTSkeGST---VGVTVSHSSLlaqCQAL 530
Cdd:PRK12476 162 NLPRLRRPRVIAIDAIPDSA-----GESFVPVELD----TDDV----SHLQY-TS--GSTrppVGVEITHRAV---GTNL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 531 TQ---ACGYTEAETLT-NVLDFKRDAGLWHGVLTSVMNRMHVITIPYALMKvNPLSWIQKVcSYKARAALV--KSRDMHW 604
Cdd:PRK12476 223 VQmilSIDLLDRNTHGvSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKAL-SEGSRTGRVvtAAPNFAY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 605 SLLAQRG----QRDVCLSSLRMLIvadGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPR 680
Cdd:PRK12476 301 EWAAQRGlpaeGDDIDLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 681 KAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGASVCVVKVDGAPYLcKTDEIGEICVNSVATGTAYYGLLGITKN 759
Cdd:PRK12476 375 VVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETER 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 760 TFETVPVT-------ADGVPVSDRPFtRTGLLGFIgPDNLVFVVGKLDGLMVVGVRRHNADDIVATALAVEPMkfVYRGR 832
Cdd:PRK12476 453 TFGAKLQSrlaegshADGAADDGTWL-RTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGY 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 833 IAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGT 912
Cdd:PRK12476 529 VTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGR 608
|
...
gi 359807008 913 LHP 915
Cdd:PRK12476 609 LGV 611
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1012-1491 |
7.18e-21 |
|
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: 98.51 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1090
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1091 LSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSi 1170
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL---PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1171 KLQCELYPSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSvmeMCTK 1247
Cdd:cd05906 199 KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1248 gLGAQTGALRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRVNVAIClqgttgpdptTVYVD 1327
Cdd:cd05906 274 -LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IYSRS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1328 MRALRHdrvrlvergsPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGEETLHADHFsa 1407
Cdd:cd05906 342 FPTYDH----------SQALEFVSLGRPIPGVSMRIV-DDEGQLLPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF-- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1408 rlsfgdTQTIWARTGYLGFLrrteltdasgeRHDALYVVGSLDETLELRGMRYHPIDIETSV----IRAHRSIAECAVF- 1482
Cdd:cd05906 406 ------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRd 468
|
490
....*....|.
gi 359807008 1483 --TWTNLLVVV 1491
Cdd:cd05906 469 pgAETEELAIF 479
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1012-1481 |
7.79e-21 |
|
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: 96.95 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1091
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STQAiTRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVASifrPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1171
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1172 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1245
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1246 TKGLGAQTGALRMkgvnlscvrtcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNvaiclqgTTGPDPTTVY 1325
Cdd:TIGR01733 227 AAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN-------LYGPTETTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1326 VDMRALRHDRVRlvergSPHSLPLmesGKILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYytvYGEETLHADHF 1405
Cdd:TIGR01733 277 STATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERF 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 359807008 1406 SARLSFGDTQTIWARTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1481
Cdd:TIGR01733 345 VPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
323-943 |
7.39e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.16 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 323 PLSLLAALQLWGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLlnkltsknEPLLNPGDRVALVFPnSDPvMF 402
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-DY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 403 MVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkGWPPlaWLVIDGkhL 482
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPE--LLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 483 TRPPKDWYPLAQDTGSRTAYIEYkTSkeGSTV---GVTVSHSSLLAQCQALTQACG--YTEAETLTNVLDFKRDAGLWHG 557
Cdd:PRK05691 151 DPALAEAWQEPALQPDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 558 VLTSVMNRMHVITIPYALMKVNPLSWIQKVCSYkaRAALVKSRDMHWSLLAQRgQRDVCLSSL---RMLIVADGANPWSI 634
Cdd:PRK05691 228 LLQPIFSGVPCVLMSPAYFLERPLRWLEAISEY--GGTISGGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 635 SSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQV 713
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARNRAEPGTGSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 714 M-------PGASVCVVKVDGAPYLcKTDEIGEICVN--SVATGtaYYGLLGITKNTFetvpVTADGvpvsdRPFTRTGLL 784
Cdd:PRK05691 369 LmscgrsqPGHAVLIVDPQSLEVL-GDNRVGEIWASgpSIAHG--YWRNPEASAKTF----VEHDG-----RTWLRTGDL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 785 GFIgPDNLVFVVGKLDGLMVvgVRRHN--ADDIVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE-----QRPDAS 857
Cdd:PRK05691 437 GFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPP 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 858 EEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVTNLPKPRQKQP 937
Cdd:PRK05691 512 QA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEA 577
|
....*.
gi 359807008 938 EVGPAS 943
Cdd:PRK05691 578 AQTAAS 583
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1012-1476 |
3.90e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 93.64 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1083
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1084 VSKSAcvlstQAITRLLKSKEAAAAvdvrtwPTILDTDDIPKKkVASIFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1160
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1161 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1234
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1235 tfcsYSVMEMCTKGLGAQTGaLRMKG---VNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrVNVAI 1311
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARG-LPKDGeppLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEAT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1312 CLQGTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNAT 1389
Cdd:PRK07769 351 LFVSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGT 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1390 GYYTvYGEETLHADH--FSARLSFGDTQ-----TIWARTGYLGflrrtelTDASGErhdaLYVVGSLDETLELRGMRYHP 1462
Cdd:PRK07769 431 GYWG-KPEETAATFQniLKSRLSESHAEgapddALWVRTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYP 498
|
490
....*....|....
gi 359807008 1463 IDIETSVIRAHRSI 1476
Cdd:PRK07769 499 QDLEYTAQEATKAL 512
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1009-1482 |
4.81e-18 |
|
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: 89.19 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1009 TCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1088
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1089 CVLSTQAITRLLKSKEAAAAVDVRTW------PTILDTDDI--PKKKVASIFRPP----SPDVLAYLDFSVSTTGILAGV 1156
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpDGVLSIEDLlsPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1157 KMSH---AATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQYKA 1232
Cdd:cd05911 165 CLSHrnlIANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1233 RVTF------CSYSVMEMCTKGlgaqtgalrmkgvNLSCVRTCMVVAeerprisltqsfSKLFKDLGlparavsTTFGCR 1306
Cdd:cd05911 238 TFLYlvppiaAALAKSPLLDKY-------------DLSSLRVILSGG------------APLSKELQ-------ELLAKR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1307 VNVAICLQG-----TTGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEIW 1381
Cdd:cd05911 286 FPNATIKQGygmteTGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEIC 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1382 VSSPHNATGYytvYGEETLHADHFsarlsfgdTQTIWARTGYLGFLRRTELtdasgerhdaLYVVGSLDETLELRGMRYH 1461
Cdd:cd05911 347 VRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYFDEDGY----------LYIVDRKKELIKYKGFQVA 405
|
490 500
....*....|....*....|.
gi 359807008 1462 PIDIEtSVIRAHRSIAECAVF 1482
Cdd:cd05911 406 PAELE-AVLLEHPGVADAAVI 425
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
968-1469 |
9.14e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.83 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 968 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGV 1044
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1045 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLSTQAITRLLksKEAAAAVDVRTWPTILDTD 1121
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1122 DIPKKKVAsiFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1200
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1201 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGAlrmkGVNLSCVRTCMVVAEE-RPR 1278
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLA----ELDLSCWRVAGIGADMiRPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1279 IslTQSFSKLFKDLGLPARAVSTTFG-CRVNVAIclqgtTGPDPTTvyvDMRALRHDRVRLVERGspHSLPLMES----- 1352
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAV-----SFSPLGS---GIVVEEVDRDRLEYQG--KAVAPGAEtrrvr 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1353 -----GKILPGVKVIIaHTETKGPLGDSHLGEIWVSSPHNATGYYTvyGEETlhADHFSArlsfgdtqTIWARTGYLGFL 1427
Cdd:PRK09192 383 tfvncGKALPGHEIEI-RNEAGMPLPERVVGHICVRGPSLMSGYFR--DEES--QDVLAA--------DGWLDTGDLGYL 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 359807008 1428 rrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV 1469
Cdd:PRK09192 450 -------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIA 480
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1005-1484 |
4.54e-16 |
|
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: 83.19 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1005 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1084
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1085 SKSACVLSTQAITRLLKSKEAAAAVDVRT----------WPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILA 1154
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1155 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVPPLELESNVslwL 1224
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAV---F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1225 SAVSQYKARVTFCS---YSVMemctkglgaqTGALRMKGVNLSCVRTCMVVAEERPRiSLTQSFSKLfkdlglparavst 1301
Cdd:cd05959 248 KRIRRYRPTVFFGVptlYAAM----------LAAPNLPSRDLSSLRLCVSAGEALPA-EVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1302 tFGCRVnvaicLQGTTGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVIIAHtETKGPLGDSHLGEIW 1381
Cdd:cd05959 304 -FGLDI-----LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1382 VSSPHNATGYYTVYgEETlhadhfsaRLSFgdtQTIWARTGYlGFLRrteltDASGerhdALYVVGSLDETLELRGMRYH 1461
Cdd:cd05959 363 VRGPSSATMYWNNR-DKT--------RDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLKVSGIWVS 420
|
490 500
....*....|....*....|...
gi 359807008 1462 PIDIEtSVIRAHRSIAECAVFTW 1484
Cdd:cd05959 421 PFEVE-SALVQHPAVLEAAVVGV 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1012-1504 |
2.12e-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: 77.57 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSACVL 1091
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1171
Cdd:cd05930 90 TD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1172 lqcELYPSR------QIAicldpycGLGF--ALWCL-CSVYSGHQSVLVPPlELESNVSLWLSAVSQYKARVTFCSYSVM 1242
Cdd:cd05930 127 ---EAYPLTpgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1243 EMCtkglgAQTGALRMkgvnLSCVRTcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNVaiclqgtTGPDPT 1322
Cdd:cd05930 196 RLL-----LQELELAA----LPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YGPTEA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1323 TVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYytvYGEETLHA 1402
Cdd:cd05930 247 TVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGY---LNRPELTA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1403 DHFSArLSFGDTQTIWaRTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAVF 1482
Cdd:cd05930 314 ERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLAHPGVREAAVV 380
|
490 500
....*....|....*....|....*...
gi 359807008 1483 TWTN------LLVVVVELDGLEQDALDL 1504
Cdd:cd05930 381 AREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
499-806 |
3.40e-13 |
|
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: 72.70 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 499 RTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPyal 575
Cdd:cd04433 1 DPALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 576 mKVNPLSWIQKVCSYKARAALVkSRDMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVIC 655
Cdd:cd04433 74 -KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 656 PCASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPylCKTDE 735
Cdd:cd04433 145 GYGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGE 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359807008 736 IGEICVNSvatgtaYYGLLGITKNTFETVPVTADGvpvsdrpFTRTGLLGFIGPDNLVFVVGKLDGLMVVG 806
Cdd:cd04433 194 IGELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1012-1501 |
5.84e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 73.26 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGRLDAgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1087
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1088 acVLSTQAITRLLKSKEAAAAV-DVRTWPtildtddipKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1166
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1167 CRSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVM 1242
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1243 emctkglgaqtG--ALRMKGVNLSCVRTCmVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFG-----CRVNVAICLQG 1315
Cdd:PRK05851 260 -----------GkyARRVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGlaestCAVTVPVPGIG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1316 ttgpdpttvyvdmraLRHDRVRLVERGSPHSLPLMesGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvY 1395
Cdd:PRK05851 328 ---------------LRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---L 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1396 GEETLHADHfsarlsfgdtqtiWARTGYLGFlrrteLTDasgerhDALYVVGSLDETLELRGMRYHPIDIET--SVIRAH 1473
Cdd:PRK05851 388 GQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERvaAQVRGV 443
|
490 500 510
....*....|....*....|....*....|..
gi 359807008 1474 RSIAECAVFTWTNL----LVVVVELDGLEQDA 1501
Cdd:PRK05851 444 REGAVVAVGTGEGSarpgLVIAAEFRGPDEAG 475
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
978-1481 |
5.87e-13 |
|
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: 72.98 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLLLNAKgtvtstATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1058 CVPVTVRPphpqnlgttlptvkmivevsksacVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifrpPSP 1137
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1138 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1211
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1212 P---PLELesnvslwLSAVSQYkaRVTFcsysvmemctkglgaqtgalrMKGVNlscvrtCMVVAeerprisLTQSFSKL 1288
Cdd:cd05936 201 PrfrPIGV-------LKEIRKH--RVTI---------------------FPGVP------TMYIA-------LLNAPEFK 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1289 FKDLGlparavsttfgcRVNVAIClqgttGPDPTTVYVDMRALRHDRVRLVErG------SP--HSLPLMES------GK 1354
Cdd:cd05936 238 KRDFS------------SLRLCIS-----GGAPLPVEVAERFEELTGVPIVE-GygltetSPvvAVNPLDGPrkpgsiGI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1355 ILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYYTvYGEETlhADHFSarlsfgDTqtiWARTGYLGFLrrteltD 1434
Cdd:cd05936 300 PLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYWN-RPEET--AEAFV------DG---WLRTGDIGYM------D 360
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 359807008 1435 ASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1481
Cdd:cd05936 361 EDGY----FFIVDRKKDMIIVGGFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
384-893 |
2.15e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 71.32 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 384 LNPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVTLALT----TDACQKGLP 456
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVLAdagaADRLRDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 457 KAPTgevatfkgwpPLAWLVIDGKHLTRPPKDWYPLAQDTgsrTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGY 536
Cdd:cd05922 89 ASPD----------PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 537 TEAETLTNVLDFKRDAGLwhGVLTSVMNR--MHVITIPYALmkvnPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQR 613
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgaTLVLTNDGVL----DDAFWEDLREHGATGlAGVPS---TYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 614 DVCLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavlsmn 687
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 688 glsygvirvdteeklsvltvQDVGQVMPGASVCVVKVDGAPylCKTDEIGEIcVNSVATGTAYYGllgiTKNTFETVPVT 767
Cdd:cd05922 286 --------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKEGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 768 ADGVpvsdrpfTRTGLLGFIGPDNLVFVVGKLDGLMVVGVRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDDRIV 847
Cdd:cd05922 339 GGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKLA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 359807008 848 LVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 893
Cdd:cd05922 407 LFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
355-804 |
3.98e-12 |
|
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: 70.70 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI-------EVPLTRKD 427
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAAnpiytadELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 428 AGSQqvgfLLGSCGVTLALTTDACQKGLPKAptgEVATFKGWPPLawlVIDGKHLTRPP---KDWYPLAQ--DTGSRTAY 502
Cdd:cd05911 81 SKPK----VIFTDPDGLEKVKEAAKELGPKD---KIIVLDDKPDG---VLSIEDLLSPTlgeEDEDLPPPlkDGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 503 IEYkTSkeGST---VGVTVSHSSLLAQC-QALTQACGYTEA-ETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPyalmK 577
Cdd:cd05911 151 ILY-SS--GTTglpKGVCLSHRNLIANLsQVQTFLYGNDGSnDVILGFLPLYHIYGLF-TTLASLLNGATVIIMP----K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 578 VNPLSWIQKVCSYKARAALVKSRDMHW---SLLAQRGQrdvcLSSLRMLIVadGANPWSISSCDAFLNVFQSRGLRP--- 651
Cdd:cd05911 223 FDSELFLDLIEKYKITFLYLVPPIAAAlakSPLLDKYD----LSSLRVILS--GGAPLSKELQELLAKRFPNATIKQgyg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 652 --EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPY 729
Cdd:cd05911 297 mtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPNVEAKIVDDDGKDS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 730 LcKTDEIGEICVNSvatGTAYYGLLGITKNTFETvpVTADGvpvsdrpFTRTGLLGFIGPDNLVFVVG------KLDGLM 803
Cdd:cd05911 337 L-GPNEPGEICVRG---PQVMKGYYNNPEATKET--FDEDG-------WLHTGDIGYFDEDGYLYIVDrkkeliKYKGFQ 403
|
.
gi 359807008 804 V 804
Cdd:cd05911 404 V 404
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
986-1168 |
7.09e-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: 69.68 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 986 AHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGRLDaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1065
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARGVGP-GDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1066 PHPQnlgttlPTVKMIVEVSKSACVLSTQAitrllkskEAAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDF 1145
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPA--------LAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 359807008 1146 SVSTTGILAGVKMSHAATSALCR 1168
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
986-1507 |
1.87e-11 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 68.43 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 986 AHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1065
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1066 PHPqnlgttlptvkmivevsksacvlstqaITRLLKSKEAAAavdvrtwPTILDTDdipkkkvasifrppsPDVLAYLDF 1145
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1146 SVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPY---CGLgFALWclCSVYSGHQSVLVPPLELEsNVSL 1222
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPFsfdLSV-MDLY--PALASGATLVPVPRDATA-DPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1223 WLSAVSQYKARVTFCSYSVMEMCTkGLGAQTGAlrmkgvNLSCVRTCMVVAEERPrISLTQSFSKLFkdlglPARAVSTT 1302
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQQRF-----PDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1303 FgcrvnvaiclqgttGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVKVIIAhTETKGPLGDSHLGEIWV 1382
Cdd:cd05945 247 Y--------------GPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVIL-DEDGRPVPPGEKGELVI 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1383 SSPHNATGYYTVygeetlhADHFSARLSFGDTQTiWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHP 1462
Cdd:cd05945 304 SGPSVSKGYLNN-------PEKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRLDFQVKLNGYRIEL 365
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 359807008 1463 IDIETSViRAHRSIAECAVFTWTNL-----LVVVVELDGlEQDALDLVAL 1507
Cdd:cd05945 366 EEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKP-GAEAGLTKAI 413
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1012-1481 |
7.62e-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: 66.49 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVpvtVRPPHPQNlgtTLPTVKMIVEVSKsACVL 1091
Cdd:cd05904 37 ELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAV---VTTANPLS---TPAEIAKQVKDSG-AKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STQAiTRLLKSKEAAAAV------DVRTWPTILDTDDIPkkkVASIFRPP-SPDVLAYLDFSVSTTGILAGVKMSHA-AT 1163
Cdd:cd05904 109 FTTA-ELAEKLASLALPVvlldsaEFDSLSFSDLLFEAD---EAEPPVVViKQDDVAALLYSSGTTGRSKGVMLTHRnLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1164 SALCRSIKLQCELYPSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLVPPLELESnvslWLSAVSQYkaRVTFCSYS-- 1240
Cdd:cd05904 185 AMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY--KVTHLPVVpp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1241 -VMEMCTKGLGaqtgalrmKGVNLSCVRTCMVVAeerprisltqsfSKLFKDLglpARAVSTTFGcrvNVAIClQG---- 1315
Cdd:cd05904 259 iVLALVKSPIV--------DKYDLSSLRQIMSGA------------APLGKEL---IEAFRAKFP---NVDLG-QGygmt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1316 TTGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvy 1395
Cdd:cd05904 312 ESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGY---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1396 geetlhadhfsarlsFGDTQ----TI----WARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEt 1467
Cdd:cd05904 373 ---------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVAPAELE- 426
|
490
....*....|....
gi 359807008 1468 SVIRAHRSIAECAV 1481
Cdd:cd05904 427 ALLLSHPEILDAAV 440
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
356-800 |
1.03e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 356 LTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqV 433
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYPAER-------L 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 434 GFLLGSCGVTLALTTDACQKGLPkaPTGEVATFKGWPPLAWLvidgkhlTRPPKDwyPLAQDTGSRTAYIEYKTSKEGST 513
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWA-------DYPDTA--PAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 514 VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPYALmkvnplsWIQKVCSYKAR 593
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDEL-------WDPEQLYDEME 2233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 594 AALVKSRDM---HWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAflnvfQSRGLRPEVIcpcasspealtvairr 670
Cdd:PRK12316 2234 RHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEALRPVYL---------------- 2290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 671 ppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGASVCVvkVDGAPYLCKTDEIGEICVNSVATGTAY 750
Cdd:PRK12316 2291 ---FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLNLLAPGMAGELYLGGEGLARGY 2359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 359807008 751 YGLLGITKNTFETVPVTADGVPVsdrpfTRTGLLGFIGPDNLVFVVGKLD 800
Cdd:PRK12316 2360 LNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRID 2404
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1012-1466 |
1.15e-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: 65.97 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGttlptvkmivevSKSACVL 1091
Cdd:cd05908 20 HLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV------PVSIG------------SNEEHKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STQAITRLLKSkeaaaavdvrtwPTILDTDDIPKKkvasifrppSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1171
Cdd:cd05908 81 KLNKVWNTLKN------------PYLITEEEVLCE---------LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1172 LQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGA 1251
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1252 QTGAlrmkGVNLSCVRtcMVVAEERPRIS-LTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQGTTGPdPTTVYVDMR 1329
Cdd:cd05908 220 EKAN----DWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEASVGASLPKAQSP-FKTITLGRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1330 ALRH-DRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGpLGDSHLGEIWVSSPHNATGYYTvyGEETlhadhfSAR 1408
Cdd:cd05908 293 HVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGYYN--NPEA------TAK 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 359807008 1409 LSFGDTqtiWARTGYLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIE 1466
Cdd:cd05908 364 VFTDDG---WLKTGDLGFIRNGR-----------LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1012-1481 |
3.54e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.63 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgTTLP-----TVKMIVEVSK 1086
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPR---TDLAvwaedTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1087 SACVLS---TQAITRLlkskeAAAAVDVRTWPTILDTDDIpkkkvasifRPP--SPDVLAYLDFSVSTTGILAGVKMSHA 1161
Cdd:PRK07768 110 KAVVVGepfLAAAPVL-----EEKGIRVLTVADLLAADPI---------DPVetGEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1162 ATSALCRSIKLQCELYPSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLVPPLELESNVSLWLSAVSQYKARVT- 1235
Cdd:PRK07768 176 NLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1236 ---FcSYSVMemcTKGLGAQTgalRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFG-CRVNVAI 1311
Cdd:PRK07768 252 apnF-AYALL---ARRLRRQA---KPGAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1312 CLqGTTGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGY 1391
Cdd:PRK07768 324 SF-SPCGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGLEVRVV-DEDGQVLPPRGVGVIELRGESVTPGY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1392 YTVYGEETLHADHfsarlsfGdtqtiWARTGYLGFLrrTELtdasGErhdaLYVVGSLDETLELRGMRYHPIDIETSVIR 1471
Cdd:PRK07768 401 LTMDGFIPAQDAD-------G-----WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIYPTDIERAAAR 458
|
490
....*....|
gi 359807008 1472 AHRSIAECAV 1481
Cdd:PRK07768 459 VEGVRPGNAV 468
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
357-800 |
4.66e-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: 63.44 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 357 TYGKLWSRSLKLAYTLLNKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 434
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVG------PGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 435 FLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkgwPPLAWLVIDGKHLTRPPKDWYPLAQDtgsrTAYIEYkTSkeGST- 513
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSGPDD----LAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 514 --VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVITIPYALMKVNPLSWiqkvcsyk 591
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 592 arAALVKSRDM-HWSLLAqrgqrdvclSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 669
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 670 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGASVCVvkVDGAPYLCKTDEIGEIC 740
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYV--LDDDLRPVPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359807008 741 VN--SVATGtaYYGLLGITKNTFetvpVTADGVPVSDRPFTRTGLLGFIGPD-NLVFvVGKLD 800
Cdd:TIGR01733 324 IGgpGVARG--YLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPDgNLEF-LGRID 379
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1012-1235 |
8.67e-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: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1089
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1090 VLSTQAItrllkskeAAAAVDVRTWPTILDTDDIPKKKVASifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1169
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359807008 1170 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1235
Cdd:cd12114 158 INRRFAVGPDdRVLAL-----SSLSFDL----SVYdifgalsAGATLVLPDEAR-RRDPAHWAELIERH--GVT 219
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1012-1518 |
1.07e-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: 63.72 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1087
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1088 ACVLSTQAITRLLKSKEAaaavdvrtwPTI-LDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1166
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1167 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYKARVT 1235
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1236 FCSYSVMEMCTKGLGAQTGALRmkgvnlscvrtCMVVAEERPrisltqsfsklfkDLGLPARAVSTTFGCR-VNVAiclq 1314
Cdd:COG1020 713 NLTPSLLRALLDAAPEALPSLR-----------LVLVGGEAL-------------PPELVRRWRARLPGARlVNLY---- 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1315 gttGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------GEIWVSSPH 1386
Cdd:COG1020 765 ---GPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL---------DAHLqpvpvgvpGELYIGGAG 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1387 NATGYytvYGEETLHADHFSArLSFGDTQTIWARTGYLGflRRTeltdASGErhdaLYVVGSLDETLELRGMRYHPIDIE 1466
Cdd:COG1020 824 LARGY---LNRPELTAERFVA-DPFGFPGARLYRTGDLA--RWL----PDGN----LEFLGRADDQVKIRGFRIELGEIE 889
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 359807008 1467 tSVIRAHRSIAECAVFTWTN-----LLVVVVELDGLEQDALDLVALVTNVVLEEHYL 1518
Cdd:COG1020 890 -AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAALLRLALALLLPPYMV 945
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
355-555 |
3.91e-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: 61.80 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 432
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 433 VGFLLGSCGVTLALTTDACQKGLPKAPtgevatfkgwppLAWLVIDGKHLTRPPKDWyPLAQDTGSRTAYIEYkTSkeGS 512
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 359807008 513 T---VGVTVSHSSLLAQCQALTQACGYTEAETLTNV--LDFkrDAGLW 555
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1012-1507 |
6.48e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 60.38 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGRlDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1091
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STQAItrllkskEAAAAVDVRTWPTILDTDDIPkkkVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1171
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1172 LQCELYPSRQIaICLDPYCglgF---ALWCLCSVYSGHQSVLVPPLELESNVSLwlsavsqyKARVTFCSYSVMEmctkg 1248
Cdd:cd12116 160 ERLGLGPGDRL-LAVTTYA---FdisLLELLLPLLAGARVVIAPRETQRDPEAL--------ARLIEAHSITVMQ----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1249 lgaQTGAL-RMkgvnlscvrtcMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTfGCRVNVaiclqgtTGPDPTTVYVD 1327
Cdd:cd12116 223 ---ATPATwRM-----------LLDAGWQGRAGLTALCGGEALPPDLAARLLSRV-GSLWNL-------YGPTETTIWST 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1328 MRALrhdrvrlveRGSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------GEIWVSSPHNATGYytvYGEET 1399
Cdd:cd12116 281 AARV---------TAAAGPIPI---GRPLANTQVYVL---------DAALrpvppgvpGELYIGGDGVAQGY---LGRPA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1400 LHADHFSArLSFGDTQTIWARTGYLgfLRRteLTDASgerhdaLYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAEC 1479
Cdd:cd12116 337 LTAERFVP-DPFAGPGSRLYRTGDL--VRR--RADGR------LEYLGRADGQVKIRGHRIELGEIEA-ALAAHPGVAQA 404
|
490 500 510
....*....|....*....|....*....|..
gi 359807008 1480 AVFTWTN----LLVVVVELDGLEqdALDLVAL 1507
Cdd:cd12116 405 AVVVREDggdrRLVAYVVLKAGA--APDAAAL 434
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
344-546 |
6.68e-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: 60.27 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 344 TALDTAGKatcTLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 423
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 424 TrkdagSQQVGFLLGSCGVTLALTtdacqkglpkaptgeVATFkgwpplawlvidgKHLTRPPKDWYPLAQDTGSRTAYI 503
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 359807008 504 EYkTSkeGST---VGVTVSHSSLLA---QCQALTQACGyTEAETLTNVL 546
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKAWLEDLL-EGDDVVLAAL 175
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1012-1508 |
1.33e-08 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 59.24 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1091
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1171
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1172 LQCELYPSRQIAICldPYCGLGFALWCLCSVYS-GHQSVLVPPLELESNVSLWLSAVSQykaRVTFCS------YSVMEM 1244
Cdd:cd17643 127 RWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLhGGRLVVVPYEVARSPEDFARLLRDE---GVTVLNqtpsafYQLVEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1245 CTKGLGAQTgALRMkgvnlscvrtcMVVAEERPRISLTQSFsklFKDLGLPARAVsttfgcrVNvaicLQGTTgpdPTTV 1324
Cdd:cd17643 202 ADRDGRDPL-ALRY-----------VIFGGEALEAAMLRPW---AGRFGLDRPQL-------VN----MYGIT---ETTV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1325 YVDMRALRHDRVRLVERGSphslplmeSGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYYtvyGEETLHADH 1404
Cdd:cd17643 253 HVTFRPLDAADLPAAAASP--------IGRPLPGLRVYVL-DADGRPVPPGVVGELYVSGAGVARGYL---GRPELTAER 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1405 FSArLSFGDTQTIWARTGYLGflRRTeltdASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVFTW 1484
Cdd:cd17643 321 FVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE-AALATHPSVRDAAVIVR 388
|
490 500 510
....*....|....*....|....*....|
gi 359807008 1485 TN------LLVVVVELDGLEQDALDLVALV 1508
Cdd:cd17643 389 EDepgdtrLVAYVVADDGAAADIAELRALL 418
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
985-1162 |
2.30e-08 |
|
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: 58.44 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 985 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1064
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1065 PPHPQnlgttlPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasifrPPSPDVLAYLD 1144
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 359807008 1145 FSVSTTGILAGVKMSHAA 1162
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
978-1482 |
3.08e-08 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 58.19 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1058 CVPVTVrpphpqnlGTTLPT--VKMIVEVSKS-ACVLSTQAI-TRLLKSKEAAAAV---------------DVRTWPTIL 1118
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEQlDKLLEVRDELPSLrhivvldprglrddpRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1119 D--TDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS-RQIAIcldpycgLGFA 1195
Cdd:COG1022 162 AlgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGdRTLSF-------LPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1196 -----LWCLCSVYSGHQSVLVPPLElesNVSLWLSAVsqykaRVTF-CS--------YS-VMEMctkglGAQTGALRMKG 1260
Cdd:COG1022 235 hvferTVSYYALAAGATVAFAESPD---TLAEDLREV-----KPTFmLAvprvwekvYAgIQAK-----AEEAGGLKRKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1261 VNLsCVRTCMVVAEER---PRISLTQS----------FSKLfkdlglpaRAVsttFGCRVNVAIC--------------- 1312
Cdd:COG1022 302 FRW-ALAVGRRYARARlagKSPSLLLRlkhaladklvFSKL--------REA---LGGRLRFAVSggaalgpelarffra 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1313 -----LQG-----TTGPdpTTVYvdmralRHDRVRLverGSphslplmeSGKILPGVKVIIAHTetkgplgdshlGEIWV 1382
Cdd:COG1022 370 lgipvLEGyglteTSPV--ITVN------RPGDNRI---GT--------VGPPLPGVEVKIAED-----------GEILV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1383 SSPHNATGYY-----TvygEETLHADhfsarlsfGdtqtiWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELR- 1456
Cdd:COG1022 420 RGPNVMKGYYknpeaT---AEAFDAD--------G-----WLHTGDIGEL------DEDGF----LRITGRKKDLIVTSg 473
|
570 580
....*....|....*....|....*.
gi 359807008 1457 GMRYHPIDIEtSVIRAHRSIAECAVF 1482
Cdd:COG1022 474 GKNVAPQPIE-NALKASPLIEQAVVV 498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
328-621 |
3.41e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 328 AALQLWGTTQ---PKAPCLTAL--DTAGKA---------TCTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALV 393
Cdd:PRK12316 4535 RIVALWNRTDagyPATRCVHQLvaERARMTpdavavvfdEEKLTYAELNRRANRLAHALI-------ARGVGPEVLVGIA 4607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 394 FPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPkAPTGevatfkgwpp 471
Cdd:PRK12316 4608 MERS--AEMMVGLLAVLKAggAYVPLDPEYPRER-------LAYMMEDSGAALLLTQSHLLQRLP-IPDG---------- 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 472 LAWLVIDgkhltrPPKDWY------PLAQDTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNV 545
Cdd:PRK12316 4668 LASLALD------RDEDWEgfpahdPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQF 4741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 546 LDFKRDA---GLWHGVLT--SVMNRMHVITIP---YALMKVNPLSWIQKVCSYkaraalvksrdmhWSLLAQRGQRDVCL 617
Cdd:PRK12316 4742 MSFSFDGsheGLYHPLINgaSVVIRDDSLWDPerlYAEIHEHRVTVLVFPPVY-------------LQQLAEHAERDGEP 4808
|
....
gi 359807008 618 SSLR 621
Cdd:PRK12316 4809 PSLR 4812
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
985-1168 |
1.43e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 56.06 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 985 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1064
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1065 PPHPQNlgttlpTVKMIVEVSKSACVLStqaitrllkSKEAAAAVDVRtwPTILDTDDIPKKKVASIFRPP-SPDVLAYL 1143
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGL--EVAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 359807008 1144 DFSVSTTGILAGVKMSHAATSALCR 1168
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
355-542 |
1.83e-07 |
|
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: 55.76 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNKLTsknepllNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 434
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 435 FLLGSCGVTLALTTDACQKGLPkaptgevatfkgWPPLAW-LVIDGKHLTRPPkdwyPLAQDTGSRTAYIEYkTSkeGST 513
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP------------AGLPVLlLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GST 138
|
170 180 190
....*....|....*....|....*....|..
gi 359807008 514 ---VGVTVSHSSLLAQCQALTQACGYTEAETL 542
Cdd:cd12116 139 grpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
384-573 |
1.84e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 55.71 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 384 LNPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEV 463
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 464 ATFKGWPPLA--------WLVIDGKHLTRPPKDwyPLAQDTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACG 535
Cdd:PRK08316 131 VDTLILSLVLggreapggWLDFADWAEAGSVAE--PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 359807008 536 YTEAETLTNVLDfkrdagLWHGVltsvmnRMHVITIPY 573
Cdd:PRK08316 209 MSADDIPLHALP------LYHCA------QLDVFLGPY 234
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
980-1503 |
8.65e-07 |
|
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: 53.28 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 980 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCV 1059
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1060 PVTVRPP-HPQNLGTTLPTVKMIVEVSKSAcVLSTQAItRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasiFRPPSPD 1138
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMTAAVIAVD-AQVMDAI-FQSGVRVLALSDLVGLGEPESAGPLIE-------DPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1139 VLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCEL-YPSRQIAICLDP-YCGLG-FALWCLCSVYSGhqsVLVPPLE 1215
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrHGRHNVVLGLMPlYHVIGfFAVLVAALALDG---TYVVVEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1216 LESNVSLWLSAvsqyKARVTfCSYSVMEMctkgLGAQTGALRMKGVNLSCVRTcmvvaeerprisLTqsfsklFKDLGLP 1295
Cdd:cd05923 228 FDPADALKLIE----QERVT-SLFATPTH----LDALAAAAEFAGLKLSSLRH------------VT------FAGATMP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1296 ARAVSTTFGCRVNVAICLQGTT-------GPDPTTVYVdMRALRHDRVRLVERG--SPHSLPLMESGKIlpgvkvIIAHT 1366
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTeamnslyMRDARTGTE-MRPGFFSEVRIVRIGgsPDEALANGEEGEL------IVAAA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1367 etkgplGDSHLGEIWvsSPHNATgyytvygeetlhadhfSARLSFGdtqtiWARTGylgflrRTELTDASGErhdaLYVV 1446
Cdd:cd05923 354 ------ADAAFTGYL--NQPEAT----------------AKKLQDG-----WYRTG------DVGYVDPSGD----VRIL 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359807008 1447 GSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV--VVVELDGLEQDALD 1503
Cdd:cd05923 395 GRVDDMIISGGENIHPSEIE-RVLSRHPGVTEVVVIgvadeRWGQSVTacVVPREGTLSADELD 457
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1007-1160 |
1.63e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 52.69 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1007 TATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 1065
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1066 -----PHPQNLGTTLP-----TVKMIvevskSACVLSTQAITRL----LKSKEAA---AAVDVRTWPTILDTDDIPKKKV 1128
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 359807008 1129 ASiFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1160
Cdd:PRK05605 211 VS-HPRPTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1005-1497 |
3.10e-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: 51.69 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1005 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP-HPQNLgttlptvkmive 1083
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDY------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1084 vsksacvlstqaitrllkskeAAAAVDVRTWPTILDTDDIpkkkvasifrppspdvlAYLDFSVSTTGILAGVKMSHAAT 1163
Cdd:cd05919 75 ---------------------AYIARDCEARLVVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1164 ----SALCRSIklqCELYPSRQIaicldpYC--------GLGFALWclCSVYSGHQSVLVPPLELESNVslwLSAVSQYK 1231
Cdd:cd05919 117 llfaDAMAREA---LGLTPGDRV------FSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1232 ARVTfcsYSVMEMCTKGLGAQTGALRMkgvnLSCVRTCMVVAEERPRisltqsfsklfkdlGLpARAVSTTFGCRVnvai 1311
Cdd:cd05919 183 PTVL---YGVPTFYANLLDSCAGSPDA----LRSLRLCVSAGEALPR--------------GL-GERWMEHFGGPI---- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1312 clqgTTGPDPTTVYVDMRALRHDRVRLverGSphslplmeSGKILPGVKVII----AHTETKGPLGDshlgeIWVSSPHN 1387
Cdd:cd05919 237 ----LDGIGATEVGHIFLSNRPGAWRL---GS--------TGRPVPGYEIRLvdeeGHTIPPGEEGD-----LLVRGPSA 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1388 ATGYYTVYgEETlhadhfSARLSFGdtqtiWARTGYLGFLrrteltDASGerhdALYVVGSLDETLELRGMRYHPIDIEt 1467
Cdd:cd05919 297 AVGYWNNP-EKS------RATFNGG-----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVE- 353
|
490 500 510
....*....|....*....|....*....|
gi 359807008 1468 SVIRAHRSIAECAVftwtnllVVVVELDGL 1497
Cdd:cd05919 354 SLIIQHPAVAEAAV-------VAVPESTGL 376
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
355-448 |
7.10e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 434
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECGVR------KGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90
....*....|....
gi 359807008 435 FLLGSCGVTLALTT 448
Cdd:PRK08314 102 HYVTDSGARVAIVG 115
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
356-875 |
9.29e-06 |
|
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: 50.17 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 356 LTYGKLWSRSLKLAYTLLNKLTSKnepllnpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqQVGF 435
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 436 LLGSCGVTLALTTDACQKglpkaptgevatfkgwpplawlvidgkhltrppkdwyplaqdtgsrTAYIEYKTSKEGSTVG 515
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 516 VTVSHSSLLAqcQALTQACGY--TEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVITIPYALMKVnplsWIQKVcsykAR 593
Cdd:cd05935 102 CMHTHFSAAA--NALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMAR----WDRET----AL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 594 AALVKSRDMHWS--------LLAQRGQRDVCLSSLRMLivADGANPWSISSCDAFLNVFqsrGLRPEVIcpcasspEALT 665
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL--TGGGAPMPPAVAEKLLKLT---GLRFVEG-------YGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 666 VAIrrPPDLGGPPPRKAVLSMnglsyGVIRVDTEEKlsVLTVQDVGQVMPGasvcvvkvdgapylcktdEIGEICVNSVA 745
Cdd:cd05935 235 ETM--SQTHTNPPLRPKLQCL-----GIP*FGVDAR--VIDIETGRELPPN------------------EVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 746 TGTAYYGLLGITKNTFetvpvtadgVPVSDRPFTRTGLLGFIGPDNLVFVVGKLDGLmvvgvrrhnaddIVATALAVEPM 825
Cdd:cd05935 288 IFKGYWNRPEETEESF---------IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRM------------INVSGFKVWPA 346
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 359807008 826 KF--VYRGRIAVFSVTVLH--DDR--------IVLVAEQRPDASEEDSFQW----MS-----RVLQAIDSI 875
Cdd:cd05935 347 EVeaKLYKHPAI*EVCVISvpDERvgeevkafIVLRPEYRGKVTEEDIIEWareqMAaykypREVEFVDEL 417
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1006-1480 |
1.30e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.77 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1006 STATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP-PHPQNLGTTLPTVkmivev 1084
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQCLQEA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1085 sksacvlSTQAITRLLKSKEAAAAVdvrtwptildtddipkkkvasifrppspdvlayldFSVSTTGILAGVKMSHAATS 1164
Cdd:cd05910 74 -------EPDAFIGIPKADEPAAIL-----------------------------------FTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1165 ALCRSIKlqcELYPSRQIAICLDpycglGFALWCLCSVYSGHQSVlVPPLE----LESNVSLWLSAVSQYKARVTFCSYS 1240
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1241 VMEMCTKgLGAQtgalrmKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDlglpARAVSTTFGCRVNVAICLQGTtgpd 1320
Cdd:cd05910 183 LLERVAR-YCAQ------HGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----EAEILTPYGATEALPVSSIGS---- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1321 pttvyvdmRALRHDRVRLVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWVSSPHNATGYY 1392
Cdd:cd05910 247 --------RELLATTTAATSGGAGTCV-----GRPIPGVRVrIIEIDDEPIAewddtleLPRGEIGEITVTGPTVTPTYV 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1393 TVYGEETLHADHFSArlsfgdtQTIWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRA 1472
Cdd:cd05910 314 NRPVATALAKIDDNS-------EGFWHRMGDLGYL------DDEGR----LWFCGRKAHRVITTGGTLYTEPVE-RVFNT 375
|
....*...
gi 359807008 1473 HRSIAECA 1480
Cdd:cd05910 376 HPGVRRSA 383
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1012-1179 |
1.84e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1091
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STQAITRLLKSKEAAAAVDVRT---WPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1168
Cdd:PRK12316 2106 TQRHLLERLPLPAGVARLPLDRdaeWADYPDTA--PAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ 2176
|
170
....*....|.
gi 359807008 1169 SIKLQCELYPS 1179
Cdd:PRK12316 2177 AAGERYELSPA 2187
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
985-1244 |
2.26e-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: 48.86 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 985 RAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1064
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1065 PPHPQNlgttlpTVKMIVEVSKSACVLSTQAitrlLKSKEAAAAVDVRtwptiLDTDDIPKKKVASIFRPPSPDVLAYLD 1144
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSH----LQPPIAFIGLIDL-----LDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1145 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1216
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 359807008 1217 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1244
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
978-1067 |
2.95e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 48.60 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 359807008 1058 CVPVTVRPPH 1067
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
982-1508 |
4.65e-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: 47.60 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 982 LQWRAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1061
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1062 tvrpphPQNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtDDipkkkvasifrppspdvLA 1141
Cdd:cd17631 74 ------PLNFRLTPPEVAYILADSGAKVLF-----------------------------DD-----------------LA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1142 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELyPSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLVPPLELESnv 1220
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1221 slWLSAVSQYKARVTFCSYSVME-MCTKGlgaqtgalRMKGVNLSCVRtCMVVAEERPRISLTQSFsklfKDLGLparAV 1299
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1300 STTFGcrvnvaiclQGTTGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVKVIIAHTETKgPLGDSHLGE 1379
Cdd:cd17631 241 VQGYG---------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR-EVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1380 IWVSSPHNATGYytvYGEETLHADhfsarlSFGDTqtiWARTGYLGFLrrteltDASGerhdALYVVGSLDETLELRGMR 1459
Cdd:cd17631 295 IVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRKKDMIISGGEN 352
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 359807008 1460 YHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV-VVVELDGLEQDALDLVALV 1508
Cdd:cd17631 353 VYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELIAHC 406
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
344-572 |
5.29e-05 |
|
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: 47.67 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 344 TALDTAGKatcTLTYGKLWSRSLKLAYTLLNKLTSknepllNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 423
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKD------LRGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLNPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 424 TRKDAgsqqvgfllgscgvtLALTTDAcqkglpkAPTgevatfkgwpplawLVIDGkhltrppkdwyplaqdtgsrtAYI 503
Cdd:cd05941 72 PLAEL---------------EYVITDS-------EPS--------------LVLDP---------------------ALI 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359807008 504 EYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIP 572
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
335-458 |
6.17e-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: 47.22 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 335 TTQPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPvmFMVAFYGCLLAEL 414
Cdd:cd17631 6 RRHPDRTALVFGGR------SLTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAAARLGA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 359807008 415 VPVPIEVPLTRKDagsqqVGFLLGSCGVTLAL-----------TTdacqkGLPKA 458
Cdd:cd17631 71 VFVPLNFRLTPPE-----VAYILADSGAKVLFddlallmytsgTT-----GRPKG 115
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
961-1162 |
6.29e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 47.73 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 961 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVY 1040
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1041 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTilDT 1120
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA--PQ 587
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 359807008 1121 DDIPKkkvasifRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1162
Cdd:PRK10252 588 GAAPL-------QLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
321-796 |
6.78e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 47.49 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 321 NGPLSLLAALQLWGTTQPKApclTALDTAGKATctlTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSDpv 400
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 401 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVTLALTTDA----CQKGLPKAPTGEvatfkgwpplAWLV 476
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDSEfvplLAAILPQLPTVR----------TVIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 477 IDGKHLTRPPKDWY------------PLAQDTGSRTAYIEYKTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEaet 541
Cdd:PRK06187 133 EGDGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 542 ltnvldfkRDAGLwhgVLTSvMNRMHVITIPYALMkvnpLSWIQKVC--SYKARAAL---VKSR--------DMHWSLLA 608
Cdd:PRK06187 208 --------DDVYL---VIVP-MFHVHAWGLPYLAL----MAGAKQVIprRFDPENLLdliETERvtfffavpTIWQMLLK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 609 QRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAV 683
Cdd:PRK06187 272 APRAYFVDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 684 LSmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPYLCKTDEIGEICVNSVATGTAYYGLLGITKNTFEt 763
Cdd:PRK06187 338 RR-----------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID- 393
|
490 500 510
....*....|....*....|....*....|...
gi 359807008 764 vpvtaDGvpvsdrpFTRTGLLGFIGPDNLVFVV 796
Cdd:PRK06187 394 -----GG-------WLHTGDVGYIDEDGYLYIT 414
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1012-1163 |
6.94e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.21 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1082
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1083 EVSKSA--CVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKkkvasIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1160
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 359807008 1161 AAT 1163
Cdd:PRK07656 189 RQL 191
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
337-647 |
9.16e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 337 QPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--EL 414
Cdd:PRK12316 524 TPEAPALAFGEE------TLDYAELNRRANRLAHALI-------ERGVGPDVLVGVAMERSIEMV--VALLAILKAggAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 415 VPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKgwPPLAWLviDGkHLTRPPKdwyplAQ 494
Cdd:PRK12316 589 VPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLD--RPAAWL--EG-YSEENPG-----TE 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 495 DTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTsVMNRMHVITIPYA 574
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPG 730
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359807008 575 LMKvNPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQRDVCLsSLRMLIVADGANPWsisscDAFLNVFQSR 647
Cdd:PRK12316 731 DHR-DPAKLVELINREGVDTlHFVPS---MLQAFLQDEDVASCT-SLRRIVCSGEALPA-----DAQEQVFAKL 794
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1016-1508 |
1.04e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 46.66 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1016 RAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLSTQA 1095
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1096 ITRLLKskeaAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE 1175
Cdd:cd05922 79 AADRLR----DALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1176 LYPSRQIAICLdpycglgfalwclcsvysghqsvlvpPLELESNVSLWLSAVSQYKARVTFCSY----SVMEMCTKglga 1251
Cdd:cd05922 155 ITADDRALTVL--------------------------PLSYDYGLSVLNTHLLRGATLVLTNDGvlddAFWEDLRE---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1252 qTGALRMKGV--NLSCVRTCMVVAEERPRIS-LTQSFSKL-------FKDLGLPARAVsttfgcrvnvaiCLQGTTGPDP 1321
Cdd:cd05922 205 -HGATGLAGVpsTYAMLTRLGFDPAKLPSLRyLTQAGGRLpqetiarLRELLPGAQVY------------VMYGQTEATR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1322 TTVYVDMRalrhdrvRLVERgsPHSLplmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYYTVYGEETlH 1401
Cdd:cd05922 272 RMTYLPPE-------RILEK--PGSI-----GLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRR-K 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1402 ADHFSARLsfgdtqtiwaRTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETSvIRAHRSIAECAV 1481
Cdd:cd05922 336 EGRGGGVL----------HTGDLARR------DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAA 394
|
490 500
....*....|....*....|....*..
gi 359807008 1482 FtwtnllvvvveldGLEQDALDLVALV 1508
Cdd:cd05922 395 V-------------GLPDPLGEKLALF 408
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
338-533 |
1.09e-04 |
|
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: 46.57 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 338 PKAPCLTAldtagkATCTLTYGKLWSRSLKLAYTLLNKLTSknepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 417
Cdd:cd17651 9 PDAPALVA------EGRRLTYAELDRRANRLAHRLRARGVG-------PGDLVALCARRS--AELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 418 PIEVpltrkDAGSQQVGFLLGSCGVTLALTTDACQKGLPkaptgevatfkgwPPLAWLVIDGKHLTRPPKDWYPLAQDTG 497
Cdd:cd17651 74 PLDP-----AYPAERLAFMLADAGPVLVLTHPALAGELA-------------VELVAVTLLDQPGAAAGADAEPDPALDA 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 359807008 498 SRTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQA 533
Cdd:cd17651 136 DDLAYVIY-TS--GSTgrpKGVVMPHRSLANLVAWQARA 171
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
355-539 |
1.42e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 46.11 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 355 TLTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsqq 432
Cdd:cd12114 12 TLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 433 vgfLLGSCGVTLALTTDACQKGLPKAPTgevatfkgwpplawLVIDGKHLTRPPKDwyPLAQDTG-SRTAYIEYkTSkeG 511
Cdd:cd12114 79 ---ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP--PPPVDVApDDLAYVIF-TS--G 136
|
170 180 190
....*....|....*....|....*....|.
gi 359807008 512 ST---VGVTVSHSSLLAQCQALTQACGYTEA 539
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINRRFAVGPD 167
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
322-450 |
2.48e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 45.80 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 322 GPLSLLAALQLWGTTQPKAPcltALDTAGKatcTLTYGKLWSRSLKLAyTLLNKLTSKnepllnPGDRVALVFPNSdPvM 401
Cdd:PRK06178 31 GERPLTEYLRAWARERPQRP---AIIFYGH---VITYAELDELSDRFA-ALLRQRGVG------AGDRVAVFLPNC-P-Q 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 359807008 402 FMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVTLALTTDA 450
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1353-1481 |
2.55e-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: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1353 GKILPGVKVIIAHTETKGPLGDSHlGEIWVSSPHNATGYYTvygEETLHADHFSARlsfgdtqtiWARTGYLGFLRrtel 1432
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 359807008 1433 tdasgeRHDALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1481
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1012-1179 |
2.80e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.10 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1091
Cdd:PRK12316 4581 ELNRRANRLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1092 STQAITRLLKSKEAAAAVDV---RTWPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1168
Cdd:PRK12316 4654 TQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
170
....*....|.
gi 359807008 1169 SIKLQCELYPS 1179
Cdd:PRK12316 4725 ATGERYELTPD 4735
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
324-520 |
5.60e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.65 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 324 LSLLAALQLWGTtqPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLlnkltskNEPLLNPGDRVALVFPNSdpVMFM 403
Cdd:PRK10252 460 LSALVAQQAAKT--PDAPALADARY------QFSYREMREQVVALANLL-------RERGVKPGDSVAVALPRS--VFLT 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 404 VAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKGWPPlawlvidgkh 481
Cdd:PRK10252 523 LALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA---------- 585
|
170 180 190
....*....|....*....|....*....|....*....
gi 359807008 482 ltrpPKDWYPLAQDTGSRTAYIEYKTSKEGSTVGVTVSH 520
Cdd:PRK10252 586 ----PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
978-1160 |
7.51e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 43.88 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1058 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLSTQAITRLLKSKEAAAAV---DVRTWPTILDT 1120
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 359807008 1121 DDI------PKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1160
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
338-447 |
9.82e-04 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 43.46 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 338 PKAPCLTALDTagkaTCTLTYGKLwsrsLKLAYTLLNKLTSKNeplLNPGDRVALVFPNSDPvmFMVAFYGCLLAELVPV 417
Cdd:cd05926 1 PDAPALVVPGS----TPALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVA 67
|
90 100 110
....*....|....*....|....*....|
gi 359807008 418 PIEvPLTRKDagsqQVGFLLGSCGVTLALT 447
Cdd:cd05926 68 PLN-PAYKKA----EFEFYLADLGSKLVLT 92
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
355-446 |
1.08e-03 |
|
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: 43.51 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVG 434
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT-----PDDYA 94
|
90
....*....|..
gi 359807008 435 FLLGSCGVTLAL 446
Cdd:cd05959 95 YYLEDSRARVVV 106
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1012-1063 |
1.12e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 43.56 E-value: 1.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 359807008 1012 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1063
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
978-1161 |
1.19e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.21 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCIQlhkRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1058 C--VPVTVRPPHPQnLGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVD---VRTWPTILDTDDIPKKKVASIF 1132
Cdd:PRK06155 96 AiaVPINTALRGPQ-LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190
....*....|....*....|....*....|
gi 359807008 1133 RPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1161
Cdd:PRK06155 175 AAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
355-417 |
1.97e-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: 42.83 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNkltsknepL-LNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 417
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1352-1481 |
2.55e-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: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 1352 SGKILPGVKVIIAHtETKGPLGDshlGEIWVSSPHNATGYY--TVYGEETlhadhfsarlsfgdTQTIWARTGYLGFLrr 1429
Cdd:cd05912 244 AGKPLFPVELKIED-DGQPPYEV---GEILLKGPNVTKGYLnrPDATEES--------------FENGWFKTGDIGYL-- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 359807008 1430 teltDASGerhdALYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAV 1481
Cdd:cd05912 304 ----DEEG----FLYVLDRRSDLIISGGENIYPAEIEE-VLLSHPAIKEAGV 346
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
338-535 |
2.98e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 338 PKAPCLTaldTAGKatcTLTYGKLWSRSLKLAYTLlnkltskNEPLLNPGDRVALVFPNSdpvMFMVAfygCLLAEL--- 414
Cdd:PRK05691 2202 PQAPALT---FAGQ---TLSYAELDARANRLARAL-------RERGVGPQVRVGLALERS---LEMVV---GLLAILkag 2262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 415 ---VPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGeVATfkgwpplaW-LVIDGKHLTRPPKDwy 490
Cdd:PRK05691 2263 gayVPLDPEYPLER-------LHYMIEDSGIGLLLSDRALFEALGELPAG-VAR--------WcLEDDAAALAAYSDA-- 2324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 359807008 491 PLAQDTGSR-TAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACG 535
Cdd:PRK05691 2325 PLPFLSLPQhQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
978-1059 |
3.43e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 41.78 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHPlFLLLNakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:PRK08279 39 LGDVFEEAAARHPDRP-ALLFE--DQSISYA---ELNARANRYAHWAAARG-VGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
..
gi 359807008 1058 CV 1059
Cdd:PRK08279 112 AV 113
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
355-417 |
6.93e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 40.81 E-value: 6.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359807008 355 TLTYGKLWSRSLKLAYTLLNKLTskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 417
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
339-419 |
7.03e-03 |
|
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: 40.69 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 339 KAPCLTALDTAGKatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVP 418
Cdd:cd05945 3 ANPDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVP 70
|
.
gi 359807008 419 I 419
Cdd:cd05945 71 L 71
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
978-1067 |
7.90e-03 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 40.77 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359807008 978 LADVLQWRAHTTPDHplFLLLNAKGTVTStatcIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1057
Cdd:cd05920 17 LGDLLARSAARHPDR--IAVVDGDRRLTY----RELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90
....*....|
gi 359807008 1058 CVPVTVRPPH 1067
Cdd:cd05920 90 AVPVLALPSH 99
|
|
| |
