|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
955-1529 |
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: 728.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 955 LFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 1033
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1034 TTLPTVKMivEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVA-----SIFRPPSPDVLAYLDFSV 1108
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1109 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1188
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1189 SQYKARVTFCSYSVMEMCTKGLGAQTGALRMKGVNLSCVRTCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRV 1268
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1269 NVAICLqpnrlgklaeQGTTGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHL 1348
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1349 GEIWVSSPHNATGYYTVYGEETLHADHF-SARLSFGDTQTIWARTGYLGFLRRTELTDASGERHDALYVVGSLDETLELR 1427
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFpSTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1428 GMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELD-GLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINS 1506
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 568968175 1507 RGEKQRMHLRDGFLADQLDPIYV 1529
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
303-879 |
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: 655.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 303 CLTALDTAGKATCTLTYGKLWSRSLKLAYTLLNKLTskneplLNPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 382
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 383 PLtrkdaGSQQVGFLLGSCGVTLALTTDACQKGLPKA-----PTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQDT 457
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 458 GSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIPYALM 537
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 538 KVNPLSWIQKVCSYKARAALVKSRDMHWSL------LAQRGQRDVCLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 611
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 612 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGASVCVVKVDGaP 689
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPET-K 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 690 YLCKTDEIGEICVNSVATGTAYYGLLGITKNTFETVPVTADGVPVSDRPFTRTGLLGFIGP----------DNLVFVVGK 759
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 760 LDGLMVVGVRRHNADDIVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 839
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 568968175 840 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 879
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
945-1487 |
9.65e-66 |
|
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: 233.67 E-value: 9.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 945 WRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1024
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1025 RPPHPqnlGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWptiLDTDDIPKKKVASIFRPPS--PDVLA 1102
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---LLVVDLLPDTSAADWPPPSpdPDDIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1103 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESN 1180
Cdd:cd05931 153 YLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1181 VSLWLSAVSQYKARVT----FcSYsvmEMCT-KGLGAQTGALrmkgvNLSCVRTCMVVAeERPRISLTQSFSKLFKDLGL 1255
Cdd:cd05931 231 PLRWLRLISRYRATISaapnF-AY---DLCVrRVRDEDLEGL-----DLSSWRVALNGA-EPVRPATLRRFAEAFAPFGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1256 PARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTTGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPG 1329
Cdd:cd05931 301 RPEAFRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1330 VKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTVyGEETlhADHFSARLSFGDtqTIWARTGYLGFLRRteltdasGE 1409
Cdd:cd05931 364 QEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGR-PEAT--AETFGALAATDE--GGWLRTGDLGFLHD-------GE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1410 rhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAE--CAVFTW----TNLLVVVVELDGLeQDALDLVALVTNV- 1482
Cdd:cd05931 432 ----LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIr 506
|
....*..
gi 568968175 1483 --VLEEH 1487
Cdd:cd05931 507 aaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
294-870 |
1.46e-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: 1.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 294 WGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLLnkltsknePLLNPGDRVALVFPNSdpVMFMVAFYGCLLA 373
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 374 ELVPVPIEVPLTRKDAgsQQVGFLLGSCGVTLALTTDACQKGLPKAptgeVATFKGWPPLAWLVIDGKHLTrPPKDWyPL 453
Cdd:cd05931 72 GAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADW-PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 454 AQDTGSRTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMH-V 529
Cdd:cd05931 144 PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPsV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 530 ITIPYALMKvNPLSWIQKVCSYKAR--AAlvksRDMHWSLLAQRGQR----DVCLSSLRMLIVadGANPWSISSCDAFLN 603
Cdd:cd05931 221 LMSPAAFLR-RPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 604 VFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPGASVCV 682
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 683 VKVDGAPyLCKTDEIGEICV--NSVATGtaYYGLLGITKNTFETVPVTADGvpvsdrPFTRTGLLGFIGPDNLvFVVGKL 760
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVrgPSVASG--YWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 761 DGLMVVGVRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVG 840
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVA 516
|
570 580 590
....*....|....*....|....*....|
gi 568968175 841 VYCLALVPANTLPKAPLGGIHISETKQRFL 870
Cdd:cd05931 517 PADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
943-1427 |
1.75e-48 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 179.05 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 943 LQWRAHTTPDHPLFlllnAKGTVTSTaTCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1022
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1023 TVrpphpqNLGTTLPTVKMIVEVSKSACVLsTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPK-----------KKVAS 1091
Cdd:pfam00501 75 PL------NPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1092 IFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1167
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1168 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAeERPRISLTQSFS 1247
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1248 KLFkdlglpARAVSTTFGcrvnvaiclqpnrlgkLAEqgTTGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 1327
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDEDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1328 PGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEETLHADHFsarlsfgdTQTIWARTGYLGFLrrteltDAS 1407
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 568968175 1408 GErhdaLYVVGSLDETLELR 1427
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
286-870 |
8.90e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 132.76 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 286 SLLAALQLWGTTQPKAPCLT----ALDTAGKATcTLTYGKLWSRSLKLAYTLlNKLTSknepllnPGDRVALVFPNSdpV 361
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVAE-TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 362 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVTLALTTDACqkglpkapTGEVATF----KGWPPLAWLV 437
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 438 IDGKHLTRPPKdwYPLAQDTGSRTAYIEYkTSkeGST---VGVTVSHSSLLAQC-QALTQACGYTEAE-----TLTNVLD 508
Cdd:PRK05850 141 VDLLDLDSPRG--SDARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 509 FKRDAGLWHGVLTSVMNRMH-VITIPYALMKvNPLSWIQkvcsykaraaLVKSRDMHWSL-------LAQRGQRDVCLSS 580
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 581 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 656
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 657 VDTeEKLSvltvqdVGQVMP-----GASVCVVKVDGAPYL----------CKTDEIGEICVN--SVATGtaYYGLLGITK 719
Cdd:PRK05850 349 FDY-EKLS------AGHAKRcetggGTPLVSYGSPRSPTVrivdpdtcieCPAGTVGEIWVHgdNVAAG--YWQKPEETE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 720 NTFETVPVT-ADGVPVSdrPFTRTGLLGFIGPDNLvFVVGKLDGLMVVGVRRHNADDIVATalavepMKFVYRGRIAVFS 798
Cdd:PRK05850 420 RTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAIS 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968175 799 VTVLHDDRIVLVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFL 870
Cdd:PRK05850 491 VPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYR 567
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1101-1479 |
9.16e-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: 127.79 E-value: 9.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1101 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1177
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1178 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEERPrISLTQSFSKLFKDlglpa 1257
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1258 rAVSTTFGcrvnvaiclqpnrlgkLAEqgtTGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVKVIIAHT 1337
Cdd:cd04433 141 -KLVNGYG----------------LTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1338 ETkGPLGDSHLGEIWVSSPHNATGYYTVygeetlhadhfsARLSFGDTQTIWARTGYLGFLRrteltdasgeRHDALYVV 1417
Cdd:cd04433 185 DG-GELPPGEIGELVVRGPSVMKGYWNN------------PEATAAVDEDGWYRTGDLGRLD----------EDGYLYIV 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968175 1418 GSLDETLELRGMRYHPIDIETsVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1479
Cdd:cd04433 242 GRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHV 308
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
939-1469 |
1.18e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.07 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1019 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLSTQAITRLLKSKEAAAAVDVrtwPTILDTDDIPKKkVASI 1092
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPA-LAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1093 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1167
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1168 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEmctkglgaqtGALrmKGVNLSCVRTCMVVAEERPR 1239
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSE----------SAL--ERLDLSRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1240 ISLtQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTTGPDPTTVYVDMRALRHDRVRLVErG 1313
Cdd:PRK05691 305 DSL-ERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-G 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1314 SPhslpLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTvYGEETlhADHFSARlsfgDTQTiWARTG 1393
Cdd:PRK05691 367 SV----LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEAS--AKTFVEH----DGRT-WLRTG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968175 1394 YLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIETSVIRahrsiaECAVFTWTNLLVVVVELDGLE 1469
Cdd:PRK05691 435 DLGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
939-1479 |
5.02e-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: 122.61 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1019 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtddipkkkVASIFrppsp 1098
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALV------------------------------------TALIL----- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1099 dvlayldFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1177
Cdd:COG0318 107 -------YT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1178 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEerpriSLTQSFSKLFKDLglpa 1257
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1258 ravsttFGCRVNvaiclqpNRLGkLAEqgtTGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVKVIIAHT 1337
Cdd:COG0318 239 ------FGVRIV-------EGYG-LTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRIVDE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1338 ETKgPLGDSHLGEIWVSSPHNATGYYTvYGEETlhadhfsaRLSFGDTqtiWARTGYLGFLrrteltDASGErhdaLYVV 1417
Cdd:COG0318 286 DGR-ELPPGEVGEIVVRGPNVMKGYWN-DPEAT--------AEAFRDG---WLRTGDLGRL------DEDGY----LYIV 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968175 1418 GSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1479
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELRAFL 409
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
287-776 |
7.73e-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: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 287 LLAALQLWGTTQPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSDPvmFMVA 366
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 367 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGVTLALTtdacqkglpkaptgevatfkgwpplawlvidgkhltrp 446
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVT-------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 447 pkdwyplaqdtgsrtAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSV 523
Cdd:COG0318 103 ---------------ALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 524 MNRMHVITIPyalmKVNPLSWIQKVCSYKA-RAALVKSrdMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFL 602
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 603 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGASVC 681
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 682 VVKVDGAPylCKTDEIGEICV--NSVATGtaYYGLLGITKNTFetvpvtADGvpvsdrpFTRTGLLGFIGPDNLVFVVGK 759
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVrgPNVMKG--YWNDPEATAEAF------RDG-------WLRTGDLGRLDEDGYLYIVGR 344
|
490
....*....|....*..
gi 568968175 760 LDGLMVVGVRRHNADDI 776
Cdd:COG0318 345 KKDMIISGGENVYPAEV 361
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
317-876 |
5.56e-28 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 121.27 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 317 LTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LTRKDAGSQQV 394
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 395 GFLLGSCGVTLALTTDACQKGLPKAPTGEvatfkgwpPLAWlVIDGKHLTRPPKDWYPLAQDTGSRTAYIEYkTSkeGST 474
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQY-SS--GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 475 ---VGVTVSHSSLLAQCQALTQ-ACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIPYALMKVNPLSWIQKVCs 550
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLIS- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 551 yKARAALVKSRDMHWSLLAQRGQ----RDVCLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEAlT 626
Cdd:PRK09192 268 -RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 627 VAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGASVCVVKVDGAPYlcKTDEIGEICVN-- 703
Cdd:PRK09192 344 LAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERVVGHICVRgp 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 704 SVATGtaYYGllgitkNTFETVPVTADGvpvsdrpFTRTGLLGFIGPDNLVfVVGKLDGLMVVGVRRHNADDIVATAlav 783
Cdd:PRK09192 420 SLMSG--YFR------DEESQDVLAADG-------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIA--- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 784 EPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKAPLGGIHI 862
Cdd:PRK09192 481 EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSR 557
|
570
....*....|....
gi 568968175 863 SETKQRFLEGTLHP 876
Cdd:PRK09192 558 AKAKKRYLSGAFAS 571
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
284-872 |
2.22e-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: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 284 PLSLLAALQLWGTTQPKAPClTALDTAGKATcTLTYGKLWSRSLKLAyTLLNKLTskneplLNPGDRVALVFP-NSDpvm 362
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSEE-FQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 363 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVtlaLTTDACQkglpkAPTGEVATFKGWPPLAWLV 437
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 438 IDGKHLTRPPKDWYPLAQDtgsrTAYIEYKTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAG 514
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 515 LWHGVLTSVMNRMHVITIPYALMKVNPLSWIQKVCSYKA------RAALVKSRDmhwsLLAQRGQRDVCLSSLRMLIVAD 588
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 589 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 665
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 666 LTVQDVGQVMPGASVCVVKVDGApyLCKTDEIGE--ICVNSVATGtaYYGLLGITKNTFetvpvTADGvpvsdrpFTRTG 743
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRlqVRGPVVTKG--YYNNPEANAEAF-----TEDG-------WFRTG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 744 LLGFIGPDNLVFVVGKLDGLMVVGVrRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSf 823
Cdd:cd05906 415 DLGFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDA- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 568968175 824 qwMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 872
Cdd:cd05906 490 --LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
973-1443 |
9.97e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 111.37 E-value: 9.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1044
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1045 vsksacVLSTQAITRLLKSKEAAAAVDVRtwPTILDTDDIPKKkVASIFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1121
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDS-AGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1122 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1198
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1199 SYSVMEmctkgLGAQTGALRM-KGVNLSCVrtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpn 1277
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG------------ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1278 rlgkLAEQ----GTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEI 1351
Cdd:PRK12476 357 ----IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1352 WVSSPHNATGYY-----TvygEETLHAdHFSARLSFG------DTQTIWARTGYLGFLRRTEltdasgerhdaLYVVGSL 1420
Cdd:PRK12476 433 WLHGDNIGRGYWgrpeeT---ERTFGA-KLQSRLAEGshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRI 497
|
490 500
....*....|....*....|...
gi 568968175 1421 DETLELRGMRYHPIDIETSVIRA 1443
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEATVAEA 520
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
305-767 |
1.25e-24 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 108.55 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 305 TALDTAGkaTCTLTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpl 384
Cdd:pfam00501 12 TALEVGE--GRRLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 385 trkDAGSQQVGFLLGSCGVTLALTTD--------ACQKGLPKAPTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQD 456
Cdd:pfam00501 79 ---RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 457 TgsrTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQAC----GYTEAETLTNVLDFKRDAGLWHGVLTSVMN--RM 527
Cdd:pfam00501 156 D---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAgaTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 528 HVITIPYALMKVNPLSWIQKvcsYKARAALVKSRDMHWsLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqs 607
Cdd:pfam00501 230 VLPPGFPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 608 rglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQVMPGASVCVVKVDG 687
Cdd:pfam00501 302 ----GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGRPLPGTEVKIVDDET 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 688 APYLcKTDEIGEICV--NSVATGtaYYGLLGITKNTFetvpvTADGvpvsdrpFTRTGLLGFIGPDNLVFVVGKLDGLMV 765
Cdd:pfam00501 351 GEPV-PPGEPGELCVrgPGVMKG--YLNDPELTAEAF-----DEDG-------WYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
..
gi 568968175 766 VG 767
Cdd:pfam00501 416 LG 417
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
347-874 |
3.13e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.82 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 347 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVTLALTTDACQKGLPKapt 421
Cdd:PRK07769 78 PGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGVRK--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 422 gevaTFKGWPP------LAwlvID------GKHLTRPPKDwyplaQDTgsrTAYIEYkTSkeGST---VGVTVSHSSLLA 486
Cdd:PRK07769 146 ----FFRARPAkerprvIA---VDavpdevGATWVPPEAN-----EDT---IAYLQY-TS--GSTripAGVQITHLNLPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 487 QCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNrmHVITI--PYALMKvNPLSWIQKVCSYKARAALVKSR--D 562
Cdd:PRK07769 208 NVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAapN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 563 MHWSLLAQRG-----QRDVCLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPPDlg 636
Cdd:PRK07769 285 FAFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTPMDE-- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 637 gpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGASVCVVKVDGAPYLcKTDEIGEICVNSVATGTAYYGLL 715
Cdd:PRK07769 361 --EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 716 GITKNTFE------TVPVTADGVPvSDRPFTRTGLLGFIGPDNLvFVVGKLDGLMVVGVRRHNADDIVATALavEPMKFV 789
Cdd:PRK07769 437 EETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKAL 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 790 YRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPA 849
Cdd:PRK07769 513 RTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPA 592
|
570 580
....*....|....*....|....*
gi 568968175 850 NTLPKAPLGGIHISETKQRFLEGTL 874
Cdd:PRK07769 593 GSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
939-1483 |
3.41e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.18 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCIQLHKRAERVAAALMEKGrlDAGDHVALVYPPGVDLIAAFYGCL 1015
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1016 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLSTqaitrllkskeAAAAVDVRTW---------PTI--LDTDDI 1084
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVieVDLLDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1085 PKKKVASIFRPPSPDVlAYLDFSVSTTGILAGVKMSHAATSALCRSI------KLQCELYPSRQIAICLDPYCGLGFALW 1158
Cdd:PRK05850 147 DSPRGSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1159 CLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaQTGALRMKGVNLSCVRTcMVVAEERP 1238
Cdd:PRK05850 226 VCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVR----KTSDDDMAGLDLGGVLG-IISGSERV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1239 RISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAE------QGTTGPDPTTVYVDMRALRHDRVR---- 1308
Cdd:PRK05850 301 HPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEKLSAGHAKrcet 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1309 -----LVERGSPHSlplmesgkilPGVKVIIAHTETKGPLGDshLGEIWVSSPHNATGYYTVyGEETLHAdhFSARL--- 1380
Cdd:PRK05850 365 gggtpLVSYGSPRS----------PTVRIVDPDTCIECPAGT--VGEIWVHGDNVAAGYWQK-PEETERT--FGATLvdp 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1381 SFGDTQTIWARTGYLGFLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV--IRAHRsiaeCAVFT---- 1454
Cdd:PRK05850 430 SPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIqeITGGR----VAAISvpdd 494
|
570 580 590
....*....|....*....|....*....|..
gi 568968175 1455 WTNLLVVVVEL---DGLEQDALDLVALVTNVV 1483
Cdd:PRK05850 495 GTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
347-876 |
6.16e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 99.05 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 347 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVTLALTTDACQ-------K 414
Cdd:PRK12476 91 PGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpghAERLDT-------ALRDAEPTVVLTTTAAAeavegflR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 415 GLPKAPTGEVATFKGWPPLAwlvidGKHLTRPPKDwyplAQDTgsrtAYIEYkTSkeGST---VGVTVSHSSLlaqCQAL 491
Cdd:PRK12476 162 NLPRLRRPRVIAIDAIPDSA-----GESFVPVELD----TDDV----SHLQY-TS--GSTrppVGVEITHRAV---GTNL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 492 TQ---ACGYTEAETLT-NVLDFKRDAGLWHGVLTSVMNRMHVITIPYALMKvNPLSWIQKVcSYKARAALV--KSRDMHW 565
Cdd:PRK12476 223 VQmilSIDLLDRNTHGvSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKAL-SEGSRTGRVvtAAPNFAY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 566 SLLAQRG----QRDVCLSSLRMLIvadGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPR 641
Cdd:PRK12476 301 EWAAQRGlpaeGDDIDLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 642 KAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGASVCVVKVDGAPYLcKTDEIGEICVNSVATGTAYYGLLGITKN 720
Cdd:PRK12476 375 VVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETER 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 721 TFETVPVT-------ADGVPVSDRPFtRTGLLGFIgPDNLVFVVGKLDGLMVVGVRRHNADDIVATALAVEPMkfVYRGR 793
Cdd:PRK12476 453 TFGAKLQSrlaegshADGAADDGTWL-RTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGY 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 794 IAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGT 873
Cdd:PRK12476 529 VTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGR 608
|
...
gi 568968175 874 LHP 876
Cdd:PRK12476 609 LGV 611
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
284-904 |
7.32e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.16 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 284 PLSLLAALQLWGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLlnkltsknEPLLNPGDRVALVFPnSDPvMF 363
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-DY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 364 MVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkGWPPlaWLVIDGkhL 443
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPE--LLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 444 TRPPKDWYPLAQDTGSRTAYIEYkTSkeGSTV---GVTVSHSSLLAQCQALTQACG--YTEAETLTNVLDFKRDAGLWHG 518
Cdd:PRK05691 151 DPALAEAWQEPALQPDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 519 VLTSVMNRMHVITIPYALMKVNPLSWIQKVCSYkaRAALVKSRDMHWSLLAQRgQRDVCLSSL---RMLIVADGANPWSI 595
Cdd:PRK05691 228 LLQPIFSGVPCVLMSPAYFLERPLRWLEAISEY--GGTISGGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 596 SSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQV 674
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARNRAEPGTGSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 675 M-------PGASVCVVKVDGAPYLcKTDEIGEICVN--SVATGtaYYGLLGITKNTFetvpVTADGvpvsdRPFTRTGLL 745
Cdd:PRK05691 369 LmscgrsqPGHAVLIVDPQSLEVL-GDNRVGEIWASgpSIAHG--YWRNPEASAKTF----VEHDG-----RTWLRTGDL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 746 GFIgPDNLVFVVGKLDGLMVvgVRRHN--ADDIVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE-----QRPDAS 818
Cdd:PRK05691 437 GFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPP 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 819 EEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVTNLPKPRQKQP 898
Cdd:PRK05691 512 QA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEA 577
|
....*.
gi 568968175 899 EVGPAS 904
Cdd:PRK05691 578 AQTAAS 583
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
973-1462 |
1.16e-19 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 94.66 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1051
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1052 LSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSi 1131
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL---PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1132 KLQCELYPSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSvmeMCTK 1208
Cdd:cd05906 199 KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1209 gLGAQTGALRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRVNVAIClqpnrlgklaeqgtt 1288
Cdd:cd05906 274 -LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV--------------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1289 gpdptTVYVDMRALRHdrvrlvergsPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGE 1368
Cdd:cd05906 337 -----IYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIV-DDEGQLLPEGEVGRLQVRGPVVTKGY---YNN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1369 ETLHADHFsarlsfgdTQTIWARTGYLGFLrrteltdasgeRHDALYVVGSLDETLELRGMRYHPIDIETSV----IRAH 1444
Cdd:cd05906 398 PEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEP 458
|
490 500
....*....|....*....|.
gi 568968175 1445 RSIAECAVF---TWTNLLVVV 1462
Cdd:cd05906 459 SFTAAFAVRdpgAETEELAIF 479
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
973-1452 |
1.39e-19 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 93.10 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1052
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STQAiTRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVASifrPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1132
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1133 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1206
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1207 TKGLGAQTGALRMkgvnlscvrtcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNvaiclqpnrlgklaeqg 1286
Cdd:TIGR01733 227 AAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN----------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1287 TTGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYytvY 1366
Cdd:TIGR01733 267 LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---L 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1367 GEETLHADHFSARLSFGDTQTIWARTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRS 1446
Cdd:TIGR01733 335 NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPG 403
|
....*.
gi 568968175 1447 IAECAV 1452
Cdd:TIGR01733 404 VREAVV 409
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
973-1447 |
1.30e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 91.71 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1044
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1045 VSKSAcvlstQAITRLLKSKEAAAAvdvrtwPTILDTDDIPKKkVASIFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1121
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1122 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1195
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1196 tfcsYSVMEMCTKGLGAQTGaLRMKG---VNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvai 1272
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARG-LPKDGeppLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1273 clqpnrlgkLAEQ----GTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDS 1346
Cdd:PRK07769 346 ---------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1347 HLGEIWVSSPHNATGYYTvYGEETLHADH--FSARLSFGDTQ-----TIWARTGYLGflrrtelTDASGErhdaLYVVGS 1419
Cdd:PRK07769 417 QIGEIWLHGNNIGTGYWG-KPEETAATFQniLKSRLSESHAEgapddALWVRTGDYG-------VYFDGE----LYITGR 484
|
490 500
....*....|....*....|....*...
gi 568968175 1420 LDETLELRGMRYHPIDIETSVIRAHRSI 1447
Cdd:PRK07769 485 VKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
929-1440 |
6.53e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 86.21 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 929 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGV 1005
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1006 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLSTQAITRLLksKEAAAAVDVRTWPTILDTD 1082
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1083 DIPKKKVAsiFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1161
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1162 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGAlrmkGVNLSCVRTCMVVAEE-RPR 1239
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLA----ELDLSCWRVAGIGADMiRPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1240 IslTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPNRLGKLAEQgttgpdpttvyVDMRALRHDR--VRLVERGSPH 1316
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPLGSGIVVEE-----------VDRDRLEYQGkaVAPGAETRRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1317 SlPLMESGKILPGVKVIIaHTETKGPLGDSHLGEIWVSSPHNATGYYTvyGEETlhADHFSArlsfgdtqTIWARTGYLG 1396
Cdd:PRK09192 382 R-TFVNCGKALPGHEIEI-RNEAGMPLPERVVGHICVRGPSLMSGYFR--DEES--QDVLAA--------DGWLDTGDLG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 568968175 1397 FLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV 1440
Cdd:PRK09192 448 YL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIA 480
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-83 |
1.13e-16 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 77.07 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 10 AAPLPAEVLESLAELELELSEGDITQKGYEKKRAKLLARYIP---------------------------LIQDVHTEAVQ 62
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLhpetptklsaeaqnqlasletklrdeeLSEEVYLEKVK 81
|
90 100
....*....|....*....|...
gi 568968175 63 AALAKYKERKM--PMPSKRRSAL 83
Cdd:pfam06464 82 ALLAKELERENglNAPTKEQSGL 104
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
970-1453 |
3.33e-16 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 83.42 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 970 TCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1049
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1050 CVLSTQAITRLLKSKEAAAAVDVRTW------PTILDTDDI--PKKKVASIFRPP----SPDVLAYLDFSVSTTGILAGV 1117
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpDGVLSIEDLlsPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1118 KMSH---AATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQYKA 1193
Cdd:cd05911 165 CLSHrnlIANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1194 RVTF------CSYSVMEMCTKGlgaqtgalrmkgvNLSCVRTCMVVAEerprisltqSFSKLFKDLglparavsttFGCR 1267
Cdd:cd05911 238 TFLYlvppiaAALAKSPLLDKY-------------DLSSLRVILSGGA---------PLSKELQEL----------LAKR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1268 VNVAICLQpnrlgklaEQGTTGPDPTTVYvdmralrhdrvrlvergSPHSLPLMES-GKILPGVKVIIAHTETKGPLGDS 1346
Cdd:cd05911 286 FPNATIKQ--------GYGMTETGGILTV-----------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDSLGPN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1347 HLGEIWVSSPHNATGYytvYGEETLHADHFsarlsfgdTQTIWARTGYLGFLRRTELtdasgerhdaLYVVGSLDETLEL 1426
Cdd:cd05911 341 EPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYFDEDGY----------LYIVDRKKELIKY 399
|
490 500
....*....|....*....|....*..
gi 568968175 1427 RGMRYHPIDIEtSVIRAHRSIAECAVF 1453
Cdd:cd05911 400 KGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
966-1455 |
1.80e-14 |
|
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: 78.18 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 966 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1045
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1046 SKSACVLSTQAITRLLKSKEAAAAVDVRT----------WPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILA 1115
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1116 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVPPLELESNVslwL 1185
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAV---F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1186 SAVSQYKARVTFCS---YSVMemctkglgaqTGALRMKGVNLSCVRTCMVVAEERPRiSLTQSFSKLfkdlglparavst 1262
Cdd:cd05959 248 KRIRRYRPTVFFGVptlYAAM----------LAAPNLPSRDLSSLRLCVSAGEALPA-EVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1263 tFGCRVNVAIclqpnrlgklaeqGTTgpDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVIIAHtETKGP 1342
Cdd:cd05959 304 -FGLDILDGI-------------GST--EMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1343 LGDSHLGEIWVSSPHNATGYYTVYgEETlhadhfsaRLSFgdtQTIWARTGYlGFLRrteltDASGerhdALYVVGSLDE 1422
Cdd:cd05959 353 VADGEPGELYVRGPSSATMYWNNR-DKT--------RDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADD 410
|
490 500 510
....*....|....*....|....*....|...
gi 568968175 1423 TLELRGMRYHPIDIEtSVIRAHRSIAECAVFTW 1455
Cdd:cd05959 411 MLKVSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
460-767 |
3.54e-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: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 460 RTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPyal 536
Cdd:cd04433 1 DPALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 537 mKVNPLSWIQKVCSYKARAALVkSRDMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVIC 616
Cdd:cd04433 74 -KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 617 PCASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPylCKTDE 696
Cdd:cd04433 145 GYGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGE 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968175 697 IGEICVNSvatgtaYYGLLGITKNTFETVPVTADGvpvsdrpFTRTGLLGFIGPDNLVFVVGKLDGLMVVG 767
Cdd:cd04433 194 IGELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
973-1475 |
3.63e-13 |
|
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: 73.72 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSACVL 1052
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1132
Cdd:cd05930 90 TD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1133 lqcELYPSR------QIAicldpycGLGF--ALWCL-CSVYSGHQSVLVPPlELESNVSLWLSAVSQYKARVTFCSYSVM 1203
Cdd:cd05930 127 ---EAYPLTpgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1204 EMCtkglgAQTGALRMkgvnLSCVRTcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNVaiclqpnrlgkla 1283
Cdd:cd05930 196 RLL-----LQELELAA----LPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1284 eqgtTGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYy 1363
Cdd:cd05930 241 ----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGY- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1364 tvYGEETLHADHFSArLSFGDTQTIWaRTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETsVIRA 1443
Cdd:cd05930 306 --LNRPELTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLA 370
|
490 500 510
....*....|....*....|....*....|....*...
gi 568968175 1444 HRSIAECAVFTWTN------LLVVVVELDGLEQDALDL 1475
Cdd:cd05930 371 HPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
345-854 |
1.97e-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: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 345 LNPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVTLALT----TDACQKGLP 417
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVLAdagaADRLRDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 418 KAPTgevatfkgwpPLAWLVIDGKHLTRPPKDWYPLAQDTgsrTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGY 497
Cdd:cd05922 89 ASPD----------PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 498 TEAETLTNVLDFKRDAGLwhGVLTSVMNR--MHVITIPYALmkvnPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQR 574
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgaTLVLTNDGVL----DDAFWEDLREHGATGlAGVPS---TYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 575 DVCLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavlsmn 648
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 649 glsygvirvdteeklsvltvQDVGQVMPGASVCVVKVDGAPylCKTDEIGEIcVNSVATGTAYYGllgiTKNTFETVPVT 728
Cdd:cd05922 286 --------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKEGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 729 ADGVpvsdrpfTRTGLLGFIGPDNLVFVVGKLDGLMVVGVRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDDRIV 808
Cdd:cd05922 339 GGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKLA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568968175 809 LVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 854
Cdd:cd05922 407 LFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
973-1472 |
2.53e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.34 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGRLDAgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1048
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1049 acVLSTQAITRLLKSKEAAAAV-DVRTWPtildtddipKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1127
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1128 CRSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVM 1203
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1204 emctkglgaqtG--ALRMKGVNLSCVRTCmVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgk 1281
Cdd:PRK05851 260 -----------GkyARRVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG---------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1282 LAEQ--GTTGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNA 1359
Cdd:PRK05851 312 LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1360 TGYytvYGEETLHADHfsarlsfgdtqtiWARTGYLGFlrrteLTDasgerhDALYVVGSLDETLELRGMRYHPIDIET- 1438
Cdd:PRK05851 384 SGY---LGQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERv 436
|
490 500 510
....*....|....*....|....*....|....*....
gi 568968175 1439 -SVIRAHRSIAECAVFTWTNL----LVVVVELDGLEQDA 1472
Cdd:PRK05851 437 aAQVRGVREGAVVAVGTGEGSarpgLVIAAEFRGPDEAG 475
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
316-765 |
4.44e-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: 70.32 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI-------EVPLTRKD 388
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAAnpiytadELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 389 AGSQqvgfLLGSCGVTLALTTDACQKGLPKAptgEVATFKGWPPLawlVIDGKHLTRPP---KDWYPLAQ--DTGSRTAY 463
Cdd:cd05911 81 SKPK----VIFTDPDGLEKVKEAAKELGPKD---KIIVLDDKPDG---VLSIEDLLSPTlgeEDEDLPPPlkDGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 464 IEYkTSkeGST---VGVTVSHSSLLAQC-QALTQACGYTEA-ETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPyalmK 538
Cdd:cd05911 151 ILY-SS--GTTglpKGVCLSHRNLIANLsQVQTFLYGNDGSnDVILGFLPLYHIYGLF-TTLASLLNGATVIIMP----K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 539 VNPLSWIQKVCSYKARAALVKSRDMHW---SLLAQRGQrdvcLSSLRMLIVadGANPWSISSCDAFLNVFQSRGLRP--- 612
Cdd:cd05911 223 FDSELFLDLIEKYKITFLYLVPPIAAAlakSPLLDKYD----LSSLRVILS--GGAPLSKELQELLAKRFPNATIKQgyg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 613 --EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPY 690
Cdd:cd05911 297 mtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPNVEAKIVDDDGKDS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 691 LcKTDEIGEICVNSvatGTAYYGLLGITKNTFETvpVTADGvpvsdrpFTRTGLLGFIGPDNLVFVVG------KLDGLM 764
Cdd:cd05911 337 L-GPNEPGEICVRG---PQVMKGYYNNPEATKET--FDEDG-------WLHTGDIGYFDEDGYLYIVDrkkeliKYKGFQ 403
|
.
gi 568968175 765 V 765
Cdd:cd05911 404 V 404
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
939-1173 |
6.06e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 69.90 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLLLNAKgtvtstATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1019 CVPVTVRPphpqnlgttlptvkmivevsksacVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifrpPSP 1098
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1099 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1172
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 568968175 1173 P 1173
Cdd:cd05936 201 P 201
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
947-1129 |
6.64e-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: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 947 AHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGRLDaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1026
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARGVGP-GDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1027 PHPQnlgttlPTVKMIVEVSKSACVLSTQAitrllkskEAAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDF 1106
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPA--------LAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 568968175 1107 SVSTTGILAGVKMSHAATSALCR 1129
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
317-761 |
1.00e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 317 LTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqV 394
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYPAER-------L 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 395 GFLLGSCGVTLALTTDACQKGLPkaPTGEVATFKGWPPLAWLvidgkhlTRPPKDwyPLAQDTGSRTAYIEYKTSKEGST 474
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWA-------DYPDTA--PAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 475 VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPYALmkvnplsWIQKVCSYKAR 554
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDEL-------WDPEQLYDEME 2233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 555 AALVKSRDM---HWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAflnvfQSRGLRPEVIcpcasspealtvairr 631
Cdd:PRK12316 2234 RHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEALRPVYL---------------- 2290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 632 ppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGASVCVvkVDGAPYLCKTDEIGEICVNSVATGTAY 711
Cdd:PRK12316 2291 ---FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLNLLAPGMAGELYLGGEGLARGY 2359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568968175 712 YGLLGITKNTFETVPVTADGVPVsdrpfTRTGLLGFIGPDNLVFVVGKLD 761
Cdd:PRK12316 2360 LNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRID 2404
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
947-1478 |
2.96e-10 |
|
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: 64.58 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 947 AHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1026
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1027 PHPqnlgttlptvkmivevsksacvlstqaITRLLKSKEAAAavdvrtwPTILDTDdipkkkvasifrppsPDVLAYLDF 1106
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1107 SVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPY---CGLgFALWclCSVYSGHQSVLVPPLELEsNVSL 1183
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPFsfdLSV-MDLY--PALASGATLVPVPRDATA-DPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1184 WLSAVSQYKARVTFCSYSVMEMCTkGLGAQTGAlrmkgvNLSCVRTCMVVAEERPrISLTQSFSKLFkdlglPARAVSTT 1263
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQQRF-----PDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1264 FgcrvnvaiclqpnrlgklaeqgttGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVKVIIAhTETKGPL 1343
Cdd:cd05945 247 Y------------------------GPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVIL-DEDGRPV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1344 GDSHLGEIWVSSPHNATGYYTVygeetlhADHFSARLSFGDTQTiWARTGYLGFLrrteltDASGErhdaLYVVGSLDET 1423
Cdd:cd05945 294 PPGEKGELVISGPSVSKGYLNN-------PEKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRLDFQ 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1424 LELRGMRYHPIDIETSViRAHRSIAECAVFTWTNL-----LVVVVELDGlEQDALDLVAL 1478
Cdd:cd05945 356 VKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKP-GAEAGLTKAI 413
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
318-761 |
4.48e-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: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 318 TYGKLWSRSLKLAYTLLNKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 395
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVG------PGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 396 FLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkgwPPLAWLVIDGKHLTRPPKDWYPLAQDtgsrTAYIEYkTSkeGST- 474
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSGPDD----LAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 475 --VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVITIPYALMKVNPLSWiqkvcsyk 552
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 553 arAALVKSRDM-HWSLLAqrgqrdvclSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 630
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 631 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGASVCVvkVDGAPYLCKTDEIGEIC 701
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYV--LDDDLRPVPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968175 702 VN--SVATGtaYYGLLGITKNTFetvpVTADGVPVSDRPFTRTGLLGFIGPD-NLVFvVGKLD 761
Cdd:TIGR01733 324 IGgpGVARG--YLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPDgNLEF-LGRID 379
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
973-1437 |
4.78e-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: 64.05 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGttlptvkmivevSKSACVL 1052
Cdd:cd05908 20 HLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV------PVSIG------------SNEEHKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STQAITRLLKSkeaaaavdvrtwPTILDTDDIPKKkvasifrppSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1132
Cdd:cd05908 81 KLNKVWNTLKN------------PYLITEEEVLCE---------LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1133 LQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGA 1212
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1213 QTGAlrmkGVNLSCVRtcMVVAEERPRIS-LTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPnrlgklaeqgtTGP 1290
Cdd:cd05908 220 EKAN----DWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEASVGASLPK-----------AQS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1291 DPTTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGpLGDSHLGEIWVSSPHNATGYYTvyGEE 1369
Cdd:cd05908 283 PFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGYYN--NPE 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968175 1370 TlhadhfSARLSFGDTqtiWARTGYLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIE 1437
Cdd:cd05908 360 A------TAKVFTDDG---WLKTGDLGFIRNGR-----------LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
973-1196 |
8.41e-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: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1050
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1051 VLSTQAItrllkskeAAAAVDVRTWPTILDTDDIPKKKVASifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1130
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968175 1131 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1196
Cdd:cd12114 158 INRRFAVGPDdRVLAL-----SSLSFDL----SVYdifgalsAGATLVLPDEAR-RRDPAHWAELIERH--GVT 219
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
973-1452 |
1.27e-09 |
|
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: 62.64 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVpvtVRPPHPQNlgtTLPTVKMIVEVSKsACVL 1052
Cdd:cd05904 37 ELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAV---VTTANPLS---TPAEIAKQVKDSG-AKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STQAiTRLLKSKEAAAAV------DVRTWPTILDTDDIPkkkVASIFRPP-SPDVLAYLDFSVSTTGILAGVKMSHA-AT 1124
Cdd:cd05904 109 FTTA-ELAEKLASLALPVvlldsaEFDSLSFSDLLFEAD---EAEPPVVViKQDDVAALLYSSGTTGRSKGVMLTHRnLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1125 SALCRSIKLQCELYPSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLVPPLELESnvslWLSAVSQYkaRVTFCSYS-- 1201
Cdd:cd05904 185 AMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY--KVTHLPVVpp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1202 -VMEMCTKGLGaqtgalrmKGVNLSCVRTCMVVAeerprisltqsfSKLFKDLglpARAVSTTFGcrvNVAIClqpnrlg 1280
Cdd:cd05904 259 iVLALVKSPIV--------DKYDLSSLRQIMSGA------------APLGKEL---IEAFRAKFP---NVDLG------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1281 klaeQG----TTGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSP 1356
Cdd:cd05904 306 ----QGygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1357 HNATGYytvygeetlhadhfsarlsFGDTQ----TI----WARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRG 1428
Cdd:cd05904 367 SIMKGY-------------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKG 417
|
490 500
....*....|....*....|....
gi 568968175 1429 MRYHPIDIEtSVIRAHRSIAECAV 1452
Cdd:cd05904 418 FQVAPAELE-ALLLSHPEILDAAV 440
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
973-1478 |
1.51e-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: 62.31 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGRlDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1052
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STQAItrllkskEAAAAVDVRTWPTILDTDDIPkkkVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1132
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1133 LQCELYPSRQIaICLDPYCglgF---ALWCLCSVYSGHQSVLVPPlelesnvslwlsavsqykarvtfcsysvmemctkg 1209
Cdd:cd12116 160 ERLGLGPGDRL-LAVTTYA---FdisLLELLLPLLAGARVVIAPR----------------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1210 lGAQTGALRMKGvnlscvrtcmvvAEERPRISLTQ---SFSKLFKDLGLPARAVSTtfgcrvnvAIC----LQPNRLGKL 1282
Cdd:cd12116 201 -ETQRDPEALAR------------LIEAHSITVMQatpATWRMLLDAGWQGRAGLT--------ALCggeaLPPDLAARL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1283 AEQGTT-----GPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------G 1349
Cdd:cd12116 260 LSRVGSlwnlyGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVL---------DAALrpvppgvpG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1350 EIWVSSPHNATGYytvYGEETLHADHFSArLSFGDTQTIWARTGYLgfLRRteLTDASgerhdaLYVVGSLDETLELRGM 1429
Cdd:cd12116 319 ELYIGGDGVAQGY---LGRPALTAERFVP-DPFAGPGSRLYRTGDL--VRR--RADGR------LEYLGRADGQVKIRGH 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568968175 1430 RYHPIDIETsVIRAHRSIAECAVFTWTN----LLVVVVELDGLEqdALDLVAL 1478
Cdd:cd12116 385 RIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA--APDAAAL 434
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
973-1452 |
1.71e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 62.32 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgTTLP-----TVKMIVEVSK 1047
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPR---TDLAvwaedTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1048 SACVLS---TQAITRLlkskeAAAAVDVRTWPTILDTDDIpkkkvasifRPP--SPDVLAYLDFSVSTTGILAGVKMSHA 1122
Cdd:PRK07768 110 KAVVVGepfLAAAPVL-----EEKGIRVLTVADLLAADPI---------DPVetGEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1123 ATSALCRSIKLQCELYPSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLVPPLELESNVSLWLSAVSQYKARVT- 1196
Cdd:PRK07768 176 NLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1197 ---FcSYSVMemcTKGLGAQTgalRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFG-CRVNVAI 1272
Cdd:PRK07768 252 apnF-AYALL---ARRLRRQA---KPGAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1273 CLQPnrlgklaeqgtTGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIW 1352
Cdd:PRK07768 324 SFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGLEVRVV-DEDGQVLPPRGVGVIE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1353 VSSPHNATGYYTVYGEETLHADHfsarlsfGdtqtiWARTGYLGFLrrTELtdasGErhdaLYVVGSLDETLELRGMRYH 1432
Cdd:PRK07768 391 LRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 568968175 1433 PIDIETSVIRAHRSIAECAV 1452
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
316-516 |
3.88e-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: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 393
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 394 VGFLLGSCGVTLALTTDACQKGLPKAPtgevatfkgwppLAWLVIDGKHLTRPPKDWyPLAQDTGSRTAYIEYkTSkeGS 473
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568968175 474 T---VGVTVSHSSLLAQCQALTQACGYTEAETLTNV--LDFkrDAGLW 516
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
305-507 |
6.65e-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: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 305 TALDTAGKatcTLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 384
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 385 TrkdagSQQVGFLLGSCGVTLALTtdacqkglpkaptgeVATFkgwpplawlvidgKHLTRPPKDWYPLAQDTGSRTAYI 464
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568968175 465 EYkTSkeGST---VGVTVSHSSLLA---QCQALTQACGyTEAETLTNVL 507
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKAWLEDLL-EGDDVVLAAL 175
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
973-1197 |
1.17e-08 |
|
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: 60.26 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1048
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1049 ACVLSTQAITRLLKSKEAaaavdvrtwPTI-LDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1127
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1128 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYkaRVT 1196
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARH--RVT 710
|
.
gi 568968175 1197 F 1197
Cdd:COG1020 711 V 711
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
946-1123 |
2.16e-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: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 946 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1025
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1026 PPHPQnlgttlPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasifrPPSPDVLAYLD 1105
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 568968175 1106 FSVSTTGILAGVKMSHAA 1123
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
289-582 |
3.36e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 289 AALQLWGTTQ---PKAPCLTAL--DTAGKA---------TCTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALV 354
Cdd:PRK12316 4535 RIVALWNRTDagyPATRCVHQLvaERARMTpdavavvfdEEKLTYAELNRRANRLAHALI-------ARGVGPEVLVGIA 4607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 355 FPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPkAPTGevatfkgwpp 432
Cdd:PRK12316 4608 MERS--AEMMVGLLAVLKAggAYVPLDPEYPRER-------LAYMMEDSGAALLLTQSHLLQRLP-IPDG---------- 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 433 LAWLVIDgkhltrPPKDWY------PLAQDTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNV 506
Cdd:PRK12316 4668 LASLALD------RDEDWEgfpahdPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQF 4741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 507 LDFKRDA---GLWHGVLT--SVMNRMHVITIP---YALMKVNPLSWIQKVCSYkaraalvksrdmhWSLLAQRGQRDVCL 578
Cdd:PRK12316 4742 MSFSFDGsheGLYHPLINgaSVVIRDDSLWDPerlYAEIHEHRVTVLVFPPVY-------------LQQLAEHAERDGEP 4808
|
....
gi 568968175 579 SSLR 582
Cdd:PRK12316 4809 PSLR 4812
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
939-1453 |
4.55e-08 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 57.80 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1019 CVPVTVrpphpqnlGTTLPT--VKMIVEVSKS-ACVLSTQAI-TRLLKSKEAAAAV---------------DVRTWPTIL 1079
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEQlDKLLEVRDELPSLrhivvldprglrddpRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1080 D--TDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS-RQIAIcldpycgLGFA 1156
Cdd:COG1022 162 AlgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGdRTLSF-------LPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1157 -----LWCLCSVYSGHQSVLVPPLElesNVSLWLSAVsqykaRVTF-CS--------YS-VMEMctkglGAQTGALRMKG 1221
Cdd:COG1022 235 hvferTVSYYALAAGATVAFAESPD---TLAEDLREV-----KPTFmLAvprvwekvYAgIQAK-----AEEAGGLKRKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1222 VNLsCVRTCMVVAEER---PRISLTQS----------FSKLfkdlglpaRAVsttFGCRVNVAIC----LQPNrlgkLAE 1284
Cdd:COG1022 302 FRW-ALAVGRRYARARlagKSPSLLLRlkhaladklvFSKL--------REA---LGGRLRFAVSggaaLGPE----LAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1285 ----------QG-----TTGPdpTTVYvdmralRHDRVRLverGSphslplmeSGKILPGVKVIIAHTetkgplgdshlG 1349
Cdd:COG1022 366 ffralgipvlEGyglteTSPV--ITVN------RPGDNRI---GT--------VGPPLPGVEVKIAED-----------G 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1350 EIWVSSPHNATGYY-----TvygEETLHADhfsarlsfGdtqtiWARTGYLGFLrrteltDASGErhdaLYVVGSLDETL 1424
Cdd:COG1022 416 EILVRGPNVMKGYYknpeaT---AEAFDAD--------G-----WLHTGDIGEL------DEDGF----LRITGRKKDLI 469
|
570 580 590
....*....|....*....|....*....|
gi 568968175 1425 ELR-GMRYHPIDIEtSVIRAHRSIAECAVF 1453
Cdd:COG1022 470 VTSgGKNVAPQPIE-NALKASPLIEQAVVV 498
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
946-1129 |
1.35e-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: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 946 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1025
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1026 PPHPQNlgttlpTVKMIVEVSKSACVLStqaitrllkSKEAAAAVDVRtwPTILDTDDIPKKKVASIFRPP-SPDVLAYL 1104
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGL--EVAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 568968175 1105 DFSVSTTGILAGVKMSHAATSALCR 1129
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
973-1479 |
1.61e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 55.78 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1052
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1132
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1133 LQCELYPSRQIAICldPYCGLGFALWCLCSVYS-GHQSVLVPPLELESNVSLWLSAVSQykaRVTFCSysvmemctkglg 1211
Cdd:cd17643 127 RWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLhGGRLVVVPYEVARSPEDFARLLRDE---GVTVLN------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1212 aQTGalrmkgvnlSCVRTCMVVAEERPRISLtqsfsklfkdlglPARAVstTFGCRVnvaicLQPNRLGKLAEQ-GTTGP 1290
Cdd:cd17643 190 -QTP---------SAFYQLVEAADRDGRDPL-------------ALRYV--IFGGEA-----LEAAMLRPWAGRfGLDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1291 D--------PTTVYVDMRALRHDRVRLVERGSphslplmeSGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGY 1362
Cdd:cd17643 240 QlvnmygitETTVHVTFRPLDAADLPAAAASP--------IGRPLPGLRVYVL-DADGRPVPPGVVGELYVSGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1363 YtvyGEETLHADHFSArLSFGDTQTIWARTGYLGflRRTeltdASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIR 1442
Cdd:cd17643 311 L---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE-AALA 375
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568968175 1443 AHRSIAECAVFTWTN------LLVVVVELDGLEQDALDLVALV 1479
Cdd:cd17643 376 THPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRALL 418
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
316-503 |
1.73e-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: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNKLTsknepllNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 395
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 396 FLLGSCGVTLALTTDACQKGLPkaptgevatfkgWPPLAW-LVIDGKHLTRPPkdwyPLAQDTGSRTAYIEYkTSkeGST 474
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP------------AGLPVLlLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GST 138
|
170 180 190
....*....|....*....|....*....|..
gi 568968175 475 ---VGVTVSHSSLLAQCQALTQACGYTEAETL 503
Cdd:cd12116 139 grpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
345-534 |
1.80e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 55.71 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 345 LNPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEV 424
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 425 ATFKGWPPLA--------WLVIDGKHLTRPPKDwyPLAQDTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACG 496
Cdd:PRK08316 131 VDTLILSLVLggreapggWLDFADWAEAGSVAE--PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 568968175 497 YTEAETLTNVLDfkrdagLWHGVltsvmnRMHVITIPY 534
Cdd:PRK08316 209 MSADDIPLHALP------LYHCA------QLDVFLGPY 234
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
941-1474 |
7.13e-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: 53.67 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 941 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCV 1020
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1021 PVTVRPP-HPQNLGTTLPTVKMIVEVSKSAcVLSTQAItRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasiFRPPSPD 1099
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMTAAVIAVD-AQVMDAI-FQSGVRVLALSDLVGLGEPESAGPLIE-------DPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1100 VLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCEL-YPSRQIAICLDP-YCGLG-FALWCLCSVYSGhqsVLVPPLE 1176
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrHGRHNVVLGLMPlYHVIGfFAVLVAALALDG---TYVVVEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1177 LESNVSLWLSAvsqyKARVTfCSYSVMEMctkgLGAQTGALRMKGVNLSCVRTcmvvaeerprisltqsfsklfkdLGLP 1256
Cdd:cd05923 228 FDPADALKLIE----QERVT-SLFATPTH----LDALAAAAEFAGLKLSSLRH-----------------------VTFA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1257 ARAVSTTFGCRVNVAIclqPNRlgKLAEQGTT-------GPDPTTVYVdMRALRHDRVRLVERG--SPHSLPLMESGKIl 1327
Cdd:cd05923 276 GATMPDAVLERVNQHL---PGE--KVNIYGTTeamnslyMRDARTGTE-MRPGFFSEVRIVRIGgsPDEALANGEEGEL- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1328 pgvkvIIAHTetkgplGDSHLGEIWvsSPHNATgyytvygeetlhadhfSARLSFGdtqtiWARTGylgflrRTELTDAS 1407
Cdd:cd05923 349 -----IVAAA------ADAAFTGYL--NQPEAT----------------AKKLQDG-----WYRTG------DVGYVDPS 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968175 1408 GErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV--VVVELDGLEQDALD 1474
Cdd:cd05923 389 GD----VRILGRVDDMIISGGENIHPSEIE-RVLSRHPGVTEVVVIgvadeRWGQSVTacVVPREGTLSADELD 457
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
968-1121 |
1.57e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 52.69 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 968 TATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 1026
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1027 -----PHPQNLGTTLP-----TVKMIvevskSACVLSTQAITRL----LKSKEAA---AAVDVRTWPTILDTDDIPKKKV 1089
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 568968175 1090 ASiFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1121
Cdd:PRK05605 211 VS-HPRPTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
316-409 |
6.95e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 395
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECGVR------KGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90
....*....|....
gi 568968175 396 FLLGSCGVTLALTT 409
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 ... |
317-836 |
9.50e-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: 49.78 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 317 LTYGKLWSRSLKLAYTLLNKLTSKnepllnpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqQVGF 396
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 397 LLGSCGVTLALTTDACQKglpkaptgevatfkgwpplawlvidgkhltrppkdwyplaqdtgsrTAYIEYKTSKEGSTVG 476
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 477 VTVSHSSLLAqcQALTQACGY--TEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVITIPYALMKVnplsWIQKVcsykAR 554
Cdd:cd05935 102 CMHTHFSAAA--NALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMAR----WDRET----AL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 555 AALVKSRDMHWS--------LLAQRGQRDVCLSSLRMLivADGANPWSISSCDAFLNVFqsrGLRPEVIcpcasspEALT 626
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL--TGGGAPMPPAVAEKLLKLT---GLRFVEG-------YGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 627 VAIrrPPDLGGPPPRKAVLSMnglsyGVIRVDTEEKlsVLTVQDVGQVMPGasvcvvkvdgapylcktdEIGEICVNSVA 706
Cdd:cd05935 235 ETM--SQTHTNPPLRPKLQCL-----GIP*FGVDAR--VIDIETGRELPPN------------------EVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 707 TGTAYYGLLGITKNTFetvpvtadgVPVSDRPFTRTGLLGFIGPDNLVFVVGKLDGLmvvgvrrhnaddIVATALAVEPM 786
Cdd:cd05935 288 IFKGYWNRPEETEESF---------IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRM------------INVSGFKVWPA 346
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968175 787 KF--VYRGRIAVFSVTVLH--DDR--------IVLVAEQRPDASEEDSFQW----MS-----RVLQAIDSI 836
Cdd:cd05935 347 EVeaKLYKHPAI*EVCVISvpDERvgeevkafIVLRPEYRGKVTEEDIIEWareqMAaykypREVEFVDEL 417
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
966-1468 |
1.01e-05 |
|
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: 49.77 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 966 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP-HPQNLgttlptvkmive 1044
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDY------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1045 vsksacvlstqaitrllkskeAAAAVDVRTWPTILDTDDIpkkkvasifrppspdvlAYLDFSVSTTGILAGVKMSHAAT 1124
Cdd:cd05919 75 ---------------------AYIARDCEARLVVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1125 ----SALCRSIklqCELYPSRQIaicldpYC--------GLGFALWclCSVYSGHQSVLVPPLELESNVslwLSAVSQYK 1192
Cdd:cd05919 117 llfaDAMAREA---LGLTPGDRV------FSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1193 ARVTfcsYSVMEMCTKGLGAQTGALRMkgvnLSCVRTCMVVAEERPRiSLTQSFSKLFkdlGLParaVSTTFGCRVNVAI 1272
Cdd:cd05919 183 PTVL---YGVPTFYANLLDSCAGSPDA----LRSLRLCVSAGEALPR-GLGERWMEHF---GGP---ILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1273 CLQpNRLGKlAEQGTTGpdpttvyvdmRALRHDRVRLVERgsphslplmesgkilpgvkviIAHTETKGPLGDshlgeIW 1352
Cdd:cd05919 249 FLS-NRPGA-WRLGSTG----------RPVPGYEIRLVDE---------------------EGHTIPPGEEGD-----LL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1353 VSSPHNATGYYTVYgEETlhadhfSARLSFGdtqtiWARTGYLGFLrrteltDASGerhdALYVVGSLDETLELRGMRYH 1432
Cdd:cd05919 291 VRGPSAAVGYWNNP-EKS------RATFNGG-----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVS 348
|
490 500 510
....*....|....*....|....*....|....*.
gi 568968175 1433 PIDIEtSVIRAHRSIAECAVftwtnllVVVVELDGL 1468
Cdd:cd05919 349 PVEVE-SLIIQHPAVAEAAV-------VAVPESTGL 376
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
977-1479 |
1.37e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 49.36 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 977 RAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLSTQA 1056
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1057 ITRLLKskeaAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE 1136
Cdd:cd05922 79 AADRLR----DALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1137 LYPSRQIAICLdpycglgfalwclcsvysghqsvlvpPLELESNVSLWLSAVSQYKARVTFCSY----SVMEMCTKglga 1212
Cdd:cd05922 155 ITADDRALTVL--------------------------PLSYDYGLSVLNTHLLRGATLVLTNDGvlddAFWEDLRE---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1213 qTGALRMKGVnlscvrtcmvvaeerPriSLTQSFSKL-FKDLGLPARAVSTTFGCRvnvaicLQPNRLGKLAEQGTtGPD 1291
Cdd:cd05922 205 -HGATGLAGV---------------P--STYAMLTRLgFDPAKLPSLRYLTQAGGR------LPQETIARLRELLP-GAQ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1292 PTTVYVDMRALRH----DRVRLVERgsPHSLplmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYYTVYG 1367
Cdd:cd05922 260 VYVMYGQTEATRRmtylPPERILEK--PGSI-----GLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1368 EETlHADHFSARLsfgdtqtiwaRTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETSvIRAHRSI 1447
Cdd:cd05922 332 YRR-KEGRGGGVL----------HTGDLARR------DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLI 389
|
490 500 510
....*....|....*....|....*....|..
gi 568968175 1448 AECAVFtwtnllvvvveldGLEQDALDLVALV 1479
Cdd:cd05922 390 IEAAAV-------------GLPDPLGEKLALF 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
973-1140 |
1.80e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1052
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STQAITRLLKSKEAAAAVDVRT---WPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1129
Cdd:PRK12316 2106 TQRHLLERLPLPAGVARLPLDRdaeWADYPDTA--PAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ 2176
|
170
....*....|.
gi 568968175 1130 SIKLQCELYPS 1140
Cdd:PRK12316 2177 AAGERYELSPA 2187
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
946-1205 |
2.22e-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: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 946 RAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1025
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1026 PPHPQNlgttlpTVKMIVEVSKSACVLSTQAitrlLKSKEAAAAVDVRtwptiLDTDDIPKKKVASIFRPPSPDVLAYLD 1105
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSH----LQPPIAFIGLIDL-----LDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1106 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1177
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 568968175 1178 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1205
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
939-1028 |
2.89e-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: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 568968175 1019 CVPVTVRPPH 1028
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
305-533 |
5.10e-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: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 305 TALDTAGKatcTLTYGKLWSRSLKLAYTLLNKLTSknepllNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 384
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKD------LRGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLNPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 385 TRKDAgsqqvgfllgscgvtLALTTDAcqkglpkAPTgevatfkgwpplawLVIDGkhltrppkdwyplaqdtgsrtAYI 464
Cdd:cd05941 72 PLAEL---------------EYVITDS-------EPS--------------LVLDP---------------------ALI 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568968175 465 EYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIP 533
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
922-1123 |
6.06e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.12 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 922 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVY 1001
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1002 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTilDT 1081
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA--PQ 587
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568968175 1082 DDIPKkkvasifRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1123
Cdd:PRK10252 588 GAAPL-------QLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
296-419 |
6.15e-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: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 296 TTQPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPvmFMVAFYGCLLAEL 375
Cdd:cd17631 6 RRHPDRTALVFGGR------SLTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAAARLGA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568968175 376 VPVPIEVPLTRKDagsqqVGFLLGSCGVTLAL-----------TTdacqkGLPKA 419
Cdd:cd17631 71 VFVPLNFRLTPPE-----VAYILADSGAKVLFddlallmytsgTT-----GRPKG 115
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
973-1124 |
6.97e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.21 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1043
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1044 EVSKSA--CVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKkkvasIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1121
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 568968175 1122 AAT 1124
Cdd:PRK07656 189 RQL 191
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
282-757 |
7.75e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 47.10 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 282 NGPLSLLAALQLWGTTQPKApclTALDTAGKATctlTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSDpv 361
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 362 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVTLALTTDA----CQKGLPKAPTGEvatfkgwpplAWLV 437
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDSEfvplLAAILPQLPTVR----------TVIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 438 IDGKHLTRPPKDWY------------PLAQDTGSRTAYIEYKTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEaet 502
Cdd:PRK06187 133 EGDGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 503 ltnvldfkRDAGLwhgVLTSvMNRMHVITIPYALMkvnpLSWIQKVC--SYKARAAL---VKSR--------DMHWSLLA 569
Cdd:PRK06187 208 --------DDVYL---VIVP-MFHVHAWGLPYLAL----MAGAKQVIprRFDPENLLdliETERvtfffavpTIWQMLLK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 570 QRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAV 644
Cdd:PRK06187 272 APRAYFVDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 645 LSmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPYLCKTDEIGEICVNSVATGTAYYGLLGITKNTFEt 724
Cdd:PRK06187 338 RR-----------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID- 393
|
490 500 510
....*....|....*....|....*....|...
gi 568968175 725 vpvtaDGvpvsdrpFTRTGLLGFIGPDNLVFVV 757
Cdd:PRK06187 394 -----GG-------WLHTGDVGYIDEDGYLYIT 414
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
298-608 |
8.89e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 298 QPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--EL 375
Cdd:PRK12316 524 TPEAPALAFGEE------TLDYAELNRRANRLAHALI-------ERGVGPDVLVGVAMERSIEMV--VALLAILKAggAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 376 VPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKgwPPLAWLviDGkHLTRPPKdwyplAQ 455
Cdd:PRK12316 589 VPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLD--RPAAWL--EG-YSEENPG-----TE 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 456 DTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTsVMNRMHVITIPYA 535
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPG 730
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968175 536 LMKvNPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQRDVCLsSLRMLIVADGANPWsisscDAFLNVFQSR 608
Cdd:PRK12316 731 DHR-DPAKLVELINREGVDTlHFVPS---MLQAFLQDEDVASCT-SLRRIVCSGEALPA-----DAQEQVFAKL 794
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
299-494 |
9.44e-05 |
|
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: 46.95 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 299 PKAPCLTAldtagkATCTLTYGKLWSRSLKLAYTLLNKLTSknepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 378
Cdd:cd17651 9 PDAPALVA------EGRRLTYAELDRRANRLAHRLRARGVG-------PGDLVALCARRS--AELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 379 PIEVpltrkDAGSQQVGFLLGSCGVTLALTTDACQKGLPkaptgevatfkgwPPLAWLVIDGKHLTRPPKDWYPLAQDTG 458
Cdd:cd17651 74 PLDP-----AYPAERLAFMLADAGPVLVLTHPALAGELA-------------VELVAVTLLDQPGAAAGADAEPDPALDA 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 568968175 459 SRTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQA 494
Cdd:cd17651 136 DDLAYVIY-TS--GSTgrpKGVVMPHRSLANLVAWQARA 171
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
316-500 |
1.36e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 46.50 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 316 TLTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsqq 393
Cdd:cd12114 12 TLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 394 vgfLLGSCGVTLALTTDACQKGLPKAPTgevatfkgwpplawLVIDGKHLTRPPKDwyPLAQDTG-SRTAYIEYkTSkeG 472
Cdd:cd12114 79 ---ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP--PPPVDVApDDLAYVIF-TS--G 136
|
170 180 190
....*....|....*....|....*....|.
gi 568968175 473 ST---VGVTVSHSSLLAQCQALTQACGYTEA 500
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINRRFAVGPD 167
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
283-411 |
2.36e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 45.80 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 283 GPLSLLAALQLWGTTQPKAPcltALDTAGKatcTLTYGKLWSRSLKLAyTLLNKLTSKnepllnPGDRVALVFPNSdPvM 362
Cdd:PRK06178 31 GERPLTEYLRAWARERPQRP---AIIFYGH---VITYAELDELSDRFA-ALLRQRGVG------AGDRVAVFLPNC-P-Q 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568968175 363 FMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVTLALTTDA 411
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1324-1452 |
2.50e-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: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1324 GKILPGVKVIIAHTETKGPLGDSHlGEIWVSSPHNATGYYTvygEETLHADHFSARlsfgdtqtiWARTGYLGFLRrtel 1403
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568968175 1404 tdasgeRHDALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1452
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
973-1140 |
2.76e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.10 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1052
Cdd:PRK12316 4581 ELNRRANRLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1053 STQAITRLLKSKEAAAAVDV---RTWPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1129
Cdd:PRK12316 4654 TQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
170
....*....|.
gi 568968175 1130 SIKLQCELYPS 1140
Cdd:PRK12316 4725 ATGERYELTPD 4735
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
967-1451 |
2.87e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 45.14 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 967 STATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP-PHPQNLGTTLPTVkmivev 1045
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQCLQEA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1046 sksacvlSTQAITRLLKSKEAAAAVdvrtwptildtddipkkkvasifrppspdvlayldFSVSTTGILAGVKMSHAATS 1125
Cdd:cd05910 74 -------EPDAFIGIPKADEPAAIL-----------------------------------FTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1126 ALCRSIKlqcELYPSRQIAICLDpycglGFALWCLCSVYSGHQSVlVPPLE----LESNVSLWLSAVSQYKARVTFCSYS 1201
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1202 VMEMCTKgLGAQtgalrmKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDlglparavsttfgcrvNVAIclqpnrlgk 1281
Cdd:cd05910 183 LLERVAR-YCAQ------HGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----------------EAEI--------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1282 LAEQGTTGPDPTTVyVDMRALRHDRVRLVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWV 1353
Cdd:cd05910 230 LTPYGATEALPVSS-IGSRELLATTTAATSGGAGTCV-----GRPIPGVRVrIIEIDDEPIAewddtleLPRGEIGEITV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1354 SSPHNATGYYTVYGEETLHADHFSArlsfgdtQTIWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHP 1433
Cdd:cd05910 304 TGPTVTPTYVNRPVATALAKIDDNS-------EGFWHRMGDLGYL------DDEGR----LWFCGRKAHRVITTGGTLYT 366
|
490
....*....|....*...
gi 568968175 1434 IDIEtSVIRAHRSIAECA 1451
Cdd:cd05910 367 EPVE-RVFNTHPGVRRSA 383
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
285-481 |
5.53e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.65 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 285 LSLLAALQLWGTtqPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLlnkltskNEPLLNPGDRVALVFPNSdpVMFM 364
Cdd:PRK10252 460 LSALVAQQAAKT--PDAPALADARY------QFSYREMREQVVALANLL-------RERGVKPGDSVAVALPRS--VFLT 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 365 VAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKGWPPlawlvidgkh 442
Cdd:PRK10252 523 LALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA---------- 585
|
170 180 190
....*....|....*....|....*....|....*....
gi 568968175 443 ltrpPKDWYPLAQDTGSRTAYIEYKTSKEGSTVGVTVSH 481
Cdd:PRK10252 586 ----PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
939-1121 |
7.11e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 44.26 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1019 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLSTQAITRLLKSKEAAAAV---DVRTWPTILDT 1081
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568968175 1082 DDI------PKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1121
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
943-1479 |
7.41e-04 |
|
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: 43.75 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 943 LQWRAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1022
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1023 tvrpphPQNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtDDipkkkvasifrppspdvLA 1102
Cdd:cd17631 74 ------PLNFRLTPPEVAYILADSGAKVLF-----------------------------DD-----------------LA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1103 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELyPSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLVPPLELESnv 1181
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1182 slWLSAVSQYKARVTFCSYSVME-MCTKGlgaqtgalRMKGVNLSCVRtCMVVAEERPRISLTQSFsklfKDLGLparAV 1260
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1261 STTFGcrvnvaiclqpnrlgklaeQGTTGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVKVIIAHTETK 1340
Cdd:cd17631 241 VQGYG-------------------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1341 gPLGDSHLGEIWVSSPHNATGYytvYGEETLHADhfsarlSFGDTqtiWARTGYLGFLrrteltDASGerhdALYVVGSL 1420
Cdd:cd17631 286 -EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRK 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968175 1421 DETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV-VVVELDGLEQDALDLVALV 1479
Cdd:cd17631 343 KDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELIAHC 406
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
299-408 |
9.45e-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: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 299 PKAPCLTALDTagkaTCTLTYGKLwsrsLKLAYTLLNKLTSKNeplLNPGDRVALVFPNSDPvmFMVAFYGCLLAELVPV 378
Cdd:cd05926 1 PDAPALVVPGS----TPALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVA 67
|
90 100 110
....*....|....*....|....*....|
gi 568968175 379 PIEvPLTRKDagsqQVGFLLGSCGVTLALT 408
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 ... |
316-407 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVG 395
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT-----PDDYA 94
|
90
....*....|..
gi 568968175 396 FLLGSCGVTLAL 407
Cdd:cd05959 95 YYLEDSRARVVV 106
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
939-1122 |
1.10e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.59 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCIQlhkRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1019 C--VPVTVRPPHPQnLGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVD---VRTWPTILDTDDIPKKKVASIF 1093
Cdd:PRK06155 96 AiaVPINTALRGPQ-LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190
....*....|....*....|....*....|
gi 568968175 1094 RPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1122
Cdd:PRK06155 175 AAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
973-1024 |
1.13e-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: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568968175 973 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1024
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
316-378 |
1.93e-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: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNkltsknepL-LNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 378
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1323-1452 |
2.50e-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: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 1323 SGKILPGVKVIIAHtETKGPLGDshlGEIWVSSPHNATGYY--TVYGEETlhadhfsarlsfgdTQTIWARTGYLGFLrr 1400
Cdd:cd05912 244 AGKPLFPVELKIED-DGQPPYEV---GEILLKGPNVTKGYLnrPDATEES--------------FENGWFKTGDIGYL-- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568968175 1401 teltDASGerhdALYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAV 1452
Cdd:cd05912 304 ----DEEG----FLYVLDRRSDLIISGGENIYPAEIEE-VLLSHPAIKEAGV 346
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
299-496 |
2.92e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 299 PKAPCLTaldTAGKatcTLTYGKLWSRSLKLAYTLlnkltskNEPLLNPGDRVALVFPNSdpvMFMVAfygCLLAEL--- 375
Cdd:PRK05691 2202 PQAPALT---FAGQ---TLSYAELDARANRLARAL-------RERGVGPQVRVGLALERS---LEMVV---GLLAILkag 2262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 376 ---VPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGeVATfkgwpplaW-LVIDGKHLTRPPKDwy 451
Cdd:PRK05691 2263 gayVPLDPEYPLER-------LHYMIEDSGIGLLLSDRALFEALGELPAG-VAR--------WcLEDDAAALAAYSDA-- 2324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568968175 452 PLAQDTGSR-TAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACG 496
Cdd:PRK05691 2325 PLPFLSLPQhQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
939-1020 |
3.33e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 41.78 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHPlFLLLNakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:PRK08279 39 LGDVFEEAAARHPDRP-ALLFE--DQSISYA---ELNARANRYAHWAAARG-VGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
..
gi 568968175 1019 CV 1020
Cdd:PRK08279 112 AV 113
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
300-380 |
6.77e-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: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 300 KAPCLTALDTAGKatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVP 379
Cdd:cd05945 3 ANPDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVP 70
|
.
gi 568968175 380 I 380
Cdd:cd05945 71 L 71
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
316-378 |
6.79e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 40.81 E-value: 6.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968175 316 TLTYGKLWSRSLKLAYTLLNKLTskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 378
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
939-1028 |
7.74e-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: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968175 939 LADVLQWRAHTTPDHplFLLLNAKGTVTStatcIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1018
Cdd:cd05920 17 LGDLLARSAARHPDR--IAVVDGDRRLTY----RELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90
....*....|
gi 568968175 1019 CVPVTVRPPH 1028
Cdd:cd05920 90 AVPVLALPSH 99
|
|
| |
