|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
918-1492 |
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 568968177 918 LFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 996
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 997 TTLPTVKMivEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVA-----SIFRPPSPDVLAYLDFSV 1071
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1072 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1151
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1152 SQYKARVTFCSYSVMEMCTKGLGAQTGALRMKGVNLSCVRTCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRV 1231
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1232 NVAICLqpnrlgklaeQGTTGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHL 1311
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1312 GEIWVSSPHNATGYYTVYGEETLHADHF-SARLSFGDTQTIWARTGYLGFLRRTELTDASGERHDALYVVGSLDETLELR 1390
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFpSTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1391 GMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELD-GLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINS 1469
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 568968177 1470 RGEKQRMHLRDGFLADQLDPIYV 1492
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
266-842 |
0e+00 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 656.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 266 CLTALDTAGKATCTLTYGKLWSRSLKLAYTLLNKLTskneplLNPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 345
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 346 PLtrkdaGSQQVGFLLGSCGVTLALTTDACQKGLPKA-----PTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQDT 420
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 421 GSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIPYALM 500
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 501 KVNPLSWIQKVCSYKARAALVKSRDMHWSL------LAQRGQRDVCLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 574
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 575 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGASVCVVKVDGaP 652
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPET-K 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 653 YLCKTDEIGEICVNSVATGTAYYGLLGITKNTFETVPVTADGVPVSDRPFTRTGLLGFIGP----------DNLVFVVGK 722
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 723 LDGLMVVGVRRHNADDIVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 802
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 568968177 803 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 842
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
908-1450 |
7.07e-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: 7.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 908 WRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 987
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 988 RPPHPqnlGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWptiLDTDDIPKKKVASIFRPPS--PDVLA 1065
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---LLVVDLLPDTSAADWPPPSpdPDDIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1066 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESN 1143
Cdd:cd05931 153 YLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1144 VSLWLSAVSQYKARVT----FcSYsvmEMCT-KGLGAQTGALrmkgvNLSCVRTCMVVAeERPRISLTQSFSKLFKDLGL 1218
Cdd:cd05931 231 PLRWLRLISRYRATISaapnF-AY---DLCVrRVRDEDLEGL-----DLSSWRVALNGA-EPVRPATLRRFAEAFAPFGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1219 PARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTTGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPG 1292
Cdd:cd05931 301 RPEAFRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1293 VKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTVyGEETlhADHFSARLSFGDtqTIWARTGYLGFLRRteltdasGE 1372
Cdd:cd05931 364 QEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGR-PEAT--AETFGALAATDE--GGWLRTGDLGFLHD-------GE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1373 rhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAE--CAVFTW----TNLLVVVVELDGLeQDALDLVALVTNV- 1445
Cdd:cd05931 432 ----LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIr 506
|
....*..
gi 568968177 1446 --VLEEH 1450
Cdd:cd05931 507 aaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
257-833 |
1.14e-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: 233.28 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 257 WGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLLnkltsknePLLNPGDRVALVFPNSdpVMFMVAFYGCLLA 336
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 337 ELVPVPIEVPLTRKDAgsQQVGFLLGSCGVTLALTTDACQKGLPKAptgeVATFKGWPPLAWLVIDGKHLTrPPKDWyPL 416
Cdd:cd05931 72 GAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADW-PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 417 AQDTGSRTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMH-V 492
Cdd:cd05931 144 PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPsV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 493 ITIPYALMKvNPLSWIQKVCSYKAR--AAlvksRDMHWSLLAQRGQR----DVCLSSLRMLIVadGANPWSISSCDAFLN 566
Cdd:cd05931 221 LMSPAAFLR-RPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 567 VFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPGASVCV 645
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 646 VKVDGAPyLCKTDEIGEICV--NSVATGtaYYGLLGITKNTFETVPVTADGvpvsdrPFTRTGLLGFIGPDNLvFVVGKL 723
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVrgPSVASG--YWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 724 DGLMVVGVRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVG 803
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVA 516
|
570 580 590
....*....|....*....|....*....|
gi 568968177 804 VYCLALVPANTLPKAPLGGIHISETKQRFL 833
Cdd:cd05931 517 PADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
906-1390 |
1.26e-48 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 179.43 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 906 LQWRAHTTPDHPLFlllnAKGTVTSTaTCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 985
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 986 TVrpphpqNLGTTLPTVKMIVEVSKSACVLsTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPK-----------KKVAS 1054
Cdd:pfam00501 75 PL------NPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1055 IFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1130
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1131 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAeERPRISLTQSFS 1210
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1211 KLFkdlglpARAVSTTFGcrvnvaiclqpnrlgkLAEqgTTGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 1290
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDEDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1291 PGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEETLHADHFsarlsfgdTQTIWARTGYLGFLrrteltDAS 1370
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 568968177 1371 GErhdaLYVVGSLDETLELR 1390
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1064-1442 |
5.81e-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: 128.56 E-value: 5.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1064 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1140
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1141 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEERPrISLTQSFSKLFKDlglpa 1220
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1221 rAVSTTFGcrvnvaiclqpnrlgkLAEqgtTGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVKVIIAHT 1300
Cdd:cd04433 141 -KLVNGYG----------------LTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1301 ETkGPLGDSHLGEIWVSSPHNATGYYTVygeetlhadhfsARLSFGDTQTIWARTGYLGFLRrteltdasgeRHDALYVV 1380
Cdd:cd04433 185 DG-GELPPGEIGELVVRGPSVMKGYWNN------------PEATAAVDEDGWYRTGDLGRLD----------EDGYLYIV 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968177 1381 GSLDETLELRGMRYHPIDIETsVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1442
Cdd:cd04433 242 GRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHV 308
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
249-833 |
7.18e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 133.14 E-value: 7.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 249 SLLAALQLWGTTQPKAPCLT----ALDTAGKATcTLTYGKLWSRSLKLAYTLlNKLTSknepllnPGDRVALVFPNSdpV 324
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVAE-TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 325 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVTLALTTDACqkglpkapTGEVATF----KGWPPLAWLV 400
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 401 IDGKHLTRPPKdwYPLAQDTGSRTAYIEYkTSkeGST---VGVTVSHSSLLAQC-QALTQACGYTEAE-----TLTNVLD 471
Cdd:PRK05850 141 VDLLDLDSPRG--SDARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 472 FKRDAGLWHGVLTSVMNRMH-VITIPYALMKvNPLSWIQkvcsykaraaLVKSRDMHWSL-------LAQRGQRDVCLSS 543
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 544 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 619
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 620 VDTeEKLSvltvqdVGQVMP-----GASVCVVKVDGAPYL----------CKTDEIGEICVN--SVATGtaYYGLLGITK 682
Cdd:PRK05850 349 FDY-EKLS------AGHAKRcetggGTPLVSYGSPRSPTVrivdpdtcieCPAGTVGEIWVHgdNVAAG--YWQKPEETE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 683 NTFETVPVT-ADGVPVSdrPFTRTGLLGFIGPDNLvFVVGKLDGLMVVGVRRHNADDIVATalavepMKFVYRGRIAVFS 761
Cdd:PRK05850 420 RTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAIS 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568968177 762 VTVLHDDRIVLVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFL 833
Cdd:PRK05850 491 VPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYR 567
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
902-1432 |
8.12e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.45 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 982 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLSTQAITRLLKSKEAAAAVDVrtwPTILDTDDIPKKkVASI 1055
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPA-LAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1056 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1130
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1131 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEmctkglgaqtGALrmKGVNLSCVRTCMVVAEERPR 1202
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSE----------SAL--ERLDLSRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1203 ISLtQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTTGPDPTTVYVDMRALRHDRVRLVErG 1276
Cdd:PRK05691 305 DSL-ERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-G 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1277 SPhslpLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTvYGEETlhADHFSARlsfgDTQTiWARTG 1356
Cdd:PRK05691 367 SV----LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEAS--AKTFVEH----DGRT-WLRTG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968177 1357 YLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIETSVIRahrsiaECAVFTWTNLLVVVVELDGLE 1432
Cdd:PRK05691 435 DLGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
902-1442 |
3.62e-29 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 123.00 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 982 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtddipkkkVASIFrppsp 1061
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALV------------------------------------TALIL----- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1062 dvlayldFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1140
Cdd:COG0318 107 -------YT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1141 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEerpriSLTQSFSKLFKDLglpa 1220
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1221 ravsttFGCRVNvaiclqpNRLGkLAEqgtTGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVKVIIAHT 1300
Cdd:COG0318 239 ------FGVRIV-------EGYG-LTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRIVDE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1301 ETKgPLGDSHLGEIWVSSPHNATGYYTvYGEETlhadhfsaRLSFGDTqtiWARTGYLGFLrrteltDASGErhdaLYVV 1380
Cdd:COG0318 286 DGR-ELPPGEVGEIVVRGPNVMKGYWN-DPEAT--------AEAFRDG---WLRTGDLGRL------DEDGY----LYIV 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968177 1381 GSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1442
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELRAFL 409
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
250-739 |
5.63e-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: 122.23 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 250 LLAALQLWGTTQPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSDPvmFMVA 329
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 330 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGVTLALTtdacqkglpkaptgevatfkgwpplawlvidgkhltrp 409
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVT-------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 410 pkdwyplaqdtgsrtAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSV 486
Cdd:COG0318 103 ---------------ALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 487 MNRMHVITIPyalmKVNPLSWIQKVCSYKA-RAALVKSrdMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFL 565
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 566 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGASVC 644
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 645 VVKVDGAPylCKTDEIGEICV--NSVATGtaYYGLLGITKNTFetvpvtADGvpvsdrpFTRTGLLGFIGPDNLVFVVGK 722
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVrgPNVMKG--YWNDPEATAEAF------RDG-------WLRTGDLGRLDEDGYLYIVGR 344
|
490
....*....|....*..
gi 568968177 723 LDGLMVVGVRRHNADDI 739
Cdd:COG0318 345 KKDMIISGGENVYPAEV 361
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
280-839 |
4.96e-28 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 121.27 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 280 LTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LTRKDAGSQQV 357
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 358 GFLLGSCGVTLALTTDACQKGLPKAPTGEvatfkgwpPLAWlVIDGKHLTRPPKDWYPLAQDTGSRTAYIEYkTSkeGST 437
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQY-SS--GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 438 ---VGVTVSHSSLLAQCQALTQ-ACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIPYALMKVNPLSWIQKVCs 513
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLIS- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 514 yKARAALVKSRDMHWSLLAQRGQ----RDVCLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEAlT 589
Cdd:PRK09192 268 -RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 590 VAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGASVCVVKVDGAPYlcKTDEIGEICVN-- 666
Cdd:PRK09192 344 LAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERVVGHICVRgp 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 667 SVATGtaYYGllgitkNTFETVPVTADGvpvsdrpFTRTGLLGFIGPDNLVfVVGKLDGLMVVGVRRHNADDIVATAlav 746
Cdd:PRK09192 420 SLMSG--YFR------DEESQDVLAADG-------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWIA--- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 747 EPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKAPLGGIHI 825
Cdd:PRK09192 481 EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSR 557
|
570
....*....|....
gi 568968177 826 SETKQRFLEGTLHP 839
Cdd:PRK09192 558 AKAKKRYLSGAFAS 571
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
247-835 |
1.47e-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: 116.23 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 247 PLSLLAALQLWGTTQPKAPClTALDTAGKATcTLTYGKLWSRSLKLAyTLLNKLTskneplLNPGDRVALVFP-NSDpvm 325
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSEE-FQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 326 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVtlaLTTDACQkglpkAPTGEVATFKGWPPLAWLV 400
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 401 IDGKHLTRPPKDWYPLAQDtgsrTAYIEYKTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAG 477
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 478 LWHGVLTSVMNRMHVITIPYALMKVNPLSWIQKVCSYKA------RAALVKSRDmhwsLLAQRGQRDVCLSSLRMLIVAD 551
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 552 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 628
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 629 LTVQDVGQVMPGASVCVVKVDGApyLCKTDEIGE--ICVNSVATGtaYYGLLGITKNTFetvpvTADGvpvsdrpFTRTG 706
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRlqVRGPVVTKG--YYNNPEANAEAF-----TEDG-------WFRTG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 707 LLGFIGPDNLVFVVGKLDGLMVVGVrRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSf 786
Cdd:cd05906 415 DLGFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDA- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 568968177 787 qwMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 835
Cdd:cd05906 490 --LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
936-1406 |
8.09e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 111.37 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1007
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1008 vsksacVLSTQAITRLLKSKEAAAAVDVRtwPTILDTDDIPKKkVASIFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1084
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDS-AGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1085 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1161
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1162 SYSVMEmctkgLGAQTGALRM-KGVNLSCVrtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpn 1240
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG------------ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1241 rlgkLAEQ----GTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEI 1314
Cdd:PRK12476 357 ----IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1315 WVSSPHNATGYY-----TvygEETLHAdHFSARLSFG------DTQTIWARTGYLGFLRRTEltdasgerhdaLYVVGSL 1383
Cdd:PRK12476 433 WLHGDNIGRGYWgrpeeT---ERTFGA-KLQSRLAEGshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRI 497
|
490 500
....*....|....*....|...
gi 568968177 1384 DETLELRGMRYHPIDIETSVIRA 1406
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEATVAEA 520
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
268-730 |
9.65e-25 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 108.94 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 268 TALDTAGkaTCTLTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpl 347
Cdd:pfam00501 12 TALEVGE--GRRLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 348 trkDAGSQQVGFLLGSCGVTLALTTD--------ACQKGLPKAPTGEVATFKGWPPLAWLVIDGKHLTRPPKDWYPLAQD 419
Cdd:pfam00501 79 ---RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 420 TgsrTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQAC----GYTEAETLTNVLDFKRDAGLWHGVLTSVMN--RM 490
Cdd:pfam00501 156 D---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAgaTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 491 HVITIPYALMKVNPLSWIQKvcsYKARAALVKSRDMHWsLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqs 570
Cdd:pfam00501 230 VLPPGFPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 571 rglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQVMPGASVCVVKVDG 650
Cdd:pfam00501 302 ----GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGRPLPGTEVKIVDDET 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 651 APYLcKTDEIGEICV--NSVATGtaYYGLLGITKNTFetvpvTADGvpvsdrpFTRTGLLGFIGPDNLVFVVGKLDGLMV 728
Cdd:pfam00501 351 GEPV-PPGEPGELCVrgPGVMKG--YLNDPELTAEAF-----DEDG-------WYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
..
gi 568968177 729 VG 730
Cdd:pfam00501 416 LG 417
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
310-837 |
2.82e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.82 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 310 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVTLALTTDACQKGLPKapt 384
Cdd:PRK07769 78 PGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGVRK--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 385 gevaTFKGWPP------LAwlvID------GKHLTRPPKDwyplaQDTgsrTAYIEYkTSkeGST---VGVTVSHSSLLA 449
Cdd:PRK07769 146 ----FFRARPAkerprvIA---VDavpdevGATWVPPEAN-----EDT---IAYLQY-TS--GSTripAGVQITHLNLPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 450 QCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNrmHVITI--PYALMKvNPLSWIQKVCSYKARAALVKSR--D 525
Cdd:PRK07769 208 NVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAapN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 526 MHWSLLAQRG-----QRDVCLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPPDlg 599
Cdd:PRK07769 285 FAFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTPMDE-- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 600 gpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGASVCVVKVDGAPYLcKTDEIGEICVNSVATGTAYYGLL 678
Cdd:PRK07769 361 --EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 679 GITKNTFE------TVPVTADGVPvSDRPFTRTGLLGFIGPDNLvFVVGKLDGLMVVGVRRHNADDIVATALavEPMKFV 752
Cdd:PRK07769 437 EETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKAL 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 753 YRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPA 812
Cdd:PRK07769 513 RTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPA 592
|
570 580
....*....|....*....|....*
gi 568968177 813 NTLPKAPLGGIHISETKQRFLEGTL 837
Cdd:PRK07769 593 GSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-122 |
1.28e-23 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 96.72 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 10 AAPLPAEVLESLAELELELSEGDITQKGYEKKRAKLLARYipliqgvdpcLQTENRIPGPLltAATAKPQKSRATNSRDE 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKF----------LLHPETPTKLS--AEAQNQLASLETKLRDE 69
|
90 100 110
....*....|....*....|....*....|....*
gi 568968177 90 RFRSDVHTEAVQAALAKYKERKM--PMPSKRRSAL 122
Cdd:pfam06464 70 ELSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
902-1446 |
2.84e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.18 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCIQLHKRAERVAAALMEKGrlDAGDHVALVYPPGVDLIAAFYGCL 978
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 979 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLSTqaitrllkskeAAAAVDVRTW---------PTI--LDTDDI 1047
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVieVDLLDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1048 PKKKVASIFRPPSPDVlAYLDFSVSTTGILAGVKMSHAATSALCRSI------KLQCELYPSRQIAICLDPYCGLGFALW 1121
Cdd:PRK05850 147 DSPRGSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1122 CLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaQTGALRMKGVNLSCVRTcMVVAEERP 1201
Cdd:PRK05850 226 VCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVR----KTSDDDMAGLDLGGVLG-IISGSERV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1202 RISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAE------QGTTGPDPTTVYVDMRALRHDRVR---- 1271
Cdd:PRK05850 301 HPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEKLSAGHAKrcet 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1272 -----LVERGSPHSlplmesgkilPGVKVIIAHTETKGPLGDshLGEIWVSSPHNATGYYTVyGEETLHAdhFSARL--- 1343
Cdd:PRK05850 365 gggtpLVSYGSPRS----------PTVRIVDPDTCIECPAGT--VGEIWVHGDNVAAGYWQK-PEETERT--FGATLvdp 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1344 SFGDTQTIWARTGYLGFLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV--IRAHRsiaeCAVFT---- 1417
Cdd:PRK05850 430 SPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIqeITGGR----VAAISvpdd 494
|
570 580 590
....*....|....*....|....*....|..
gi 568968177 1418 WTNLLVVVVEL---DGLEQDALDLVALVTNVV 1446
Cdd:PRK05850 495 GTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
310-839 |
5.14e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 99.43 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 310 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVTLALTTDACQ-------K 377
Cdd:PRK12476 91 PGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpghAERLDT-------ALRDAEPTVVLTTTAAAeavegflR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 378 GLPKAPTGEVATFKGWPPLAwlvidGKHLTRPPKDwyplAQDTgsrtAYIEYkTSkeGST---VGVTVSHSSLlaqCQAL 454
Cdd:PRK12476 162 NLPRLRRPRVIAIDAIPDSA-----GESFVPVELD----TDDV----SHLQY-TS--GSTrppVGVEITHRAV---GTNL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 455 TQ---ACGYTEAETLT-NVLDFKRDAGLWHGVLTSVMNRMHVITIPYALMKvNPLSWIQKVcSYKARAALV--KSRDMHW 528
Cdd:PRK12476 223 VQmilSIDLLDRNTHGvSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKAL-SEGSRTGRVvtAAPNFAY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 529 SLLAQRG----QRDVCLSSLRMLIvadGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPR 604
Cdd:PRK12476 301 EWAAQRGlpaeGDDIDLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 605 KAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGASVCVVKVDGAPYLcKTDEIGEICVNSVATGTAYYGLLGITKN 683
Cdd:PRK12476 375 VVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETER 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 684 TFETVPVT-------ADGVPVSDRPFtRTGLLGFIgPDNLVFVVGKLDGLMVVGVRRHNADDIVATALAVEPMkfVYRGR 756
Cdd:PRK12476 453 TFGAKLQSrlaegshADGAADDGTWL-RTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGY 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 757 IAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGT 836
Cdd:PRK12476 529 VTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGR 608
|
...
gi 568968177 837 LHP 839
Cdd:PRK12476 609 LGV 611
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
247-867 |
5.05e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.93 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 247 PLSLLAALQLWGTTQPKAPCLTALDTAGKATCTLTYGKLWSRSLKLAYTLlnkltsknEPLLNPGDRVALVFPnSDPvMF 326
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-DY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 327 MVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkGWPPlaWLVIDGkhL 406
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPE--LLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 407 TRPPKDWYPLAQDTGSRTAYIEYkTSkeGSTV---GVTVSHSSLLAQCQALTQACG--YTEAETLTNVLDFKRDAGLWHG 481
Cdd:PRK05691 151 DPALAEAWQEPALQPDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 482 VLTSVMNRMHVITIPYALMKVNPLSWIQKVCSYkaRAALVKSRDMHWSLLAQRgQRDVCLSSL---RMLIVADGANPWSI 558
Cdd:PRK05691 228 LLQPIFSGVPCVLMSPAYFLERPLRWLEAISEY--GGTISGGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 559 SSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQV 637
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARNRAEPGTGSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 638 M-------PGASVCVVKVDGAPYLcKTDEIGEICVN--SVATGtaYYGLLGITKNTFetvpVTADGvpvsdRPFTRTGLL 708
Cdd:PRK05691 369 LmscgrsqPGHAVLIVDPQSLEVL-GDNRVGEIWASgpSIAHG--YWRNPEASAKTF----VEHDG-----RTWLRTGDL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 709 GFIgPDNLVFVVGKLDGLMVvgVRRHN--ADDIVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE-----QRPDAS 781
Cdd:PRK05691 437 GFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPP 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 782 EEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVTNLPKPRQKQP 861
Cdd:PRK05691 512 QA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEA 577
|
....*.
gi 568968177 862 EVGPAS 867
Cdd:PRK05691 578 AQTAAS 583
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
936-1425 |
8.28e-20 |
|
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: 95.04 E-value: 8.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1014
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1015 LSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSi 1094
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL---PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1095 KLQCELYPSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSvmeMCTK 1171
Cdd:cd05906 199 KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1172 gLGAQTGALRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRVNVAIClqpnrlgklaeqgtt 1251
Cdd:cd05906 274 -LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV--------------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1252 gpdptTVYVDMRALRHdrvrlvergsPHSLPLMESGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYytvYGE 1331
Cdd:cd05906 337 -----IYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGY---YNN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1332 ETLHADHFsarlsfgdTQTIWARTGYLGFLrrteltdasgeRHDALYVVGSLDETLELRGMRYHPIDIETSV----IRAH 1407
Cdd:cd05906 398 PEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEP 458
|
490 500
....*....|....*....|.
gi 568968177 1408 RSIAECAVF---TWTNLLVVV 1425
Cdd:cd05906 459 SFTAAFAVRdpgAETEELAIF 479
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
936-1415 |
1.12e-19 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 93.48 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1015
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STQAiTRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVASifrPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1095
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1096 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1169
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1170 TKGLGAQTGALRMkgvnlscvrtcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNvaiclqpnrlgklaeqg 1249
Cdd:TIGR01733 227 AAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN----------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1250 TTGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYytvY 1329
Cdd:TIGR01733 267 LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---L 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1330 GEETLHADHFSARLSFGDTQTIWARTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRS 1409
Cdd:TIGR01733 335 NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPG 403
|
....*.
gi 568968177 1410 IAECAV 1415
Cdd:TIGR01733 404 VREAVV 409
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
936-1410 |
1.18e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 92.10 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1007
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1008 VSKSAcvlstQAITRLLKSKEAAAAvdvrtwPTILDTDDIPKKkVASIFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1084
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1085 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1158
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1159 tfcsYSVMEMCTKGLGAQTGaLRMKG---VNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvai 1235
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARG-LPKDGeppLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1236 clqpnrlgkLAEQ----GTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDS 1309
Cdd:PRK07769 346 ---------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1310 HLGEIWVSSPHNATGYYTvYGEETLHADH--FSARLSFGDTQ-----TIWARTGYLGflrrtelTDASGErhdaLYVVGS 1382
Cdd:PRK07769 417 QIGEIWLHGNNIGTGYWG-KPEETAATFQniLKSRLSESHAEgapddALWVRTGDYG-------VYFDGE----LYITGR 484
|
490 500
....*....|....*....|....*...
gi 568968177 1383 LDETLELRGMRYHPIDIETSVIRAHRSI 1410
Cdd:PRK07769 485 VKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
892-1403 |
6.06e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 86.21 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 892 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGV 968
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 969 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLSTQAITRLLksKEAAAAVDVRTWPTILDTD 1045
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1046 DIPKKKVAsiFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1124
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1125 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGAlrmkGVNLSCVRTCMVVAEE-RPR 1202
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLA----ELDLSCWRVAGIGADMiRPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1203 IslTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPNRLGKLAEQgttgpdpttvyVDMRALRHDR--VRLVERGSPH 1279
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPLGSGIVVEE-----------VDRDRLEYQGkaVAPGAETRRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1280 SlPLMESGKILPGVKVIIaHTETKGPLGDSHLGEIWVSSPHNATGYYTvyGEETlhADHFSArlsfgdtqTIWARTGYLG 1359
Cdd:PRK09192 382 R-TFVNCGKALPGHEIEI-RNEAGMPLPERVVGHICVRGPSLMSGYFR--DEES--QDVLAA--------DGWLDTGDLG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 568968177 1360 FLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV 1403
Cdd:PRK09192 448 YL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIA 480
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
933-1416 |
2.81e-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: 83.80 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 933 TCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1012
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1013 CVLSTQAITRLLKSKEAAAAVDVRTW------PTILDTDDI--PKKKVASIFRPP----SPDVLAYLDFSVSTTGILAGV 1080
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpDGVLSIEDLlsPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1081 KMSH---AATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQYKA 1156
Cdd:cd05911 165 CLSHrnlIANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1157 RVTF------CSYSVMEMCTKGlgaqtgalrmkgvNLSCVRTCMVVAeerprisltqsfSKLFKDLGlparavsTTFGCR 1230
Cdd:cd05911 238 TFLYlvppiaAALAKSPLLDKY-------------DLSSLRVILSGG------------APLSKELQ-------ELLAKR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1231 VNVAICLQpnrlgklaEQGTTGPDPTTVYvdmralrhdrvrlvergSPHSLPLMES-GKILPGVKVIIAHTETKGPLGDS 1309
Cdd:cd05911 286 FPNATIKQ--------GYGMTETGGILTV-----------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDSLGPN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1310 HLGEIWVSSPHNATGYytvYGEETLHADHFsarlsfgdTQTIWARTGYLGFLRRTELtdasgerhdaLYVVGSLDETLEL 1389
Cdd:cd05911 341 EPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYFDEDGY----------LYIVDRKKELIKY 399
|
490 500
....*....|....*....|....*..
gi 568968177 1390 RGMRYHPIDIEtSVIRAHRSIAECAVF 1416
Cdd:cd05911 400 KGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
929-1418 |
1.66e-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: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 929 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1008
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1009 SKSACVLSTQAITRLLKSKEAAAAVDVRT----------WPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILA 1078
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1079 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVPPLELESNVslwL 1148
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAV---F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1149 SAVSQYKARVTFCS---YSVMemctkglgaqTGALRMKGVNLSCVRTCMVVAEERPRiSLTQSFSKLfkdlglparavst 1225
Cdd:cd05959 248 KRIRRYRPTVFFGVptlYAAM----------LAAPNLPSRDLSSLRLCVSAGEALPA-EVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1226 tFGCRVNVAIclqpnrlgklaeqGTTgpDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVIIAHtETKGP 1305
Cdd:cd05959 304 -FGLDILDGI-------------GST--EMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1306 LGDSHLGEIWVSSPHNATGYYTVYgEETlhadhfsaRLSFgdtQTIWARTGYlGFLRrteltDASGerhdALYVVGSLDE 1385
Cdd:cd05959 353 VADGEPGELYVRGPSSATMYWNNR-DKT--------RDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADD 410
|
490 500 510
....*....|....*....|....*....|...
gi 568968177 1386 TLELRGMRYHPIDIEtSVIRAHRSIAECAVFTW 1418
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 ... |
423-730 |
2.55e-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: 73.09 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 423 RTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPyal 499
Cdd:cd04433 1 DPALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 500 mKVNPLSWIQKVCSYKARAALVkSRDMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVIC 579
Cdd:cd04433 74 -KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 580 PCASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPylCKTDE 659
Cdd:cd04433 145 GYGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGE 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968177 660 IGEICVNSvatgtaYYGLLGITKNTFETVPVTADGvpvsdrpFTRTGLLGFIGPDNLVFVVGKLDGLMVVG 730
Cdd:cd04433 194 IGELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
936-1438 |
2.95e-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: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSACVL 1015
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1095
Cdd:cd05930 90 TD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1096 lqcELYPSR------QIAicldpycGLGF--ALWCL-CSVYSGHQSVLVPPlELESNVSLWLSAVSQYKARVTFCSYSVM 1166
Cdd:cd05930 127 ---EAYPLTpgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1167 EMCtkglgAQTGALRMkgvnLSCVRTcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNVaiclqpnrlgkla 1246
Cdd:cd05930 196 RLL-----LQELELAA----LPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1247 eqgtTGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYy 1326
Cdd:cd05930 241 ----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGY- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1327 tvYGEETLHADHFSArLSFGDTQTIWaRTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETsVIRA 1406
Cdd:cd05930 306 --LNRPELTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLA 370
|
490 500 510
....*....|....*....|....*....|....*...
gi 568968177 1407 HRSIAECAVFTWTN------LLVVVVELDGLEQDALDL 1438
Cdd:cd05930 371 HPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
308-817 |
1.69e-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: 71.70 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 308 LNPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVTLALT----TDACQKGLP 380
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVLAdagaADRLRDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 381 KAPTgevatfkgwpPLAWLVIDGKHLTRPPKDWYPLAQDTgsrTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGY 460
Cdd:cd05922 89 ASPD----------PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 461 TEAETLTNVLDFKRDAGLwhGVLTSVMNR--MHVITIPYALmkvnPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQR 537
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgaTLVLTNDGVL----DDAFWEDLREHGATGlAGVPS---TYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 538 DVCLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavlsmn 611
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 612 glsygvirvdteeklsvltvQDVGQVMPGASVCVVKVDGAPylCKTDEIGEIcVNSVATGTAYYGllgiTKNTFETVPVT 691
Cdd:cd05922 286 --------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKEGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 692 ADGVpvsdrpfTRTGLLGFIGPDNLVFVVGKLDGLMVVGVRRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDDRIV 771
Cdd:cd05922 339 GGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKLA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 568968177 772 LVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 817
Cdd:cd05922 407 LFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
936-1435 |
1.89e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.72 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGRLDAgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1011
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1012 acVLSTQAITRLLKSKEAAAAV-DVRTWPtildtddipKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1090
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1091 CRSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVM 1166
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1167 emctkglgaqtG--ALRMKGVNLSCVRTCmVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgk 1244
Cdd:PRK05851 260 -----------GkyARRVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG---------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1245 LAEQ--GTTGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNA 1322
Cdd:PRK05851 312 LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1323 TGYytvYGEETLHADHfsarlsfgdtqtiWARTGYLGFlrrteLTDasgerhDALYVVGSLDETLELRGMRYHPIDIET- 1401
Cdd:PRK05851 384 SGY---LGQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERv 436
|
490 500 510
....*....|....*....|....*....|....*....
gi 568968177 1402 -SVIRAHRSIAECAVFTWTNL----LVVVVELDGLEQDA 1435
Cdd:PRK05851 437 aAQVRGVREGAVVAVGTGEGSarpgLVIAAEFRGPDEAG 475
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
279-728 |
4.16e-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: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI-------EVPLTRKD 351
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAAnpiytadELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 352 AGSQqvgfLLGSCGVTLALTTDACQKGLPKAptgEVATFKGWPPLawlVIDGKHLTRPP---KDWYPLAQ--DTGSRTAY 426
Cdd:cd05911 81 SKPK----VIFTDPDGLEKVKEAAKELGPKD---KIIVLDDKPDG---VLSIEDLLSPTlgeEDEDLPPPlkDGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 427 IEYkTSkeGST---VGVTVSHSSLLAQC-QALTQACGYTEA-ETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPyalmK 501
Cdd:cd05911 151 ILY-SS--GTTglpKGVCLSHRNLIANLsQVQTFLYGNDGSnDVILGFLPLYHIYGLF-TTLASLLNGATVIIMP----K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 502 VNPLSWIQKVCSYKARAALVKSRDMHW---SLLAQRGQrdvcLSSLRMLIVadGANPWSISSCDAFLNVFQSRGLRP--- 575
Cdd:cd05911 223 FDSELFLDLIEKYKITFLYLVPPIAAAlakSPLLDKYD----LSSLRVILS--GGAPLSKELQELLAKRFPNATIKQgyg 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 576 --EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPY 653
Cdd:cd05911 297 mtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPNVEAKIVDDDGKDS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 654 LcKTDEIGEICVNSvatGTAYYGLLGITKNTFETvpVTADGvpvsdrpFTRTGLLGFIGPDNLVFVVG------KLDGLM 727
Cdd:cd05911 337 L-GPNEPGEICVRG---PQVMKGYYNNPEATKET--FDEDG-------WLHTGDIGYFDEDGYLYIVDrkkeliKYKGFQ 403
|
.
gi 568968177 728 V 728
Cdd:cd05911 404 V 404
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
902-1136 |
5.99e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 69.90 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLLLNAKgtvtstATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 982 CVPVTVRPphpqnlgttlptvkmivevsksacVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifrpPSP 1061
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1062 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1135
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 568968177 1136 P 1136
Cdd:cd05936 201 P 201
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
910-1092 |
6.44e-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: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 910 AHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGRLDaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 989
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARGVGP-GDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 990 PHPQnlgttlPTVKMIVEVSKSACVLSTQAitrllkskEAAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDF 1069
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPA--------LAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 568968177 1070 SVSTTGILAGVKMSHAATSALCR 1092
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
280-724 |
7.57e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.67 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 280 LTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqV 357
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYPAER-------L 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 358 GFLLGSCGVTLALTTDACQKGLPkaPTGEVATFKGWPPLAWLvidgkhlTRPPKDwyPLAQDTGSRTAYIEYKTSKEGST 437
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWA-------DYPDTA--PAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 438 VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVITIPYALmkvnplsWIQKVCSYKAR 517
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDEL-------WDPEQLYDEME 2233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 518 AALVKSRDM---HWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAflnvfQSRGLRPEVIcpcasspealtvairr 594
Cdd:PRK12316 2234 RHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEALRPVYL---------------- 2290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 595 ppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGASVCVvkVDGAPYLCKTDEIGEICVNSVATGTAY 674
Cdd:PRK12316 2291 ---FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLNLLAPGMAGELYLGGEGLARGY 2359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568968177 675 YGLLGITKNTFETVPVTADGVPVsdrpfTRTGLLGFIGPDNLVFVVGKLD 724
Cdd:PRK12316 2360 LNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRID 2404
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
910-1441 |
2.90e-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: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 910 AHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 989
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 990 PHPqnlgttlptvkmivevsksacvlstqaITRLLKSKEAAAavdvrtwPTILDTDdipkkkvasifrppsPDVLAYLDF 1069
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1070 SVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPY---CGLgFALWclCSVYSGHQSVLVPPLELEsNVSL 1146
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPFsfdLSV-MDLY--PALASGATLVPVPRDATA-DPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1147 WLSAVSQYKARVTFCSYSVMEMCTkGLGAQTGAlrmkgvNLSCVRTCMVVAEERPrISLTQSFSKLFkdlglPARAVSTT 1226
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQQRF-----PDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1227 FgcrvnvaiclqpnrlgklaeqgttGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVKVIIAhTETKGPL 1306
Cdd:cd05945 247 Y------------------------GPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVIL-DEDGRPV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1307 GDSHLGEIWVSSPHNATGYYTVygeetlhADHFSARLSFGDTQTiWARTGYLGFLrrteltDASGErhdaLYVVGSLDET 1386
Cdd:cd05945 294 PPGEKGELVISGPSVSKGYLNN-------PEKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRLDFQ 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1387 LELRGMRYHPIDIETSViRAHRSIAECAVFTWTNL-----LVVVVELDGlEQDALDLVAL 1441
Cdd:cd05945 356 VKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKP-GAEAGLTKAI 413
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
281-724 |
3.32e-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: 63.82 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 281 TYGKLWSRSLKLAYTLLNKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 358
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVG------PGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 359 FLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkgwPPLAWLVIDGKHLTRPPKDWYPLAQDtgsrTAYIEYkTSkeGST- 437
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSGPDD----LAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 438 --VGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVITIPYALMKVNPLSWiqkvcsyk 515
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 516 arAALVKSRDM-HWSLLAqrgqrdvclSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 593
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 594 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGASVCVvkVDGAPYLCKTDEIGEIC 664
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYV--LDDDLRPVPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968177 665 VN--SVATGtaYYGLLGITKNTFetvpVTADGVPVSDRPFTRTGLLGFIGPD-NLVFvVGKLD 724
Cdd:TIGR01733 324 IGgpGVARG--YLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPDgNLEF-LGRID 379
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
936-1400 |
4.64e-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: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGttlptvkmivevSKSACVL 1015
Cdd:cd05908 20 HLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV------PVSIG------------SNEEHKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STQAITRLLKSkeaaaavdvrtwPTILDTDDIPKKkvasifrppSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1095
Cdd:cd05908 81 KLNKVWNTLKN------------PYLITEEEVLCE---------LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1096 LQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGA 1175
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1176 QTGAlrmkGVNLSCVRtcMVVAEERPRIS-LTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPnrlgklaeqgtTGP 1253
Cdd:cd05908 220 EKAN----DWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEASVGASLPK-----------AQS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1254 DPTTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGpLGDSHLGEIWVSSPHNATGYYTvyGEE 1332
Cdd:cd05908 283 PFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGYYN--NPE 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968177 1333 TlhadhfSARLSFGDTqtiWARTGYLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIE 1400
Cdd:cd05908 360 A------TAKVFTDDG---WLKTGDLGFIRNGR-----------LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
936-1159 |
7.89e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 63.06 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1013
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1014 VLSTQAItrllkskeAAAAVDVRTWPTILDTDDIPKKKVASifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1093
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968177 1094 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1159
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 ... |
936-1415 |
1.32e-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: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVpvtVRPPHPQNlgtTLPTVKMIVEVSKsACVL 1015
Cdd:cd05904 37 ELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAV---VTTANPLS---TPAEIAKQVKDSG-AKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STQAiTRLLKSKEAAAAV------DVRTWPTILDTDDIPkkkVASIFRPP-SPDVLAYLDFSVSTTGILAGVKMSHA-AT 1087
Cdd:cd05904 109 FTTA-ELAEKLASLALPVvlldsaEFDSLSFSDLLFEAD---EAEPPVVViKQDDVAALLYSSGTTGRSKGVMLTHRnLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1088 SALCRSIKLQCELYPSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLVPPLELESnvslWLSAVSQYkaRVTFCSYS-- 1164
Cdd:cd05904 185 AMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY--KVTHLPVVpp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1165 -VMEMCTKGLGaqtgalrmKGVNLSCVRTCMVVAeerprisltqsfSKLFKDLglpARAVSTTFGcrvNVAIClqpnrlg 1243
Cdd:cd05904 259 iVLALVKSPIV--------DKYDLSSLRQIMSGA------------APLGKEL---IEAFRAKFP---NVDLG------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1244 klaeQG----TTGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSP 1319
Cdd:cd05904 306 ----QGygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1320 HNATGYytvygeetlhadhfsarlsFGDTQ----TI----WARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRG 1391
Cdd:cd05904 367 SIMKGY-------------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKG 417
|
490 500
....*....|....*....|....
gi 568968177 1392 MRYHPIDIEtSVIRAHRSIAECAV 1415
Cdd:cd05904 418 FQVAPAELE-ALLLSHPEILDAAV 440
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
936-1441 |
1.38e-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: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGRlDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1015
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STQAItrllkskEAAAAVDVRTWPTILDTDDIPkkkVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1095
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1096 LQCELYPSRQIaICLDPYCglgF---ALWCLCSVYSGHQSVLVPPlelesnvslwlsavsqykarvtfcsysvmemctkg 1172
Cdd:cd12116 160 ERLGLGPGDRL-LAVTTYA---FdisLLELLLPLLAGARVVIAPR----------------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1173 lGAQTGALRMKGvnlscvrtcmvvAEERPRISLTQ---SFSKLFKDLGLPARAVSTtfgcrvnvAIC----LQPNRLGKL 1245
Cdd:cd12116 201 -ETQRDPEALAR------------LIEAHSITVMQatpATWRMLLDAGWQGRAGLT--------ALCggeaLPPDLAARL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1246 AEQGTT-----GPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------G 1312
Cdd:cd12116 260 LSRVGSlwnlyGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVL---------DAALrpvppgvpG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1313 EIWVSSPHNATGYytvYGEETLHADHFSArLSFGDTQTIWARTGYLgfLRRteLTDASgerhdaLYVVGSLDETLELRGM 1392
Cdd:cd12116 319 ELYIGGDGVAQGY---LGRPALTAERFVP-DPFAGPGSRLYRTGDL--VRR--RADGR------LEYLGRADGQVKIRGH 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568968177 1393 RYHPIDIETsVIRAHRSIAECAVFTWTN----LLVVVVELDGLEqdALDLVAL 1441
Cdd:cd12116 385 RIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA--APDAAAL 434
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
936-1415 |
1.58e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 62.32 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgTTLP-----TVKMIVEVSK 1010
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPR---TDLAvwaedTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1011 SACVLS---TQAITRLlkskeAAAAVDVRTWPTILDTDDIpkkkvasifRPP--SPDVLAYLDFSVSTTGILAGVKMSHA 1085
Cdd:PRK07768 110 KAVVVGepfLAAAPVL-----EEKGIRVLTVADLLAADPI---------DPVetGEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1086 ATSALCRSIKLQCELYPSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLVPPLELESNVSLWLSAVSQYKARVT- 1159
Cdd:PRK07768 176 NLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1160 ---FcSYSVMemcTKGLGAQTgalRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFG-CRVNVAI 1235
Cdd:PRK07768 252 apnF-AYALL---ARRLRRQA---KPGAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1236 CLQPnrlgklaeqgtTGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIW 1315
Cdd:PRK07768 324 SFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGLEVRVV-DEDGQVLPPRGVGVIE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1316 VSSPHNATGYYTVYGEETLHADHfsarlsfGdtqtiWARTGYLGFLrrTELtdasGErhdaLYVVGSLDETLELRGMRYH 1395
Cdd:PRK07768 391 LRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 568968177 1396 PIDIETSVIRAHRSIAECAV 1415
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
279-479 |
3.00e-09 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 62.18 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 356
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 357 VGFLLGSCGVTLALTTDACQKGLPKAPtgevatfkgwppLAWLVIDGKHLTRPPKDWyPLAQDTGSRTAYIEYkTSkeGS 436
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568968177 437 T---VGVTVSHSSLLAQCQALTQACGYTEAETLTNV--LDFkrDAGLW 479
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
268-470 |
6.69e-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: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 268 TALDTAGKatcTLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 347
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 348 TrkdagSQQVGFLLGSCGVTLALTtdacqkglpkaptgeVATFkgwpplawlvidgKHLTRPPKDWYPLAQDTGSRTAYI 427
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568968177 428 EYkTSkeGST---VGVTVSHSSLLA---QCQALTQACGyTEAETLTNVL 470
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKAWLEDLL-EGDDVVLAAL 175
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
936-1160 |
9.23e-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: 60.26 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1011
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1012 ACVLSTQAITRLLKSKEAaaavdvrtwPTI-LDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1090
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1091 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYkaRVT 1159
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARH--RVT 710
|
.
gi 568968177 1160 F 1160
Cdd:COG1020 711 V 711
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
909-1086 |
1.97e-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: 58.83 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 909 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 988
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 989 PPHPQnlgttlPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasifrPPSPDVLAYLD 1068
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 568968177 1069 FSVSTTGILAGVKMSHAA 1086
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
252-545 |
2.83e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 252 AALQLWGTTQ---PKAPCLTAL--DTAGKA---------TCTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALV 317
Cdd:PRK12316 4535 RIVALWNRTDagyPATRCVHQLvaERARMTpdavavvfdEEKLTYAELNRRANRLAHALI-------ARGVGPEVLVGIA 4607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 318 FPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPkAPTGevatfkgwpp 395
Cdd:PRK12316 4608 MERS--AEMMVGLLAVLKAggAYVPLDPEYPRER-------LAYMMEDSGAALLLTQSHLLQRLP-IPDG---------- 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 396 LAWLVIDgkhltrPPKDWY------PLAQDTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNV 469
Cdd:PRK12316 4668 LASLALD------RDEDWEgfpahdPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQF 4741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 470 LDFKRDA---GLWHGVLT--SVMNRMHVITIP---YALMKVNPLSWIQKVCSYkaraalvksrdmhWSLLAQRGQRDVCL 541
Cdd:PRK12316 4742 MSFSFDGsheGLYHPLINgaSVVIRDDSLWDPerlYAEIHEHRVTVLVFPPVY-------------LQQLAEHAERDGEP 4808
|
....
gi 568968177 542 SSLR 545
Cdd:PRK12316 4809 PSLR 4812
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
902-1416 |
3.63e-08 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 58.19 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 982 CVPVTVrpphpqnlGTTLPT--VKMIVEVSKS-ACVLSTQAI-TRLLKSKEAAAAV---------------DVRTWPTIL 1042
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEQlDKLLEVRDELPSLrhivvldprglrddpRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1043 D--TDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS-RQIAIcldpycgLGFA 1119
Cdd:COG1022 162 AlgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGdRTLSF-------LPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1120 -----LWCLCSVYSGHQSVLVPPLElesNVSLWLSAVsqykaRVTF-CS--------YS-VMEMctkglGAQTGALRMKG 1184
Cdd:COG1022 235 hvferTVSYYALAAGATVAFAESPD---TLAEDLREV-----KPTFmLAvprvwekvYAgIQAK-----AEEAGGLKRKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1185 VNLsCVRTCMVVAEER---PRISLTQS----------FSKLfkdlglpaRAVsttFGCRVNVAIC----LQPNrlgkLAE 1247
Cdd:COG1022 302 FRW-ALAVGRRYARARlagKSPSLLLRlkhaladklvFSKL--------REA---LGGRLRFAVSggaaLGPE----LAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1248 ----------QG-----TTGPdpTTVYvdmralRHDRVRLverGSphslplmeSGKILPGVKVIIAHTetkgplgdshlG 1312
Cdd:COG1022 366 ffralgipvlEGyglteTSPV--ITVN------RPGDNRI---GT--------VGPPLPGVEVKIAED-----------G 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1313 EIWVSSPHNATGYY-----TvygEETLHADhfsarlsfGdtqtiWARTGYLGFLrrteltDASGErhdaLYVVGSLDETL 1387
Cdd:COG1022 416 EILVRGPNVMKGYYknpeaT---AEAFDAD--------G-----WLHTGDIGEL------DEDGF----LRITGRKKDLI 469
|
570 580 590
....*....|....*....|....*....|
gi 568968177 1388 ELR-GMRYHPIDIEtSVIRAHRSIAECAVF 1416
Cdd:COG1022 470 VTSgGKNVAPQPIE-NALKASPLIEQAVVV 498
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
909-1092 |
1.27e-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: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 909 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 988
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 989 PPHPQNlgttlpTVKMIVEVSKSACVLStqaitrllkSKEAAAAVDVRtwPTILDTDDIPKKKVASIFRPP-SPDVLAYL 1067
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGL--EVAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 568968177 1068 DFSVSTTGILAGVKMSHAATSALCR 1092
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
936-1442 |
1.43e-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: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1015
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1095
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1096 LQCELYPSRQIAICldPYCGLGFALWCLCSVYS-GHQSVLVPPLELESNVSLWLSAVSQykaRVTFCSysvmemctkglg 1174
Cdd:cd17643 127 RWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLhGGRLVVVPYEVARSPEDFARLLRDE---GVTVLN------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1175 aQTGalrmkgvnlSCVRTCMVVAEERPRISLtqsfsklfkdlglPARAVstTFGCRVnvaicLQPNRLGKLAEQ-GTTGP 1253
Cdd:cd17643 190 -QTP---------SAFYQLVEAADRDGRDPL-------------ALRYV--IFGGEA-----LEAAMLRPWAGRfGLDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1254 D--------PTTVYVDMRALRHDRVRLVERGSphslplmeSGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGY 1325
Cdd:cd17643 240 QlvnmygitETTVHVTFRPLDAADLPAAAASP--------IGRPLPGLRVYVL-DADGRPVPPGVVGELYVSGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1326 YtvyGEETLHADHFSArLSFGDTQTIWARTGYLGflRRTeltdASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIR 1405
Cdd:cd17643 311 L---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE-AALA 375
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 568968177 1406 AHRSIAECAVFTWTN------LLVVVVELDGLEQDALDLVALV 1442
Cdd:cd17643 376 THPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRALL 418
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
308-497 |
1.59e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 55.71 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 308 LNPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEV 387
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 388 ATFKGWPPLA--------WLVIDGKHLTRPPKDwyPLAQDTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACG 459
Cdd:PRK08316 131 VDTLILSLVLggreapggWLDFADWAEAGSVAE--PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 568968177 460 YTEAETLTNVLDfkrdagLWHGVltsvmnRMHVITIPY 497
Cdd:PRK08316 209 MSADDIPLHALP------LYHCA------QLDVFLGPY 234
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
279-466 |
1.63e-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: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNKLTsknepllNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 358
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 359 FLLGSCGVTLALTTDACQKGLPkaptgevatfkgWPPLAW-LVIDGKHLTRPPkdwyPLAQDTGSRTAYIEYkTSkeGST 437
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP------------AGLPVLlLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GST 138
|
170 180 190
....*....|....*....|....*....|..
gi 568968177 438 ---VGVTVSHSSLLAQCQALTQACGYTEAETL 466
Cdd:cd12116 139 grpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
904-1437 |
6.93e-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: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 904 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCV 983
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 984 PVTVRPP-HPQNLGTTLPTVKMIVEVSKSAcVLSTQAItRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasiFRPPSPD 1062
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMTAAVIAVD-AQVMDAI-FQSGVRVLALSDLVGLGEPESAGPLIE-------DPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1063 VLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCEL-YPSRQIAICLDP-YCGLG-FALWCLCSVYSGhqsVLVPPLE 1139
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrHGRHNVVLGLMPlYHVIGfFAVLVAALALDG---TYVVVEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1140 LESNVSLWLSAvsqyKARVTfCSYSVMEMctkgLGAQTGALRMKGVNLSCVRTcmvvaeerprisltqsfsklfkdLGLP 1219
Cdd:cd05923 228 FDPADALKLIE----QERVT-SLFATPTH----LDALAAAAEFAGLKLSSLRH-----------------------VTFA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1220 ARAVSTTFGCRVNVAIclqPNRlgKLAEQGTT-------GPDPTTVYVdMRALRHDRVRLVERG--SPHSLPLMESGKIl 1290
Cdd:cd05923 276 GATMPDAVLERVNQHL---PGE--KVNIYGTTeamnslyMRDARTGTE-MRPGFFSEVRIVRIGgsPDEALANGEEGEL- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1291 pgvkvIIAHTetkgplGDSHLGEIWvsSPHNATgyytvygeetlhadhfSARLSFGdtqtiWARTGylgflrRTELTDAS 1370
Cdd:cd05923 349 -----IVAAA------ADAAFTGYL--NQPEAT----------------AKKLQDG-----WYRTG------DVGYVDPS 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968177 1371 GErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV--VVVELDGLEQDALD 1437
Cdd:cd05923 389 GD----VRILGRVDDMIISGGENIHPSEIE-RVLSRHPGVTEVVVIgvadeRWGQSVTacVVPREGTLSADELD 457
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
931-1084 |
1.53e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 52.69 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 931 TATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 989
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 990 -----PHPQNLGTTLP-----TVKMIvevskSACVLSTQAITRL----LKSKEAA---AAVDVRTWPTILDTDDIPKKKV 1052
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 568968177 1053 ASiFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1084
Cdd:PRK05605 211 VS-HPRPTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
279-372 |
6.53e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 358
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECGVR------KGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90
....*....|....
gi 568968177 359 FLLGSCGVTLALTT 372
Cdd:PRK08314 102 HYVTDSGARVAIVG 115
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
929-1431 |
8.83e-06 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 50.15 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 929 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP-HPQNLgttlptvkmive 1007
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDY------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1008 vsksacvlstqaitrllkskeAAAAVDVRTWPTILDTDDIpkkkvasifrppspdvlAYLDFSVSTTGILAGVKMSHAAT 1087
Cdd:cd05919 75 ---------------------AYIARDCEARLVVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1088 ----SALCRSIklqCELYPSRQIaicldpYC--------GLGFALWclCSVYSGHQSVLVPPLELESNVslwLSAVSQYK 1155
Cdd:cd05919 117 llfaDAMAREA---LGLTPGDRV------FSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1156 ARVTfcsYSVMEMCTKGLGAQTGALRMkgvnLSCVRTCMVVAEERPRiSLTQSFSKLFkdlGLParaVSTTFGCRVNVAI 1235
Cdd:cd05919 183 PTVL---YGVPTFYANLLDSCAGSPDA----LRSLRLCVSAGEALPR-GLGERWMEHF---GGP---ILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1236 CLQpNRLGKlAEQGTTGpdpttvyvdmRALRHDRVRLVERgsphslplmesgkilpgvkviIAHTETKGPLGDshlgeIW 1315
Cdd:cd05919 249 FLS-NRPGA-WRLGSTG----------RPVPGYEIRLVDE---------------------EGHTIPPGEEGD-----LL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1316 VSSPHNATGYYTVYgEETlhadhfSARLSFGdtqtiWARTGYLGFLrrteltDASGerhdALYVVGSLDETLELRGMRYH 1395
Cdd:cd05919 291 VRGPSAAVGYWNNP-EKS------RATFNGG-----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVS 348
|
490 500 510
....*....|....*....|....*....|....*.
gi 568968177 1396 PIDIEtSVIRAHRSIAECAVftwtnllVVVVELDGL 1431
Cdd:cd05919 349 PVEVE-SLIIQHPAVAEAAV-------VAVPESTGL 376
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
280-799 |
8.85e-06 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 50.17 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 280 LTYGKLWSRSLKLAYTLLNKLTSKnepllnpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqQVGF 359
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 360 LLGSCGVTLALTTDACQKglpkaptgevatfkgwpplawlvidgkhltrppkdwyplaqdtgsrTAYIEYKTSKEGSTVG 439
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 440 VTVSHSSLLAqcQALTQACGY--TEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVITIPYALMKVnplsWIQKVcsykAR 517
Cdd:cd05935 102 CMHTHFSAAA--NALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMAR----WDRET----AL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 518 AALVKSRDMHWS--------LLAQRGQRDVCLSSLRMLivADGANPWSISSCDAFLNVFqsrGLRPEVIcpcasspEALT 589
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL--TGGGAPMPPAVAEKLLKLT---GLRFVEG-------YGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 590 VAIrrPPDLGGPPPRKAVLSMnglsyGVIRVDTEEKlsVLTVQDVGQVMPGasvcvvkvdgapylcktdEIGEICVNSVA 669
Cdd:cd05935 235 ETM--SQTHTNPPLRPKLQCL-----GIP*FGVDAR--VIDIETGRELPPN------------------EVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 670 TGTAYYGLLGITKNTFetvpvtadgVPVSDRPFTRTGLLGFIGPDNLVFVVGKLDGLmvvgvrrhnaddIVATALAVEPM 749
Cdd:cd05935 288 IFKGYWNRPEETEESF---------IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRM------------INVSGFKVWPA 346
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968177 750 KF--VYRGRIAVFSVTVLH--DDR--------IVLVAEQRPDASEEDSFQW----MS-----RVLQAIDSI 799
Cdd:cd05935 347 EVeaKLYKHPAI*EVCVISvpDERvgeevkafIVLRPEYRGKVTEEDIIEWareqMAaykypREVEFVDEL 417
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
940-1442 |
1.17e-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: 49.75 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 940 RAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLSTQA 1019
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1020 ITRLLKskeaAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE 1099
Cdd:cd05922 79 AADRLR----DALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1100 LYPSRQIAICLdpycglgfalwclcsvysghqsvlvpPLELESNVSLWLSAVSQYKARVTFCSY----SVMEMCTKglga 1175
Cdd:cd05922 155 ITADDRALTVL--------------------------PLSYDYGLSVLNTHLLRGATLVLTNDGvlddAFWEDLRE---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1176 qTGALRMKGVnlscvrtcmvvaeerPriSLTQSFSKL-FKDLGLPARAVSTTFGCRvnvaicLQPNRLGKLAEQGTtGPD 1254
Cdd:cd05922 205 -HGATGLAGV---------------P--STYAMLTRLgFDPAKLPSLRYLTQAGGR------LPQETIARLRELLP-GAQ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1255 PTTVYVDMRALRH----DRVRLVERgsPHSLplmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYYTVYG 1330
Cdd:cd05922 260 VYVMYGQTEATRRmtylPPERILEK--PGSI-----GLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1331 EETlHADHFSARLsfgdtqtiwaRTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETSvIRAHRSI 1410
Cdd:cd05922 332 YRR-KEGRGGGVL----------HTGDLARR------DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLI 389
|
490 500 510
....*....|....*....|....*....|..
gi 568968177 1411 AECAVFtwtnllvvvveldGLEQDALDLVALV 1442
Cdd:cd05922 390 IEAAAV-------------GLPDPLGEKLALF 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
936-1103 |
1.69e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1015
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STQAITRLLKSKEAAAAVDVRT---WPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1092
Cdd:PRK12316 2106 TQRHLLERLPLPAGVARLPLDRdaeWADYPDTA--PAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ 2176
|
170
....*....|.
gi 568968177 1093 SIKLQCELYPS 1103
Cdd:PRK12316 2177 AAGERYELSPA 2187
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
909-1168 |
2.16e-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: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 909 RAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 988
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 989 PPHPQNlgttlpTVKMIVEVSKSACVLSTQAitrlLKSKEAAAAVDVRtwptiLDTDDIPKKKVASIFRPPSPDVLAYLD 1068
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSH----LQPPIAFIGLIDL-----LDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1069 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1140
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 568968177 1141 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1168
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
902-991 |
2.76e-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: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 568968177 982 CVPVTVRPPH 991
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
268-496 |
4.59e-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: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 268 TALDTAGKatcTLTYGKLWSRSLKLAYTLLNKLTSknepllNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 347
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKD------LRGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLNPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 348 TRKDAgsqqvgfllgscgvtLALTTDAcqkglpkAPTgevatfkgwpplawLVIDGkhltrppkdwyplaqdtgsrtAYI 427
Cdd:cd05941 72 PLAEL---------------EYVITDS-------EPS--------------LVLDP---------------------ALI 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568968177 428 EYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVITIP 496
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
885-1086 |
5.55e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.12 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 885 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVY 964
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 965 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTilDT 1044
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA--PQ 587
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568968177 1045 DDIPKkkvasifRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1086
Cdd:PRK10252 588 GAAPL-------QLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
259-382 |
5.78e-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: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 259 TTQPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPvmFMVAFYGCLLAEL 338
Cdd:cd17631 6 RRHPDRTALVFGGR------SLTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAAARLGA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568968177 339 VPVPIEVPLTRKDagsqqVGFLLGSCGVTLAL-----------TTdacqkGLPKA 382
Cdd:cd17631 71 VFVPLNFRLTPPE-----VAYILADSGAKVLFddlallmytsgTT-----GRPKG 115
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
245-720 |
6.35e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 47.49 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 245 NGPLSLLAALQLWGTTQPKApclTALDTAGKATctlTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSDpv 324
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 325 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVTLALTTDA----CQKGLPKAPTGEvatfkgwpplAWLV 400
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDSEfvplLAAILPQLPTVR----------TVIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 401 IDGKHLTRPPKDWY------------PLAQDTGSRTAYIEYKTSkeGST---VGVTVSHSSLLAQCQALTQACGYTEaet 465
Cdd:PRK06187 133 EGDGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 466 ltnvldfkRDAGLwhgVLTSvMNRMHVITIPYALMkvnpLSWIQKVC--SYKARAAL---VKSR--------DMHWSLLA 532
Cdd:PRK06187 208 --------DDVYL---VIVP-MFHVHAWGLPYLAL----MAGAKQVIprRFDPENLLdliETERvtfffavpTIWQMLLK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 533 QRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAV 607
Cdd:PRK06187 272 APRAYFVDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 608 LSmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGAPYLCKTDEIGEICVNSVATGTAYYGLLGITKNTFEt 687
Cdd:PRK06187 338 RR-----------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID- 393
|
490 500 510
....*....|....*....|....*....|...
gi 568968177 688 vpvtaDGvpvsdrpFTRTGLLGFIGPDNLVFVV 720
Cdd:PRK06187 394 -----GG-------WLHTGDVGYIDEDGYLYIT 414
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
936-1087 |
6.78e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.21 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1006
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1007 EVSKSA--CVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKkkvasIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1084
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 568968177 1085 AAT 1087
Cdd:PRK07656 189 RQL 191
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
261-571 |
8.15e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 261 QPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--EL 338
Cdd:PRK12316 524 TPEAPALAFGEE------TLDYAELNRRANRLAHALI-------ERGVGPDVLVGVAMERSIEMV--VALLAILKAggAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 339 VPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKgwPPLAWLviDGkHLTRPPKdwyplAQ 418
Cdd:PRK12316 589 VPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLD--RPAAWL--EG-YSEENPG-----TE 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 419 DTGSRTAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACGYTEAETLTNVLDFKRDAGLWHGVLTsVMNRMHVITIPYA 498
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPG 730
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968177 499 LMKvNPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQRDVCLsSLRMLIVADGANPWsisscDAFLNVFQSR 571
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) ... |
262-457 |
9.26e-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: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 262 PKAPCLTAldtagkATCTLTYGKLWSRSLKLAYTLLNKLTSknepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 341
Cdd:cd17651 9 PDAPALVA------EGRRLTYAELDRRANRLAHRLRARGVG-------PGDLVALCARRS--AELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 342 PIEVpltrkDAGSQQVGFLLGSCGVTLALTTDACQKGLPkaptgevatfkgwPPLAWLVIDGKHLTRPPKDWYPLAQDTG 421
Cdd:cd17651 74 PLDP-----AYPAERLAFMLADAGPVLVLTHPALAGELA-------------VELVAVTLLDQPGAAAGADAEPDPALDA 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 568968177 422 SRTAYIEYkTSkeGST---VGVTVSHSSLLAQCQALTQA 457
Cdd:cd17651 136 DDLAYVIY-TS--GSTgrpKGVVMPHRSLANLVAWQARA 171
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
279-463 |
1.34e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 46.11 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 279 TLTYGKLWSRSLKLAytllNKLTSKNeplLNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsqq 356
Cdd:cd12114 12 TLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 357 vgfLLGSCGVTLALTTDACQKGLPKAPTgevatfkgwpplawLVIDGKHLTRPPKDwyPLAQDTG-SRTAYIEYkTSkeG 435
Cdd:cd12114 79 ---ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP--PPPVDVApDDLAYVIF-TS--G 136
|
170 180 190
....*....|....*....|....*....|.
gi 568968177 436 ST---VGVTVSHSSLLAQCQALTQACGYTEA 463
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINRRFAVGPD 167
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
246-374 |
2.24e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 45.80 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 246 GPLSLLAALQLWGTTQPKAPcltALDTAGKatcTLTYGKLWSRSLKLAyTLLNKLTSKnepllnPGDRVALVFPNSdPvM 325
Cdd:PRK06178 31 GERPLTEYLRAWARERPQRP---AIIFYGH---VITYAELDELSDRFA-ALLRQRGVG------AGDRVAVFLPNC-P-Q 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568968177 326 FMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVTLALTTDA 374
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1287-1415 |
2.43e-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: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1287 GKILPGVKVIIAHTETKGPLGDSHlGEIWVSSPHNATGYYTvygEETLHADHFSARlsfgdtqtiWARTGYLGFLRrtel 1366
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568968177 1367 tdasgeRHDALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1415
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
936-1103 |
2.53e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.10 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1015
Cdd:PRK12316 4581 ELNRRANRLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1016 STQAITRLLKSKEAAAAVDV---RTWPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1092
Cdd:PRK12316 4654 TQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
170
....*....|.
gi 568968177 1093 SIKLQCELYPS 1103
Cdd:PRK12316 4725 ATGERYELTPD 4735
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
930-1414 |
2.67e-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: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 930 STATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP-PHPQNLGTTLPTVkmivev 1008
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQCLQEA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1009 sksacvlSTQAITRLLKSKEAAAAVdvrtwptildtddipkkkvasifrppspdvlayldFSVSTTGILAGVKMSHAATS 1088
Cdd:cd05910 74 -------EPDAFIGIPKADEPAAIL-----------------------------------FTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1089 ALCRSIKlqcELYPSRQIAICLDpycglGFALWCLCSVYSGHQSVlVPPLE----LESNVSLWLSAVSQYKARVTFCSYS 1164
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1165 VMEMCTKgLGAQtgalrmKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDlglparavsttfgcrvNVAIclqpnrlgk 1244
Cdd:cd05910 183 LLERVAR-YCAQ------HGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----------------EAEI--------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1245 LAEQGTTGPDPTTVyVDMRALRHDRVRLVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWV 1316
Cdd:cd05910 230 LTPYGATEALPVSS-IGSRELLATTTAATSGGAGTCV-----GRPIPGVRVrIIEIDDEPIAewddtleLPRGEIGEITV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1317 SSPHNATGYYTVYGEETLHADHFSArlsfgdtQTIWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHP 1396
Cdd:cd05910 304 TGPTVTPTYVNRPVATALAKIDDNS-------EGFWHRMGDLGYL------DDEGR----LWFCGRKAHRVITTGGTLYT 366
|
490
....*....|....*...
gi 568968177 1397 IDIEtSVIRAHRSIAECA 1414
Cdd:cd05910 367 EPVE-RVFNTHPGVRRSA 383
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
248-444 |
5.11e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 45.04 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 248 LSLLAALQLWGTtqPKAPCLTALDTagkatcTLTYGKLWSRSLKLAYTLlnkltskNEPLLNPGDRVALVFPNSdpVMFM 327
Cdd:PRK10252 460 LSALVAQQAAKT--PDAPALADARY------QFSYREMREQVVALANLL-------RERGVKPGDSVAVALPRS--VFLT 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 328 VAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKGWPPlawlvidgkh 405
Cdd:PRK10252 523 LALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA---------- 585
|
170 180 190
....*....|....*....|....*....|....*....
gi 568968177 406 ltrpPKDWYPLAQDTGSRTAYIEYKTSKEGSTVGVTVSH 444
Cdd:PRK10252 586 ----PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
906-1442 |
6.34e-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: 44.14 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 906 LQWRAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 985
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 986 tvrpphPQNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtDDipkkkvasifrppspdvLA 1065
Cdd:cd17631 74 ------PLNFRLTPPEVAYILADSGAKVLF-----------------------------DD-----------------LA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1066 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELyPSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLVPPLELESnv 1144
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1145 slWLSAVSQYKARVTFCSYSVME-MCTKGlgaqtgalRMKGVNLSCVRtCMVVAEERPRISLTQSFsklfKDLGLparAV 1223
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1224 STTFGcrvnvaiclqpnrlgklaeQGTTGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVKVIIAHTETK 1303
Cdd:cd17631 241 VQGYG-------------------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1304 gPLGDSHLGEIWVSSPHNATGYytvYGEETLHADhfsarlSFGDTqtiWARTGYLGFLrrteltDASGerhdALYVVGSL 1383
Cdd:cd17631 286 -EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRK 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968177 1384 DETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV-VVVELDGLEQDALDLVALV 1442
Cdd:cd17631 343 KDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELIAHC 406
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
902-1084 |
6.46e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 44.26 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 982 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLSTQAITRLLKSKEAAAAV---DVRTWPTILDT 1044
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568968177 1045 DDI------PKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1084
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
262-371 |
9.20e-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: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 262 PKAPCLTALDTagkaTCTLTYGKLwsrsLKLAYTLLNKLTSKNeplLNPGDRVALVFPNSDPvmFMVAFYGCLLAELVPV 341
Cdd:cd05926 1 PDAPALVVPGS----TPALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVA 67
|
90 100 110
....*....|....*....|....*....|
gi 568968177 342 PIEvPLTRKDagsqQVGFLLGSCGVTLALT 371
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 ... |
279-370 |
9.95e-04 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 43.51 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNKLtskneplLNPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVG 358
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT-----PDDYA 94
|
90
....*....|..
gi 568968177 359 FLLGSCGVTLAL 370
Cdd:cd05959 95 YYLEDSRARVVV 106
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
936-987 |
1.01e-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: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 568968177 936 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 987
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
902-1085 |
1.07e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.59 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCIQlhkRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 982 C--VPVTVRPPHPQnLGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVD---VRTWPTILDTDDIPKKKVASIF 1056
Cdd:PRK06155 96 AiaVPINTALRGPQ-LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190
....*....|....*....|....*....|
gi 568968177 1057 RPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1085
Cdd:PRK06155 175 AAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
279-341 |
1.84e-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: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNkltsknepL-LNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 341
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1286-1415 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 1286 SGKILPGVKVIIAHtETKGPLGDshlGEIWVSSPHNATGYY--TVYGEETlhadhfsarlsfgdTQTIWARTGYLGFLrr 1363
Cdd:cd05912 244 AGKPLFPVELKIED-DGQPPYEV---GEILLKGPNVTKGYLnrPDATEES--------------FENGWFKTGDIGYL-- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568968177 1364 teltDASGerhdALYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAV 1415
Cdd:cd05912 304 ----DEEG----FLYVLDRRSDLIISGGENIYPAEIEE-VLLSHPAIKEAGV 346
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
262-459 |
2.52e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 262 PKAPCLTaldTAGKatcTLTYGKLWSRSLKLAYTLlnkltskNEPLLNPGDRVALVFPNSdpvMFMVAfygCLLAEL--- 338
Cdd:PRK05691 2202 PQAPALT---FAGQ---TLSYAELDARANRLARAL-------RERGVGPQVRVGLALERS---LEMVV---GLLAILkag 2262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 339 ---VPVPIEVPLTRkdagsqqVGFLLGSCGVTLALTTDACQKGLPKAPTGeVATfkgwpplaW-LVIDGKHLTRPPKDwy 414
Cdd:PRK05691 2263 gayVPLDPEYPLER-------LHYMIEDSGIGLLLSDRALFEALGELPAG-VAR--------WcLEDDAAALAAYSDA-- 2324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568968177 415 PLAQDTGSR-TAYIEYKTSKEGSTVGVTVSHSSLLAQCQALTQACG 459
Cdd:PRK05691 2325 PLPFLSLPQhQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
902-983 |
3.16e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.17 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHPlFLLLNakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:PRK08279 39 LGDVFEEAAARHPDRP-ALLFE--DQSISYA---ELNARANRYAHWAAARG-VGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
..
gi 568968177 982 CV 983
Cdd:PRK08279 112 AV 113
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
279-341 |
6.60e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 40.81 E-value: 6.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968177 279 TLTYGKLWSRSLKLAYTLLNKLTskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 341
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
263-343 |
6.70e-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: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 263 KAPCLTALDTAGKatcTLTYGKLWSRSLKLAYTLLnkltsknEPLLNPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVP 342
Cdd:cd05945 3 ANPDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVP 70
|
.
gi 568968177 343 I 343
Cdd:cd05945 71 L 71
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
902-991 |
7.47e-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: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968177 902 LADVLQWRAHTTPDHplFLLLNAKGTVTStatcIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 981
Cdd:cd05920 17 LGDLLARSAARHPDR--IAVVDGDRRLTY----RELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90
....*....|
gi 568968177 982 CVPVTVRPPH 991
Cdd:cd05920 90 AVPVLALPSH 99
|
|
| |
