|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
999-1563 |
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: 730.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 999 LFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 1077
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1078 TTLPTVKMivEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFR-----PPSPDVLAYLDFSV 1152
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKwgphpPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1153 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1232
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1233 SQYKARVTFCSYSVMEMCTKGLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRV 1312
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1313 NVAICLQGTAGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHN 1392
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1393 ATGYYTVYGEEALHADHF-SARLSFGDTQTIWARTGYLGFLRRTELTDASGGRHDALYVVGSLDETLELRGMRYHPIDIE 1471
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFpSTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1472 TSVIRAHRSIAECAVFTWTNLLVVVVELD-GLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINSRGEKQRMHLR 1550
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 225735629 1551 DGFLADQLDPIYV 1563
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
347-923 |
0e+00 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 655.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 347 CLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 426
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 427 PLtrkdaGSQQVGFLLGSCGVFLALTTDACQKGLPKA-----QTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDT 501
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 502 GTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALM 581
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 582 KANPLSWIQKVCFYKARAALVKSRDMHWSL------LAQRGQRDVSLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 655
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 656 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEgTP 733
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPE-TK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 734 YLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGP----------DNLVFIVGK 803
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPtkctdlnveeHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 804 LDGLMVTGVRRHNADDVVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 883
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 225735629 884 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 923
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
989-1521 |
7.97e-68 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 239.45 E-value: 7.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 989 WRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRlsVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1068
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1069 RPPHPqnlGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRtwPTILDTDDIPKKKIASVFRP-PSPDVLAY 1147
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGT--PRLLVVDLLPDTSAADWPPPsPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1148 LDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESNV 1225
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1226 SLWLSAVSQYKARVT----FcSYsvmEMCTK-GLGAQTGvlrmkGVNLSCVRTCMVVAEeRPRIALTQSFSKLFKDLGLP 1300
Cdd:cd05931 232 LRWLRLISRYRATISaapnF-AY---DLCVRrVRDEDLE-----GLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1301 ARAVSTTFG---CRVNVAIclqGTAGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPL 1377
Cdd:cd05931 302 PEAFRPSYGlaeATLFVSG---GPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGREL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1378 GDSHLGEIWVSSPHNATGYytvYGEEALHADHFSARLSFGDtqTIWARTGYLGFLRRTEltdasggrhdaLYVVGSLDET 1457
Cdd:cd05931 378 PDGEVGEIWVRGPSVASGY---WGRPEATAETFGALAATDE--GGWLRTGDLGFLHDGE-----------LYITGRLKDL 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735629 1458 LELRGMRYHPIDIETSVIRAHRSIAE--CAVFTW----TNLLVVVVELDGLeQDALDLVALVTNV---VLEEH 1521
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
337-914 |
2.34e-64 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 229.43 E-value: 2.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 337 RWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLnkltsknePLLKPGDRVALVFPNSdpVMFMVAFYGCLL 416
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 417 AELVPVPIEVPLTRKDAgsQQVGFLLGSCGVFLALTTDACQKGLPKAqtgeVAAFKGWPPLSWLVIDGKHLAkPPKDWHP 496
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 497 LAQDTGTgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHV 573
Cdd:cd05931 144 PSPDPDD-IAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 574 VsvpyaLMK-----ANPLSWIQKVCFYKAR--AAlvksRDMHWSLLAQRGQR----DVSLSSLRMLIVadGANPWSISSC 642
Cdd:cd05931 220 V-----LMSpaaflRRPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 643 DAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPG 721
Cdd:cd05931 289 RRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 722 ANVCVVKLEGTPyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGapifdrPFTRTGLLGFIGPDNLvFIV 801
Cdd:cd05931 364 QEVRIVDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YIT 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 802 GKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIH 881
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREH 513
|
570 580 590
....*....|....*....|....*....|...
gi 225735629 882 QVGVYCLALVPANTLPKAPLGGIHISETKQRFL 914
Cdd:cd05931 514 GVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
987-1461 |
5.82e-49 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 180.59 E-value: 5.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 987 LQWRAHTTPDHPLFlllnAKGTVTSTaTCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1066
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1067 TVrpphpqNLGTTLPTVKMIVEVSKSACVLtTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPK-----------KKIAS 1135
Cdd:pfam00501 75 PL------NPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1136 VFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1211
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1212 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAeERPRIALTQSFS 1291
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1292 KLFkdlglpARAVSTTFGCRVNVAICLQGTAGPDPTTVYvdmralrhdrvrlverGSphslplmeSGKILPGVKVIIAHT 1371
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLRSL----------------GS--------VGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1372 ETKGPLGDSHLGEIWVSSPHNATGYytvYGEEALHADHFsarlsfgdTQTIWARTGYLGFLrrteltDASGgrhdALYVV 1451
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DEDG----YLEIV 407
|
490
....*....|
gi 225735629 1452 GSLDETLELR 1461
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
983-1503 |
6.96e-33 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 140.30 E-value: 6.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEkgRLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQA--RASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1063 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIrtwPTILDTDDIPkKKIASV 1136
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD-PALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1137 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1211
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1212 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEMCTKGLgaqtgvlrmkgvNLSCVRTCMVVAEerP- 1282
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSESALERL------------DLSRWRVAYSGSE--Pi 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1283 RIALTQSFSKLFKDLGLPARAVSTTFGCRVNVAICLQGTAGPDPTTVYVDMRALRHDRVRLVErGSphslPLMESGKILP 1362
Cdd:PRK05691 303 RQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGT-GS----VLMSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1363 GVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTvyGEEAlHADHFSARlsfgDTQTiWARTGYLGFLRRTEltdasg 1442
Cdd:PRK05691 378 GHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-SAKTFVEH----DGRT-WLRTGDLGFLRDGE------ 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225735629 1443 grhdaLYVVGSLDETLELRGMRYHPIDIETSVIRahrsiaECAVFTWTNLLVVVVELDGLE 1503
Cdd:PRK05691 444 -----LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1145-1513 |
1.32e-31 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 127.40 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1145 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1221
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1222 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAEERPrIALTQSFSKLFKDlglpa 1301
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1302 rAVSTTFGcrvnvaiclQGTAGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVKVIIAHTETkGPLGDSH 1381
Cdd:cd04433 141 -KLVNGYG---------LTETGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVDPDG-GELPPGE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1382 LGEIWVSSPHNATGYYTVygeealhadhfsARLSFGDTQTIWARTGYLGFLRrteltdasggRHDALYVVGSLDETLELR 1461
Cdd:cd04433 194 IGELVVRGPSVMKGYWNN------------PEATAAVDEDGWYRTGDLGRLD----------EDGYLYIVGRLKDMIKSG 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 225735629 1462 GMRYHPIDIETsVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1513
Cdd:cd04433 252 GENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHV 308
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
328-916 |
1.07e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 122.78 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 328 PPSLLATLQRWGTTQPKSPClTALDTTGkAVYTLTYGKLWSRSLKLAyTLLNKLTskneplLKPGDRVALVFP-NSDpvm 406
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDdNED--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 407 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----QVGFLLGSCGVflaLTTDACQkglpkAQTGEVAAFKGWPPLSWLV 481
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 482 IDGKHLAKPPKDWHPLAQDtgtgTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAG 558
Cdd:cd05906 149 IEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 559 LWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKA------RAALVKSRDmhwsLLAQRGQRDVSLSSLRMLIVAD 632
Cdd:cd05906 223 LVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSSLRYLVNAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 633 GANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVDTEEKLS-V 709
Cdd:cd05906 299 EAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSFPTYDHSqA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 710 LTVQDVGQVMPGANVCVVKLEGTpyLCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLL 789
Cdd:cd05906 351 LEFVSLGRPIPGVSMRIVDDEGQ--LLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDG-------WFRTGDL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 790 GFIGPDNLVFIVGKLDGLMVTGVrRHNADDVVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSfqw 869
Cdd:cd05906 417 GFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDA--- 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 225735629 870 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 916
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
983-1513 |
1.10e-28 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 121.46 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRLTYA---ELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1063 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLTtqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsp 1142
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1143 dvlAYLDFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1221
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1222 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgVLRMKGVNLSCVRTCMVVAEerpriALTQSFSKLFKDLglpa 1301
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1302 ravsttFGCRVNVA-----ICLQGTAGPDpttvyvDMRALRHDRVrlvergsphslplmesGKILPGVKVIIAHTETKgP 1376
Cdd:COG0318 239 ------FGVRIVEGyglteTSPVVTVNPE------DPGERRPGSV----------------GRPLPGVEVRIVDEDGR-E 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1377 LGDSHLGEIWVSSPHNATGYYTvyGEEALhadhfsaRLSFGDTqtiWARTGYLGFLrrteltDASGgrhdALYVVGSLDE 1456
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWN--DPEAT-------AEAFRDG---WLRTGDLGRL------DEDG----YLYIVGRKKD 347
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735629 1457 TLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1513
Cdd:COG0318 348 MIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELRAFL 409
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-123 |
6.85e-28 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 109.05 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 10 AAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIpliqgidpsLQAENripgPSQTTAAAPKQQKSRPTASRD 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFL---------LHPET----PTKLSAEAQNQLASLETKLRD 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 225735629 90 ERFRSDVHTEAVQAALAKYKERKM--PMPSKRRSVL 123
Cdd:pfam06464 69 EELSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
330-914 |
1.35e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.05 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 330 SLLATLQRWGTTQPKSPCLT----ALDTTGKAvYTLTYGKLWSRSLKLAYTLlNKLTSknepllkPGDRVALVFPNSdpV 405
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVA-ETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 406 MFMVAFYGCLLAELVPVPIEVPLTRkdAGSQQVGFLLGSCGVFLALTTDACqkglpkaqTGEVAAF----KGWPPLSWLV 481
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 482 IDGKHLAKPPKDwhPLAQDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQA----CGYSEAETLTNV--LD 552
Cdd:PRK05850 141 VDLLDLDSPRGS--DARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFEQLMSDyfgdTGGVPPPDTTVVswLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 553 FKRDAGLWHGVLTSVMNRMHVV-SVPYALMkANPLSWIQkvcfykaraaLVKSRDMHWSL-------LAQRGQRDVSLSS 624
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCPAVlTSPVAFL-QRPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 625 L---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygVIR 700
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------SVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 701 VDTEeKLSVltvqdvGQVMPGANVcvvklEGTPYL--------------------CKTDEVGEICVSSSATGTAYYGLLG 760
Cdd:PRK05850 349 FDYE-KLSA------GHAKRCETG-----GGTPLVsygsprsptvrivdpdtcieCPAGTVGEIWVHGDNVAAGYWQKPE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 761 ITKNVFEAVPVT-TGGAPifDRPFTRTGLLGFIGPDNLvFIVGKL-DGLMVTGvRRHNADDVVATalavepMKFVYRGRI 838
Cdd:PRK05850 417 ETERTFGATLVDpSPGTP--EGPWLRTGDLGFISEGEL-FIVGRIkDLLIVDG-RNHYPDDIEAT------IQEITGGRV 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 839 AVFSVTVLHDDRIVLVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRF 913
Cdd:PRK05850 487 AAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQY 566
|
.
gi 225735629 914 L 914
Cdd:PRK05850 567 R 567
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
983-1517 |
1.16e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 116.97 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCVQLHKRAERVAAALMEKGrlSVGDHVALVYPPGVDLIAAFYGCL 1059
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1060 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLTTQAVTRLLRskEAAAAVDIRTWPTI--LDTDDIPKKKIASVF 1137
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVT--EYVAPQPGQSAPPVieVDLLDLDSPRGSDAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1138 RPPSPDVlAYLDFSVSTTGILAGVKMSHAATSALCRSI------KLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1211
Cdd:PRK05850 156 PRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1212 QSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaQTGVLRMKGVNLSCVRTcMVVAEERPRIALTQSFS 1291
Cdd:PRK05850 235 PAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVR----KTSDDDMAGLDLGGVLG-IISGSERVHPATLKRFA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1292 KLFKDLGLPARAVSTTFG---CRVNVAIclqGTAGPDPTTVYVDMRALRHDRVR---------LVERGSPHSlplmesgk 1359
Cdd:PRK05850 310 DRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYGSPRS-------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1360 ilPGVKVIIAHTETKGPLGDshLGEIWVSSPHNATGYYTVYGEEalhADHFSARL---SFGDTQTIWARTGYLGFLrrte 1436
Cdd:PRK05850 379 --PTVRIVDPDTCIECPAGT--VGEIWVHGDNVAAGYWQKPEET---ERTFGATLvdpSPGTPEGPWLRTGDLGFI---- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1437 ltdaSGGrhdALYVVGSLDETLELRGMRYHPIDIETSV--IRAHRsiaeCAVFT----WTNLLVVVVEL---DGLEQDAL 1507
Cdd:PRK05850 448 ----SEG---ELFIVGRIKDLLIVDGRNHYPDDIEATIqeITGGR----VAAISvpddGTEKLVAIIELkkrGDSDEEAM 516
|
570
....*....|
gi 225735629 1508 DLVALVTNVV 1517
Cdd:PRK05850 517 DRLRTVKREV 526
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1017-1477 |
1.23e-26 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 117.15 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGRLsvGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1088
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1089 vsksacVLTTQAVTRLLRSKEAAAAVDIRtwPTILDTDDIPKKkIASVFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1165
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDS-AGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1166 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1242
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1243 SYSVMEmctkgLGAQTGVLRM-KGVNLSCVrtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrVNVAICLQGT 1321
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVAT 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1322 AGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYY-- 1397
Cdd:PRK12476 367 IAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWgr 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1398 ---TvygEEALHAdHFSARLSFG------DTQTIWARTGYLGFLRRTEltdasggrhdaLYVVGSLDETLELRGMRYHPI 1468
Cdd:PRK12476 447 peeT---ERTFGA-KLQSRLAEGshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNHYPQ 511
|
....*....
gi 225735629 1469 DIETSVIRA 1477
Cdd:PRK12476 512 DIEATVAEA 520
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
335-811 |
1.84e-26 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 113.95 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 335 LQRWGTTQPKSPCLTALDTTgkavyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 414
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR-----RLTYRELDERANRLA----AGLRALG---VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 415 LLAELVPVPIEVpltrkDAGSQQVGFLLGSCGVFLALTTD--------ACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKH 486
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 487 LAKPPKDWHPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQAC----GYSEAETLTNVLDFKRDAGL 559
Cdd:pfam00501 142 ADVPPPPPPPPDPDD---LAYIIY-TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 560 WHGVLTSVMNRMHVVSVP--YALMKANPLSWIQKvcfYKARAALVKSRDMHWsLLAQRGQRDVSLSSLRMLIVadGANPW 637
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPPgfPALDPAALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 638 SISSCDAFLNVFqsrglrPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQ 717
Cdd:pfam00501 290 PPELARRFRELF------GGALVNGYGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGR 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 718 VMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvttggapiFDRPFTRTGLLGFIGPDNL 797
Cdd:pfam00501 337 PLPGTEVKIVDDETGEPV-PPGEPGELCVRGPGVMKGYLNDPELTAEAF------------DEDGWYRTGDLGRRDEDGY 403
|
490
....*....|....
gi 225735629 798 VFIVGKLDGLMVTG 811
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
331-820 |
3.24e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 114.14 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 331 LLATLQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSDPvmFMVA 410
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 411 FYGCLLAELVPVPIEVPLTRKdagsqQVGFLLGSCGvflalttdacqkglPKAqtgevaafkgwpplswlVIdgkhlakp 490
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSG--------------ARA-----------------LV-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 491 pkdwhplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSV 567
Cdd:COG0318 102 --------------TALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 568 MNRMHVVSVPyalmKANPLSWIQKVCFYKA-RAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFL 646
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 647 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGANVC 725
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 726 VVKLEGTPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttGGapifdrpFTRTGLLGFIGPDNLVFIVGKLD 805
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVGRKK 346
|
490
....*....|....*
gi 225735629 806 GLMVTGVRRHNADDV 820
Cdd:COG0318 347 DMIISGGENVYPAEV 361
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
352-920 |
6.70e-26 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 114.72 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 352 DTTGKAVYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LT 429
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 430 RKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEvaafkgwpPLSWlVIDGKHLAKPPKDWHPLAQDTGTGTAYIE 509
Cdd:PRK09192 112 GRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGN--------PLLH-VLSHAWFKALPEADVALPRPTPDDIAYLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 510 YkTSkeGST---VGVTVSHASLLAQCRALTQ-ACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANP 585
Cdd:PRK09192 183 Y-SS--GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 586 LSWIQKVCfyKARAALVKSRDMHWSLLAQRGQ----RDVSLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICP 661
Cdd:PRK09192 260 LQWLDLIS--RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 662 CASSPEAlTVAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGANVCVVKLEGTPYlcKTDE 740
Cdd:PRK09192 336 SYGLAEA-TLAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGMPL--PERV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 741 VGEICVSSSATGTAYYGllgitKNVFEAVPVTTGgapifdrpFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDV 820
Cdd:PRK09192 411 VGHICVRGPSLMSGYFR-----DEESQDVLAADG--------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 821 VATAlavEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKA 899
Cdd:PRK09192 477 EWIA---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRT 550
|
570 580
....*....|....*....|.
gi 225735629 900 PLGGIHISETKQRFLEGTLHP 920
Cdd:PRK09192 551 SSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
390-918 |
2.97e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 103.66 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 390 KPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP-----LTRKDAgsqqvgfLLGSCGVFLALTTDACQKG----- 459
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGvrkff 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 460 --LPKAQTGEVAAFKGWPP---LSWlvidgkhlaKPPkdwhPLAQDTgtgTAYIEYkTSkeGST---VGVTVSHASLLAQ 531
Cdd:PRK07769 148 raRPAKERPRVIAVDAVPDevgATW---------VPP----EANEDT---IAYLQY-TS--GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 532 CRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKaNPLSWIqkvcfykaRAALVKSRDMH--- 608
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWI--------RELARKPGGTGgtf 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 609 -------WSLLAQRG-----QRDVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRR 675
Cdd:PRK07769 280 saapnfaFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 676 PPDlggpPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTA 754
Cdd:PRK07769 358 MDE----EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 755 YYGLLGITKNVFEAV------PVTTGGAPIfDRPFTRTGLLGFIGPDNLvFIVGKLDGLMVTGVRRHNADDVVATALavE 828
Cdd:PRK07769 432 YWGKPEETAATFQNIlksrlsESHAEGAPD-DALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--E 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 829 PMKFVYRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCL 888
Cdd:PRK07769 508 ATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDV 587
|
570 580 590
....*....|....*....|....*....|
gi 225735629 889 ALVPANTLPKAPLGGIHISETKQRFLEGTL 918
Cdd:PRK07769 588 LLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
327-948 |
5.85e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 101.01 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 327 RPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLlnkltsknEPLLKPGDRVALVFPnSDPvM 406
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFP-SGP-D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 407 FMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLpkAQTGEVAAfKGWPPlsWLVIDGKh 486
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL--LQMEELAA-ANAPE--LLCVDTL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 487 LAKPPKDWHPLAQDtGTGTAYIEYkTSkeGSTV---GVTVSHASLLAQCRALTQACG--YSEAETLTNVLDFKRDAGLWH 561
Cdd:PRK05691 151 DPALAEAWQEPALQ-PDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 562 GVLTSVMNrmhvvSVPYALMK-----ANPLSWIQKVCFYkaRAALVKSRDMHWSLLAQRgqrdVSLSSLRML------IV 630
Cdd:PRK05691 227 GLLQPIFS-----GVPCVLMSpayflERPLRWLEAISEY--GGTISGGPDFAYRLCSER----VSESALERLdlsrwrVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 631 ADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSV 709
Cdd:PRK05691 296 YSGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 710 LTVQDVGQVM-------PGANVCVV---KLEGTPylckTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGapif 779
Cdd:PRK05691 360 RAEPGTGSVLmscgrsqPGHAVLIVdpqSLEVLG----DNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDG---- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 780 dRPFTRTGLLGFIgPDNLVFIVGKLDGLMVtgVRRHN--ADDVVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE- 856
Cdd:PRK05691 428 -RTWLRTGDLGFL-RDGELFVTGRLKDMLI--VRGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEi 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 857 ----QRPDASEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVT 932
Cdd:PRK05691 502 srsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYA 567
|
650
....*....|....*.
gi 225735629 933 NLPKPRQKQPEVGPAS 948
Cdd:PRK05691 568 LFPALQAVEAAQTAAS 583
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1017-1486 |
5.95e-21 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 97.34 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1096
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1097 TTQAvTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1176
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAP---PPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1177 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1250
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1251 TKGLGAQTGVLRMkgvnlscvrtcMVVAEERPRIALTQSFSKLFKDLGLparavsttfgcrVNvaiclqgTAGPDPTTVY 1330
Cdd:TIGR01733 227 AAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN-------LYGPTETTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1331 VDMRALRHDRVRlvergSPHSLPLmesGKILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYytvYGEEALHADHF 1410
Cdd:TIGR01733 277 STATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERF 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225735629 1411 SARLSFGDTQTIWARTGYLGflRRteltdasggRHD-ALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1486
Cdd:TIGR01733 345 VPDPFAGGDGARLYRTGDLV--RY---------LPDgNLEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1017-1496 |
2.95e-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: 96.58 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGRLSvGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1095
Cdd:cd05906 44 DLLEDARRLAAGLRQLGLRP-GDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1096 LTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSi 1175
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAA---DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1176 KLQCELYPSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVMEM 1249
Cdd:cd05906 199 KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWApnfAFALLND 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1250 CTKGLGAQTGvlrmkgvNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRVNVAIClqgtagpdptTV 1329
Cdd:cd05906 277 LLEEIEDGTW-------DLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1330 YVDMRALRHdrvrlvergsPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGEEALHADH 1409
Cdd:cd05906 339 SRSFPTYDH----------SQALEFVSLGRPIPGVSMRIV-DDEGQLLPEGEVGRLQVRGPVVTKGY---YNNPEANAEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1410 FsarlsfgdTQTIWARTGYLGFLrrteltdasggRHDALYVVGSLDETLELRGMRYHPIDIETSV----IRAHRSIAECA 1485
Cdd:cd05906 405 F--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFA 465
|
490
....*....|....
gi 225735629 1486 VF---TWTNLLVVV 1496
Cdd:cd05906 466 VRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
352-920 |
6.56e-19 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 92.88 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 352 DTTGKAVyTLTYGKLWSRslklaytlLNKLTSKNEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP---- 427
Cdd:PRK12476 61 SAAGCAV-ELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 428 -LTRKDAgsqqvgfLLGSCGVFLALTTDACQ-------KGLPKAQTGEVAAFKGWPplswlvidgkhlAKPPKDWHPLAQ 499
Cdd:PRK12476 130 hAERLDT-------ALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIP------------DSAGESFVPVEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 500 DTgTGTAYIEYkTSkeGST---VGVTVSHasllaqcRAltqACgyseaetlTNVLDFKRDAGLW----HGV--------- 563
Cdd:PRK12476 191 DT-DDVSHLQY-TS--GSTrppVGVEITH-------RA---VG--------TNLVQMILSIDLLdrntHGVswlplyhdm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 564 -LTSVM------NRMHVVSvPYALMKaNPLSWIQKVCfYKARAALV--KSRDMHWSLLAQRG----QRDVSLSSLRMLIv 630
Cdd:PRK12476 249 gLSMIGfpavygGHSTLMS-PTAFVR-RPQRWIKALS-EGSRTGRVvtAAPNFAYEWAAQRGlpaeGDDIDLSNVVLII- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 631 adGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSMNGLSYG-VIRVDTEEKLSV 709
Cdd:PRK12476 325 --GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPSVVYLDREQLGAGrAVRVAADAPNAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 710 LTVQdVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTT-------GGAPIfDRP 782
Cdd:PRK12476 400 AHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSRlaegshaDGAAD-DGT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 783 FTRTGLLGFIgPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDAS 862
Cdd:PRK12476 477 WLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTS 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 225735629 863 EEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHP 920
Cdd:PRK12476 554 RADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1017-1481 |
1.65e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 91.71 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGRlsVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1088
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1089 VSKSAcvlttQAVTRLLRSKEAAAAvdirtwPTILDTDDIPKKkIASVFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1165
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1166 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1239
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1240 tfcsYSVMEMCTKGLGAQTGVLR--MKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGcrVNVAIC 1317
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARGLPKdgEPPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1318 LQGTAGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATG 1395
Cdd:PRK07769 352 FVSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1396 YytvYGEEALHADHFSARLSFGDTQT---------IWARTGYLGFLRRTEltdasggrhdaLYVVGSLDETLELRGMRYH 1466
Cdd:PRK07769 432 Y---WGKPEETAATFQNILKSRLSEShaegapddaLWVRTGDYGVYFDGE-----------LYITGRVKDLVIIDGRNHY 497
|
490
....*....|....*
gi 225735629 1467 PIDIETSVIRAHRSI 1481
Cdd:PRK07769 498 PQDLEYTAQEATKAL 512
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1014-1487 |
6.93e-18 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 88.81 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1014 TCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1093
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1094 CVLTTQAVtrLLRSKEAAAAVDIRT----------WPTILDTDDIPKKKIASVFRPP----SPDVLAYLDFSVSTTGILA 1159
Cdd:cd05911 85 VIFTDPDG--LEKVKEAAKELGPKDkiivlddkpdGVLSIEDLLSPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1160 GVKMSH---AATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQY 1235
Cdd:cd05911 163 GVCLSHrnlIANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1236 KARVTF------CSYSVMEMCTKGlgaqtgvlrmkgvNLSCVRTCMVVAEerpriALTQSFSKLFKdlglparavsttfg 1309
Cdd:cd05911 236 KITFLYlvppiaAALAKSPLLDKY-------------DLSSLRVILSGGA-----PLSKELQELLA-------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1310 CRVNVAICLQG-----TAGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGE 1384
Cdd:cd05911 284 KRFPNATIKQGygmteTGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1385 IWVSSPHNATGYYTvyGEEALHADHfsarlsfgdTQTIWARTGYLGFLRRTELtdasggrhdaLYVVGSLDETLELRGMR 1464
Cdd:cd05911 345 ICVRGPQVMKGYYN--NPEATKETF---------DEDGWLHTGDIGYFDEDGY----------LYIVDRKKELIKYKGFQ 403
|
490 500
....*....|....*....|...
gi 225735629 1465 YHPIDIEtSVIRAHRSIAECAVF 1487
Cdd:cd05911 404 VAPAELE-AVLLEHPGVADAAVI 425
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
973-1474 |
7.92e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 82.75 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 973 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGV 1049
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1050 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLTTQAVTRLLrsKEAAAAVDIRTWPTILDTD 1126
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1127 DIPKKKIAsvFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1205
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1206 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTgvlrMKGVNLSCVRTCMVVAEE-RPR 1283
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKD----LAELDLSCWRVAGIGADMiRPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1284 IalTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLqgtagPDPTTvyvDMRALRHDRVRLVERGspHSLPLMES----- 1357
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSF-----SPLGS---GIVVEEVDRDRLEYQG--KAVAPGAEtrrvr 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1358 -----GKILPGVKVIIaHTETKGPLGDSHLGEIWVSSPHNATGYYtvygeealhADHFSARLSFGDTqtiWARTGYLGFL 1432
Cdd:PRK09192 383 tfvncGKALPGHEIEI-RNEAGMPLPERVVGHICVRGPSLMSGYF---------RDEESQDVLAADG---WLDTGDLGYL 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 225735629 1433 rrteltdaSGGRhdaLYVVGSLDETLELRGMRYHPIDIETSV 1474
Cdd:PRK09192 450 --------LDGY---LYITGRAKDLIIINGRNIWPQDIEWIA 480
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1014-1509 |
2.37e-15 |
|
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: 80.65 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1014 TCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSA 1093
Cdd:cd05930 14 TYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1094 CVLTTqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1173
Cdd:cd05930 87 LVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1174 SIKlqcELYPSR------QIAicldpycGLGF--ALWCL-CSVYSGHQSVLVPPlELESNVSLWLSAVSQYKARVTFCSY 1244
Cdd:cd05930 124 WMQ---EAYPLTpgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1245 SVMEMCTKGLGAQtgvlrmkgvNLSCVRTcMVVAEERPRIALTQSFSKLFKDLGLparavsttfgcrVNVaiclqgtAGP 1324
Cdd:cd05930 193 SLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YGP 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1325 DPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYytvYGEEA 1404
Cdd:cd05930 244 TEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGY---LNRPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1405 LHADHFSArLSFGDTQTIWaRTGYLGflRRteltDASGGrhdaLYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAEC 1484
Cdd:cd05930 311 LTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLAHPGVREA 377
|
490 500 510
....*....|....*....|....*....|.
gi 225735629 1485 AVFTWTN------LLVVVVELDGLEQDALDL 1509
Cdd:cd05930 378 AVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1010-1489 |
3.71e-15 |
|
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: 80.49 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1010 TSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1089
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1090 SKSACVLTTQAVTRLLRSKEAAAAVDIRT----------WPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILA 1159
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1160 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVPPLELESNVslwL 1229
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAV---F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1230 SAVSQYKARVTFCS---YSVMemctkglgaqTGVLRMKGVNLSCVRTCMVVAEerpriALTQSFSKLFKDLglparavst 1306
Cdd:cd05959 248 KRIRRYRPTVFFGVptlYAAM----------LAAPNLPSRDLSSLRLCVSAGE-----ALPAEVGERWKAR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1307 tFGCRVnvaicLQGTAGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVIIAHtETKGPLGDSHLGEIW 1386
Cdd:cd05959 304 -FGLDI-----LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1387 VSSPHNATGYYTVYGEealhadhfsARLSFgdtQTIWARTGYlGFLRRTEltdasgGRHdalYVVGSLDETLELRGMRYH 1466
Cdd:cd05959 363 VRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVRDDD------GFY---TYAGRADDMLKVSGIWVS 420
|
490 500
....*....|....*....|...
gi 225735629 1467 PIDIEtSVIRAHRSIAECAVFTW 1489
Cdd:cd05959 421 PFEVE-SALVQHPAVLEAAVVGV 442
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
389-898 |
3.51e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 73.63 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 389 LKPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQQVGFLLGSCGVFLALttdaCQKGL-PKAQ 464
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVL----ADAGAaDRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 465 TGEVAAFKgwpPLSWLVIDGKHLAKPPKDWHPLAQDTgtgTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEA 544
Cdd:cd05922 85 DALPASPD---PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 545 ETLTNVLDFKRDAGLwhGVLTS--------VMNRMHVVsvPYALMKAnplswiqkvcFYKARAALVKSRDMHWSLLAQRG 616
Cdd:cd05922 159 DRALTVLPLSYDYGL--SVLNThllrgatlVLTNDGVL--DDAFWED----------LREHGATGLAGVPSTYAMLTRLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 617 QRDVSLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavls 690
Cdd:cd05922 225 FDPAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 691 mnglsygvirvdteeklsvltvQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIcVSSSATGTAYYGllgiTKNVFEAVP 770
Cdd:cd05922 286 ----------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGYW----NDPPYRRKE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 771 VTTGGApifdrpfTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMkfvyrGRIAVFSVTVLHDDR 850
Cdd:cd05922 337 GRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEK 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 225735629 851 IVLVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 898
Cdd:cd05922 405 LALFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1017-1506 |
4.64e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 73.65 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGRLSVgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1092
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1093 acVLTTQAVTRLLRSKEAAAAVDirtwptilDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALC 1172
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVH--------DLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1173 RSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVMe 1248
Cdd:PRK05851 182 RGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1249 mctkGLGAQtgvlRMKGVNLSCVRTCmVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFG-----CRVNVAICLQGtag 1323
Cdd:PRK05851 260 ----GKYAR----RVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGlaestCAVTVPVPGIG--- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1324 pdpttvyvdmraLRHDRVRLVERGSPHSLPLMesGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEE 1403
Cdd:PRK05851 328 ------------LRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1404 ALHADHfsarlsfgdtqtiWARTGYLGFlrrteLTDasggrhDALYVVGSLDETLELRGMRYHPIDIET--SVIRAHRSI 1481
Cdd:PRK05851 391 PIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERvaAQVRGVREG 446
|
490 500
....*....|....*....|....*....
gi 225735629 1482 AECAVFTWTNL----LVVVVELDGLEQDA 1506
Cdd:PRK05851 447 AVVAVGTGEGSarpgLVIAAEFRGPDEAG 475
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
983-1486 |
1.70e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 71.83 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLLLNAKGTVTstatcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1063 CVPVTVRPphpqnlgttlptvkmivevsksacVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIAsvfrpPSP 1142
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1143 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1216
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1217 PplelesnvslwlsavsqykarvTFCSYSVMEMCTKGlgaqtGVLRMKGVNlscvrtCMVvaeerprIALTQSFSKLFKD 1296
Cdd:cd05936 201 P----------------------RFRPIGVLKEIRKH-----RVTIFPGVP------TMY-------IALLNAPEFKKRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1297 LGlparavsttfgcRVNVAIClqgtaGPDPTTVYVDMRALRHDRVRLVErG------SP--HSLPLMES------GKILP 1362
Cdd:cd05936 241 FS------------SLRLCIS-----GGAPLPVEVAERFEELTGVPIVE-GygltetSPvvAVNPLDGPrkpgsiGIPLP 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1363 GVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYYTvygeealHADHFSARLSFGdtqtiWARTGYLGFLrrteltDASG 1442
Cdd:cd05936 303 GTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYWN-------RPEETAEAFVDG-----WLRTGDIGYM------DEDG 363
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225735629 1443 grhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1486
Cdd:cd05936 364 ----YFFIVDRKKDMIIVGGFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
991-1173 |
4.77e-12 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 70.45 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 991 AHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1070
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1071 PHPQnlgttlPTVKMIVEVSKSACVLTTQAVTrllrskeAAAAVDiRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDF 1150
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPALA-------GELAVE-LVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 225735629 1151 SVSTTGILAGVKMSHAATSALCR 1173
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1017-1486 |
5.95e-12 |
|
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: 69.96 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVpvtVRPPHPQNlgtTLPTVKMIVEVSKSACVL 1096
Cdd:cd05904 37 ELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAV---VTTANPLS---TPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1097 TTQAVTrllrSKEAAAAVdirtwPTILdTDDIPKKKIASVFR--------PPSPDV----LAYLDFSVSTTGILAGVKMS 1164
Cdd:cd05904 110 TTAELA----EKLASLAL-----PVVL-LDSAEFDSLSFSDLlfeadeaePPVVVIkqddVAALLYSSGTTGRSKGVMLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1165 HA-ATSALCRSIKLQCELYPSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLVPPLELESnvslWLSAVSQYkaRVTFC 1242
Cdd:cd05904 180 HRnLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY--KVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1243 SYS---VMEMCTKGLGaqtgvlrmKGVNLSCVRTCMVVAeerprialtqsfSKLFKDLglpARAVSTTFGcrvNVAIClQ 1319
Cdd:cd05904 254 PVVppiVLALVKSPIV--------DKYDLSSLRQIMSGA------------APLGKEL---IEAFRAKFP---NVDLG-Q 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1320 G----TAGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATG 1395
Cdd:cd05904 307 GygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1396 YytVYGEEALHAdhfsarlsfgdtqTI----WARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELRGMRYHPIDIE 1471
Cdd:cd05904 372 Y--LNNPEATAA-------------TIdkegWLHTGDLCYI------DEDG----YLFIVDRLKELIKYKGFQVAPAELE 426
|
490
....*....|....*
gi 225735629 1472 tSVIRAHRSIAECAV 1486
Cdd:cd05904 427 -ALLLSHPEILDAAV 440
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1142-1471 |
4.75e-11 |
|
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: 67.13 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1142 PDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1221
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1222 ESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTgvlrMKGVNLSCVRtcMVVAEERP-RIALTQSFSKLFKDLGLP 1300
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEK----ANDWDLSSIR--MILNGAEPiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1301 ARAVSTTFG-CRVNVAICLQgTAGPDPTTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGpLG 1378
Cdd:cd05908 259 RNAILPVYGlAEASVGASLP-KAQSPFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1379 DSHLGEIWVSSPHNATGYYTvyGEEAlhadhfSARLSFGDTqtiWARTGYLGFLRRTEltdasggrhdaLYVVGSLDETL 1458
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYN--NPEA------TAKVFTDDG---WLKTGDLGFIRNGR-----------LVITGREKDII 394
|
330
....*....|...
gi 225735629 1459 ELRGMRYHPIDIE 1471
Cdd:cd05908 395 FVNGQNVYPHDIE 407
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
505-811 |
1.10e-10 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 65.00 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 505 TAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPyalm 581
Cdd:cd04433 2 PALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 582 KANPLSWIQKVCFYKARAALVkSRDMHWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVICP 661
Cdd:cd04433 74 KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 662 CASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPylCKTDEV 741
Cdd:cd04433 146 YGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGEI 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 742 GEICVSSsatgtaYYGLLGITKNVFEAVPVTTGGapifdrpFTRTGLLGFIGPDNLVFIVGKLDGLMVTG 811
Cdd:cd04433 195 GELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
991-1512 |
1.57e-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: 65.35 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 991 AHTTPDHPLFLLLNAkgtvtsTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1070
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1071 PHPqnlgttlptvkmivevsksacvlttqaVTRLLRSKEAAAavdirtwPTILDTDdipkkkiasvfrppsPDVLAYLDF 1150
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1151 SVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPY---CGLgFALWclCSVYSGHQSVLVPPLELEsNVSL 1227
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPFsfdLSV-MDLY--PALASGATLVPVPRDATA-DPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1228 WLSAVSQYKARVTFCSYSVMEMCT--KGLGAQtgvlrmkgvNLSCVRTCMVVAEERPrIALTQSFSKLFkdlglPARAVS 1305
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCLlsPTFTPE---------SLPSLRHFLFCGEVLP-HKTARALQQRF-----PDARIY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1306 TTFgcrvnvaiclqgtaGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVKVIIAhTETKGPLGDSHLGEI 1385
Cdd:cd05945 245 NTY--------------GPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVIL-DEDGRPVPPGEKGEL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1386 WVSSPHNATGYytvYGEEALHADHFsarlsFGDTQTIWARTGYLGFLrrteltDASGGrhdaLYVVGSLDETLELRGMRY 1465
Cdd:cd05945 302 VISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVRL------EADGL----LFYRGRLDFQVKLNGYRI 363
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 225735629 1466 HPIDIETSViRAHRSIAECAVFTWTNL-----LVVVVELDGlEQDALDLVAL 1512
Cdd:cd05945 364 ELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKP-GAEAGLTKAI 413
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1017-1523 |
1.74e-10 |
|
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: 66.03 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1092
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1093 ACVLTTQAVTRLLRSKEAaaavdirtwPTI-LDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1171
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1172 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYKARVT 1240
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1241 FCSYSVMEMCTKGLGAQtgvlrmkgvnLSCVRTCMVVAEerpriALTQSfsklfkdlgLPARAVSTTFGCR-VNVaiclq 1319
Cdd:COG1020 713 NLTPSLLRALLDAAPEA----------LPSLRLVLVGGE-----ALPPE---------LVRRWRARLPGARlVNL----- 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1320 gtAGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------GEIWVSSPH 1391
Cdd:COG1020 764 --YGPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL---------DAHLqpvpvgvpGELYIGGAG 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1392 NATGYytvYGEEALHADHFSArLSFGDTQTIWARTGYLGflRRteltdasggRHD-ALYVVGSLDETLELRGMRYHPIDI 1470
Cdd:COG1020 824 LARGY---LNRPELTAERFVA-DPFGFPGARLYRTGDLA--RW---------LPDgNLEFLGRADDQVKIRGFRIELGEI 888
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 225735629 1471 EtSVIRAHRSIAECAVFTWTN-----LLVVVVELDGLEQDALDLVALVTNVVLEEHYL 1523
Cdd:COG1020 889 E-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAALLRLALALLLPPYMV 945
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
362-805 |
1.83e-10 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 64.98 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 362 TYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqqvg 439
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 440 FLLGSCGVFLALTTdacqkglpkAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYkTSkeGST- 518
Cdd:TIGR01733 66 FILEDAGARLLLTD---------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 519 --VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVVSVPYALMKANPLSWiqkvcfyk 596
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 597 arAALVKSRDM-HWSLLAqrgqrdvslSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 674
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 675 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGANVCVVKLEGTPylCKTDEVGEIC 745
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRP--VPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 746 VSSSATGTAYYGLLGITKNVFEAVPVTTGGapifDRPFTRTGLLGFIGPDNLVFIVGKLD 805
Cdd:TIGR01733 324 IGGPGVARGYLNRPELTAERFVPDPFAGGD----GARLYRTGDLVRYLPDGNLEFLGRID 379
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
352-809 |
3.45e-10 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 64.54 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 352 DTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIevpltrk 431
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 432 DAGSQQ--VGFLLGSCGVFLALTTdacQKGLPKAQtgevAAFKGWPPLSWLVIDGKHLAK---PPKDWHPLA-------- 498
Cdd:cd05911 66 NPIYTAdeLAHQLKISKPKVIFTD---PDGLEKVK----EAAKELGPKDKIIVLDDKPDGvlsIEDLLSPTLgeededlp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 499 ---QDTGTGTAYIEYkTSkeGST---VGVTVSHASLLAQCralTQACGYSEA-----ETLTNVLDFKRDAGLWhGVLTSV 567
Cdd:cd05911 139 pplKDGKDDTAAILY-SS--GTTglpKGVCLSHRNLIANL---SQVQTFLYGndgsnDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 568 MNRMHVVSVPyalmKANPLSWIQKVCFYKARAALVKSRDMHWslLAQRGQRDV-SLSSLRMLIVadGANPWSISSCDAFL 646
Cdd:cd05911 212 LNGATVIIMP----KFDSELFLDLIEKYKITFLYLVPPIAAA--LAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 647 NVFQSRGLRP-----EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPG 721
Cdd:cd05911 284 KRFPNATIKQgygmtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPN 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 722 ANVCVVKLEGTPYLcKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpvTTGGapifdrpFTRTGLLGFIGPDNLVFIV 801
Cdd:cd05911 324 VEAKIVDDDGKDSL-GPNEPGEICVRGPQVMKGYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIV 390
|
490
....*....|....
gi 225735629 802 G------KLDGLMV 809
Cdd:cd05911 391 DrkkeliKYKGFQV 404
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1017-1240 |
7.25e-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: 63.44 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1094
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1095 VLTTQAVtrllrskeAAAAVDIRTWPTILDTDDIPKKKIASvfRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1174
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225735629 1175 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1240
Cdd:cd12114 158 INRRFAVGPDdRVLAL-----SSLSFDL----SVYdifgalsAGATLVLPDEAR-RRDPAHWAELIERH--GVT 219
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1017-1512 |
1.26e-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: 62.69 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGRlSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1096
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1097 TTQAVtrllrskEAAAAVDIRTWPTILDTDDIPKkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1176
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAAP---AAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1177 LQCELYPSRQIaICLDPYCglgF---ALWCLCSVYSGHQSVLVPPLELESNVSLwlsavsqyKARVTFCSYSVMEmctkg 1253
Cdd:cd12116 160 ERLGLGPGDRL-LAVTTYA---FdisLLELLLPLLAGARVVIAPRETQRDPEAL--------ARLIEAHSITVMQ----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1254 lgAQTGVLRMkgvnlscvrtcMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTfGCRVNVaiclqgtAGPDPTTVYVDM 1333
Cdd:cd12116 223 --ATPATWRM-----------LLDAGWQGRAGLTALCGGEALPPDLAARLLSRV-GSLWNL-------YGPTETTIWSTA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1334 RALrhdrvrlveRGSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------GEIWVSSPHNATGYytvYGEEAL 1405
Cdd:cd12116 282 ARV---------TAAAGPIPI---GRPLANTQVYVL---------DAALrpvppgvpGELYIGGDGVAQGY---LGRPAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1406 HADHFSArLSFGDTQTIWARTGYLGFLRRteltdasGGRhdaLYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECA 1485
Cdd:cd12116 338 TAERFVP-DPFAGPGSRLYRTGDLVRRRA-------DGR---LEYLGRADGQVKIRGHRIELGEIEA-ALAAHPGVAQAA 405
|
490 500 510
....*....|....*....|....*....|.
gi 225735629 1486 VFTWTN----LLVVVVELDGLEqdALDLVAL 1512
Cdd:cd12116 406 VVVREDggdrRLVAYVVLKAGA--APDAAAL 434
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
361-805 |
1.47e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 361 LTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqV 438
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYPAER-------L 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 439 GFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKgwPPLSWlvidgkhlakppKDW---HPLAQDTGTGTAYIEYKTSKE 515
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLPLPAGVARLPLD--RDAEW------------ADYpdtAPAVQLAGENLAYVIYTSGST 2158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 516 GSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVvsvpyaLMKANPLsWIQKVCFY 595
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARV------LIRDDEL-WDPEQLYD 2230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 596 KARAALVKSRDM---HWSLLAQRGQRDVSLSSLRMLIVadGANPWSISSCDAflnvfQSRGLRPEVIcpcasspealtva 672
Cdd:PRK12316 2231 EMERHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEALRPVYL------------- 2290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 673 irrppdLGGPPPRKAVLSMngLSYGVIRVDTEEKLSVltvqDVGQVMPGANVCVvkLEGTPYLCKTDEVGEICVSSSATG 752
Cdd:PRK12316 2291 ------FNGYGPTEAVVTP--LLWKCRPQDPCGAAYV----PIGRALGNRRAYI--LDADLNLLAPGMAGELYLGGEGLA 2356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 225735629 753 TAYYGLLGITKNVFEAVPVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 805
Cdd:PRK12316 2357 RGYLNRPGLTAERFVPDPFSASGERLY-----RTGDLARYRADGVVEYLGRID 2404
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1017-1486 |
2.29e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgTTLP-----TVKMIVEVSK 1091
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPR---TDLAvwaedTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1092 SACVLTT--QAVTRLLRskeaAAAVDIRTWPTILDTDDIpkkkiasvfRPP--SPDVLAYLDFSVSTTGILAGVKMSHAA 1167
Cdd:PRK07768 110 KAVVVGEpfLAAAPVLE----EKGIRVLTVADLLAADPI---------DPVetGEDDLALMQLTSGSTGSPKAVQITHGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1168 TSALCRSIKLQCELYPSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC 1242
Cdd:PRK07768 177 LYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1243 SYSVMEMCTKGLGAQTgvlRMKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLqGT 1321
Cdd:PRK07768 253 PNFAYALLARRLRRQA---KPGAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAVSF-SP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1322 AGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYYTVYG 1401
Cdd:PRK07768 328 CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGLEVRVV-DEDGQVLPPRGVGVIELRGESVTPGYLTMDG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1402 EEALHADHfsarlsfGdtqtiWARTGYLGFLrrTEltdasGGRhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSI 1481
Cdd:PRK07768 406 FIPAQDAD-------G-----WLDTGDLGYL--TE-----EGE---VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVR 463
|
....*
gi 225735629 1482 AECAV 1486
Cdd:PRK07768 464 PGNAV 468
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
349-534 |
4.06e-09 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 61.04 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 349 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 428
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQNLG-------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 429 TrkdagSQQVGFLLGSCGVFLALTtdacqkglpkaqtgeVAAFkgwpplswlvidgKHLAKPPKDWHPLAQDTGTGTAYI 508
Cdd:cd05936 84 T-----PRELEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190
....*....|....*....|....*....|..
gi 225735629 509 EYkTSkeGST---VGVTVSHASLLA---QCRA 534
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKA 159
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
360-560 |
4.12e-09 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.80 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 360 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 437
Cdd:COG1020 501 SLTYAELNARANRLAHHLRALG-------VGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 438 VGFLLGSCGVFLALTTDACQKGLPKAQtgevaafkgwppLSWLVIDGKHLAKPPKDWhPLAQDTGTGTAYIEYkTSkeGS 517
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 225735629 518 T---VGVTVSHASLLAQCRALTQACGYSEAETLTNV--LDFkrDAGLW 560
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
990-1167 |
6.17e-09 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 60.37 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 990 RAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1069
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1070 PPHPQnlgttlPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPkkkiasvfrPPSPDVLAYLD 1149
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 225735629 1150 FSVSTTGILAGVKMSHAA 1167
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1017-1513 |
5.52e-08 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 57.32 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1096
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1097 TTqavtrllrskeaaaavdirtwptildtddipkkkiasvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1176
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1177 LQCELYPSRQIAICldPYCGLGFALWCLCSVYS-GHQSVLVPPLELESNVSLWLSAVSQykaRVTFCS------YSVMEM 1249
Cdd:cd17643 127 RWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLhGGRLVVVPYEVARSPEDFARLLRDE---GVTVLNqtpsafYQLVEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1250 CTKGLGAQTGvLRMkgvnlscvrtcMVVAEERPRIALTQSFsklFKDLGLPARAVsttfgcrVNVAiclqgtaGPDPTTV 1329
Cdd:cd17643 202 ADRDGRDPLA-LRY-----------VIFGGEALEAAMLRPW---AGRFGLDRPQL-------VNMY-------GITETTV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1330 YVDMRALRHDRVRLVERGSphslplmeSGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYYtvyGEEALHADH 1409
Cdd:cd17643 253 HVTFRPLDAADLPAAAASP--------IGRPLPGLRVYVL-DADGRPVPPGVVGELYVSGAGVARGYL---GRPELTAER 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1410 FSArLSFGDTQTIWARTGYLGflRRTeltdaSGGRhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVFTW 1489
Cdd:cd17643 321 FVA-NPFGGPGSRMYRTGDLA--RRL-----PDGE---LEYLGRADEQVKIRGFRIELGEIE-AALATHPSVRDAAVIVR 388
|
490 500 510
....*....|....*....|....*....|
gi 225735629 1490 TN------LLVVVVELDGLEQDALDLVALV 1513
Cdd:cd17643 389 EDepgdtrLVAYVVADDGAAADIAELRALL 418
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
360-547 |
8.46e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 56.53 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 360 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQQVG 439
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 440 FLLGSCGVFLALTTDACQKGLPkaqtgevaafkGWPPLSWLVIDGKHLAKPPkdwhPLAQDTGTGTAYIEYkTSkeGST- 518
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP-----------AGLPVLLLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GSTg 139
|
170 180 190
....*....|....*....|....*....|.
gi 225735629 519 --VGVTVSHASLLAQCRALTQACGYSEAETL 547
Cdd:cd12116 140 rpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
990-1173 |
9.09e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 56.44 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 990 RAHTTPDHPLfllLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1069
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1070 PPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEaaaavdirtwpTILDTDDIPKKKIASVFRPP-SPDVLAYL 1148
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLTDRSLAGRAGGLE-----------VAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 225735629 1149 DFSVSTTGILAGVKMSHAATSALCR 1173
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1010-1502 |
4.04e-07 |
|
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: 54.39 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1010 TSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPphpqnlgttlptvkmivev 1089
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1090 sksacVLTTQAVTRLLRSKEAAAavdirtwpTILDTDDIpkkkiasvfrppspdvlAYLDFSVSTTGILAGVKMSHAAT- 1168
Cdd:cd05919 68 -----LLHPDDYAYIARDCEARL--------VVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDPl 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1169 ---SALCRSIklqCELYPSRQIaicldpYC--------GLGFALWclCSVYSGHQSVLVPPLELESNVslwLSAVSQYKA 1237
Cdd:cd05919 118 lfaDAMAREA---LGLTPGDRV------FSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1238 RVTFcsysvmemctkglGAQTG---VLRMKGVN---LSCVRTCMVVAEERPRiALTQSFSKlfkdlglparavstTFGCR 1311
Cdd:cd05919 184 TVLY-------------GVPTFyanLLDSCAGSpdaLRSLRLCVSAGEALPR-GLGERWME--------------HFGGP 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1312 VnvaicLQGTAGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVII----AHTETKGPLGDshlgeIWV 1387
Cdd:cd05919 236 I-----LDGIGATEVGHIFLSNRP---GAWRL---GS--------TGRPVPGYEIRLvdeeGHTIPPGEEGD-----LLV 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1388 SSPHNATGYYTVYGEEalhadhfSARLSFGdtqtiWARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELRGMRYHP 1467
Cdd:cd05919 292 RGPSAAVGYWNNPEKS-------RATFNGG-----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSP 349
|
490 500 510
....*....|....*....|....*....|....*
gi 225735629 1468 IDIEtSVIRAHRSIAECAVftwtnllVVVVELDGL 1502
Cdd:cd05919 350 VEVE-SLIIQHPAVAEAAV-------VAVPESTGL 376
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1012-1165 |
4.35e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 54.62 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1012 TATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 1070
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1071 -----PHPQNLGTTLP-----TVKMIvevskSACVLTTQAVTRL----LRSKEAA---AAVDIRTWPTILDTDDIPKKKI 1133
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 225735629 1134 ASVFRpPSPDVLAYLDFSVSTTGILAGVKMSH 1165
Cdd:PRK05605 211 VSHPR-PTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
389-543 |
7.17e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 53.78 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 389 LKPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEV 468
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 469 AAFKGWPPL--------SWLVIDgkHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACG 540
Cdd:PRK08316 131 VDTLILSLVlggreapgGWLDFA--DWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGD 208
|
...
gi 225735629 541 YSE 543
Cdd:PRK08316 209 MSA 211
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
360-626 |
7.79e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.19 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 360 TLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqq 437
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERS--AEMMVGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 438 VGFLLGSCGVFLALTTDACQKGLPKAqtgevaafKGwppLSWLVIDgkhlakPPKDW------HPLAQDTGTGTAYIEYK 511
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPIP--------DG---LASLALD------RDEDWegfpahDPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 512 TSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVVSVPYALmkANPLSWIQK 591
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHE-GLYHPLINGASVVIRDDSL--WDPERLYAE 4779
|
250 260 270
....*....|....*....|....*....|....*
gi 225735629 592 VcfYKARAALVKSRDMHWSLLAQRGQRDVSLSSLR 626
Cdd:PRK12316 4780 I--HEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
983-1487 |
3.54e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 51.64 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1063 CVPVTVrpphpqnlGTTLPT--VKMIVEVSKS-ACVLTTQA-VTRLLRSKEAAAAV---------------DIRTWPTIL 1123
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEqLDKLLEVRDELPSLrhivvldprglrddpRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1124 D--TDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS-RQIAIcldpycgLGFA 1200
Cdd:COG1022 162 AlgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGdRTLSF-------LPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1201 -----LWCLCSVYSGHQSVLVPPLE--------------------LE---SNVSLWLSAVSQYKARVtfcsysvMEMCTK 1252
Cdd:COG1022 235 hvferTVSYYALAAGATVAFAESPDtlaedlrevkptfmlavprvWEkvyAGIQAKAEEAGGLKRKL-------FRWALA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1253 gLGAQTGVLRMKGVNLScvrtcmvvAEERPRIALTQS--FSKLfkdlglpaRAVsttFGCRVNVAIC------------- 1317
Cdd:COG1022 308 -VGRRYARARLAGKSPS--------LLLRLKHALADKlvFSKL--------REA---LGGRLRFAVSggaalgpelarff 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1318 -------LQG-----TAGPdpTTVYvdmralRHDRVRLverGSphslplmeSGKILPGVKVIIAHTetkgplgdshlGEI 1385
Cdd:COG1022 368 ralgipvLEGyglteTSPV--ITVN------RPGDNRI---GT--------VGPPLPGVEVKIAED-----------GEI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1386 WVSSPHNATGYY-----TvygEEALHADhfsarlsfGdtqtiWARTGYLGFLrrteltDASGgrHdaLYVVGSLDETLEL 1460
Cdd:COG1022 418 LVRGPNVMKGYYknpeaT---AEAFDAD--------G-----WLHTGDIGEL------DEDG--F--LRITGRKKDLIVT 471
|
570 580
....*....|....*....|....*...
gi 225735629 1461 R-GMRYHPIDIEtSVIRAHRSIAECAVF 1487
Cdd:COG1022 472 SgGKNVAPQPIE-NALKASPLIEQAVVV 498
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
323-455 |
4.16e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 51.58 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 323 AGVPRPP-------SLLATLQRWGTTQPKSPcltALDTTGkavYTLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRV 395
Cdd:PRK06178 20 AGIPREPeyphgerPLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFAALLRQRG-------VGAGDRV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 396 ALVFPNSdPvMFMVAFYGCLLAELVPVPIEvPLTRKdagsQQVGFLLGSCGVFLALTTDA 455
Cdd:PRK06178 87 AVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
987-1513 |
5.98e-06 |
|
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: 50.69 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 987 LQWRAHTTPDHPLFLLLNakgtvtSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1066
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1067 tvrpphPQNLGTTLPTVKMIVEVSKSACVLttqavtrllrskeaaaavdirtwptildtDDipkkkiasvfrppspdvLA 1146
Cdd:cd17631 74 ------PLNFRLTPPEVAYILADSGAKVLF-----------------------------DD-----------------LA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1147 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELyPSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLVPPLELESnv 1225
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1226 slWLSAVSQYKARVTFCSYSVME-MCTKGlgaqtgvlRMKGVNLSCVRtCMVVAEERPRIALTQSFsklfKDLGLparAV 1304
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1305 STTFGcrvnvaiclQGTAGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVKVIIAHTETKgPLGDSHLGE 1384
Cdd:cd17631 241 VQGYG---------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR-EVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1385 IWVSSPHNATGYytvYGEEALHADhfsarlSFGDTqtiWARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELRGMR 1464
Cdd:cd17631 295 IVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRKKDMIISGGEN 352
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 225735629 1465 YHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV-VVVELDGLEQDALDLVALV 1513
Cdd:cd17631 353 VYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELIAHC 406
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
360-499 |
6.32e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 50.73 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 360 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQQVG 439
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735629 440 FLLGSCGVFLALTT-DACQKGLPKAQTGE-----VAAFKGW-------PPLSWLVIDGKHLAKPPKDWHPLAQ 499
Cdd:PRK08314 102 HYVTDSGARVAIVGsELAPKVAPAVGNLRlrhviVAQYSDYlpaepeiAVPAWLRAEPPLQALAPGGVVAWKE 174
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1011-1485 |
9.75e-06 |
|
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: 50.15 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1011 STATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP-PHPQNLGTTLptvkmivev 1089
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQCL--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1090 sksacvlttqavtrllrsKEAAAAVDIrtwptildtdDIPKKkiasvfrppspDVLAYLDFSVSTTGILAGVKMSHAATS 1169
Cdd:cd05910 71 ------------------QEAEPDAFI----------GIPKA-----------DEPAAILFTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1170 ALCRSIKlqcELYPSRQIAICLDpycglGFALWCLCSVYSGHQSVlVPPLE----LESNVSLWLSAVSQYKARVTFCSYS 1245
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1246 VMEMCTKgLGAQtgvlrmKGVNLSCVRtCMVVAEERPRIALTQSFSKLFKDlglpARAVSTTFGCRVNVAICLQGTagpd 1325
Cdd:cd05910 183 LLERVAR-YCAQ------HGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----EAEILTPYGATEALPVSSIGS---- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1326 pttvyvdmRALRHDRVRLVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWVSSPHNATGYY 1397
Cdd:cd05910 247 --------RELLATTTAATSGGAGTCV-----GRPIPGVRVrIIEIDDEPIAewddtleLPRGEIGEITVTGPTVTPTYV 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1398 TVYGEEALHADHFSArlsfgdtQTIWARTGYLGFLrrteltDASGgrhdALYVVGSLDETLELRGMRYHPIDIEtSVIRA 1477
Cdd:cd05910 314 NRPVATALAKIDDNS-------EGFWHRMGDLGYL------DDEG----RLWFCGRKAHRVITTGGTLYTEPVE-RVFNT 375
|
....*...
gi 225735629 1478 HRSIAECA 1485
Cdd:cd05910 376 HPGVRRSA 383
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
326-801 |
1.52e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 49.41 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 326 PRPPSLLATLQRWGTTQPKSpclTALDTTGKAVytlTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDpv 405
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDK---EAVYFDGRRT---TYAELDERVNRLA----NALRALG---VKKGDRVAVFDWNSH-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 406 MFMVAFYGCLLAELVPVPIEVPLTrkdagSQQVGFLLGSCGVFLALTTDacqKGLPkaqtgEVAAFKGWPPL--SWLVID 483
Cdd:PRK06187 68 EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVDS---EFVP-----LLAAILPQLPTvrTVIVEG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 484 GKHLAKPPKDWH------------PLAQDTGTGTAYIEYKTSkeGST---VGVTVSHASLLAQCRALTQACGYSEaetlt 548
Cdd:PRK06187 135 DGPAAPLAPEVGeyeellaaasdtFDFPDIDENDAAAMLYTS--GTTghpKGVVLSHRNLFLHSLAVCAWLKLSR----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 549 nvldfkRDAGLwhgVLTSvMNRMHVVSVPY-ALMKANPLSWIQKVCFYKARAALVKSR--------DMHWSLLAQRGQRD 619
Cdd:PRK06187 208 ------DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDPENLLDLIETERvtfffavpTIWQMLLKAPRAYF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 620 VSLSSLRMLIVadGANPWSISSCDAFLNVF-----QSRGLrPEvICPcasspealTVAIRRPPDlgGPPPRKAVLSmngl 694
Cdd:PRK06187 278 VDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-TE-TSP--------VVSVLPPED--QLPGQWTKRR---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 695 sygvirvdteeklsvltvqDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEavpvttG 774
Cdd:PRK06187 340 -------------------SAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------G 394
|
490 500
....*....|....*....|....*..
gi 225735629 775 GapifdrpFTRTGLLGFIGPDNLVFIV 801
Cdd:PRK06187 395 G-------WLHTGDVGYIDEDGYLYIT 414
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
990-1249 |
1.91e-05 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 49.25 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 990 RAHTTPDHPLFLLLNakgtvtSTATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1069
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1070 PPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAaavdirtwpTILDTDDIPKKKIASVFRPPSPDVLAYLD 1149
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1150 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1221
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 225735629 1222 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1249
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
990-1486 |
2.63e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 990 RAHTTPDHPLfLLLNAKgtvtsTATCVQLHKRAERVAAALMEKGrlsVGDH--VALVYPPGVDLIAAFYGCLYCGCVPVT 1067
Cdd:PRK12316 4560 RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEvlVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1068 VRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDI---RTWPTILDTDdiPKKKIAsvfrppsPDV 1144
Cdd:PRK12316 4631 LDPEYPRE------RLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDN 4695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1145 LAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRqiaiCLDPYCGLGF--ALWCLCSVYSGHQSVLVPPlele 1222
Cdd:PRK12316 4696 LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD----RVLQFMSFSFdgSHEGLYHPLINGASVVIRD---- 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1223 snVSLWLSAVSQ---YKARVTF--CSYSVMEMCTKGLGAQTGVLRMKGVNLScvrtcmvvAEERPRIALTQSFSKLFKDl 1297
Cdd:PRK12316 4768 --DSLWDPERLYaeiHEHRVTVlvFPPVYLQQLAEHAERDGEPPSLRVYCFG--------GEAVAQASYDLAWRALKPV- 4836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1298 glparavsttfgcrvnvaiCLQGTAGPDPTTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVKVIIAHTETkGPL 1377
Cdd:PRK12316 4837 -------------------YLFNGYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVLDGQL-NPL 4888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1378 GDSHLGEIWVSSPHNATGYYTvygEEALHADHFSARlSFGDTQTIWARTGylgflrrteltDASGGRHDALY-VVGSLDE 1456
Cdd:PRK12316 4889 PVGVAGELYLGGEGVARGYLE---RPALTAERFVPD-PFGAPGGRLYRTG-----------DLARYRADGVIdYLGRVDH 4953
|
490 500 510
....*....|....*....|....*....|
gi 225735629 1457 TLELRGMRYHPIDIETSvIRAHRSIAECAV 1486
Cdd:PRK12316 4954 QVKIRGFRIELGEIEAR-LREHPAVREAVV 4982
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
959-1184 |
2.93e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 959 RIAQASGRELAHLEDSDQARKFLFLADvlqWRAHTTP---DHPLFLLLNAKGTVTSTATCV----------QLHKRAERV 1025
Cdd:PRK12316 1965 QMAEDAQAALGELALLDAGERQRILAD---WDRTPEAyprGPGVHQRIAEQAARAPEAIAVvfgdqhlsyaELDSRANRL 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1026 AAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVT-RL 1104
Cdd:PRK12316 2042 AHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLLTQRHLLeRL 2114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1105 -----LRSKEAAAAVDIRTWPtildtDDIPKKKIAsvfrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQC 1179
Cdd:PRK12316 2115 plpagVARLPLDRDAEWADYP-----DTAPAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY 2182
|
....*
gi 225735629 1180 ELYPS 1184
Cdd:PRK12316 2183 ELSPA 2187
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
293-652 |
3.01e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 293 VDDFEELLEDPNQPKPEGSEtSVLRGEPLTAGVPRppSLLATLQRwgttQPKSPCLTALDTTgkavytLTYGKLWSRSLK 372
Cdd:PRK12316 482 VDELPMLDAEERGQLVEGWN-ATAAEYPLQRGVHR--LFEEQVER----TPEAPALAFGEET------LDYAELNRRANR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 373 LAYTLLnkltsknEPLLKPGDRVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqqVGFLLGSCGVFLA 450
Cdd:PRK12316 549 LAHALI-------ERGVGPDVLVGVAMERSIEMV--VALLAILKAggAYVPLDPEYPAER-------LAYMLEDSGVQLL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 451 LTTDACQKGLPKAQTGEVAAFKgwPPLSWLviDGKHLAKPPKDWHPLaqdtgtGTAYIEYKTSKEGSTVGVTVSHASLLA 530
Cdd:PRK12316 613 LSQSHLGRKLPLAAGVQVLDLD--RPAAWL--EGYSEENPGTELNPE------NLAYVIYTSGSTGKPKGAGNRHRALSN 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 531 QCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTsVMNRMHVVSVPYALMKaNPLSWIQkvcfYKARAAlVKSRDMHWS 610
Cdd:PRK12316 683 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVE----LINREG-VDTLHFVPS 755
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 225735629 611 LLA--QRGQRDVSLSSLRMLIVADGANPWsisscDAFLNVFQSR 652
Cdd:PRK12316 756 MLQafLQDEDVASCTSLRRIVCSGEALPA-----DAQEQVFAKL 794
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
966-1167 |
3.22e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.89 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 966 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatcvQLHKRAERVAAALMEKGrLSVGDHVALVY 1045
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1046 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDt 1125
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQG- 588
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 225735629 1126 ddipkkkiASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1167
Cdd:PRK10252 589 --------AAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
983-1485 |
3.52e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 48.36 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLLLNAKGTVT----STATCVQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGC 1058
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1059 LYCGCVPVTVRPphpqnlGTTLPTVKMIVEVSKSACVLT---TQAVTRLLRSKEAAA----AVDIRTWPTILDTDDIPKK 1131
Cdd:PRK09274 87 FKAGAVPVLVDP------GMGIKNLKQCLAEAQPDAFIGipkAHLARRLFGWGKPSVrrlvTVGGRLLWGGTTLATLLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1132 KIASVFRPP--SPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKlqcELYPSRQIAICL---------DPYCGLgfa 1200
Cdd:PRK09274 161 GAAAPFPMAdlAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfGPALGM--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1201 lwclCSVysghqsvlVPPLEL----ESNVSLWLSAVSQYKARVTFCSYSVMEMCTkglgaQTGvlRMKGVNLSCVRTcMV 1276
Cdd:PRK09274 235 ----TSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLG-----RYG--EANGIKLPSLRR-VI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1277 VAEERPRIALTQSFSKLfkdlgLPARA-VSTTFGCRVNVAICLqgtagpdpttvyVDMRALRHDRVRLVERGSPHSLplm 1355
Cdd:PRK09274 295 SAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFATRAATDNGAGICV--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1356 esGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWVSSPHNATGYYTvyGEEALHAdhfsARLSFGDTQtIWARTG 1427
Cdd:PRK09274 355 --GRPVDGVEVrIIAISDAPIPewddalrLATGEIGEIVVAGPMVTRSYYN--RPEATRL----AKIPDGQGD-VWHRMG 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 225735629 1428 YLGFLrrteltDASGgrhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECA 1485
Cdd:PRK09274 426 DLGYL------DAQG----RLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
335-811 |
3.86e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 47.99 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 335 LQRWGTTQPKSPCLTALDTTgkavytLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVALVFPNSDPvmFMVAFYGC 414
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRS------LTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 415 LLAELVPVPIEVPLTRKDagsqqVGFLLGSCGvflalttdacqkglpkaqtgevaafkgwpplSWLVIDgkhlakppkDw 494
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSG-------------------------------AKVLFD---------D- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 495 hplaqdtgtgTAYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETL--------TNVLDFKRDAGLWHGV 563
Cdd:cd17631 100 ----------LALLMY-TS--GTTgrpKGAMLTHRNLLWNAVNALAALDLGPDDVLlvvaplfhIGGLGVFTLPTLLRGG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 564 LTSVMNRMHVVSVpyalmkanpLSWIQ--KVCFykarAALVKSrdMHWSLLAQRGQRDVSLSSLRMLIVADGANPwsiss 641
Cdd:cd17631 167 TVVILRKFDPETV---------LDLIErhRVTS----FFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMP----- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 642 cDAFLNVFQSRGLRpevICPCASSPEALTVAIRRPPDlggppprkavlsmnglsygvirvDTEEKLSvltvqDVGQVMPG 721
Cdd:cd17631 227 -ERLLRALQARGVK---FVQGYGMTETSPGVTFLSPE-----------------------DHRRKLG-----SAGRPVFF 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 722 ANVCVVKLEGTPylCKTDEVGEICVSSSATGTAYYGLlgitknvfeavPVTTGGApIFDRPFtRTGLLGFIGPDNLVFIV 801
Cdd:cd17631 275 VEVRIVDPDGRE--VPPGEVGEIVVRGPHVMAGYWNR-----------PEATAAA-FRDGWF-HTGDLGRLDEDGYLYIV 339
|
490
....*....|
gi 225735629 802 GKLDGLMVTG 811
Cdd:cd17631 340 DRKKDMIISG 349
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1021-1500 |
7.16e-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: 47.05 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1021 RAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLTTQA 1100
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1101 vtrlLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE 1180
Cdd:cd05922 79 ----AADRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1181 LYPSRQIAICLdpycglgfalwclcsvysghqsvlvpPLELESNVSLWLSAVSQYKARVTFCSY----SVMEMCTKglga 1256
Cdd:cd05922 155 ITADDRALTVL--------------------------PLSYDYGLSVLNTHLLRGATLVLTNDGvlddAFWEDLRE---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1257 qTGVLRMKGVnlscvrtcmvvaeerPRIaltqsFSKL----FKDLGLPA-RAVSTTFGCRVNVAICLQGTAGPDpTTVYV 1331
Cdd:cd05922 205 -HGATGLAGV---------------PST-----YAMLtrlgFDPAKLPSlRYLTQAGGRLPQETIARLRELLPG-AQVYV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1332 ---------DMRALRHDRVRlvERgsPHSLplmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYytvyge 1402
Cdd:cd05922 263 mygqteatrRMTYLPPERIL--EK--PGSI-----GLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGY------ 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1403 ealhadhfsarlsfgdtqtiWARTGYLGFLRRTELTDASG--GRHDA---LYVVGSLDETLELRGMRYHPIDIETSvIRA 1477
Cdd:cd05922 327 --------------------WNDPPYRRKEGRGGGVLHTGdlARRDEdgfLFIVGRRDRMIKLFGNRISPTEIEAA-ARS 385
|
490 500
....*....|....*....|....*..
gi 225735629 1478 HRSIAECAVF----TWTNLLVVVVELD 1500
Cdd:cd05922 386 IGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
524-900 |
9.28e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.07 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 524 SHASLLAQCRALTQACGyseaetltnvLDFKRDAG-----LWHG-----VLTSVMNRMHVVSVPYALMKANPLSWIQKVC 593
Cdd:PRK05851 173 SPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 594 fyKARAALVKSRDMHWSLLAQRGQR--DVSLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPC---ASSPEA 668
Cdd:PRK05851 243 --DSRATLTAAPNFAYNLIGKYARRvsDVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSyglAESTCA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 669 LTVairrppdlggPPPrkavlsmnGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLcKTDEVGEICVSS 748
Cdd:PRK05851 319 VTV----------PVP--------GIGLRVDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIRG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 749 SATGTAYygllgitknvfeavpvtTGGAPIFDRPFTRTGLLGFIGPDNLVfIVGKLDGLMVTGVRRHNADDVVATALAVE 828
Cdd:PRK05851 380 ASMMSGY-----------------LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225735629 829 PmkfVYRGRIavfsVTVLHDD-----RIVLVAEQRpdASEEDSFQwmSRVLQAIDSihQVGVyclalVPANTLPKAP 900
Cdd:PRK05851 442 G---VREGAV----VAVGTGEgsarpGLVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDVVFVAP 500
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
346-805 |
1.09e-04 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 46.47 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 346 PCLTALDTTGKavyTLTYGKLWSRSLKLAYTLLnkltsknEPLLKPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVPIe 425
Cdd:cd05945 5 PDRPAVVEGGR---TLTYRELKERADALAAALA-------SLGLDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVPL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 426 vpltrkDAGSqqvgfllgscgvflalttdacqkglPKAQTGEVAAfkgwpplswlvidgkhLAKPpkdwhPLAQDTGTGT 505
Cdd:cd05945 72 ------DASS-------------------------PAERIREILD----------------AAKP-----ALLIADGDDN 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 506 AYIEYkTSkeGST---VGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLwHGVLTSVMNRMHVVSVPYAlMK 582
Cdd:cd05945 100 AYIIF-TS--GSTgrpKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPVPRD-AT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 583 ANPLSWIqkvcfykarAALVKSRDMHWsllaqrgqrdVSL-SSLRMLIVADGANPWSISSCDAFLnvFqsrglrpevicp 661
Cdd:cd05945 175 ADPKQLF---------RFLAEHGITVW----------VSTpSFAAMCLLSPTFTPESLPSLRHFL--F------------ 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 662 CAsspEALTVA-----IRRPPD-----LGGPPPrkavlSMNGLSYGVIrvdTEEKLSVLTVQDVGQVMPGANVCVVKLEG 731
Cdd:cd05945 222 CG---EVLPHKtaralQQRFPDariynTYGPTE-----ATVAVTYIEV---TPEVLDGYDRLPIGYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225735629 732 TPylCKTDEVGEICVSSSATGTAYYGLLGITKNVFeavpVTTGGAPIFdrpftRTGLLGFIGPDNLVFIVGKLD 805
Cdd:cd05945 291 RP--VPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAY-----RTGDLVRLEADGLLFYRGRLD 353
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
985-1508 |
1.10e-04 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 46.73 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 985 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCV 1064
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1065 PVTVRPP-HPQNLGTTLPTVKM---IVEVSKSACVLTTQAVTRLLRskeaaAAVDIRTWPTILDTDDIPkkkiasvFRPP 1140
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMtaaVIAVDAQVMDAIFQSGVRVLA-----LSDLVGLGEPESAGPLIE-------DPPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1141 SPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCEL-YPSRQIAICLDP-YCGLGF-ALWCLCSVYSGhqsVLVP 1217
Cdd:cd05923 148 EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrHGRHNVVLGLMPlYHVIGFfAVLVAALALDG---TYVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1218 PLELESNVSLWLSAvsqyKARVTfCSYSVMEMctkgLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIAL---TQSFSKLF 1294
Cdd:cd05923 225 VEEFDPADALKLIE----QERVT-SLFATPTH----LDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLervNQHLPGEK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1295 KDLGLPARAVSTTFgcrvnvaiclqgtaGPDPTTVYVdMRALRHDRVRLVERG--SPHSLPLMESGKIlpgvkvIIAHTe 1372
Cdd:cd05923 296 VNIYGTTEAMNSLY--------------MRDARTGTE-MRPGFFSEVRIVRIGgsPDEALANGEEGEL------IVAAA- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1373 tkgplGDSHLGEIWvsSPHNATgyytvygeealhadhfSARLSFGdtqtiWARTGylgflrRTELTDASGgrhdALYVVG 1452
Cdd:cd05923 354 -----ADAAFTGYL--NQPEAT----------------AKKLQDG-----WYRTG------DVGYVDPSG----DVRILG 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735629 1453 SLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV--VVVELDGLEQDALD 1508
Cdd:cd05923 396 RVDDMIISGGENIHPSEIE-RVLSRHPGVTEVVVIgvadeRWGQSVTacVVPREGTLSADELD 457
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
983-1072 |
1.11e-04 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 46.68 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 225735629 1063 CVPVTVRPPH 1072
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
359-537 |
1.25e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 46.50 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 359 YTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEV--PLTRKDAgsq 436
Cdd:cd12114 11 GTLTYGELAERARRVA----GALKAAG---VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 437 qvgfLLGSCGVFLALTTDACQKGLPKAqtgevaafkgwPPLSWLVIDGKHLAKPPKDWHPLAQDTgtgtAYIEYkTSkeG 516
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAV-----------FDVLILDLDALAAPAPPPPVDVAPDDL----AYVIF-TS--G 136
|
170 180
....*....|....*....|....
gi 225735629 517 ST---VGVTVSHASLLAQCRALTQ 537
Cdd:cd12114 137 STgtpKGVMISHRAALNTILDINR 160
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1017-1168 |
1.65e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 46.05 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1087
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1088 EVSKSA--CVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKkkiasVFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1165
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 225735629 1166 AAT 1168
Cdd:PRK07656 189 RQL 191
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
361-880 |
1.71e-04 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 45.93 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 361 LTYGKLWSRSLKLAYTLLNKLTSKnepllkpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqQVGF 440
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 441 LLGSCGVFLALTTDACQKglpkaqtgevaafkgwpplswlvidgkhlakppkdwhplaqdtgtgTAYIEYKTSKEGSTVG 520
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 521 VTVSHASLLAQcrALTQACGY--SEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVVSVPYALMKanplSWIQKVcfykAR 598
Cdd:cd05935 102 CMHTHFSAAAN--ALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMA----RWDRET----AL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 599 AALVKSRDMHWS--------LLAQRGQRDVSLSSLRMLivADGANPWSISSCDAFLNVFqsrGLRPEVIcpcasspEALT 670
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL--TGGGAPMPPAVAEKLLKLT---GLRFVEG-------YGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 671 VAIrrPPDLGGPPPRKAVLSMnglsyGVIRVDTEEKlsVLTVQDVGQVMPGanvcvvklegtpylcktdEVGEICVSSSA 750
Cdd:cd05935 235 ETM--SQTHTNPPLRPKLQCL-----GIP*FGVDAR--VIDIETGRELPPN------------------EVGEIVVRGPQ 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 751 TGTAYYGLLGITKNVFeavpVTTGGapifdRPFTRTGLLGFIGPDNLVFIVGKLDGLM-VTGVRRHNADdvVATALAVEP 829
Cdd:cd05935 288 IFKGYWNRPEETEESF----IEIKG-----RRFFRTGDLGYMDEEGYFFFVDRVKRMInVSGFKVWPAE--VEAKLYKHP 356
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 830 mkfvyrgriAVFSVTVLH--DDR--------IVLVAEQRPDASEEDSFQW----MS-----RVLQAIDSI 880
Cdd:cd05935 357 ---------AI*EVCVISvpDERvgeevkafIVLRPEYRGKVTEEDIIEWareqMAaykypREVEFVDEL 417
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
355-534 |
2.17e-04 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 45.82 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 355 GKAVY-----TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLT 429
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 430 rkdagSQQVGFLLGSCGVFLALTTDACqkgLPKAQTgevAAFKGWPPLSWLVIDGKHLAKPPKDWhpLAQDTGTGT---- 505
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGEL---APVLAA---ALTKSEHTLVVLIVSGGAGPEAGALL--LAELVAAEAeqlk 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 225735629 506 ---------AYIEYKTSKEGSTVGVTVSHASLLAQCRA 534
Cdd:cd05959 157 paathaddpAFWLYSSGSTGRPKGVVHLHADIYWTAEL 194
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
715-818 |
2.49e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 45.72 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 715 VGQVMPGANVCVVKLEGT-PYL--CKTDEVGEICVSssatgtayygllgiTKNVFEA-VPVTTGGAPIFDRPFTRTGLLG 790
Cdd:PRK07529 388 VGLRLPYQRVRVVILDDAgRYLrdCAVDEVGVLCIA--------------GPNVFSGyLEAAHNKGLWLEDGWLNTGDLG 453
|
90 100
....*....|....*....|....*...
gi 225735629 791 FIGPDNLVFIVGKLDGLMVTGvrRHNAD 818
Cdd:PRK07529 454 RIDADGYFWLTGRAKDLIIRG--GHNID 479
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1358-1486 |
2.60e-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: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1358 GKILPGVKVIIAHTETKGPLGDSHlGEIWVSSPHNATGYYTvygEEALHADHFSARlsfgdtqtiWARTGYLGFLRrtel 1437
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 225735629 1438 tdasggRHDALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1486
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
350-432 |
3.62e-04 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 45.00 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 350 ALDTTGKAVyTLTYGKLwsrsLKLAYTLLNKLTSKNeplLKPGDRVALVFPNSDPvmFMVAFYGCLLAELVPVPIEvPLT 429
Cdd:cd05926 5 ALVVPGSTP-ALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVAPLN-PAY 73
|
...
gi 225735629 430 RKD 432
Cdd:cd05926 74 KKA 76
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
319-535 |
3.71e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 45.14 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 319 EPLTAGVPRP------PSLLATL----QRWGTtqpkSPCLTALdttGKavyTLTYGKLWSRSLKLAYTLlnkltsKNEPL 388
Cdd:PRK05677 8 DKYPAGIAAEinpdeyPNIQAVLkqscQRFAD----KPAFSNL---GK---TLTYGELYKLSGAFAAWL------QQHTD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 389 LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV-------PIEVPLTRKDAGSQQVgfllgscgVFLALTTDACQKGLP 461
Cdd:PRK05677 72 LKPGDRIAVQLPNV--LQYPVAVFGAMRAGLIVVntnplytAREMEHQFNDSGAKAL--------VCLANMAHLAEKVLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 462 KAQ-----TGEVAAFKgwPPLSWLVIDG--KHLAKPPKDWH-------PLAQDTGTG------------TAYIEYKTSKE 515
Cdd:PRK05677 142 KTGvkhviVTEVADML--PPLKRLLINAvvKHVKKMVPAYHlpqavkfNDALAKGAGqpvteanpqaddVAVLQYTGGTT 219
|
250 260
....*....|....*....|...
gi 225735629 516 GSTVGVTVSHASLLA---QCRAL 535
Cdd:PRK05677 220 GVAKGAMLTHRNLVAnmlQCRAL 242
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
349-577 |
5.82e-04 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 44.20 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 349 TALDTTGKavyTLTYGKLWSRSLKLAYTLLNKLTSKnepllkPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI---- 424
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKDL------RGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLnpsy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 425 ---EVPLTRKDAGSQqvgfllgscgvflalttdacqkglpkaqtgevaafkgwpplswLVIDGkhlakppkdwhplaqdt 501
Cdd:cd05941 72 plaELEYVITDSEPS-------------------------------------------LVLDP----------------- 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225735629 502 gtgtAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVP 577
Cdd:cd05941 92 ----ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
359-422 |
1.08e-03 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 43.60 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225735629 359 YTLTYGKLWSRSLKLAYTLLNkltsknepL-LKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 422
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
983-1165 |
1.20e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 43.49 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1063 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLTTQAVTRLLRSKEAAAAV---DIRTWPTILDT 1125
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 225735629 1126 DDI------PKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1165
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1323-1507 |
2.42e-03 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 42.30 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1323 GPDPTTVYVDMRALrhdrvrlvERGSPHSLplmesGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGE 1402
Cdd:cd17653 240 GPTECTISSTMTEL--------LPGQPVTI-----GKPIPNSTCYIL-DADLQPVPEGVVGEICISGVQVARGY---LGN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1403 EALHADHFsARLSFGDTQTIWaRTGYLGFLRRteltdaSGGrhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIA 1482
Cdd:cd17653 303 PALTASKF-VPDPFWPGSRMY-RTGDYGRWTE------DGG----LEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
|
170 180
....*....|....*....|....*
gi 225735629 1483 ECAVFTWTNLLVVVVELDGLEQDAL 1507
Cdd:cd17653 371 QAAAIVVNGRLVAFVTPETVDVDGL 395
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1357-1486 |
2.94e-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: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1357 SGKILPGVKVIIAHtETKGPLGDshlGEIWVSSPHNATGYY--TVYGEEAlhadhfsarlsfgdTQTIWARTGYLGFLrr 1434
Cdd:cd05912 244 AGKPLFPVELKIED-DGQPPYEV---GEILLKGPNVTKGYLnrPDATEES--------------FENGWFKTGDIGYL-- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 225735629 1435 teltDASGgrhdALYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAV 1486
Cdd:cd05912 304 ----DEEG----FLYVLDRRSDLIISGGENIYPAEIEE-VLLSHPAIKEAGV 346
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
360-422 |
3.07e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.96 E-value: 3.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225735629 360 TLTYGKLWSRSLKLAYTLLNKLTskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 422
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNL--LQYPIALFGILRAGMIVV 102
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1017-1068 |
3.20e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 42.02 E-value: 3.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 225735629 1017 QLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1068
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
983-1166 |
3.74e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 41.67 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 983 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCVQlhkRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCG 1062
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1063 CVPVtvrpphPQNLGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAA----------AVDIRTWPTILDTDDIPKKK 1132
Cdd:PRK06155 96 AIAV------PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwlldAPASVSVPAGWSTAPLPPLD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 225735629 1133 IASVFRPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1166
Cdd:PRK06155 170 APAPAAAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
335-424 |
4.66e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 41.64 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 335 LQRWGTTQPKSPCLTALDTTGKAVyTLTYGKLWSRSLKLAytllNKLTSKNeplLKPGDRVALVFPNSdpVMFMVAFYGC 414
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA----NALRALG---VKKGDRVAIYLPNI--PEAVIAMLAC 84
|
90
....*....|
gi 225735629 415 LLAELVPVPI 424
Cdd:COG0365 85 ARIGAVHSPV 94
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
324-528 |
4.83e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 324 GVPRPPSLLATL---QRWGTtqPKSPCLTAldttgkAVYTLTYGKLWSRSLKLAYTLlnkltskNEPLLKPGDRVALVFP 400
Cdd:PRK10252 452 AVEIPETTLSALvaqQAAKT--PDAPALAD------ARYQFSYREMREQVVALANLL-------RERGVKPGDSVAVALP 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 401 NSdpVMFMVAFYGCLLAELVPVPIEV--PLTRkdagsqqVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPls 478
Cdd:PRK10252 517 RS--VFLTLALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA-- 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 225735629 479 wlvidgkhlakpPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASL 528
Cdd:PRK10252 586 ------------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
360-538 |
5.11e-03 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 41.18 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 360 TLTYGKLWSRSLKLAYTLLNKLTsknepllKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQQVG 439
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARGV-------GPGDLVALCARRS--AELVVALLAILKAGAAYVPLDP-----AYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 440 FLLGSCGVFLALTTDACQKGLPkaqtgeVAAFKGWPplswlvIDGKHLAKPPKDWHPLAQDTGTgTAYIEYkTSkeGST- 518
Cdd:cd17651 86 FMLADAGPVLVLTHPALAGELA------VELVAVTL------LDQPGAAAGADAEPDPALDADD-LAYVIY-TS--GSTg 149
|
170 180
....*....|....*....|..
gi 225735629 519 --VGVTVSHASLLAQCRALTQA 538
Cdd:cd17651 150 rpKGVVMPHRSLANLVAWQARA 171
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
360-424 |
5.38e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 41.04 E-value: 5.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225735629 360 TLTYGKLWSRSLKLAYTLLNKLtskneplLKPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI 424
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALG-------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPL 85
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
990-1100 |
6.54e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 40.83 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 990 RAHTTPDHPLFlLLNAKGTVTSTAtcvQLHKRAERVAAALMEKGrLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVr 1069
Cdd:PRK13391 6 HAQTTPDKPAV-IMASTGEVVTYR---ELDERSNRLAHLFRSLG-LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV- 79
|
90 100 110
....*....|....*....|....*....|.
gi 225735629 1070 pphpqNLGTTLPTVKMIVEVSKSACVLTTQA 1100
Cdd:PRK13391 80 -----NSHLTPAEAAYIVDDSGARALITSAA 105
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
715-829 |
6.71e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 40.54 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 715 VGQVMPGANVCVVKLEGTPYL---CKTDEVGEICVSSsatgtayygllgitKNVFEAVPVTTGGAPIFDRP-FTRTGLLG 790
Cdd:cd05944 176 VGLRLPYARVRIKVLDGVGRLlrdCAPDEVGEICVAG--------------PGVFGGYLYTEGNKNAFVADgWLNTGDLG 241
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 225735629 791 FIGPDNLVFIVGKLDGLMVTGvrRHNADDV-VATALAVEP 829
Cdd:cd05944 242 RLDADGYLFITGRAKDLIIRG--GHNIDPAlIEEALLRHP 279
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1357-1486 |
7.91e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 40.72 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1357 SGKILPGVKVIIAHTETKGPLGDShlGEIWVSSPHNATGYYtvYGEEALHAdhfsarlSFGDTqtiWARTGYLGFLrrte 1436
Cdd:PRK03640 309 AGKPLFPCELKIEKDGVVVPPFEE--GEIVVKGPNVTKGYL--NREDATRE-------TFQDG---WFKTGDIGYL---- 370
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 225735629 1437 ltDASGgrhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1486
Cdd:PRK03640 371 --DEEG----FLYVLDRRSDLIISGGENIYPAEIE-EVLLSHPGVAEAGV 413
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1358-1487 |
8.42e-03 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 40.35 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225735629 1358 GKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYY-----TvygEEALHADHfsarlsfgdtqtiWARTGYLGFL 1432
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 225735629 1433 rrteltDASGgrhdALYVVG-SLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF 1487
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVI 375
|
|
| |
