|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
993-1567 |
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: 726.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 993 LFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLG 1071
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1072 TTLPTVKMivEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVA-----SIFRPPSPDVLAYLDFSV 1146
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1147 STTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAV 1226
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1227 SQYKARVTFCSYSVMEMCTKGLGAQTGALRMKGVNLSCVRTCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRV 1306
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1307 NVAICLqpnrlgklaeQGTTGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHL 1386
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1387 GEIWVSSPHNATGYYTVYGEEALHADHF-SARLSFGDTQTIWARTGYLGFLRRTELTDASGERHDALYVVGSLDETLELR 1465
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFpSTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1466 GMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELD-GLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINS 1544
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 1958758113 1545 RGEKQRMHLRDGFLADQLDPIYV 1567
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
341-917 |
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: 644.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 341 CLTALDTSGKAICTLTYGKLWSRSLKLAYTLLSKLTskneplLNPGDRVALVFPnsDPVMFMVAFYGCLLAELVPVPIEV 420
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 421 PLtrkdaGSQHVGFLLGSCGVTLALTTDACQKGLPKA-----PTGEVATFKGWPPLAWLVIDGKHLTKPPKDWYPLAQDT 495
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 496 GSRTAYIEYKTSKDGSTVGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVISIPYALM 575
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 576 KVNPLSWIQKVCSYKARAALVKSRDMHWSL------LAQRGQRDVCLSSLRMLIVADGaNPWSISSCDAFLNVFQSRGLR 649
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 650 PEvicpcASSPEALTVAIRRPPDLG--GPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGASVCVVKVDGvP 727
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGtsGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPET-K 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 728 YLCKTDEIGEICVSSVATGTAYYGLLGITKNVFETVPVTADGVPVSDRPFTRTGLLGFIGPE----------NLVFVVGK 797
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 798 LDGLTVVGARRHNADDIVATALAVEPmkfvYRGRIAVFSVTVlhddRIVLVAEQRPdSSEEDSFQWMSRVLQAIDSIHQV 877
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSITG----LVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1958758113 878 GVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNV 917
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
983-1525 |
1.02e-65 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 233.28 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 983 WRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1062
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1063 RPPHPqnlGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWptiLDTDDIPKKKVASIFRPPS--PDVLA 1140
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR---LLVVDLLPDTSAADWPPPSpdPDDIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1141 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLVPPLELESN 1218
Cdd:cd05931 153 YLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1219 VSLWLSAVSQYKARVT----FcSYsvmEMCT-KGLGAQTGALrmkgvNLSCVRTCMVVAeERPRISLTQSFSKLFKDLGL 1293
Cdd:cd05931 231 PLRWLRLISRYRATISaapnF-AY---DLCVrRVRDEDLEGL-----DLSSWRVALNGA-EPVRPATLRRFAEAFAPFGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1294 PARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTTGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPG 1367
Cdd:cd05931 301 RPEAFRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1368 VKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEEALHADHFSARLSFGDtqTIWARTGYLGFLRRteltdasGE 1447
Cdd:cd05931 364 QEVRIVDPETGRELPDGEVGEIWVRGPSVASGY---WGRPEATAETFGALAATDE--GGWLRTGDLGFLHD-------GE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1448 rhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAE--CAVFTW----TNLLVVVVELDGLeQDALDLVALVTNV- 1520
Cdd:cd05931 432 ----LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIr 506
|
....*..
gi 1958758113 1521 --VLEEH 1525
Cdd:cd05931 507 aaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
332-908 |
1.23e-61 |
|
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: 221.34 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 332 WGTTQPKAPCLTALDTSGKAICTLTYGKLWSRSLKLAYTLLSKLTsknepllnPGDRVALVFPNSdpVMFMVAFYGCLLA 411
Cdd:cd05931 2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--------PGDRVLLLAPPG--LDFVAAFLGCLYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 412 ELVPVPIEVPLTRKDAgsQHVGFLLGSCGVTLALTTDACQKGLPKAptgeVATFKGWPPLAWLVIDGKHLTkPPKDWyPL 491
Cdd:cd05931 72 GAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADW-PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 492 AQDTGSRTAYIEYkTSkdGST---VGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVI 568
Cdd:cd05931 144 PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 569 SI-PYALMKvNPLSWIQKVCSYKAR--AAlvksRDMHWSLLAQRGQR----DVCLSSLRMLIVadGANPWSISSCDAFLN 641
Cdd:cd05931 221 LMsPAAFLR-RPLRWLRLISRYRATisAA----PNFAYDLCVRRVRDedleGLDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 642 VFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlgGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQdVGQVMPGASVCV 720
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 721 VKVDGVPyLCKTDEIGEICVS--SVATGtaYYGLLGITKNVFETVPVTADGvpvsdrPFTRTGLLGFIGpENLVFVVGKL 798
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVRgpSVASG--YWGRPEATAETFGALAATDEG------GWLRTGDLGFLH-DGELYITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 799 DGLTVVGARRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDSSEEDSFQWMSRVLQAIDSIHQVG 878
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVA 516
|
570 580 590
....*....|....*....|....*....|
gi 1958758113 879 VYCLALVPANTLPKAPLGGIHISETKQRFL 908
Cdd:cd05931 517 PADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
981-1465 |
1.01e-48 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 179.82 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 981 LQWRAHTTPDHPLFlllnAKGTVTSTaTCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1060
Cdd:pfam00501 1 LERQAARTPDKTAL----EVGEGRRL-TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1061 TVrpphpqNLGTTLPTVKMIVEVSKSACVLsTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPK-----------KKVAS 1129
Cdd:pfam00501 75 PL------NPRLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1130 IFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE----LYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1205
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1206 QSVLVPPLELESnVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAeERPRISLTQSFS 1285
Cdd:pfam00501 228 TVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNMLLE-------AGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1286 KLFkdlglpARAVSTTFGcrvnvaiclqpnrlgkLAEqgTTGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 1365
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDEDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1366 PGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYytvYGEEALHADHFsarlsfgdTQTIWARTGYLGFLrrteltDAS 1445
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 1958758113 1446 GErhdaLYVVGSLDETLELR 1465
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
977-1507 |
9.28e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.45 E-value: 9.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCIQLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1057 CVPVTVRPP------HPQNLGTtlptvkmIVEVSKSACVLSTQAITRLLKSKEAAAAVDVrtwPTILDTDDIPKKkVASI 1130
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPA-LAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1131 FRPPS--PDVLAYLDFSVSTTGILAGVKMSHA---ATSALCRSiKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGH 1205
Cdd:PRK05691 158 WQEPAlqPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1206 QSVLVPPLELESNVSLWLSAVSQYKARVT--------FCSYSVMEmctkglgaqtGALrmKGVNLSCVRTCMVVAEERPR 1277
Cdd:PRK05691 237 PCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSE----------SAL--ERLDLSRWRVAYSGSEPIRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1278 ISLtQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAEQ------GTTGPDPTTVYVDMRALRHDRVRLVErG 1351
Cdd:PRK05691 305 DSL-ERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-G 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1352 SPhslpLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTvyGEEAlHADHFSARlsfgDTQTiWARTG 1431
Cdd:PRK05691 367 SV----LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-SAKTFVEH----DGRT-WLRTG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758113 1432 YLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIETSVIRahrsiaECAVFTWTNLLVVVVELDGLE 1507
Cdd:PRK05691 435 DLGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER------EVEVVRKGRVAAFAVNHQGEE 493
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1139-1517 |
1.23e-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: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1139 LAYLDFSVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLVPPLEL 1215
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1216 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEERPrISLTQSFSKLFKDlglpa 1295
Cdd:cd04433 78 EA----ALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEAPGI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1296 rAVSTTFGcrvnvaiclqpnrlgkLAEqgtTGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVKVIIAHT 1375
Cdd:cd04433 141 -KLVNGYG----------------LTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1376 ETkGPLGDSHLGEIWVSSPHNATGYYTVygeealhadhfsARLSFGDTQTIWARTGYLGFLRrteltdasgeRHDALYVV 1455
Cdd:cd04433 185 DG-GELPPGEIGELVVRGPSVMKGYWNN------------PEATAAVDEDGWYRTGDLGRLD----------EDGYLYIV 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758113 1456 GSLDETLELRGMRYHPIDIETsVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1517
Cdd:cd04433 242 GRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHV 308
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
977-1517 |
1.45e-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: 121.07 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1057 CVPVTVrpphpqNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtddipkkkVASIFrppsp 1136
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALV------------------------------------TALIL----- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1137 dvlayldFSvS-TTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLEL 1215
Cdd:COG0318 107 -------YT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1216 ESnvslWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVRTCMVVAEerpriSLTQSFSKLFKDLglpa 1295
Cdd:COG0318 179 ER----VLELIERERVTVLFGVPTMLARLLR-------HPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER---- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1296 ravsttFGCRVNvaiclqpNRLGkLAEqgtTGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVKVIIAHT 1375
Cdd:COG0318 239 ------FGVRIV-------EGYG-LTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRIVDE 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1376 ETKgPLGDSHLGEIWVSSPHNATGYYTvyGEEALhadhfsaRLSFGDTqtiWARTGYLGFLrrteltDASGErhdaLYVV 1455
Cdd:COG0318 286 DGR-ELPPGEVGEIVVRGPNVMKGYWN--DPEAT-------AEAFRDG---WLRTGDLGRL------DEDGY----LYIV 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758113 1456 GSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLVVVVEL-DGLEQDALDLVALV 1517
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELRAFL 409
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
355-914 |
3.18e-27 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 118.95 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 355 LTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVALVfPNSDPvMFMVAFYGCLLAELVPVPIEVP--LTRKDAGSQHV 432
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALG-------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 433 GFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKGWPPLAWLvidgkhltkPPKDWYPLAQDTGSRTAYIEYkTSkdGST 512
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKA---------LPEADVALPRPTPDDIAYLQY-SS--GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 513 ---VGVTVPHSSLLAQCQALT----QVcgyTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVISIPYALMKVNPLSWIQK 585
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAIShdglKV---RPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 586 VCsyKARAALVKSRDMHWSLLAQRGQ----RDVCLSSLRmlIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPE 661
Cdd:PRK09192 266 IS--RNRGTISYSPPFGYELCARRVNskdlAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 662 AlTVAIRRPPDLGGppPRKAVLSMNGLSYGVIRVDTEEK-LSVLTVQDVGQVMPGASVCVVKVDG--VPYLcktdEIGEI 738
Cdd:PRK09192 342 A-TLAVSFSPLGSG--IVVEEVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGmpLPER----VVGHI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 739 CVS--SVATGtaYYGllgitkNVFETVPVTADGvpvsdrpFTRTGLLGFIGPENLVfVVGKLDGLTVVGARRHNADDIVA 816
Cdd:PRK09192 415 CVRgpSLMSG--YFR------DEESQDVLAADG-------WLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEW 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 817 TAlavEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPdSSEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKAPL 895
Cdd:PRK09192 479 IA---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSS 552
|
570
....*....|....*....
gi 1958758113 896 GGIHISETKQRFLEGTLHP 914
Cdd:PRK09192 553 GKLSRAKAKKRYLSGAFAS 571
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
325-814 |
4.50e-27 |
|
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: 116.45 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 325 LLAALQLWGTTQPKAPCLTALDTsgkaicTLTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVALVFPNSDPvmFMVA 404
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRALG-------VGPGDRVALLLPNSPE--FVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 405 FYGCLLAELVPVPIEVPLTRKdagsqHVGFLLGSCGVTLALTtdacqkglpkaptgevatfkgwpplawlvidgkhltkp 484
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVT-------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 485 pkdwyplaqdtgsrtAYIEYkTSkdGST---VGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHGVLTSV 561
Cdd:COG0318 103 ---------------ALILY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 562 MNRMHVISIPyalmKVNPLSWIQKVCSYKA-RAALVKSrdMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFL 640
Cdd:COG0318 165 LAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFE 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 641 NVFQSRglrpevICPC-ASSpEALTVAIRRPPDLGGPPPRKavlsmnglsygvirvdteeklsvltvqdVGQVMPGASVC 719
Cdd:COG0318 237 ERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVR 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 720 VVKVDGVPylCKTDEIGEICVS--SVATGtaYYGLLGITKNVFetvpvtADGvpvsdrpFTRTGLLGFIGPENLVFVVGK 797
Cdd:COG0318 282 IVDEDGRE--LPPGEVGEIVVRgpNVMKG--YWNDPEATAEAF------RDG-------WLRTGDLGRLDEDGYLYIVGR 344
|
490
....*....|....*..
gi 1958758113 798 LDGLTVVGARRHNADDI 814
Cdd:COG0318 345 KKDMIISGGENVYPAEV 361
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
324-908 |
2.92e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 115.81 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 324 TLLAALQLWGTTQPKAPCLT----ALDTSGKAIcTLTYGKLWSRSLKLAYTLLSkltsknepLLNPGDRVALVFPNSdpV 399
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyEQDPAGVAE-TLTWSQLYRRTLNVAEELRR--------HGSTGDRAVILAPQG--L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 400 MFMVAFYGCLLAELVPVPIEVPLTrkdaGSQH--VGFLLGSCGVTLALTTDACqkglpkapTGEVATF----KGWPPLAW 473
Cdd:PRK05850 71 EYIVAFLGALQAGLIAVPLSVPQG----GAHDerVSAVLRDTSPSVVLTTSAV--------VDDVTEYvapqPGQSAPPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 474 LVIDGKHLTKPPKdwYPLAQDTGSRTAYIEYkTSkdGST---VGVTVPHSSLLAQC-QALTQVCGYTEAE-----TLTNV 544
Cdd:PRK05850 139 IEVDLLDLDSPRG--SDARPRDLPSTAYLQY-TS--GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 545 LDFKRDAGLWHGVLTSVMNRMH-VISIPYALMKvNPLSWIQkvcsykaraaLVKSRDMHWSL-------LAQRGQRDVCL 616
Cdd:PRK05850 214 LPFYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQ----------LLASNPHAFSAapnfafeLAVRKTSDDDM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 617 SSL---RMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPpdlGGPPPrkavlsmnglsygV 692
Cdd:PRK05850 283 AGLdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP---GQPPE-------------S 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 693 IRVDTEeKLSVltvqdvGQVMP-----GASVCVVKVDGVPYL----------CKTDEIGEICV--SSVATGtaYYGLLGI 755
Cdd:PRK05850 347 VRFDYE-KLSA------GHAKRcetggGTPLVSYGSPRSPTVrivdpdtcieCPAGTVGEIWVhgDNVAAG--YWQKPEE 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 756 TKNVFETVPVT-ADGVPVSdrPFTRTGLLGFIGPENLvFVVGKLDGLTVVGARRHNADDIVATalavepMKFVYRGRIAV 834
Cdd:PRK05850 418 TERTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAA 488
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758113 835 FSVTVLHDDRIVLVAE-QRPDSSEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFL 908
Cdd:PRK05850 489 ISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKIRRAACVEQYR 567
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
314-910 |
1.53e-25 |
|
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: 113.15 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 314 PLSVGTSGPPTLLAALQLWGTTQPKAPClTALDTSGKAIcTLTYGKLWSRSLKLAyTLLSKLTskneplLNPGDRVALVF 393
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKGI-TYIDADGSEE-FQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 394 P-NSDpvmFMVAFYGCLLAELVPVPIEVPLTRKDAGSQ-----HVGFLLGSCGVtlaLTTDACQkglpkAPTGEVATFKG 467
Cdd:cd05906 72 DdNED---FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELV-----AEFAGLETLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 468 WPPLAWLVIDGKHLTKPPKDWYPLAQDtgsrTAYIEYKTSkdGST---VGVTVPHSSLLAQCQALTQVCGYTEAETLTNV 544
Cdd:cd05906 141 LPGIRVLSIEELLDTAADHDLPQSRPD----DLALLMLTS--GSTgfpKAVPLTHRNILARSAGKIQHNGLTPQDVFLNW 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 545 LDFKRDAGLWHGVLTSVMNRMHVISIPYALMKVNPLSWIQKVCSYKA------RAALVKSRDmhwsLLAQRGQRDVCLSS 618
Cdd:cd05906 215 VPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVtitwapNFAFALLND----LLEEIEDGTWDLSS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 619 LRMLIVADGANpwSISSCDAFLNVFQSRGLRPEVICPCASSPEalTVAirrppdlggppprkavlsmnglsyGVI--RVD 696
Cdd:cd05906 291 LRYLVNAGEAV--VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysRSF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 697 TEEKLS-VLTVQDVGQVMPGASVCVVKVDG--VPylckTDEIGEICVS--SVATGtaYYGLLGITKNVFetvpvTADGvp 771
Cdd:cd05906 343 PTYDHSqALEFVSLGRPIPGVSMRIVDDEGqlLP----EGEVGRLQVRgpVVTKG--YYNNPEANAEAF-----TEDG-- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 772 vsdrpFTRTGLLGFIGPENLVFVVGKLDGLTVVGArRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQ 851
Cdd:cd05906 410 -----WFRTGDLGFLDNGNLTITGRTKDTIIVNGV-NYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFF 480
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758113 852 RPDSSEEDSfqwMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKAPLGGIHISETKQRFLEG 910
Cdd:cd05906 481 VPEYDLQDA---LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1011-1481 |
5.28e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 109.06 E-value: 5.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGRLdaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP----HPQNLGTTL----PTVkmive 1082
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1083 vsksacVLSTQAITRLLKSKEAAAAVDVRtwPTILDTDDIPKKkVASIFRPPSPDV--LAYLDFSVSTTGILAGVKMSH- 1159
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDS-AGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1160 AATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHqSVLVPPLELESNVSLW---LSAVSQYKARVTFC 1236
Cdd:PRK12476 217 AVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1237 SYSVMEmctkgLGAQTGALRM-KGVNLSCVrtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpn 1315
Cdd:PRK12476 296 PNFAYE-----WAAQRGLPAEgDDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG------------ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1316 rlgkLAEQ----GTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEI 1389
Cdd:PRK12476 357 ----IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1390 WVSSPHNATGYY-----TvygEEALHAdHFSARLSFG------DTQTIWARTGYLGFLRRTEltdasgerhdaLYVVGSL 1458
Cdd:PRK12476 433 WLHGDNIGRGYWgrpeeT---ERTFGA-KLQSRLAEGshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRI 497
|
490 500
....*....|....*....|...
gi 1958758113 1459 DETLELRGMRYHPIDIETSVIRA 1481
Cdd:PRK12476 498 ADLIVIDGRNHYPQDIEATVAEA 520
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
385-912 |
3.31e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 106.74 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 385 PGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPltrKDAGsqHVGFL---LGSCGVTLALTTDACQKGLPKaptge 461
Cdd:PRK07769 78 PGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP---AEPG--HVGRLhavLDDCTPSAILTTTDSAEGVRK----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 462 vaTFKGWPP------LAwlvID------GKHLTKPPKDwyplaQDTgsrTAYIEYkTSkdGST---VGVTVPHsslLAQC 526
Cdd:PRK07769 146 --FFRARPAkerprvIA---VDavpdevGATWVPPEAN-----EDT---IAYLQY-TS--GSTripAGVQITH---LNLP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 527 QALTQVCGYTEAETLT---NVLDFKRDAGLWHGVLTSVMNRMHVISIPYALMKvNPLSWIQKVCSYKARAALVKSR--DM 601
Cdd:PRK07769 207 TNVLQVIDALEGQEGDrgvSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWIRELARKPGGTGGTFSAapNF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 602 HWSLLAQRG-----QRDVCLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAIRRPPDlgg 675
Cdd:PRK07769 286 AFEHAAARGlpkdgEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEAtLFVSTTPMDE--- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 676 pPPRKAVLSMNGLSYG-VIRVDTEEKLSVLTVQdVGQVmpGASVCVVKVDG-----VPylckTDEIGEICVSSVATGTAY 749
Cdd:PRK07769 361 -EPTVIYVDRDELNAGrFVEVPADAPNAVAQVS-AGKV--GVSEWAVIVDPetaseLP----DGQIGEIWLHGNNIGTGY 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 750 YGLLGITKNVFE------TVPVTADGVPvSDRPFTRTGLLGFIGPENLvFVVGKLDGLTVVGARRHNADDIVATALavEP 823
Cdd:PRK07769 433 WGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EA 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 824 MKFVYRGRIAVFSV-------TVLHD-------------DRIVLVAEQRPDSSEEDSFQWMSRVLQAIDSIHQVGVYCLA 883
Cdd:PRK07769 509 TKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVL 588
|
570 580
....*....|....*....|....*....
gi 1958758113 884 LVPANTLPKAPLGGIHISETKQRFLEGTL 912
Cdd:PRK07769 589 LVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
354-799 |
9.43e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 102.78 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 354 TLTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQHVG 433
Cdd:pfam00501 21 RLTYRELDERANRLAAGLRALG-------VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-----RLPAEELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 434 FLLGSCGVTLALTTD--------ACQKGLPKAPTGEVATFKGWPPLAWLVIDGKHLTKPPKDWYPLAQDTgsrTAYIEYk 505
Cdd:pfam00501 87 YILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDD---LAYIIY- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 506 TSkdGST---VGVTVPHSSLLAQCQALTQVC----GYTEAETLTNVLDFKRDAGLWHGVLTSVMN--RMHVISIPYALMK 576
Cdd:pfam00501 163 TS--GTTgkpKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAgaTVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 577 VNPLSWIQKvcsYKARAALVKSRDMHWsLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqsrglrPEVICPC 656
Cdd:pfam00501 241 AALLELIER---YKVTVLYGVPTLLNM-LLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF------GGALVNG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 657 ASSPEALTVAIRRPPDlggPPPRKAVLSmnglsygvirvdteeklsvltvqdVGQVMPGASVCVVKVDGVPYLcKTDEIG 736
Cdd:pfam00501 309 YGLTETTGVVTTPLPL---DEDLRSLGS------------------------VGRPLPGTEVKIVDDETGEPV-PPGEPG 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758113 737 EICVSSVATGTAYYGLLGITKNVFetvpvTADGvpvsdrpFTRTGLLGFIGPENLVFVVGKLD 799
Cdd:pfam00501 361 ELCVRGPGVMKGYLNDPELTAEAF-----DEDG-------WYRTGDLGRRDEDGYLEIVGRKK 411
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
977-1521 |
1.09e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 104.64 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLN---AKGTVTSTATCIQLHKRAERVAAALMEKGrlDAGDHVALVYPPGVDLIAAFYGCL 1053
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1054 YCGCVPVTVRPPHPqnlGTTLPTVKMIVEVSKSACVLSTqaitrllkskeAAAAVDVRTW---------PTI--LDTDDI 1122
Cdd:PRK05850 81 QAGLIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVieVDLLDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1123 PKKKVASIFRPPSPDVlAYLDFSVSTTGILAGVKMSHAATSALCRSI------KLQCELYPSRQIAICLDPYCGLGFALW 1196
Cdd:PRK05850 147 DSPRGSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgDTGGVPPPDTTVVSWLPFYHDMGLVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1197 CLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaQTGALRMKGVNLSCVRTcMVVAEERP 1276
Cdd:PRK05850 226 VCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVR----KTSDDDMAGLDLGGVLG-IISGSERV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1277 RISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgkLAE------QGTTGPDPTTVYVDMRALRHDRVR---- 1346
Cdd:PRK05850 301 HPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEKLSAGHAKrcet 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1347 -----LVERGSPHSlplmesgkilPGVKVIIAHTETKGPLGDshLGEIWVSSPHNATGYYTVYGEEalhADHFSARL--- 1418
Cdd:PRK05850 365 gggtpLVSYGSPRS----------PTVRIVDPDTCIECPAGT--VGEIWVHGDNVAAGYWQKPEET---ERTFGATLvdp 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1419 SFGDTQTIWARTGYLGFLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV--IRAHRsiaeCAVFT---- 1492
Cdd:PRK05850 430 SPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIqeITGGR----VAAISvpdd 494
|
570 580 590
....*....|....*....|....*....|..
gi 1958758113 1493 WTNLLVVVVEL---DGLEQDALDLVALVTNVV 1521
Cdd:PRK05850 495 GTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
10-121 |
2.43e-22 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 93.25 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 10 AAPLPAEVLESLAELELELSEGDITQKGYEKKRAKLLARYipliqgvdpcLQTESRVPGPLLTAPTAKPQKpRANSRDER 89
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKF----------LLHPETPTKLSAEAQNQLASL-ETKLRDEE 70
|
90 100 110
....*....|....*....|....*....|....
gi 1958758113 90 FRSDVHTEAVQAALAKYKERKM--PMPSKRRSAL 121
Cdd:pfam06464 71 LSEEVYLEKVKALLAKELERENglNAPTKEQSGL 104
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
356-910 |
2.46e-21 |
|
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: 99.48 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 356 TYGKLWSRSLKLAYTLlskltskNEPLLNPGDRValVFPNSDPVMFMVAFYGCLLAELVPVPIEVpltrkDAGSQHVgfl 435
Cdd:cd05908 17 SYRHLREEALGYLGAL-------QELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVPVSI-----GSNEEHK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 436 lgscgvtlalttdacqkglpkaptgeVATFKGWPPLA--WLVIDGKHLTKPPkdwyplaqdtgSRTAYIEYKTSKDGSTV 513
Cdd:cd05908 80 --------------------------LKLNKVWNTLKnpYLITEEEVLCELA-----------DELAFIQFSSGSTGDPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 514 GVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVISIPYALMKVNPLSWIQKVCSYKAra 593
Cdd:cd05908 123 GVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKA-- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 594 ALVKSRDMHWSLLAQRGQ----RDVCLSSLRMLIvaDGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEAlTVAIRR 669
Cdd:cd05908 201 TIVSSPNFGYKYFLKTLKpekaNDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 670 PPdlGGPPPRKAVLSMNGLSYG--VIRVDTEEKlSVLTVQDVGQVMPGASVCVVkvDGVPYLCKTDEIGEICVSSVATGT 747
Cdd:cd05908 278 PK--AQSPFKTITLGRRHVTHGepEPEVDKKDS-ECLTFVEVGKPIDETDIRIC--DEDNKILPDGYIGHIQIRGKNVTP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 748 AYYGLLGITKNVFetvpvTADGvpvsdrpFTRTGLLGFIGPENLVfVVGKLDGLTVVGARRHNADDIVATALAVEPmkfV 827
Cdd:cd05908 353 GYYNNPEATAKVF-----TDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIAEELEG---V 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 828 YRGRIAVFSV--TVLHDDRIVLVAEQRpdSSEEDSFQWMSRVLQAID-----SIHQVgvyclalVPANTLPKAPLGGIHI 900
Cdd:cd05908 417 ELGRVVACGVnnSNTRNEEIFCFIEHR--KSEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSGKVKR 487
|
570
....*....|
gi 1958758113 901 SETKQRFLEG 910
Cdd:cd05908 488 YELAQRYQSG 497
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1011-1490 |
4.55e-20 |
|
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: 94.64 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGRLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgttlPTVKMIVEVSKSACVL 1090
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STQAiTRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVASifrPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIk 1170
Cdd:TIGR01733 78 TDSA-LASRLAGLVLPVILLDPLELAALDDAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1171 lqCELYPSRQIAICLDpYCGLGF------ALWCLcsvYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMC 1244
Cdd:TIGR01733 153 --ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1245 TKGLGAQTGALRMkgvnlscvrtcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNvaiclqpnrlgklaeqg 1324
Cdd:TIGR01733 227 AAALPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN----------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1325 TTGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVKVIIAHTETKgPLGDSHLGEIWVSSPHNATGYytvY 1404
Cdd:TIGR01733 267 LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---L 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1405 GEEALHADHFSARLSFGDTQTIWARTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRS 1484
Cdd:TIGR01733 335 NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPG 403
|
....*.
gi 1958758113 1485 IAECAV 1490
Cdd:TIGR01733 404 VREAVV 409
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1011-1500 |
5.34e-20 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 95.81 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHP-QNLGTTLPTVKMIVEVSKSACV 1089
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1090 LSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSi 1169
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDL---PQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1170 KLQCELYPSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSvmeMCTK 1246
Cdd:cd05906 199 KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1247 gLGAQTGALRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGCRVNVAIClqpnrlgklaeqgtt 1326
Cdd:cd05906 274 -LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV--------------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1327 gpdptTVYVDMRALRHdrvrlvergsPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGE 1406
Cdd:cd05906 337 -----IYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIV-DDEGQLLPEGEVGRLQVRGPVVTKGY---YNN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1407 EALHADHFsarlsfgdTQTIWARTGYLGFLrrteltdasgeRHDALYVVGSLDETLELRGMRYHPIDIETSV----IRAH 1482
Cdd:cd05906 398 PEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEP 458
|
490 500
....*....|....*....|.
gi 1958758113 1483 RSIAECAVF---TWTNLLVVV 1500
Cdd:cd05906 459 SFTAAFAVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
346-914 |
7.08e-20 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 95.96 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 346 DTSGKAIcTLTYGKLWSRslklaytlLSKLTSKNEPLLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVP---- 421
Cdd:PRK12476 61 SAAGCAV-ELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLFAPelpg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 422 -LTRKDAgsqhvgfLLGSCGVTLALTTDACQ-------KGLPKAPTGEVATFKGWPPLAwlvidGKHLTKPPKDwyplaq 493
Cdd:PRK12476 130 hAERLDT-------ALRDAEPTVVLTTTAAAeavegflRNLPRLRRPRVIAIDAIPDSA-----GESFVPVELD------ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 494 dtGSRTAYIEYkTSkdGST---VGVTVPHSSllaqcqaltqVCgyteaetlTNVLDFKRDAGLW----HGV--------- 557
Cdd:PRK12476 192 --TDDVSHLQY-TS--GSTrppVGVEITHRA----------VG--------TNLVQMILSIDLLdrntHGVswlplyhdm 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 558 -LTSVM------NRMHVISiPYALMKvNPLSWIQKVcSYKARAALV--KSRDMHWSLLAQRG----QRDVCLSSLRMLIv 624
Cdd:PRK12476 249 gLSMIGfpavygGHSTLMS-PTAFVR-RPQRWIKAL-SEGSRTGRVvtAAPNFAYEWAAQRGlpaeGDDIDLSNVVLII- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 625 adGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDlggPPPRKAVLSMNGLSYG-VIRVDTEEKLSV 703
Cdd:PRK12476 325 --GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPD---AEPSVVYLDREQLGAGrAVRVAADAPNAV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 704 LTVQdVGQVMPGASVCVVKVDGVPYLcKTDEIGEICVSSVATGTAYYGLLGITKNVFETVPVT-------ADGVPVSDRP 776
Cdd:PRK12476 400 AHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKLQSrlaegshADGAADDGTW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 777 FtRTGLLGF-IGPEnlVFVVGKLDGLTVVGARRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDDRIVLVAEQRPDS 855
Cdd:PRK12476 478 L-RTGDLGVyLDGE--LYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGT 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758113 856 SEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHP 914
Cdd:PRK12476 553 SRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1011-1485 |
6.30e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 89.79 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGRldAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV----RPPHPQNLGTTL----PTVkmIVE 1082
Cdd:PRK07769 60 QFGARNRAVGARLQQVTK--PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddctPSA--ILT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1083 VSKSAcvlstQAITRLLKSKEAAAAvdvrtwPTILDTDDIPKKkVASIFRPPSP--DVLAYLDFSVSTTGILAGVKMSH- 1159
Cdd:PRK07769 136 TTDSA-----EGVRKFFRARPAKER------PRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1160 -AATSAL--CRSIKLQcelYPSRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLVPPLELESNVSLW---LSAVSQYKARV 1233
Cdd:PRK07769 204 nLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1234 tfcsYSVMEMCTKGLGAQTGaLRMKG---VNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvai 1310
Cdd:PRK07769 279 ----FSAAPNFAFEHAAARG-LPKDGeppLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1311 clqpnrlgkLAEQ----GTTGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDS 1384
Cdd:PRK07769 346 ---------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1385 HLGEIWVSSPHNATGYytvYGEEALHADHFSARLSFGDTQT---------IWARTGYLGflrrtelTDASGErhdaLYVV 1455
Cdd:PRK07769 417 QIGEIWLHGNNIGTGY---WGKPEETAATFQNILKSRLSEShaegapddaLWVRTGDYG-------VYFDGE----LYIT 482
|
490 500 510
....*....|....*....|....*....|
gi 1958758113 1456 GSLDETLELRGMRYHPIDIETSVIRAHRSI 1485
Cdd:PRK07769 483 GRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
322-942 |
1.14e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.23 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 322 PPTLLAALQLWGTTQPKAPCLTALDTSGKAICTLTYGKLWSRslklAYTLLSKLTSKNEPllnpGDRVALVFPnSDPvMF 401
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLR----ARTIAAALQARASF----GDRAVLLFP-SGP-DY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 402 MVAFYGCLLAELVPVPIEVPLTRKDAGSQHVGFLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkGWPPlaWLVIDGkhL 481
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPE--LLCVDT--L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 482 TKPPKDWYPLAQDTGSRTAYIEYkTSkdGSTV---GVTVPHSSLLAQCQALTQVCG--YTEAETLTNVLDFKRDAGLWHG 556
Cdd:PRK05691 151 DPALAEAWQEPALQPDDIAFLQY-TS--GSTAlpkGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 557 VLTSVMNrmhviSIPYALMKVN-----PLSWIQKVCSYkaRAALVKSRDMHWSLLAQRgQRDVCLSSL---RMLIVADGA 628
Cdd:PRK05691 228 LLQPIFS-----GVPCVLMSPAyflerPLRWLEAISEY--GGTISGGPDFAYRLCSER-VSESALERLdlsRWRVAYSGS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 629 NPWSISSCDAFLNVFQSRGLRPEVICPCASSPEA-LTVAirrppdlGGPPprkavlsmnGLSYGVIRVDTEEKLSVLTVQ 707
Cdd:PRK05691 300 EPIRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS-------GGRR---------GQGIPALELDAEALARNRAEP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 708 DVGQVM-------PGASVCVVKVDGVPYLcKTDEIGEICVS--SVATGtaYYGLLGITKNVFetvpVTADGvpvsdRPFT 778
Cdd:PRK05691 364 GTGSVLmscgrsqPGHAVLIVDPQSLEVL-GDNRVGEIWASgpSIAHG--YWRNPEASAKTF----VEHDG-----RTWL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 779 RTGLLGFIgPENLVFVVGKLDGLTVVgaRRHN--ADDIVATalAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAE-----Q 851
Cdd:PRK05691 432 RTGDLGFL-RDGELFVTGRLKDMLIV--RGHNlyPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 852 RPDSSEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLhpcnvlmcphTCVTNLPKP 931
Cdd:PRK05691 507 KILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPAL 572
|
650
....*....|.
gi 1958758113 932 RQKQPEVGPAS 942
Cdd:PRK05691 573 QAVEAAQTAAS 583
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
967-1478 |
1.16e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.44 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 967 DSDQARK---FLFLADVLQWRAHTTPDHPLFlllNAKGTVTSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGV 1043
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1044 DLIAAFYGCLYCGCVPVTVrpPHPQNLG---TTLPTVKMIVEVSKSACVLSTQAITRLLksKEAAAAVDVRTWPTILDTD 1120
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFGgreSYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAWFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1121 DIPKKKVAsiFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQ-CELYPSRQIAICLDPYCGLGFaLWCLC 1199
Cdd:PRK09192 162 ALPEADVA--LPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1200 SVYSGHQSV-LVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGAlrmkGVNLSCVRTCMVVAEE-RPR 1277
Cdd:PRK09192 239 TPVATQLSVdYLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLA----ELDLSCWRVAGIGADMiRPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1278 IslTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPNRLGKLAEQgttgpdpttvyVDMRALRHDR--VRLVERGSPH 1354
Cdd:PRK09192 315 V--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPLGSGIVVEE-----------VDRDRLEYQGkaVAPGAETRRV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1355 SlPLMESGKILPGVKVIIaHTETKGPLGDSHLGEIWVSSPHNATGYYtvygeealhADHFSARLSFGDTqtiWARTGYLG 1434
Cdd:PRK09192 382 R-TFVNCGKALPGHEIEI-RNEAGMPLPERVVGHICVRGPSLMSGYF---------RDEESQDVLAADG---WLDTGDLG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1958758113 1435 FLrrteltdASGErhdaLYVVGSLDETLELRGMRYHPIDIETSV 1478
Cdd:PRK09192 448 YL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIA 480
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1008-1491 |
1.30e-16 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 84.96 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1008 TCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCvpvtvrPPHPQNLGTTLPTVKMIVEVSKSA 1087
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1088 CVLSTQAITRLLKSKEAAAAVDVRTW------PTILDTDDI--PKKKVASIFRPP----SPDVLAYLDFSVSTTGILAGV 1155
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpDGVLSIEDLlsPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1156 KMSH---AATSALCRSIKLQCELYPSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLVPPLELEsnvsLWLSAVSQYKA 1231
Cdd:cd05911 165 CLSHrnlIANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1232 RVTF------CSYSVMEMCTKGlgaqtgalrmkgvNLSCVRTCMVVAeerprisltqsfSKLFKDLGlparavsTTFGCR 1305
Cdd:cd05911 238 TFLYlvppiaAALAKSPLLDKY-------------DLSSLRVILSGG------------APLSKELQ-------ELLAKR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1306 VNVAICLQpnrlgklaEQGTTGPDPTTVYvdmralrhdrvrlvergSPHSLPLMES-GKILPGVKVIIAHTETKGPLGDS 1384
Cdd:cd05911 286 FPNATIKQ--------GYGMTETGGILTV-----------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDSLGPN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1385 HLGEIWVSSPHNATGYYTvyGEEALHADHfsarlsfgdTQTIWARTGYLGFLRRTELtdasgerhdaLYVVGSLDETLEL 1464
Cdd:cd05911 341 EPGEICVRGPQVMKGYYN--NPEATKETF---------DEDGWLHTGDIGYFDEDGY----------LYIVDRKKELIKY 399
|
490 500
....*....|....*....|....*..
gi 1958758113 1465 RGMRYHPIDIEtSVIRAHRSIAECAVF 1491
Cdd:cd05911 400 KGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1004-1493 |
3.95e-14 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 77.02 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1004 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGTTLPTVKMIVEV 1083
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1084 SKSACVLSTQAITRLLKSKEAAAAVDVRT----------WPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILA 1153
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1154 GVKMSHAatsalcrSIKLQCELYPSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLVPPLELESNVslwL 1223
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAV---F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1224 SAVSQYKARVTFCS---YSVMemctkglgaqTGALRMKGVNLSCVRTCMVVAEERPRiSLTQSFSKLfkdlglparavst 1300
Cdd:cd05959 248 KRIRRYRPTVFFGVptlYAAM----------LAAPNLPSRDLSSLRLCVSAGEALPA-EVGERWKAR------------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1301 tFGCRVNVAIclqpnrlgklaeqGTTgpDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVKVIIAHtETKGP 1380
Cdd:cd05959 304 -FGLDILDGI-------------GST--EMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1381 LGDSHLGEIWVSSPHNATGYYTVYGEealhadhfsARLSFgdtQTIWARTGYlGFLRrteltDASGerhdALYVVGSLDE 1460
Cdd:cd05959 353 VADGEPGELYVRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADD 410
|
490 500 510
....*....|....*....|....*....|...
gi 1958758113 1461 TLELRGMRYHPIDIEtSVIRAHRSIAECAVFTW 1493
Cdd:cd05959 411 MLKVSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1011-1513 |
5.02e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 76.41 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLgttlptVKMIVEVSKSACVL 1090
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1170
Cdd:cd05930 90 TD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1171 lqcELYPSR------QIAicldpycGLGF--ALWCL-CSVYSGHQSVLVPPlELESNVSLWLSAVSQYKARVTFCSYSVM 1241
Cdd:cd05930 127 ---EAYPLTpgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1242 EMCtkglgAQTGALRMkgvnLSCVRTcMVVAEERPRISLTQSFSKLFKDLGLparavsttfgcrVNVaiclqpnrlgkla 1321
Cdd:cd05930 196 RLL-----LQELELAA----LPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1322 eqgtTGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYy 1401
Cdd:cd05930 241 ----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGY- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1402 tvYGEEALHADHFSArLSFGDTQTIWaRTGYLGflRRteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETsVIRA 1481
Cdd:cd05930 306 --LNRPELTAERFVP-NPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA-ALLA 370
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958758113 1482 HRSIAECAVFTWTN------LLVVVVELDGLEQDALDL 1513
Cdd:cd05930 371 HPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
977-1211 |
6.47e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 69.90 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLNAKgtvtstATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1057 CVPVTVRPphpqnlgttlptvkmivevsksacVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKKKVAsifrpPSP 1136
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-----LTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1137 DVLAYLDFSVSTTGILAGVKMSHAATSAlcrsIKLQC-----ELYPSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLV 1210
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 1958758113 1211 P 1211
Cdd:cd05936 201 P 201
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1011-1510 |
6.51e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 70.18 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGRLDAgdhVALVYPPGVDLIAAFYGCLYCG----CVPVTVRPPHPQNLGTTLPTVKMIVEVSKs 1086
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1087 acVLSTQAITRLLKSKEAAAAV-DVRTWPtildtddipKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1165
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1166 CRSIKLQCELYPSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFC---SYSVM 1241
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApnfAYNLI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1242 emctkglgaqtG--ALRMKGVNLSCVRTCmVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFGcrvnvaiclqpnrlgk 1319
Cdd:PRK05851 260 -----------GkyARRVSDVDLGALRVA-LNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG---------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1320 LAEQ--GTTGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNA 1397
Cdd:PRK05851 312 LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1398 TGYytvYGEEALHADHfsarlsfgdtqtiWARTGYLGFlrrteLTDasgerhDALYVVGSLDETLELRGMRYHPIDIET- 1476
Cdd:PRK05851 384 SGY---LGQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERv 436
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958758113 1477 -SVIRAHRSIAECAVFTWTNL----LVVVVELDGLEQDA 1510
Cdd:PRK05851 437 aAQVRGVREGAVVAVGTGEGSarpgLVIAAEFRGPDEAG 475
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
985-1167 |
7.85e-12 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 69.68 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 985 AHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGRLDaGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1064
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARGVGP-GDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1065 PHPQnlgttlPTVKMIVEVSKSACVLSTQAitrllkskEAAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDF 1144
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPA--------LAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 1958758113 1145 SVSTTGILAGVKMSHAATSALCR 1167
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
383-892 |
9.21e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 69.39 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 383 LNPGDRVALVFPNSDP---VMFMVAFYGCLLAeLVPVPIEvpltrKDAGSQHVGFLLGSCGVTLALT----TDACQKGLP 455
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLG-LVFVPLN-----PTLKESVLRYLVADAGGRIVLAdagaADRLRDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 456 KAPTgevatfkgwpPLAWLVIDGKHLTKPPKDWYPLAQDTgsrTAYIEYKTSKDGSTVGVTVPHSSLLAQCQALTQVCGY 535
Cdd:cd05922 89 ASPD----------PGTVLDADGIRAARASAPAHEVSHED---LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 536 TEAETLTNVLDFKRDAGLwhGVLTSVMNR--MHVISIPYALmkvnPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQR 612
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgaTLVLTNDGVL----DDAFWEDLREHGATGlAGVPS---TYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 613 DVCLSSLRMLIVADGANPwsisscDAFLNVFQS--RGLRPEVIcpcasspEALTVAIRR----PPDLGGPPPrkavlsmn 686
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLP------QETIARLREllPGAQVYVM-------YGQTEATRRmtylPPERILEKP-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 687 glsygvirvdteeklsvltvQDVGQVMPGASVCVVKVDGVPylCKTDEIGEIcVSSVATGTAYYgllgitknvFETVPVT 766
Cdd:cd05922 286 --------------------GSIGLAIPGGEFEILDDDGTP--TPPGEPGEI-VHRGPNVMKGY---------WNDPPYR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 767 ADGVPVSDRpfTRTGLLGFIGPENLVFVVGKLDGLTVVGARRHNADDIVATALAVEPMkfvyrGRIAVFSVTVLHDDRIV 846
Cdd:cd05922 334 RKEGRGGGV--LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGLPDPLGEKLA 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958758113 847 LVAEqrpdSSEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPK 892
Cdd:cd05922 407 LFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPL 445
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
498-805 |
8.90e-11 |
|
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: 65.38 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 498 RTAYIEYkTSkdGST---VGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVISIPyal 574
Cdd:cd04433 1 DPALILY-TS--GTTgkpKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 575 mKVNPLSWIQKVCSYKARAALVkSRDMHWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAFLNVFqsrglRPEVIC 654
Cdd:cd04433 74 -KFDPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP-----GIKLVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 655 PCASSPEALTVAIRRPPDLGGPPPrkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCVVKVDGVPylCKTDE 734
Cdd:cd04433 145 GYGLTETGGTVATGPPDDDARKPG-----------------------------SVGRPVPGVEVRIVDPDGGE--LPPGE 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758113 735 IGEICVSSvatgtaYYGLLGITKNVFETVPVTADGvpvsdrpFTRTGLLGFIGPENLVFVVGKLDGLTVVG 805
Cdd:cd04433 194 IGELVVRG------PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSG 251
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1011-1475 |
1.59e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 65.59 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVtvrpphPQNLGttlptvkmivevSKSACVL 1090
Cdd:cd05908 20 HLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV------PVSIG------------SNEEHKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STQAITRLLKSkeaaaavdvrtwPTILDTDDIPKKkvasifrppSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1170
Cdd:cd05908 81 KLNKVWNTLKN------------PYLITEEEVLCE---------LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1171 LQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGA 1250
Cdd:cd05908 140 NSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1251 QTGAlrmkGVNLSCVRtcMVVAEERPRIS-LTQSFSKLFKDLGLPARAVSTTFG-CRVNVAICLQPnrlgklaeqgtTGP 1328
Cdd:cd05908 220 EKAN----DWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEASVGASLPK-----------AQS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1329 DPTTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGpLGDSHLGEIWVSSPHNATGYYTvyGEE 1407
Cdd:cd05908 283 PFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGYYN--NPE 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758113 1408 AlhadhfSARLSFGDTqtiWARTGYLGFLRRTEltdasgerhdaLYVVGSLDETLELRGMRYHPIDIE 1475
Cdd:cd05908 360 A------TAKVFTDDG---WLKTGDLGFIRNGR-----------LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
985-1516 |
2.58e-10 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 64.58 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 985 AHTTPDHPLFLLLNAkgtvtsTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP 1064
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1065 PHPqnlgttlptvkmivevsksacvlstqaITRLLKSKEAAAavdvrtwPTILDTDdipkkkvasifrppsPDVLAYLDF 1144
Cdd:cd05945 74 SSP---------------------------AERIREILDAAK-------PALLIAD---------------GDDNAYIIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1145 SVSTTGILAGVKMSHAATSALCRSIkLQCELYPSRQIAICLDPY---CGLgFALWclCSVYSGHQSVLVPPLELEsNVSL 1221
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPFsfdLSV-MDLY--PALASGATLVPVPRDATA-DPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1222 WLSAVSQYKARVTFCSYSVMEMCTkGLGAQTGAlrmkgvNLSCVRTCMVVAEERPrISLTQSFSKLFkdlglPARAVSTT 1301
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQQRF-----PDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1302 FgcrvnvaiclqpnrlgklaeqgttGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVKVIIAhTETKGPL 1381
Cdd:cd05945 247 Y------------------------GPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVIL-DEDGRPV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1382 GDSHLGEIWVSSPHNATGYytvYGEEALHADHFsarlsFGDTQTIWARTGYLGFLrrteltDASGErhdaLYVVGSLDET 1461
Cdd:cd05945 294 PPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVRL------EADGL----LFYRGRLDFQ 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1462 LELRGMRYHPIDIETSViRAHRSIAECAVFTWTNL-----LVVVVELDGlEQDALDLVAL 1516
Cdd:cd05945 356 VKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKP-GAEAGLTKAI 413
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
356-799 |
3.19e-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: 64.21 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 356 TYGKLWSRSLKLAYTLLSKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEV--PLTRKDagsqhvg 433
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVG------PGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 434 FLLGSCGVTLALTTDACQKGLPKAPTGEVAtfkgwPPLAWLVIDGKHLTKPPKDWYPLAQDtgsrTAYIEYkTSkdGST- 512
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSGPDD----LAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 513 --VGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHgVLTSVMNRMHVISIPYALMKVNPLSWiqkvcsyk 590
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 591 arAALVKSRDM-HWSLLAqrgqrdvclSSLRMLIVADganpwsisscdaflnVFQSRGLRpeVICPCAsspEALTVA-IR 668
Cdd:TIGR01733 205 --AALIAEHPVtVLNLTP---------SLLALLAAAL---------------PPALASLR--LVILGG---EALTPAlVD 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 669 RppdLGGPPPRKAVLSMnglsYG---------VIRVDtEEKLSVLTVQDVGQVMPGASVCVVKVDGVPylCKTDEIGEIC 739
Cdd:TIGR01733 254 R---WRARGPGARLINL----YGptettvwstATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRP--VPVGVVGELY 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958758113 740 VS--SVATGtaYYGLLGITKNVFetvpVTADGVPVSDRPFTRTGLLGFIGPE-NLVFvVGKLD 799
Cdd:TIGR01733 324 IGgpGVARG--YLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPDgNLEF-LGRID 379
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1011-1516 |
3.23e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 64.23 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGRlDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1090
Cdd:cd12116 17 ELDERANRLAARLRARGV-GPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STQAItrllkskEAAAAVDVRTWPTILDTDDIPkkkVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1170
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1171 LQCELYPSRQIaICLDPYCglgF---ALWCLCSVYSGHQSVLVPPlelesnvslwlsavsqykarvtfcsysvmemctkg 1247
Cdd:cd12116 160 ERLGLGPGDRL-LAVTTYA---FdisLLELLLPLLAGARVVIAPR----------------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1248 lGAQTGALRMKGvnlscvrtcmvvAEERPRISLTQ---SFSKLFKDLGLPARAVSTtfgcrvnvAIC----LQPNRLGKL 1320
Cdd:cd12116 201 -ETQRDPEALAR------------LIEAHSITVMQatpATWRMLLDAGWQGRAGLT--------ALCggeaLPPDLAARL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1321 AEQGTT-----GPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL--------G 1387
Cdd:cd12116 260 LSRVGSlwnlyGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVL---------DAALrpvppgvpG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1388 EIWVSSPHNATGYytvYGEEALHADHFSArLSFGDTQTIWARTGYLgfLRRteLTDASgerhdaLYVVGSLDETLELRGM 1467
Cdd:cd12116 319 ELYIGGDGVAQGY---LGRPALTAERFVP-DPFAGPGSRLYRTGDL--VRR--RADGR------LEYLGRADGQVKIRGH 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1958758113 1468 RYHPIDIETsVIRAHRSIAECAVFTWTN----LLVVVVELDGLEqdALDLVAL 1516
Cdd:cd12116 385 RIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA--APDAAAL 434
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1011-1490 |
4.65e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.25 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQnlgTTLP-----TVKMIVEVSK 1085
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPR---TDLAvwaedTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1086 SACVLS---TQAITRLlkskeAAAAVDVRTWPTILDTDDIpkkkvasifRPP--SPDVLAYLDFSVSTTGILAGVKMSHA 1160
Cdd:PRK07768 110 KAVVVGepfLAAAPVL-----EEKGIRVLTVADLLAADPI---------DPVetGEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1161 ATSALCRSIKLQCELYPSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLVPPLELESNVSLWLSAVSQYKARVT- 1234
Cdd:PRK07768 176 NLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1235 ---FcSYSVMemcTKGLGAQTgalRMKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDLGLPARAVSTTFG-CRVNVAI 1310
Cdd:PRK07768 252 apnF-AYALL---ARRLRRQA---KPGAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1311 CLQPnrlgklaeqgtTGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPGVKVIIAhTETKGPLGDSHLGEIW 1390
Cdd:PRK07768 324 SFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGLEVRVV-DEDGQVLPPRGVGVIE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1391 VSSPHNATGYYTVYGEEALHADHfsarlsfGdtqtiWARTGYLGFLrrTELtdasGErhdaLYVVGSLDETLELRGMRYH 1470
Cdd:PRK07768 391 LRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 1958758113 1471 PIDIETSVIRAHRSIAECAV 1490
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1011-1234 |
8.96e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 63.06 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPVTVRPPhPQNLgttlptvKMIVEVSKSAC 1088
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARR-------EAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1089 VLSTQAItrllkskeAAAAVDVRTWPTILDTDDIPKKKVASifRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRS 1168
Cdd:cd12114 88 VLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPP--VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758113 1169 IKLQCELYPS-RQIAIcldpyCGLGFALwclcSVY-------SGHQSVLVPPLElESNVSLWLSAVSQYkaRVT 1234
Cdd:cd12114 158 INRRFAVGPDdRVLAL-----SSLSFDL----SVYdifgalsAGATLVLPDEAR-RRDPAHWAELIERH--GVT 219
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1011-1490 |
9.63e-10 |
|
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: 63.02 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVpvtVRPPHPQNlgtTLPTVKMIVEVSKsACVL 1090
Cdd:cd05904 37 ELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAV---VTTANPLS---TPAEIAKQVKDSG-AKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STQAiTRLLKSKEAAAAV------DVRTWPTILDTDDIPkkkVASIFRPP-SPDVLAYLDFSVSTTGILAGVKMSHA-AT 1162
Cdd:cd05904 109 FTTA-ELAEKLASLALPVvlldsaEFDSLSFSDLLFEAD---EAEPPVVViKQDDVAALLYSSGTTGRSKGVMLTHRnLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1163 SALCRSIKLQCELYPSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLVPPLELESnvslWLSAVSQYkaRVTFCSYS-- 1239
Cdd:cd05904 185 AMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY--KVTHLPVVpp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1240 -VMEMCTKGLGaqtgalrmKGVNLSCVRTCMVVAeerprisltqsfSKLFKDLglpARAVSTTFGcrvNVAIClqpnrlg 1318
Cdd:cd05904 259 iVLALVKSPIV--------DKYDLSSLRQIMSGA------------APLGKEL---IEAFRAKFP---NVDLG------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1319 klaeQG----TTGPDPTTVYVDmralRHDRVRlveRGSphslplmeSGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSP 1394
Cdd:cd05904 306 ----QGygmtESTGVVAMCFAP----EKDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1395 HNATGYytVYGEEALHAdhfsarlsfgdtqTI----WARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYH 1470
Cdd:cd05904 367 SIMKGY--LNNPEATAA-------------TIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVA 421
|
490 500
....*....|....*....|
gi 1958758113 1471 PIDIEtSVIRAHRSIAECAV 1490
Cdd:cd05904 422 PAELE-ALLLSHPEILDAAV 440
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
346-798 |
1.46e-09 |
|
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: 62.23 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 346 DTSGKaicTLTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPI------- 418
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGLRKLG-------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAAnpiytad 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 419 EVPLTRKDAGSQHVgFllgSCGVTLALTTDACQKGLPKAptgEVATFKGWPPlawLVIDGKHLTKPP---KDWYPLAQ-- 493
Cdd:cd05911 73 ELAHQLKISKPKVI-F---TDPDGLEKVKEAAKELGPKD---KIIVLDDKPD---GVLSIEDLLSPTlgeEDEDLPPPlk 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 494 DTGSRTAYIEYkTSkdGST---VGVTVPHSSLLAQC-QALTQVCGYTEA-ETLTNVLDFKRDAGLWhGVLTSVMNRMHVI 568
Cdd:cd05911 143 DGKDDTAAILY-SS--GTTglpKGVCLSHRNLIANLsQVQTFLYGNDGSnDVILGFLPLYHIYGLF-TTLASLLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 569 SIPyalmKVNPLSWIQKVCSYKARAALVKSRDMHW---SLLAQRGQrdvcLSSLRMLIVadGANPWSISSCDAFLNVFQS 645
Cdd:cd05911 219 IMP----KFDSELFLDLIEKYKITFLYLVPPIAAAlakSPLLDKYD----LSSLRVILS--GGAPLSKELQELLAKRFPN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 646 RGLRP-----EVICPCASSPEAltvairrpPDLGGppprkavlsmnglsygvirvdteeklsvltvqDVGQVMPGASVCV 720
Cdd:cd05911 289 ATIKQgygmtETGGILTVNPDG--------DDKPG--------------------------------SVGRLLPNVEAKI 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758113 721 VKVDGVPYLcKTDEIGEICVSSvatGTAYYGLLGITKNVFETvpVTADGvpvsdrpFTRTGLLGFIGPENLVFVVGKL 798
Cdd:cd05911 329 VDDDGKDSL-GPNEPGEICVRG---PQVMKGYYNNPEATKET--FDEDG-------WLHTGDIGYFDEDGYLYIVDRK 393
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1011-1527 |
5.33e-09 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 61.41 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGC--VPvtvrpphpqnLGTTLPT--VKMIVEVSKS 1086
Cdd:COG1020 506 ELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1087 ACVLSTQAITRLLKSKEAaaavdvrtwPTI-LDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSAL 1165
Cdd:COG1020 575 RLVLTQSALAARLPELGV---------PVLaLDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1166 CRSIKLQCELYPSRQIaicldpycgLGFA-----------LWCLCsvySGHQSVLVPPlELESNVSLWLSAVSQYKARVT 1234
Cdd:COG1020 646 LAWMQRRYGLGPGDRV---------LQFAslsfdasvweiFGALL---SGATLVLAPP-EARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1235 FCSYSVMEMCTKGLGAQTGALRmkgvnlscvrtCMVVAEERPrisltqsfsklfkDLGLPARAVSTTFGCR-VNvaiclq 1313
Cdd:COG1020 713 NLTPSLLRALLDAAPEALPSLR-----------LVLVGGEAL-------------PPELVRRWRARLPGARlVN------ 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1314 pnrLGklaeqgttGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVKVIIAhtetkgplgDSHL------- 1386
Cdd:COG1020 763 ---LY--------GPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVYVL---------DAHLqpvpvgv 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1387 -GEIWVSSPHNATGYytvYGEEALHADHFSArLSFGDTQTIWARTGYLGflRRTeltdASGErhdaLYVVGSLDETLELR 1465
Cdd:COG1020 814 pGELYIGGAGLARGY---LNRPELTAERFVA-DPFGFPGARLYRTGDLA--RWL----PDGN----LEFLGRADDQVKIR 879
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758113 1466 GMRYHPIDIEtSVIRAHRSIAECAVFTWTN-----LLVVVVELDGLEQDALDLVALVTNVVLEEHYL 1527
Cdd:COG1020 880 GFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAALLRLALALLLPPYMV 945
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
354-554 |
6.69e-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: 61.03 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 354 TLTYGKLWSRSLKLAYTLLSKltsknepLLNPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqh 431
Cdd:COG1020 501 SLTYAELNARANRLAHHLRAL-------GVGPGDLVGVCLERS--LEMVVALLAVLKAgaAYVPLDPAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 432 VGFLLGSCGVTLALTTDACQKGLPKAptgevatfkgwpPLAWLVIDGKHLTKPPKDWyPLAQDTGSRTAYIEYkTSkdGS 511
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPEL------------GVPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TS--GS 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958758113 512 T---VGVTVPHSSLLAQCQALTQVCGYTEAETLTNV--LDFkrDAGLW 554
Cdd:COG1020 629 TgrpKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
355-653 |
2.13e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.59 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 355 LTYGKLWSRSLKLAYTLLskltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--ELVPVPIEVPLTRkdagsqhV 432
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYPAER-------L 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 433 GFLLGSCGVTLALTTDACQKGLPkaPTGEVATFKGWPPLAWlvidgkhltkppKDW---YPLAQDTGSRTAYIEYKTSKD 509
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEW------------ADYpdtAPAVQLAGENLAYVIYTSGST 2158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 510 GSTVGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWhGVLTSVMNRMHVISIPYALmkvnplsWIQKVCSY 589
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDEL-------WDPEQLYD 2230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958758113 590 KARAALVKSRDM---HWSLLAQRGQRDVCLSSLRMLIVadGANPWSISSCDAflnvfQSRGLRPEVI 653
Cdd:PRK12316 2231 EMERHGVTILDFppvYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRL-----AWEALRPVYL 2290
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
984-1161 |
2.68e-08 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 58.44 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 984 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1063
Cdd:cd17646 7 QAARTPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1064 PPHPQnlgttlPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasifrPPSPDVLAYLD 1143
Cdd:cd17646 80 PGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDNLAYVI 144
|
170
....*....|....*...
gi 1958758113 1144 FSVSTTGILAGVKMSHAA 1161
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAG 162
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
977-1491 |
2.73e-08 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 58.57 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLNAKGTVTSTATciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1057 CVPVTVrpphpqnlGTTLPT--VKMIVEVSKS-ACVLSTQAI-TRLLKSKEAAAAV---------------DVRTWPTIL 1117
Cdd:COG1022 90 AVTVPI--------YPTSSAeeVAYILNDSGAkVLFVEDQEQlDKLLEVRDELPSLrhivvldprglrddpRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1118 D--TDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPS-RQIAIcldpycgLGFA 1194
Cdd:COG1022 162 AlgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGdRTLSF-------LPLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1195 -----LWCLCSVYSGHQSVLVPPLElesNVSLWLSAVsqykaRVTF-CS--------YS-VMEMctkglGAQTGALRMKG 1259
Cdd:COG1022 235 hvferTVSYYALAAGATVAFAESPD---TLAEDLREV-----KPTFmLAvprvwekvYAgIQAK-----AEEAGGLKRKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1260 VNLsCVRTCMVVAEER---PRISLTQS----------FSKLfkdlglpaRAVsttFGCRVNVAIC----LQPNrlgkLAE 1322
Cdd:COG1022 302 FRW-ALAVGRRYARARlagKSPSLLLRlkhaladklvFSKL--------REA---LGGRLRFAVSggaaLGPE----LAR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1323 ----------QG-----TTGPdpTTVYvdmralRHDRVRLverGSphslplmeSGKILPGVKVIIAHTetkgplgdshlG 1387
Cdd:COG1022 366 ffralgipvlEGyglteTSPV--ITVN------RPGDNRI---GT--------VGPPLPGVEVKIAED-----------G 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1388 EIWVSSPHNATGYY-----TvygEEALHADhfsarlsfGdtqtiWARTGYLGFLrrteltDASGErhdaLYVVGSLDETL 1462
Cdd:COG1022 416 EILVRGPNVMKGYYknpeaT---AEAFDAD--------G-----WLHTGDIGEL------DEDGF----LRITGRKKDLI 469
|
570 580 590
....*....|....*....|....*....|
gi 1958758113 1463 ELR-GMRYHPIDIEtSVIRAHRSIAECAVF 1491
Cdd:COG1022 470 VTSgGKNVAPQPIE-NALKASPLIEQAVVV 498
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1011-1517 |
5.30e-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: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPqnlgttLPTVKMIVEVSKSACVL 1090
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STqaitrllkskeaaaavdvrtwptildtddipkkkvasifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIK 1170
Cdd:cd17643 90 TD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1171 LQCELYPSRQIAICldPYCGLGFALWCLCSVYS-GHQSVLVPPLELESNVSLWLSAVSQykaRVTFCSysvmemctkglg 1249
Cdd:cd17643 127 RWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLhGGRLVVVPYEVARSPEDFARLLRDE---GVTVLN------------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1250 aQTGalrmkgvnlSCVRTCMVVAEERPRISLtqsfsklfkdlglPARAVstTFGCRVnvaicLQPNRLGKLAEQ-GTTGP 1328
Cdd:cd17643 190 -QTP---------SAFYQLVEAADRDGRDPL-------------ALRYV--IFGGEA-----LEAAMLRPWAGRfGLDRP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1329 D--------PTTVYVDMRALRHDRVRLVERGSphslplmeSGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGY 1400
Cdd:cd17643 240 QlvnmygitETTVHVTFRPLDAADLPAAAASP--------IGRPLPGLRVYVL-DADGRPVPPGVVGELYVSGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1401 YtvyGEEALHADHFSArLSFGDTQTIWARTGYLGflRRTeltdASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIR 1480
Cdd:cd17643 311 L---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE-AALA 375
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958758113 1481 AHRSIAECAVFTWTN------LLVVVVELDGLEQDALDLVALV 1517
Cdd:cd17643 376 THPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRALL 418
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
343-545 |
6.42e-08 |
|
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: 57.19 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 343 TALDTSGKaicTLTYGKLWSRSLKLAYTLLsklTSKneplLNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 422
Cdd:cd05936 16 TALIFMGR---KLTYRELDALAEAFAAGLQ---NLG----VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 423 TRKDagsqhVGFLLGSCGVTLALTtdacqkglpkaptgeVATFkgwpplawlvidgKHLTKPPKDWYPLAQDTGSRTAYI 502
Cdd:cd05936 84 TPRE-----LEHILNDSGAKALIV---------------AVSF-------------TDLLAAGAPLGERVALTPEDVAVL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958758113 503 EYkTSkdGST---VGVTVPHSSLLA---QCQALTQVCGyTEAETLTNVL 545
Cdd:cd05936 131 QY-TS--GTTgvpKGAMLTHRNLVAnalQIKAWLEDLL-EGDDVVLAAL 175
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
984-1167 |
1.50e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 56.06 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 984 RAHTTPDHPLfllLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1063
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1064 PPHPQNlgttlpTVKMIVEVSKSACVLStqaitrllkSKEAAAAVDVRtwPTILDTDDIPKKKVASIFRPP-SPDVLAYL 1142
Cdd:cd12117 79 PELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGL--EVAVVIDEALDAGPAGNPAVPvSPDDLAYV 141
|
170 180
....*....|....*....|....*
gi 1958758113 1143 DFSVSTTGILAGVKMSHAATSALCR 1167
Cdd:cd12117 142 MYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
354-541 |
4.49e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 54.22 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 354 TLTYGKLWSRSLKLAYTLLSKLTsknepllNPGDRVALVFPNSDPVMfmVAFYGCLLAELVPVPIEvpltrKDAGSQHVG 433
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 434 FLLGSCGVTLALTTDACQKGLPkaptgevatfkgWPPLAW-LVIDGKHLTKPPkdwyPLAQDTGSRTAYIEYkTSkdGST 512
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP------------AGLPVLlLALAAAAAAPAA----PRTPVSPDDLAYVIY-TS--GST 138
|
170 180 190
....*....|....*....|....*....|..
gi 1958758113 513 ---VGVTVPHSSLLAQCQALTQVCGYTEAETL 541
Cdd:cd12116 139 grpKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
354-620 |
5.31e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.96 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 354 TLTYGKLWSRSLKLAYTLLskltsknEPLLNPGDRVALVFPNSdpVMFMVAFYGCLLA--ELVPVPIEVPLTRkdagsqh 431
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERS--AEMMVGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 432 VGFLLGSCGVTLALTTDACQKGLPkAPTGevatfkgwppLAWLVIDgkhltkPPKDWY------PLAQDTGSRTAYIEYK 505
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLP-IPDG----------LASLALD------RDEDWEgfpahdPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 506 TSKDGSTVGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDA---GLWHGVLT--SVMNRMHVISIP---YALMKV 577
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGsheGLYHPLINgaSVVIRDDSLWDPerlYAEIHE 4782
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958758113 578 NPLSWIQKVCSYkaraalvksrdmhWSLLAQRGQRDVCLSSLR 620
Cdd:PRK12316 4783 HRVTVLVFPPVY-------------LQQLAEHAERDGEPPSLR 4812
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
979-1512 |
9.24e-07 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 53.28 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 979 DVLQWRAHTTPDhPLFLLLNAKGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCV 1058
Cdd:cd05923 5 EMLRRAASRAPD-ACAIADPARGLRLTYS---ELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1059 PVTVRPP-HPQNLGTTLPTVKMIVEVSKSAcVLSTQAItRLLKSKEAAAAVDVRTWPTILDTDDIPkkkvasiFRPPSPD 1137
Cdd:cd05923 80 PALINPRlKAAELAELIERGEMTAAVIAVD-AQVMDAI-FQSGVRVLALSDLVGLGEPESAGPLIE-------DPPREPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1138 VLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCEL-YPSRQIAICLDP-YCGLGF-ALWCLCSVYSGhqsVLVPPLE 1214
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrHGRHNVVLGLMPlYHVIGFfAVLVAALALDG---TYVVVEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1215 LESNVSLWLSAvsqyKARVTfCSYSVMEMctkgLGAQTGALRMKGVNLSCVRTcmvvaeerprisltqsfsklfkdLGLP 1294
Cdd:cd05923 228 FDPADALKLIE----QERVT-SLFATPTH----LDALAAAAEFAGLKLSSLRH-----------------------VTFA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1295 ARAVSTTFGCRVNVAIclqPNRlgKLAEQGTT-------GPDPTTVYVdMRALRHDRVRLVERG--SPHSLPLMESGKIl 1365
Cdd:cd05923 276 GATMPDAVLERVNQHL---PGE--KVNIYGTTeamnslyMRDARTGTE-MRPGFFSEVRIVRIGgsPDEALANGEEGEL- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1366 pgvkvIIAHTetkgplGDSHLGEIWvsSPHNATgyytvygeealhadhfSARLSFGdtqtiWARTGylgflrRTELTDAS 1445
Cdd:cd05923 349 -----IVAAA------ADAAFTGYL--NQPEAT----------------AKKLQDG-----WYRTG------DVGYVDPS 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958758113 1446 GErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV--VVVELDGLEQDALD 1512
Cdd:cd05923 389 GD----VRILGRVDDMIISGGENIHPSEIE-RVLSRHPGVTEVVVIgvadeRWGQSVTacVVPREGTLSADELD 457
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1006-1159 |
1.80e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 52.69 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1006 TATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP--------------------- 1064
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1065 -----PHPQNLGTTLP-----TVKMIvevskSACVLSTQAITRL----LKSKEAA---AAVDVRTWPTILDTDDIPKKKV 1127
Cdd:PRK05605 136 wdkvaPTVERLRRTTPletivSVNMI-----AAMPLLQRLALRLpipaLRKARAAltgPAPGTVPWETLVDAAIGGDGSD 210
|
170 180 190
....*....|....*....|....*....|..
gi 1958758113 1128 ASiFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1159
Cdd:PRK05605 211 VS-HPRPTPDDVALILYTSGTTGKPKGAQLTH 241
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1011-1178 |
1.79e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1090
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STQAITRLLKSKEAAAAVDVRT---WPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1167
Cdd:PRK12316 2106 TQRHLLERLPLPAGVARLPLDRdaeWADYPDTA--PAVQLA-------GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ 2176
|
170
....*....|.
gi 1958758113 1168 SIKLQCELYPS 1178
Cdd:PRK12316 2177 AAGERYELSPA 2187
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1004-1506 |
1.81e-05 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 49.00 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1004 TSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPP-HPQNLgttlptvkmive 1082
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDY------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1083 vsksacvlstqaitrllkskeAAAAVDVRTWPTILDTDDIpkkkvasifrppspdvlAYLDFSVSTTGILAGVKMSHAAT 1162
Cdd:cd05919 75 ---------------------AYIARDCEARLVVTSADDI-----------------AYLLYSSGTTGPPKGVMHAHRDP 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1163 ----SALCRSIklqCELYPSRQIaicldpYC--------GLGFALWclCSVYSGHQSVLVPPLELESNVslwLSAVSQYK 1230
Cdd:cd05919 117 llfaDAMAREA---LGLTPGDRV------FSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPTAERV---LATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1231 ARVTfcsYSVMEMCTKGLGAQTGALRMkgvnLSCVRTCMVVAEERPRiSLTQSFSKLFkdlGLParaVSTTFGCRVNVAI 1310
Cdd:cd05919 183 PTVL---YGVPTFYANLLDSCAGSPDA----LRSLRLCVSAGEALPR-GLGERWMEHF---GGP---ILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1311 CLQpNRLGKlAEQGTTGpdpttvyvdmRALRHDRVRLVERgsphslplmesgkilpgvkviIAHTETKGPLGDshlgeIW 1390
Cdd:cd05919 249 FLS-NRPGA-WRLGSTG----------RPVPGYEIRLVDE---------------------EGHTIPPGEEGD-----LL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1391 VSSPHNATGYYTVYGEEalhadhfSARLSFGdtqtiWARTGYLGFLrrteltDASGerhdALYVVGSLDETLELRGMRYH 1470
Cdd:cd05919 291 VRGPSAAVGYWNNPEKS-------RATFNGG-----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVS 348
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958758113 1471 PIDIEtSVIRAHRSIAECAVftwtnllVVVVELDGL 1506
Cdd:cd05919 349 PVEVE-SLIIQHPAVAEAAV-------VAVPESTGL 376
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1015-1517 |
1.96e-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: 48.98 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1015 RAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPhpQNLGTTLPTVKMIVEVSKSACVLSTQA 1094
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP--LNPTLKESVLRYLVADAGGRIVLADAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1095 ITRLLKskeaAAAVDVRTWPTILDTDDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCE 1174
Cdd:cd05922 79 AADRLR----DALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1175 LYPSRQIAICLdpycglgfalwclcsvysghqsvlvpPLELESNVSLWLSAVSQYKARVTFCSY----SVMEMCTKglga 1250
Cdd:cd05922 155 ITADDRALTVL--------------------------PLSYDYGLSVLNTHLLRGATLVLTNDGvlddAFWEDLRE---- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1251 qTGALRMKGVnlscvrtcmvvaeerPriSLTQSFSKL-FKDLGLPARAVSTTFGCRvnvaicLQPNRLGKLAEQGTtGPD 1329
Cdd:cd05922 205 -HGATGLAGV---------------P--STYAMLTRLgFDPAKLPSLRYLTQAGGR------LPQETIARLRELLP-GAQ 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1330 PTTVYVDMRALRH----DRVRLVERgsPHSLplmesGKILPGVKVIIAHtETKGPLGDSHLGEIWVSSPHNATGYYTVYG 1405
Cdd:cd05922 260 VYVMYGQTEATRRmtylPPERILEK--PGSI-----GLAIPGGEFEILD-DDGTPTPPGEPGEIVHRGPNVMKGYWNDPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1406 EEAlHADHFSARLsfgdtqtiwaRTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIETSvIRAHRSI 1485
Cdd:cd05922 332 YRR-KEGRGGGVL----------HTGDLARR------DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLI 389
|
490 500 510
....*....|....*....|....*....|..
gi 1958758113 1486 AECAVFtwtnllvvvveldGLEQDALDLVALV 1517
Cdd:cd05922 390 IEAAAV-------------GLPDPLGEKLALF 408
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
984-1243 |
2.28e-05 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 984 RAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVR 1063
Cdd:cd17655 6 QAEKTPDHTAVVFED------QTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1064 PPHPQNlgttlpTVKMIVEVSKSACVLSTQAitrlLKSKEAAAAVDVRtwptiLDTDDIPKKKVASIFRPPSPDVLAYLD 1143
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSH----LQPPIAFIGLIDL-----LDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1144 FSVSTTGILAGVKMSH--------AATSALCRSIKLQCELYPSrqiaICLDPYCGLGFAlwclcSVYSGHQSVLVPPLEL 1215
Cdd:cd17655 144 YTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTLYIVRKETV 214
|
250 260
....*....|....*....|....*...
gi 1958758113 1216 ESNVSLwLSAVSQYKARVTFCSYSVMEM 1243
Cdd:cd17655 215 LDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
383-525 |
2.37e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 48.78 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 383 LNPGDRVALVFPNSDpvMFMVAFYGCLLAELVPVPIEVPLTRKDagsqhVGFLLGSCGVTLALTTDACQKGLPKAPTGEV 462
Cdd:PRK08316 58 LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAYILDHSGARAFLVDPALAPTAEAALALLP 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958758113 463 ATFKGWPPLAWLV------IDGKHLTKPPKDWYPLAQDTGSRTAYIEYkTSkdGSTV---GVTVPHSSLLAQ 525
Cdd:PRK08316 131 VDTLILSLVLGGReapggwLDFADWAEAGSVAEPDVELADDDLAQILY-TS--GTESlpkGAMLTHRALIAE 199
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
354-447 |
2.58e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 48.80 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 354 TLTYGKLWSRSLKLAYTLLSKLTSKnepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRkdagSQHVG 433
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECGVR------KGDRVLLYMQNS--PQFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90
....*....|....
gi 1958758113 434 FLLGSCGVTLALTT 447
Cdd:PRK08314 102 HYVTDSGARVAIVG 115
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
977-1066 |
2.97e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 48.60 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:COG1021 27 LGDLLRRRAERHPDRIA--VVDGERRLSYA----ELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90
....*....|
gi 1958758113 1057 CVPVTVRPPH 1066
Cdd:COG1021 100 AIPVFALPAH 109
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
337-532 |
3.87e-05 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 48.11 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 337 PKAPCLTALDTsgkaicTLTYGKLWSRSLKLAYTLLSKLTSknepllnPGDRVALVFPNSdpVMFMVAFYGCLLAELVPV 416
Cdd:cd17651 9 PDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVG-------PGDLVALCARRS--AELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 417 PIEVpltrkDAGSQHVGFLLGSCGVTLALTTDACQKGLPkaptgevatfkgwPPLAWLVIDGKHLTKPPKDWYPLAQDTG 496
Cdd:cd17651 74 PLDP-----AYPAERLAFMLADAGPVLVLTHPALAGELA-------------VELVAVTLLDQPGAAAGADAEPDPALDA 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958758113 497 SRTAYIEYkTSkdGST---VGVTVPHSSLLAQCQALTQV 532
Cdd:cd17651 136 DDLAYVIY-TS--GSTgrpKGVVMPHRSLANLVAWQARA 171
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
334-445 |
4.68e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 47.60 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 334 TTQPKAPCLTALDTSgkaictLTYGKLWSRSLKLAYTLLSkltsknePLLNPGDRVALVFPNSDPvmFMVAFYGCLLAEL 413
Cdd:cd17631 6 RRHPDRTALVFGGRS------LTYAELDERVNRLAHALRA-------LGVAKGDRVAVLSKNSPE--FLELLFAAARLGA 70
|
90 100 110
....*....|....*....|....*....|..
gi 1958758113 414 VPVPIEVPLTRKDagsqhVGFLLGSCGVTLAL 445
Cdd:cd17631 71 VFVPLNFRLTPPE-----VAYILADSGAKVLF 97
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
960-1161 |
6.61e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 47.73 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 960 RELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLflLLNAKGTVTSTatciQLHKRAERVAAALMEKGrLDAGDHVALVY 1039
Cdd:PRK10252 443 AQLAQVNATAVEIPETTLSALVAQQAAKTPDAPA--LADARYQFSYR----EMREQVVALANLLRERG-VKPGDSVAVAL 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1040 PPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVDVRTWPTilDT 1119
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA--PQ 587
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958758113 1120 DDIPKkkvasifRPPSPDVLAYLDFSVSTTGILAGVKMSHAA 1161
Cdd:PRK10252 588 GAAPL-------QLSQPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1011-1162 |
7.04e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 47.21 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPH-PQNLGTTLPT--VKMIV------ 1081
Cdd:PRK07656 35 ELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYtADEAAYILARgdAKALFvlglfl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1082 EVSKSA--CVLSTQAITRLLKSKEAAAAVDVRTWPTILDTDDIPKkkvasIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1159
Cdd:PRK07656 114 GVDYSAttRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE-----RAPEVDPDDVADILFTSGTTGRPKGAMLTH 188
|
...
gi 1958758113 1160 AAT 1162
Cdd:PRK07656 189 RQL 191
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
977-1489 |
9.75e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 46.82 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLNAKGTVT----STATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGC 1052
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1053 LYCGCVPVTVRPphpqnlGTTLPTVKMIVEVSKSACVLS---TQAITRLLKSKEAaaavDVRTWPTI----------LDT 1119
Cdd:PRK09274 87 FKAGAVPVLVDP------GMGIKNLKQCLAEAQPDAFIGipkAHLARRLFGWGKP----SVRRLVTVggrllwggttLAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1120 DDIPKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKlqcELYPSRQIAICL---------DPYCG 1190
Cdd:PRK09274 157 LLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfGPALG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1191 LgfalwclCSVysghqsvlVPPLEL----ESNVSLWLSAVSQYKARVTFCSYSVMEMCTKglgaqtgALRMKGVNLSCVR 1266
Cdd:PRK09274 234 M-------TSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YGEANGIKLPSLR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1267 TcMVVAEERPRISLTQSFSKLFKDlglparavsttfGCRVnvaiclqpnrlgkLAEQGTTGPDPTTVyVDMRALRHDRVR 1346
Cdd:PRK09274 292 R-VISAGAPVPIAVIERFRAMLPP------------DAEI-------------LTPYGATEALPISS-IESREILFATRA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1347 LVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWVSSPHNATGYYTvyGEEALHAdhfsARL 1418
Cdd:PRK09274 345 ATDNGAGICV-----GRPVDGVEVrIIAISDAPIPewddalrLATGEIGEIVVAGPMVTRSYYN--RPEATRL----AKI 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958758113 1419 SFGDTQtIWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECA 1489
Cdd:PRK09274 414 PDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
343-571 |
1.75e-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: 45.74 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 343 TALDTSGKaicTLTYGKLWSRSLKLAYTLLSKLTSknepllNPGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEVPL 422
Cdd:cd05941 3 IAIVDDGD---SITYADLVARAARLANRLLALGKD------LRGDRVAFLAPPS--AEYVVAQLAIWRAGGVAVPLNPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 423 TRKDAgsQHVgfllgscgvtlalTTDAcqkglpkAPTgevatfkgwpplawLVIDGkhltkppkdwyplaqdtgsrtAYI 502
Cdd:cd05941 72 PLAEL--EYV-------------ITDS-------EPS--------------LVLDP---------------------ALI 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958758113 503 EYKTSKDGSTVGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVISIP 571
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP 163
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
322-519 |
1.83e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.58 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 322 PPTLLAAL---QLWGTtqPKAPCLTALDTsgkaicTLTYGKLWSRSLKLAYTLlskltskNEPLLNPGDRVALVFPNSdp 398
Cdd:PRK10252 456 PETTLSALvaqQAAKT--PDAPALADARY------QFSYREMREQVVALANLL-------RERGVKPGDSVAVALPRS-- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 399 VMFMVAFYGCLLAELVPVPIEV--PLTRkdagsqhVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKGWPPlawlvi 476
Cdd:PRK10252 519 VFLTLALHAIVEAGAAWLPLDTgyPDDR-------LKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLA------ 585
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958758113 477 dgkhltkpPKDWYPLAQDTGSRTAYIEYKTSKDGSTVGVTVPH 519
Cdd:PRK10252 586 --------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
981-1517 |
2.08e-04 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 45.68 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 981 LQWRAHTTPDHPLFLLLNakgtvtSTATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPV 1060
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1061 tvrpphPQNLGTTLPTVKMIVEVSKSACVLstqaitrllkskeaaaavdvrtwptildtDDipkkkvasifrppspdvLA 1140
Cdd:cd17631 74 ------PLNFRLTPPEVAYILADSGAKVLF-----------------------------DD-----------------LA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1141 YLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELyPSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLVPPLELESnv 1219
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1220 slWLSAVSQYKARVTFCSYSVME-MCTKGlgaqtgalRMKGVNLSCVRtCMVVAEERPRISLTQSFsklfKDLGLparAV 1298
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1299 STTFGcrvnvaiclqpnrlgklaeQGTTGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVKVIIAHTETK 1378
Cdd:cd17631 241 VQGYG-------------------MTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1379 gPLGDSHLGEIWVSSPHNATGYytvYGEEALHADhfsarlSFGDTqtiWARTGYLGFLrrteltDASGerhdALYVVGSL 1458
Cdd:cd17631 286 -EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVDRK 342
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958758113 1459 DETLELRGMRYHPIDIEtSVIRAHRSIAECAVF-----TWTNLLV-VVVELDGLEQDALDLVALV 1517
Cdd:cd17631 343 KDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELIAHC 406
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1362-1490 |
2.61e-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: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1362 GKILPGVKVIIAHTETKGPLGDSHlGEIWVSSPHNATGYYTvygEEALHADHFSARlsfgdtqtiWARTGYLGFLRrtel 1441
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958758113 1442 tdasgeRHDALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1490
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1011-1178 |
3.01e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.72 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNlgttlpTVKMIVEVSKSACVL 1090
Cdd:PRK12316 4581 ELNRRANRLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1091 STQAITRLLKSKEAAAAVDV---RTWPTILDTDdiPKKKVAsifrppsPDVLAYLDFSVSTTGILAGVKMSHAATSALCR 1167
Cdd:PRK12316 4654 TQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD--PAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
170
....*....|.
gi 1958758113 1168 SIKLQCELYPS 1178
Cdd:PRK12316 4725 ATGERYELTPD 4735
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
340-862 |
3.11e-04 |
|
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: 44.99 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 340 PCLTALDTSGKaicTLTYGKLWSRSLKLAyTLLSKLTSKnepllnPGDRVALVfpnSDPVMFMVAfygCLLAEL------ 413
Cdd:cd17653 11 PDAVAVESLGG---SLTYGELDAASNALA-NRLLQLGVV------PGDVVPLL---SDRSLEMLV---AILAILkagaay 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 414 VPVPIEVPLTRKDAgsqhvgfLLGSCGVTLALTTDAcqkglpkaptgevatfkgwpplawlvidgkhltkpPKDwyplaq 493
Cdd:cd17653 75 VPLDAKLPSARIQA-------ILRTSGATLLLTTDS-----------------------------------PDD------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 494 dtgsrTAYIEYkTSkdGST---VGVTVPHSSLLaqcqaltqvcgyteaetltnvldfkrdaglwhgvltsvmnrmHVISI 570
Cdd:cd17653 107 -----LAYIIF-TS--GSTgipKGVMVPHRGVL------------------------------------------NYVSQ 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 571 PYALMKVNPLSWIQKVCSYKARAALvksrdmhWSLLAqrgqrdvCLSSLRMLIVADGANPWS--ISSCDAFlnvfqsrgl 648
Cdd:cd17653 137 PPARLDVGPGSRVAQVLSIAFDACI-------GEIFS-------TLCNGGTLVLADPSDPFAhvARTVDAL--------- 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 649 rpevicpcASSPEALTVAIRRPPD------LGGPPPRKAVLS--------MNGlsYGvirvDTEEKLSVLTVQ------- 707
Cdd:cd17653 194 --------MSTPSILSTLSPQDFPnlktifLGGEAVPPSLLDrwspgrrlYNA--YG----PTECTISSTMTEllpgqpv 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 708 DVGQVMPGASVCVVKVDGVPYLckTDEIGEICVSSVATGTAYYGLLGITKNVFetvpvtadgVPVSDRP---FTRTGLLG 784
Cdd:cd17653 260 TIGKPIPNSTCYILDADLQPVP--EGVVGEICISGVQVARGYLGNPALTASKF---------VPDPFWPgsrMYRTGDYG 328
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958758113 785 FIGPENLVFVVGKLDGLTVVGARRHNADDIVATALAVEPMkfvyrgriAVFSVTVLHDDRivLVAEQRPDSSEEDSFQ 862
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPE--------VTQAAAIVVNGR--LVAFVTPETVDVDGLR 396
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1005-1489 |
3.21e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 45.14 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1005 STATCIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRP-PHPQNLGTTLPTVkmivev 1083
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLKQCLQEA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1084 sksacvlSTQAITRLLKSKEAAAAVdvrtwptildtddipkkkvasifrppspdvlayldFSVSTTGILAGVKMSHAATS 1163
Cdd:cd05910 74 -------EPDAFIGIPKADEPAAIL-----------------------------------FTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1164 ALCRSIKlqcELYPSRQIAICLDpycglGFALWCLCSVYSGHQSVlVPPLE----LESNVSLWLSAVSQYKARVTFCSYS 1239
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1240 VMEMCTKgLGAQtgalrmKGVNLSCVRtCMVVAEERPRISLTQSFSKLFKDlglpARAVSTTFGCRVNVAICLqpnrlgk 1319
Cdd:cd05910 183 LLERVAR-YCAQ------HGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----EAEILTPYGATEALPVSS------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1320 laeqgttgpdpttvyVDMRALRHDRVRLVERGSPHSLplmesGKILPGVKV-IIAHTETKGP-------LGDSHLGEIWV 1391
Cdd:cd05910 244 ---------------IGSRELLATTTAATSGGAGTCV-----GRPIPGVRVrIIEIDDEPIAewddtleLPRGEIGEITV 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1392 SSPHNATGYYTVYGEEALHADHFSArlsfgdtQTIWARTGYLGFLrrteltDASGErhdaLYVVGSLDETLELRGMRYHP 1471
Cdd:cd05910 304 TGPTVTPTYVNRPVATALAKIDDNS-------EGFWHRMGDLGYL------DDEGR----LWFCGRKAHRVITTGGTLYT 366
|
490
....*....|....*...
gi 1958758113 1472 IDIEtSVIRAHRSIAECA 1489
Cdd:cd05910 367 EPVE-RVFNTHPGVRRSA 383
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
355-622 |
4.05e-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: 44.78 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 355 LTYGKLWSRSLKLAYTLLSKLTSKnepllnpGDRVALVFPNSdpVMFMVAFYGCLLAELVPVPIEvPLTRKDagsqHVGF 434
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK-------GDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 435 LLGSCGVTLALTTDACQKglpkaptgevatfkgwpplawlvidgkhltkppkdwyplaqdtgsrTAYIEYKTSKDGSTVG 514
Cdd:cd05935 68 ILNDSGAKVAVVGSELDD----------------------------------------------LALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 515 VTVPHSSLLAqcQALTQVCGY--TEAETLTNVLDFKRDAGLWHGVLTSVmnrmhVISIPYALMKVnplsWIQKVcsykAR 592
Cdd:cd05935 102 CMHTHFSAAA--NALQSAVWTglTPSDVILACLPLFHVTGFVGSLNTAV-----YVGGTYVLMAR----WDRET----AL 166
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958758113 593 AALVKSRDMHWS--------LLAQRGQRDVCLSSLRML 622
Cdd:cd05935 167 ELIEKYKVTFWTniptmlvdLLATPEFKTRDLSSLKVL 204
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
321-449 |
5.85e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 44.26 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 321 GPPTLLAALQLWGTTQPKAPcltALDTSGKaicTLTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVALVFPNSdPvM 400
Cdd:PRK06178 31 GERPLTEYLRAWARERPQRP---AIIFYGH---VITYAELDELSDRFAALLRQRG-------VGAGDRVAVFLPNC-P-Q 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958758113 401 FMVAFYGCLLAELVPVPIEvPLTRKdagsQHVGFLLGSCGVTLALTTDA 449
Cdd:PRK06178 96 FHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
977-1159 |
8.24e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 43.88 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLLLnakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFY---GHVITYA---ELDELSDRFAALLRQRG-VGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1057 CVPVTVRP-------PHpqNLGTTLPTVKM-------IVEVSKSACVLSTQAITRLLKSKEAAAAV---DVRTWPTILDT 1119
Cdd:PRK06178 108 AVHVPVSPlfrehelSY--ELNDAGAEVLLaldqlapVVEQVRAETSLRHVIVTSLADVLPAEPTLplpDSLRAPRLAAA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958758113 1120 DDI------PKKKVASIFRPPSPDVLAYLDFSVSTTGILAGVKMSH 1159
Cdd:PRK06178 186 GAIdllpalRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQ 231
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
354-445 |
8.41e-04 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 43.90 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 354 TLTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVALVFpnSDPVMFMVAFYGCLLAELVPVPIEVPLTRKDagsqhVG 433
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALG-------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD-----YA 94
|
90
....*....|..
gi 1958758113 434 FLLGSCGVTLAL 445
Cdd:cd05959 95 YYLEDSRARVVV 106
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
324-416 |
8.56e-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: 43.98 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 324 TLLAALQLWGTTQPKAPCLTALDTSgkaictLTYGKLWSRSLKLAYTLLSkltsknepL-LNPGDRVALVFPNSdpVMFM 402
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERR------LSYAELDRRADRLAAGLLA--------LgLRPGDRVVVQLPNV--AEFV 89
|
90
....*....|....
gi 1958758113 403 VAFYGCLLAELVPV 416
Cdd:COG1021 90 IVFFALFRAGAIPV 103
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1011-1062 |
1.16e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 43.56 E-value: 1.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958758113 1011 QLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCGCVPVTV 1062
Cdd:COG0365 44 ELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
977-1160 |
1.24e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.21 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPLFLllnAKGTVTSTATCIQlhkRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLV---FGGTRWTYAEAAR---AAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1057 C--VPVTVRPPHPQnLGTTLPTVKMIVEVSKSACVLSTQAITRLLKSKEAAAAVD---VRTWPTILDTDDIPKKKVASIF 1131
Cdd:PRK06155 96 AiaVPINTALRGPQ-LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190
....*....|....*....|....*....|
gi 1958758113 1132 RPPSP-DVLAYLDFSvSTTGILAGVKMSHA 1160
Cdd:PRK06155 175 AAVQPgDTAAILYTS-GTTGPSKGVCCPHA 203
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
336-646 |
2.24e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 43.02 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 336 QPKAPCLTALDTsgkaicTLTYGKLWSRSLKLAYTLLskltsknEPLLNPGDRVALVFPNSDPVMfmVAFYGCLLA--EL 413
Cdd:PRK12316 524 TPEAPALAFGEE------TLDYAELNRRANRLAHALI-------ERGVGPDVLVGVAMERSIEMV--VALLAILKAggAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 414 VPVPIEVPLTRkdagsqhVGFLLGSCGVTLALTTDACQKGLPKAPTGEVATFKgwPPLAWLviDGkHLTKPPKdwyplAQ 493
Cdd:PRK12316 589 VPLDPEYPAER-------LAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLD--RPAAWL--EG-YSEENPG-----TE 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 494 DTGSRTAYIEYKTSKDGSTVGVTVPHSSLLAQCQALTQVCGYTEAETLTNVLDFKRDAGLWHGVLTsVMN--RMHVISip 571
Cdd:PRK12316 652 LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSgaRLVVAA-- 728
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758113 572 yALMKVNPLSWIQKVCSYKARA-ALVKSrdmHWSLLAQRGQRDVCLsSLRMLIVADGANPWsisscDAFLNVFQSR 646
Cdd:PRK12316 729 -PGDHRDPAKLVELINREGVDTlHFVPS---MLQAFLQDEDVASCT-SLRRIVCSGEALPA-----DAQEQVFAKL 794
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1327-1511 |
2.45e-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: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1327 GPDPTTVYVDMRALrhdrvrlvERGSPHSLplmesGKILPGVKVIIAhTETKGPLGDSHLGEIWVSSPHNATGYytvYGE 1406
Cdd:cd17653 240 GPTECTISSTMTEL--------LPGQPVTI-----GKPIPNSTCYIL-DADLQPVPEGVVGEICISGVQVARGY---LGN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1407 EALHADHFsARLSFGDTQTIWaRTGYLGFLRRteltdaSGErhdaLYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIA 1486
Cdd:cd17653 303 PALTASKF-VPDPFWPGSRMY-RTGDYGRWTE------DGG----LEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
|
170 180
....*....|....*....|....*
gi 1958758113 1487 ECAVFTWTNLLVVVVELDGLEQDAL 1511
Cdd:cd17653 371 QAAAIVVNGRLVAFVTPETVDVDGL 395
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1361-1490 |
2.95e-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: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1361 SGKILPGVKVIIAHtETKGPLGDshlGEIWVSSPHNATGYY--TVYGEEAlhadhfsarlsfgdTQTIWARTGYLGFLrr 1438
Cdd:cd05912 244 AGKPLFPVELKIED-DGQPPYEV---GEILLKGPNVTKGYLnrPDATEES--------------FENGWFKTGDIGYL-- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1958758113 1439 teltDASGerhdALYVVGSLDETLELRGMRYHPIDIETsVIRAHRSIAECAV 1490
Cdd:cd05912 304 ----DEEG----FLYVLDRRSDLIISGGENIYPAEIEE-VLLSHPAIKEAGV 346
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
977-1058 |
3.28e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.17 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHPlFLLLNakGTVTSTAtciQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:PRK08279 39 LGDVFEEAAARHPDRP-ALLFE--DQSISYA---ELNARANRYAHWAAARG-VGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
..
gi 1958758113 1057 CV 1058
Cdd:PRK08279 112 AV 113
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
337-426 |
6.39e-03 |
|
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: 41.14 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 337 PKAPcltALDTSGKAIcTLTYGKLwsrsLKLAYTLLSKLTSKNeplLNPGDRVALVFPNSDPvmFMVAFYGCLLAELVPV 416
Cdd:cd05926 1 PDAP---ALVVPGSTP-ALTYADL----AELVDDLARQLAALG---IKKGDRVAIALPNGLE--FVVAFLAAARAGAVVA 67
|
90
....*....|
gi 1958758113 417 PIEvPLTRKD 426
Cdd:cd05926 68 PLN-PAYKKA 76
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
338-418 |
6.44e-03 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 41.08 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 338 KAPCLTALDTSGKaicTLTYGKLWSRSLKLAYTLLSKLtskneplLNPGDRVAlVFPNSDPVMFmVAFYGCLLAELVPVP 417
Cdd:cd05945 3 ANPDRPAVVEGGR---TLTYRELKERADALAAALASLG-------LDAGDPVV-VYGHKSPDAI-AAFLAALKAGHAYVP 70
|
.
gi 1958758113 418 I 418
Cdd:cd05945 71 L 71
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1361-1490 |
7.94e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 40.72 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1361 SGKILPGVKVIIAHTETKGPLGDShlGEIWVSSPHNATGYYtvYGEEALHAdhfsarlSFGDTqtiWARTGYLGFLrrte 1440
Cdd:PRK03640 309 AGKPLFPCELKIEKDGVVVPPFEE--GEIVVKGPNVTKGYL--NREDATRE-------TFQDG---WFKTGDIGYL---- 370
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1441 ltDASGerhdALYVVGSLDETLELRGMRYHPIDIEtSVIRAHRSIAECAV 1490
Cdd:PRK03640 371 --DEEG----FLYVLDRRSDLIISGGENIYPAEIE-EVLLSHPGVAEAGV 413
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1362-1491 |
7.95e-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: 40.74 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 1362 GKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYY-----TvygEEALHADHfsarlsfgdtqtiWARTGYLGFL 1436
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958758113 1437 rrteltDASGerhdALYVVG-SLDETLELRGMRYHPIDIEtSVIRAHRSIAECAVF 1491
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVI 375
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
977-1066 |
8.44e-03 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 40.39 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958758113 977 LADVLQWRAHTTPDHplFLLLNAKGTVTStatcIQLHKRAERVAAALMEKGrLDAGDHVALVYPPGVDLIAAFYGCLYCG 1056
Cdd:cd05920 17 LGDLLARSAARHPDR--IAVVDGDRRLTY----RELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90
....*....|
gi 1958758113 1057 CVPVTVRPPH 1066
Cdd:cd05920 90 AVPVLALPSH 99
|
|
| |
